STRINGSTRING
ddl ddl citC citC guaA guaA glnS glnS cysS cysS asnS asnS serS serS AHG84061.1 AHG84061.1 alaS alaS bioD bioD purC purC purM purM purD purD purK purK AHG84109.1 AHG84109.1 lysS lysS accD accD AHG84221.1 AHG84221.1 AHG84238.1 AHG84238.1 accA accA pheT pheT pheS pheS F543_1420 F543_1420 aspS aspS AHG84341.1 AHG84341.1 moeB moeB AHG84432.1 AHG84432.1 queC queC hisS hisS sucD sucD sucC sucC ligA ligA pyrG pyrG ileS ileS murC murC murD murD murF murF murE murE AHG84697.1 AHG84697.1 metG metG mpl mpl AHG84750.1 AHG84750.1 tyrS tyrS purA purA accC accC AHG84788.1 AHG84788.1 valS valS asnA asnA glyS glyS glyQ glyQ AHG84916.1 AHG84916.1 epmA epmA purL purL proS proS tilS tilS AHG84984.1 AHG84984.1 AHG84989.1 AHG84989.1 trpS trpS gshB gshB atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB glnA glnA argS argS coaBC coaBC carB carB carA carA gltX gltX F543_580 F543_580 tcdA tcdA F543_7240 F543_7240 F543_7250 F543_7250 F543_730 F543_730 F543_7320 F543_7320 leuS leuS thrS thrS argG argG fadD fadD
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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ddlD-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (303 aa)
citC[citrate (Pro-3S)-lyase] ligase; Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'- dephosphocoenzyme-A) of the gamma subunit of citrate lyase. (335 aa)
guaAGMP synthase; Catalyzes the synthesis of GMP from XMP. (522 aa)
glnSglutaminyl-tRNA synthetase PRK05347; Glutaminyl-tRNA synthetase of Bacteria UniRef RepID=SYQ_PECCP. (557 aa)
cysScysteinyl-tRNA synthetase PRK00260; Cysteinyl-tRNA synthetase of Gammaproteobacteria UniRef RepID=E0WSA9_9ENTR; Belongs to the class-I aminoacyl-tRNA synthetase family. (461 aa)
asnSasparaginyl-tRNA synthetase PRK03932; Asparaginyl-tRNA synthetase of Bacteria UniRef RepID=SYN_HAEIN. (467 aa)
serSSeryl-tRNA synthetase; 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). (434 aa)
AHG84061.1O-succinylbenzoic acid--CoA ligase PRK09029; O-succinylbenzoic acid--CoA ligase of Actinobacillus minor UniRef RepID=C5S0N7_9PAST. (470 aa)
alaSAlanyl-tRNA synthetase; 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. (875 aa)
bioDATP-dependent dethiobiotin synthetase BioD 1; 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. (239 aa)
purCPhosphoribosylaminoimidazole-succinocarboxamide synthase PRK09362; Phosphoribosylaminoimidazole-succinocarboxamide synthase of Bacteria UniRef RepID=PUR7_EXIS2; Belongs to the SAICAR synthetase family. (236 aa)
purMPhosphoribosylaminoimidazole synthetase PRK05385; Phosphoribosylformylglycinamidine cyclo-ligase of Bacteria UniRef RepID=PUR5_BIFA0. (339 aa)
purDPhosphoribosylamine--glycine ligase PRK00885; Phosphoribosylamine--glycine ligase of Bacteria UniRef RepID=PUR2_BACHD; Belongs to the GARS family. (419 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). (260 aa)
AHG84109.1N5-carboxyaminoimidazole ribonucleotide synthase; Phosphoribosylaminoimidazole carboxylase ATPase subunit PRK06019; N5-carboxyaminoimidazole ribonucleotide synthase of Staphylococcaceae UniRef RepID=PURK_STAEQ. (118 aa)
lysSlysyl-tRNA synthetase PRK00484; Lysyl-tRNA synthetase of Gammaproteobacteria UniRef RepID=SYK_COLP3; Belongs to the class-II aminoacyl-tRNA synthetase family. (500 aa)
accDAcetyl-CoA carboxylase, carboxyl transferase, beta subunit; 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. (298 aa)
AHG84221.1Bifunctional folylpolyglutamate synthase/ dihydrofolate synthase PRK10846; Folylpolyglutamate synthase of Bacteria UniRef RepID=FOLC_HAEIN; Belongs to the folylpolyglutamate synthase family. (432 aa)
AHG84238.1Ribosomal protein S6 modification protein PRK10446; Ribosomal protein S6 modification protein, glutamic acid ligase of Pasteurellaceae UniRef RepID=B8F3P5_HAEPS; Belongs to the RimK family. (301 aa)
