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NTE_01631 NTE_01631 proS proS NTE_01647 NTE_01647 aspS aspS cbiA cbiA NTE_01746 NTE_01746 serS serS bioD bioD purC purC purK purK pyrG pyrG NTE_01934 NTE_01934 NTE_01937 NTE_01937 NTE_01967 NTE_01967 NTE_01982 NTE_01982 purL purL purQ purQ purS purS NTE_02004 NTE_02004 NTE_02006 NTE_02006 NTE_02008 NTE_02008 sucD sucD NTE_02034 NTE_02034 NTE_02164 NTE_02164 NTE_02168 NTE_02168 purD purD NTE_02172 NTE_02172 carA carA lig lig NTE_02235 NTE_02235 gltX gltX NTE_02371 NTE_02371 NTE_02510 NTE_02510 NTE_02600 NTE_02600 NTE_02602 NTE_02602 NTE_02620 NTE_02620 NTE_02629 NTE_02629 NTE_02641 NTE_02641 rtcA rtcA gatD gatD gatE gatE NTE_02738 NTE_02738 NTE_02762 NTE_02762 NTE_02772 NTE_02772 NTE_02773 NTE_02773 gatB gatB gatA gatA NTE_02819 NTE_02819 aspS-2 aspS-2 NTE_02823 NTE_02823 purP purP lysS lysS purM purM rtcB rtcB NTE_02976 NTE_02976 argS argS NTE_03025 NTE_03025 NTE_03045 NTE_03045 NTE_03081 NTE_03081 NTE_03142 NTE_03142 NTE_03216 NTE_03216 guaA guaA NTE_03272 NTE_03272 atpD atpD atpB atpB atpA atpA atpE atpE cysS cysS metG metG NTE_03474 NTE_03474 NTE_00024 NTE_00024 tiaS tiaS NTE_00077 NTE_00077 nadE nadE NTE_00424 NTE_00424 NTE_00444 NTE_00444 purA purA thrS thrS argG argG NTE_00775 NTE_00775 NTE_00791 NTE_00791 NTE_00824 NTE_00824 NTE_00855 NTE_00855 NTE_00858 NTE_00858 NTE_00936 NTE_00936 NTE_00981 NTE_00981 NTE_01051 NTE_01051 NTE_01075 NTE_01075 NTE_01106 NTE_01106 NTE_01256 NTE_01256 alaS alaS leuS leuS NTE_01418 NTE_01418 NTE_01419 NTE_01419 NTE_01420 NTE_01420 hisS hisS
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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
filled nodes:
a 3D structure is known or predicted
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from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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NTE_01631acyl-CoA synthetase (NDP forming); PFAM: CoA binding domain; ATP-grasp domain; Succinyl-CoA ligase like flavodoxin domain. (707 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). (486 aa)
NTE_01647PFAM: tRNA synthetases class I (C) catalytic domain. (371 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). (431 aa)
cbiAHydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) /cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. (465 aa)
NTE_01746Hypothetical protein. (93 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). (425 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. (231 aa)
purCPFAM: SAICAR synthetase; TIGRFAM: phosphoribosylaminoimidazole-succinocarboxamide synthase. (277 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). (391 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. (551 aa)
NTE_01934PFAM: ATP synthase (F/14-kDa) subunit. (98 aa)
NTE_01937Putative ester cyclase; PFAM: SnoaL-like polyketide cyclase; TIGRFAM: conserved hypothetical protein, steroid delta-isomerase-related. (175 aa)
NTE_01967GMP synthase family protein; PFAM: Glutamine amidotransferase class-I. (191 aa)
NTE_01982birA, biotin-(acetyl-CoA-carboxylase) ligase; PFAM: HTH domain; Biotin protein ligase C terminal domain; Biotin/lipoate A/B protein ligase family; TIGRFAM: BirA biotin operon repressor domain; birA, biotin-[acetyl-CoA-carboxylase] ligase region. (349 aa)
purLPhosphoribosylformylglycinamidine synthase II; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist [...] (727 aa)
purQPhosphoribosylformylglycinamidine synthase subunit I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to [...] (231 aa)
purSPhosphoribosylformylglycinamidine synthase, purS protein; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought [...] (92 aa)
NTE_02004PFAM: SnoaL-like domain. (126 aa)
NTE_02006Ketosteroid isomerase-like protein; PFAM: SnoaL-like domain. (125 aa)
NTE_02008Hypothetical protein; PFAM: SnoaL-like polyketide cyclase. (132 aa)
sucDsuccinyl-CoA synthetase (ADP-forming) alpha subunit; 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. (310 aa)
NTE_02034PFAM: CoA-ligase; ATP-grasp domain; TIGRFAM: succinyl-CoA synthetase, beta subunit. (369 aa)
NTE_02164PFAM: Asparagine synthase. (405 aa)
