(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9Q9_METMS

ID   D5E9Q9_METMS            Unreviewed;       438 AA.
AC   D5E9Q9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.11 {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Ni-sirohydrochlorin a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.12 {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Ni-sirohydrochlorin a,c-diamide synthetase {ECO:0000256|HAMAP-Rule:MF_00027};
GN   Name=cbiA {ECO:0000256|HAMAP-Rule:MF_00027};
GN   Synonyms=cfbB {ECO:0000256|HAMAP-Rule:MF_00027};
GN   OrderedLocusNames=Mmah_0378 {ECO:0000313|EMBL:ADE35910.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35910.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35910.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate
CC       groups at positions a and c of cobyrinate, using either L-glutamine or
CC       ammonia as the nitrogen source. Involved in the biosynthesis of the
CC       unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic
CC       group of methyl-coenzyme M reductase (MCR), which plays a key role in
CC       methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-
CC       dependent amidation of the two carboxylate groups at positions a and c
CC       of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen
CC       source. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP +
CC         2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2
CC         phosphate; Xref=Rhea:RHEA:52896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:136841,
CC         ChEBI:CHEBI:136887, ChEBI:CHEBI:456216; EC=6.3.5.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00027};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP +
CC         cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate;
CC         Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, ChEBI:CHEBI:58894,
CC         ChEBI:CHEBI:456216; EC=6.3.5.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00027};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 10/10. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the
CC       binding site for glutamine and catalyzes the hydrolysis of this
CC       substrate to glutamate and ammonia. The N-terminal domain is
CC       anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and
CC       catalyzes the ultimate synthesis of the diamide product. The ammonia
CC       produced via the glutaminase domain is probably translocated to the
CC       adjacent domain via a molecular tunnel, where it reacts with an
CC       activated intermediate. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate and Ni-
CC       sirohydrochlorin are activated for nucleophilic attack via formation of
CC       a phosphorylated intermediate by ATP. CbiA catalyzes first the
CC       amidation of the c-carboxylate, and then that of the a-carboxylate.
CC       {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
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DR   EMBL; CP001994; ADE35910.1; -; Genomic_DNA.
DR   RefSeq; WP_013036853.1; NC_014002.1.
DR   EnsemblBacteria; ADE35910; ADE35910; Mmah_0378.
DR   GeneID; 8982512; -.
DR   KEGG; mmh:Mmah_0378; -.
DR   eggNOG; arCOG00106; Archaea.
DR   eggNOG; COG1797; LUCA.
DR   HOGENOM; HOG000289958; -.
DR   KO; K02224; -.
DR   OMA; PANTRMT; -.
DR   OrthoDB; 14023at2157; -.
DR   BioCyc; MMAH547558:G1GHT-374-MONOMER; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043775; F:cobyrinate a,c-diamide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00027; CobB_CbiA; 1.
DR   InterPro; IPR004484; CbiA_synth.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017929; CobB/CobQ_GATase.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43873; PTHR43873; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00379; cobB; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9Q9.
DR   SWISS-2DPAGE; D5E9Q9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00027,
KW   ECO:0000256|PROSITE-ProRule:PRU00606};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00027, ECO:0000313|EMBL:ADE35910.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Methanogenesis {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          239..425
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51274"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT   SITE            417
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   438 AA;  48207 MW;  0F912439DFD326BC CRC64;
     MKKSIVIAGT HSGVGKTTVS MGIMAALTRR GMNVQPYKVG PDYIDPTHHT AICGRPSRNL
     DTFMMGEEGV RQSFHCSYGN ADIGVVEGVM GLFDGMNSSD LASSAHVAKS LGAPVILVVN
     VHGMSRSAAA LIKGYSEFDS DVRIDGVVLN RVGSPRHAQM IRDALGDVPV VGALPRNQDL
     TVPSRHLGLH MADERDYDLE RLGNFIEENI DLDSVLSLAN DPRPAAPEEC IVNREVDVTI
     GVAMDSAFCF YYQDMLDYFR RSGAEIKFFS PLEGEIPDVD GMYFGGGYPE LHIAELEKSR
     TTHKLKDLSA DGMPIYGECG GLQYLCTSYE IEDRIYKMAD LFPAETVMTK KLQALGYTKG
     YADSPIFRGE VRGHEFHYSV TDCACDSRLA YTMERGKGIV DGMDGIYEHN SVASYMHAHP
     GSFPVDDFVQ SCRKYKQR
//

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