accAAcetyl-coenzyme A carboxylase carboxyl transferase 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. (317 aa)
pheTphenylalanyl-tRNA synthetase subunit beta PRK00629; Phenylalanyl-tRNA synthetase beta chain of cellular organisms UniRef RepID=SYFB_HAEDU; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
pheSphenylalanyl-tRNA synthetase subunit alpha PRK00488; Phenylalanyl-tRNA synthetase alpha chain of Gammaproteobacteria UniRef RepID=SYFA_HAES1; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 aa)
F543_1420long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetases (AMP-forming) COG1022; long-chain-fatty-acid--CoA ligase of Bacteria UniRef RepID=LCFH_HAEIN. (593 aa)
aspSAspartyl-tRNA synthetase; 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. (424 aa)
AHG84341.1aspartyl-tRNA synthetase PRK00476; Aspartyl-tRNA synthetase of Buchnera aphidicola UniRef RepID=SYD_BUCBP; overlaps CDS with the same product name. (165 aa)
moeBMolybdopterin biosynthesis protein MoeB PRK05690; Sulfur carrier protein moaD adenylyltransferase of Proteobacteria UniRef RepID=MOEB_ECOLI. (252 aa)
AHG84432.1Uncharacterized protein of Pasteurellaceae UniRef RepID=A3N009_ACTP2. (59 aa)
queC7-cyano-7-deazaguanine synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. (220 aa)
hisShistidyl-tRNA synthetase PRK00037; Histidyl-tRNA synthetase of Gammaproteobacteria UniRef RepID=SYH_MANSM. (428 aa)
sucDSuccinyl-CoA ligase [ADP-forming] 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. (289 aa)
sucCSuccinyl-CoA ligase [ADP-forming] 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)
ligADNA ligase; 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. (670 aa)
pyrGCTP synthase; 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. (544 aa)
ileSIsoleucyl-tRNA synthetase; 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. (933 aa)
murCUDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (475 aa)
murDUDP-N-acetylmuramoylalanine--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. (430 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. (464 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. (493 aa)
AHG84697.1methionyl-tRNA synthetase PRK00133; Methionyl-tRNA synthetase of root UniRef RepID=SYM_VIBC3; overlaps CDS with the same product name. (199 aa)
metGMethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (493 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. (453 aa)
AHG84750.15-formyltetrahydrofolate cyclo-ligase family protein PRK10333; 5-formyltetrahydrofolate cyclo-ligase of Pasteurellaceae UniRef RepID=B8F621_HAEPS; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (191 aa)
tyrSTyrosyl-tRNA synthetase 2; 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 2 subfamily. (396 aa)
purAAdenylosuccinate synthetase; 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. (431 aa)
accCBiotin carboxylase; 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. (447 aa)
AHG84788.1Biotin carboxyl carrier protein of acetyl-CoA carboxylase; 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. (155 aa)
valSValyl-tRNA synthetase; 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. (948 aa)
asnAAspartate--ammonia ligase; Asparagine synthetase AsnA PRK05425; Aspartate--ammonia ligase of cellular organisms UniRef RepID=ASNA_HAEIE. (330 aa)
glySglycyl-tRNA synthetase subunit beta PRK01233; Glycyl-tRNA synthetase beta subunit of Bacteria UniRef RepID=SYGB_HAEI8. (726 aa)
glyQglycyl-tRNA synthetase subunit alpha PRK09348; Glycyl-tRNA synthetase alpha subunit of cellular organisms UniRef RepID=SYGA_PSEA6. (327 aa)
AHG84916.1Uncharacterized conserved protein COG4285; Biotin apo-protein ligase-related protein of Mannheimia haemolytica UniRef RepID=E2P2V1_PASHA. (248 aa)