NTE_02168PFAM: 5-formyltetrahydrofolate cyclo-ligase family; TIGRFAM: 5,10-methenyltetrahydrofolate synthetase. (172 aa)
purDPhosphoribosylamine--glycine ligase; PFAM: Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, C domain; TIGRFAM: phosphoribosylamine--glycine ligase; Belongs to the GARS family. (431 aa)
NTE_02172Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; MGS-like domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit. (1029 aa)
carAPFAM: Carbamoyl-phosphate synthase small chain, CPSase domain; Glutamine amidotransferase class-I; TIGRFAM: carbamoyl-phosphate synthase, small subunit; Belongs to the CarA family. (403 aa)
ligATP-dependent DNA ligase I; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. (606 aa)
NTE_02235PFAM: F420-0:Gamma-glutamyl ligase; TIGRFAM: F420-0:gamma-glutamyl ligase. (257 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). (594 aa)
NTE_02371Acetyl-coenzyme A synthetase; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain; TIGRFAM: acetate--CoA ligase. (649 aa)
NTE_02510Hypothetical protein; PFAM: Domain of unknown function (DUF4443). (223 aa)
NTE_02600Pantothenate synthetase; PFAM: Protein of unknown function DUF137. (251 aa)
NTE_02602PFAM: DNA / pantothenate metabolism flavoprotein; Flavoprotein; TIGRFAM: phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase. (431 aa)
NTE_02620PFAM: SnoaL-like domain. (124 aa)
NTE_02629PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I. (508 aa)
NTE_02641EMAP domain-containing protein; PFAM: Putative tRNA binding domain; TIGRFAM: methionyl-tRNA synthetase C-terminal region/beta chain. (138 aa)
rtcARNA 3'-phosphate cyclase; Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing. (354 aa)
gatDglutamyl-tRNA(Gln) amidotransferase subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (445 aa)
gatEglutamyl-tRNA(Gln) amidotransferase subunit E; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (636 aa)
NTE_02738Hypothetical protein. (90 aa)
NTE_02762Putative PP-loop superfamily ATPase; PFAM: Queuosine biosynthesis protein QueC; TIGRFAM: queuosine biosynthesis protein QueC. (234 aa)
NTE_02772acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta); PFAM: Carboxyl transferase domain. (514 aa)
NTE_02773acetyl/propionyl-CoA carboxylase, alpha subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit. (502 aa)
gatBaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (479 aa)
gatAaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (478 aa)
NTE_02819PFAM: Glu-tRNAGln amidotransferase C subunit; TIGRFAM: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit. (94 aa)
aspS-2aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). (446 aa)
NTE_02823Hypothetical protein. (330 aa)
purPATP-utilizing enzymes of ATP-grasp superfamily (probably carboligase); Catalyzes the ATP- and formate-dependent formylation of 5- aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates. (351 aa)
lysSPFAM: tRNA synthetases class I (K); TIGRFAM: lysyl-tRNA synthetase, archaeal and spirochete; Belongs to the class-I aminoacyl-tRNA synthetase family. (548 aa)
purMPhosphoribosylformylglycinamidine cyclo-ligase; PFAM: AIR synthase related protein, N-terminal domain; AIR synthase related protein, C-terminal domain; TIGRFAM: phosphoribosylaminoimidazole synthetase. (345 aa)
rtcBHypothetical protein; PFAM: tRNA-splicing ligase RtcB; Belongs to the RtcB family. (490 aa)
NTE_02976PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: asparaginyl-tRNA synthetase. (432 aa)
argSarginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (647 aa)
NTE_03025PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain of tRNA; TIGRFAM: isoleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (1078 aa)
NTE_030452'-5' RNA ligase; Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester; Belongs to the 2H phosphoesterase superfamily. ThpR family. (185 aa)
NTE_03081PFAM: SnoaL-like polyketide cyclase. (51 aa)
NTE_03142PFAM: SnoaL-like domain. (107 aa)
NTE_03216PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain of tRNA; TIGRFAM: valyl-tRNA synthetase. (786 aa)
guaAGMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (517 aa)
NTE_03272PFAM: ATP synthase (C/AC39) subunit. (353 aa)
