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glnA glnA glyS glyS glyQ glyQ purD purD caiC caiC accA_1 accA_1 tilS tilS proS proS purK purK cysS cysS AND12145.1 AND12145.1 murE murE murF murF murD murD murC murC AND12194.1 AND12194.1 lysS lysS purL purL nadE nadE hisS hisS ligA ligA gltX gltX accD accD AND12477.1 AND12477.1 AND12527.1 AND12527.1 AND12612.1 AND12612.1 purM purM purC purC guaA guaA AND12801.1 AND12801.1 tyrS tyrS bioD-2 bioD-2 ddlA ddlA fadD fadD aspS aspS argS argS lplA lplA pheT pheT pheS pheS thrS thrS pncB pncB asnS asnS serS serS fhs fhs AND13667.1 AND13667.1 metG metG bioD bioD sucD sucD sucC sucC glnS glnS leuS leuS gshA gshA alaS alaS AND15140.1 AND15140.1 gshB gshB pyrG pyrG panC panC queC queC carB carB carA carA ileS ileS accB accB accC accC epmA epmA AND14523.1 AND14523.1 valS valS mpl mpl purA purA birA birA argG argG AND14818.1 AND14818.1 coaBC coaBC asnA asnA acs acs trpS trpS
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glnAForms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology. (469 aa)
glySglycine--tRNA ligase beta chain; glyS; class II aminoacyl tRNA synthetase; tetramer of alpha(2)beta(2); catalyzes a two-step reaction; first charging a glycine molecule by linking the carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology. (690 aa)
glyQglycine--tRNA ligase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. (301 aa)
purDPhosphoribosylamine--glycine ligase; Catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GARS family. (429 aa)
caiCcrotonobetaine/carnitine-CoA ligase; Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine. (518 aa)
accA_1acetyl-CoA carboxylase carboxyltransferase subunit alpha; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. (319 aa)
tilStRNA lysidine(34) synthetase TilS; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (441 aa)
proSproline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] (571 aa)
purK5-(carboxyamino)imidazole ribonucleotide synthase; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (355 aa)
cysScysteine--tRNA ligase; Catalyzes a two-step reaction; charges a cysteine by linking its carboxyl group to the alpha-phosphate of ATP then transfers the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (463 aa)
AND12145.1Long-chain fatty acid--CoA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (602 aa)
murEUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. (495 aa)
murFUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily. (460 aa)
murDUDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. (436 aa)
murCUDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (487 aa)
AND12194.15-formyltetrahydrofolate cyclo-ligase; ygfA expression increases five to eight fold in Escherichia coli cells growing as biofilms; unknown function; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (205 aa)
lysSlysine--tRNA ligase; Class II; LysRS2; catalyzes a two-step reaction, first charging a lysine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Methanosarcina barkeri, LysRS2 charges both tRNA molecules for lysine that exist in this organism and in addition can charge the tRNAPyl with lysine in the presence of LysRS1; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. (504 aa)
purLPhosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. (1296 aa)
nadENAD+ synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (538 aa)
hisShistidine--tRNA ligase; Catalyzes a two-step reaction, first charging a histidine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class II aminoacyl-tRNA synthetase; forms homodimers; some organisms have a paralogous gene, hisZ, that is similar to hisS and produces a protein that performs the first step in histidine biosynthesis along with HisG; Derived by automated computational analysis using gene prediction method: Protein Homology. (427 aa)
ligADNA ligase (NAD(+)) LigA; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (675 aa)
gltXglutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (472 aa)
accDacetyl-CoA carboxylase subunit beta; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family. (320 aa)
AND12477.1Bifunctional tetrahydrofolate synthase/dihydrofolate synthase; Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10- formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives. (432 aa)
AND12527.1o-succinylbenzoate--CoA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (474 aa)
AND12612.1tryptophan--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (339 aa)
purMPhosphoribosylformylglycinamidine cyclo-ligase; Catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. (346 aa)
purCPhosphoribosylaminoimidazolesuccinocarboxamide synthase; Catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis; SAICAR synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (237 aa)
guaAGlutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP. (525 aa)
AND12801.12'-5' RNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (237 aa)
tyrStyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (424 aa)
bioD-2Dethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family. (223 aa)
ddlAD-alanine--D-alanine ligase A; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (366 aa)
fadDlong-chain-fatty-acid--CoA ligase; Activates fatty acids by binding to coenzyme A; Derived by automated computational analysis using gene prediction method: Protein Homology. (562 aa)
aspSaspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (594 aa)
argSarginine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (576 aa)
lplAAraC family transcriptional regulator; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Belongs to the LplA family. (339 aa)
pheTphenylalanine--tRNA ligase subunit beta; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
pheSphenylalanine--tRNA ligase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 aa)
thrSthreonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). (642 aa)
pncBNicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP; Belongs to the NAPRTase family. (404 aa)
asnSasparagine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (466 aa)
serSserine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). (429 aa)
fhsFormate--tetrahydrofolate ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the formate--tetrahydrofolate ligase family. (556 aa)
AND13667.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (165 aa)
metGmethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (675 aa)
bioDDethiobiotin synthase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family. (228 aa)
sucDsuccinate--CoA ligase subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (290 aa)
sucCsuccinate--CoA ligase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (388 aa)
glnSglutamine--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology. (555 aa)
leuSleucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by automated computational [...] (860 aa)
gshAGlutamate--cysteine ligase; Involved in the first step of glutathione biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. (526 aa)
alaSalanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family. (875 aa)
AND15140.1Bifunctional 2-acylglycerophosphoethanolamine acyltransferase/acyl-ACP synthetase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. (718 aa)
gshBGlutathione synthase; Catalyzes the second step in the glutathione biosynthesis pathway, where it synthesizes ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic GSH synthase family. (318 aa)
pyrGCTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (545 aa)
panCPantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (283 aa)
queC7-cyano-7-deazaguanine synthase QueC; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. (232 aa)
carBCarbamoyl phosphate synthase large subunit; Four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology. (1075 aa)
carACarbamoyl-phosphate synthase small subunit; Catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers; Derived by automated computational analysis using gene prediction method: Protein Homology. (387 aa)
ileSisoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (936 aa)
accBacetyl-CoA carboxylase biotin carboxyl carrier protein subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (156 aa)
accCacetyl-CoA carboxylase biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (449 aa)
epmApoxB regulator PoxA; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. (325 aa)
AND14523.1RNA ligase RtcB family protein; Mutations in this gene result in a compromised ability for drug-inducible mexXY expression; expression is inducible by the same ribosome-targeting agents that induce mexXY; Derived by automated computational analysis using gene prediction method: Protein Homology. (378 aa)
valSvaline--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (962 aa)
mplUDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl- meso-diaminopimelate ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. Belongs to the MurCDEF family. Mpl subfamily. (459 aa)
purAAdenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family. (432 aa)
birAbiotin--[acetyl-CoA-carboxylase] synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (320 aa)
argGArgininosuccinate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (403 aa)
AND14818.1Ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (422 aa)
coaBCBifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (402 aa)
asnACatalyzes the formation of asparagine from aspartate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology. (330 aa)
acsAcetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. (652 aa)
trpStryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (342 aa)
Your Current Organism:
Proteus mirabilis
NCBI taxonomy Id: 584
Other names: ATCC 29906, CCUG 26767, CIP 103181, DSM 4479, LMG 3257, LMG:3257, NCTC 11938, P. mirabilis
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