epmAProtein YjeA; 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. (327 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. (1320 aa)
proSProlyl-tRNA synthetase; 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 dea [...] (571 aa)
tilStRNA(Ile)-lysidine synthase; 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. (423 aa)
AHG84984.1Biotin operon represssor; Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor PRK11886; Biotin operon represssor of Pasteurellaceae UniRef RepID=Q7VPJ1_HAEDU. (266 aa)
AHG84989.1Lipoate-protein ligase of Aerococcus viridans ATCC 11563 UniRef RepID=D4YEM5_9LACT. (340 aa)
trpSTryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (342 aa)
gshBGlutathione biosynthesis bifunctional protein gshAB; Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine; In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. (745 aa)
atpCATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa)
atpDATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (457 aa)
atpGATP synthase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (288 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (513 aa)
atpHATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (177 aa)
atpFATP synthase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (156 aa)
atpEATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (84 aa)
atpBF0F1-type ATP synthase, alpha subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (263 aa)
glnAGlutamine synthetase PRK09469; Glutamine synthetase of cellular organisms UniRef RepID=GLNA_SYNY3. (523 aa)
argSarginyl-tRNA synthetase PRK12451; Arginyl-tRNA synthetase of Proteobacteria UniRef RepID=SYR_NEIG2. (575 aa)
coaBCPhosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase; 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. (403 aa)
carBCarbamoyl phosphate synthase large subunit PRK05294; Carbamoyl-phosphate synthase large chain of cellular organisms UniRef RepID=CARB_HAEDU; Belongs to the CarB family. (1067 aa)
carACarbamoyl phosphate synthase small subunit PRK12564; Carbamoyl-phosphate synthase small chain of root UniRef RepID=CARA_POLSQ; Belongs to the CarA family. (379 aa)
gltXGlutamyl-tRNA synthetase; 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. (479 aa)
F543_580Possible molybdopterin/thiamine biosynthesis protein of Mannheimia haemolytica PHL213 UniRef RepID=A7JRA8_PASHA. (243 aa)
tcdAThiF domain protein; Sulfur acceptor protein CsdL PRK15116; ThiF domain protein of Actinobacillus UniRef RepID=E8KG60_9PAST. (254 aa)
F543_7240RfaL protein; Lipid A core - O-antigen ligase and enzymes COG3307; RfaL protein of Actinobacillus UniRef RepID=E8KIT4_9PAST. (144 aa)
F543_7250Hypothetical protein; Lipid A core - O-antigen ligase and enzymes COG3307; uncharacterized protein of Actinobacillus minor UniRef RepID=C5RYT1_9PAST. (269 aa)
F543_730Acyl-coenzyme A synthetases/AMP-(fatty) acid ligases COG0365; acyl-coenzyme A synthetase-related protein of Histophilus somni UniRef RepID=Q0I109_HAES1. (401 aa)
F543_7320DNA ligase PRK09125; DNA ligase of Proteobacteria UniRef RepID=DNLI_HAEIN. (272 aa)
leuSleucyl-tRNA synthetase PRK00390; Leucyl-tRNA synthetase of Proteobacteria UniRef RepID=SYL_SALDC; Belongs to the class-I aminoacyl-tRNA synthetase family. (863 aa)
thrSThreonyl-tRNA synthetase; 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). (652 aa)
argGArgininosuccinate synthase PRK05370; Argininosuccinate synthase of root UniRef RepID=Q46QJ6_CUPPJ; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (443 aa)
fadDlong-chain-fatty-acid--CoA ligase PRK08974; Long-chain-fatty-acid--CoA ligase of root UniRef RepID=LCFA_HAEIN. (561 aa)
Your Current Organism:
Bibersteinia trehalosi
NCBI taxonomy Id: 1263831
Other names: B. trehalosi USDA-ARS-USMARC-189, Bibersteinia trehalosi USDA-ARS-USMARC-189
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