atpDH(+)-transporting ATP synthase, vacuolar type, subunit D; Produces ATP from ADP in the presence of a proton gradient across the membrane. (220 aa)
atpBArchaeal/vacuolar-type H+-ATPase subunit B; Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. (443 aa)
atpAArchaeal/vacuolar-type H+-ATPase subunit A; Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. Belongs to the ATPase alpha/beta chains family. (600 aa)
atpEArchaeal/vacuolar-type H+-ATPase subunit E; Produces ATP from ADP in the presence of a proton gradient across the membrane. (208 aa)
cysSPFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase. (475 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. (553 aa)
NTE_03474Asparagine synthase, glutamine-hydrolyzing; PFAM: Glutamine amidotransferase domain; Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). (665 aa)
NTE_00024Ketosteroid isomerase-like protein; PFAM: SnoaL-like polyketide cyclase; SnoaL-like domain; TIGRFAM: conserved hypothetical protein, steroid delta-isomerase-related. (271 aa)
tiaSPutative DNA-binding protein containing a Zn-ribbon domain; ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA. (438 aa)
NTE_00077Dinucleotide-utilizing enzyme possibly involved in molybdopterin or thiamin biosynthesis; PFAM: ThiS family; MoeZ/MoeB domain; ThiF family. (444 aa)
nadENAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (279 aa)
NTE_00424PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain; TIGRFAM: glutamine synthetase, type I. (488 aa)
NTE_00444acyl-CoA synthetase/AMP-acid ligase; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (641 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. (335 aa)
thrSPFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); Archaea-specific editing domain of threonyl-tRNA synthetase; TIGRFAM: threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (631 aa)
argGPFAM: Arginosuccinate synthase; TIGRFAM: argininosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (413 aa)
NTE_00775PFAM: ATP-binding region; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. (229 aa)
NTE_00791Amidase, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit; PFAM: Amidase. (477 aa)
NTE_00824ATP-utilizing enzymes of ATP-grasp superfamily (probably carboligase); PFAM: Domain of unknown function (DUF1297); Protein of unknown function (DUF1246). (366 aa)
NTE_00855Putative PP-loop superfamily ATPase; PFAM: Queuosine biosynthesis protein QueC; TIGRFAM: queuosine biosynthesis protein QueC. (219 aa)
NTE_00858PFAM: Asparagine synthase. (265 aa)
NTE_00936Phosphoribosylamine--glycine ligase; PFAM: Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, C domain. (423 aa)
NTE_00981glycyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: glycyl-tRNA synthetase, dimeric type. (495 aa)
NTE_01051acyl-CoA synthetase (NDP forming); PFAM: CoA binding domain; ATP-grasp domain; Succinyl-CoA ligase like flavodoxin domain; TIGRFAM: acetyl coenzyme A synthetase (ADP forming), alpha domain. (701 aa)
NTE_01075PFAM: tRNA synthetases class I (W and Y); TIGRFAM: tyrosyl-tRNA synthetase. (348 aa)
NTE_01106PFAM: Asparagine synthase. (320 aa)
NTE_01256PFAM: F420-0:Gamma-glutamyl ligase; TIGRFAM: F420-0:gamma-glutamyl ligase. (250 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. (908 aa)
leuSPFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain of tRNA; TIGRFAM: leucyl-tRNA synthetase, archaeal and cytosolic family; Belongs to the class-I aminoacyl-tRNA synthetase family. (966 aa)
NTE_01418PFAM: tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. (551 aa)
NTE_01419phenylalanyl-tRNA synthetase, alpha subunit; PFAM: tRNA synthetases class II core domain (F); TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit. (498 aa)
NTE_01420PFAM: tRNA synthetases class I (W and Y); TIGRFAM: tryptophanyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (391 aa)
hisSPFAM: Anticodon binding domain; Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (424 aa)
Your Current Organism:
Nitrososphaera evergladensis
NCBI taxonomy Id: 1459636
Other names: C. Nitrososphaera evergladensis SR1, Candidatus Nitrososphaera evergladensis SR1
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