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Database: UniProt
Entry: G7GU37_9ACTN
LinkDB: G7GU37_9ACTN
Original site: G7GU37_9ACTN 
ID   G7GU37_9ACTN            Unreviewed;       463 AA.
AC   G7GU37;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Hydrogenobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.9 {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Hydrogenobyrinic acid a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_00027,
GN   ECO:0000313|EMBL:GAB07112.1};
GN   ORFNames=GOAMR_62_00170 {ECO:0000313|EMBL:GAB07112.1};
OS   Gordonia amarae NBRC 15530.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB07112.1, ECO:0000313|Proteomes:UP000006023};
RN   [1] {ECO:0000313|EMBL:GAB07112.1, ECO:0000313|Proteomes:UP000006023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB07112.1,
RC   ECO:0000313|Proteomes:UP000006023};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL   Submitted (NOV-2011) 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 hydrogenobyrinate, using either L-
CC       glutamine or ammonia as the nitrogen source. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP + 2
CC         H(+) + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 phosphate;
CC         Xref=Rhea:RHEA:12544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:77873, ChEBI:CHEBI:77874,
CC         ChEBI:CHEBI:456216; EC=6.3.5.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00027};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10.
CC       {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 hydrogenobyrinate and catalyzes the
CC       ultimate synthesis of the diamide product. The ammonia produced via the
CC       glutaminase domain is probably translocated to the adjacent domain via
CC       a molecular tunnel, where it reacts with an activated intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- MISCELLANEOUS: The a and c carboxylates of hydrogenobyrinate are
CC       activated for nucleophilic attack via formation of a phosphorylated
CC       intermediate by ATP. CobB catalyzes first the amidation of the c-
CC       carboxylate, and then that of the a-carboxylate. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB07112.1}.
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DR   EMBL; BAED01000062; GAB07112.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7GU37; -.
DR   STRING; 1075090.GOAMR_62_00170; -.
DR   eggNOG; COG1797; Bacteria.
DR   UniPathway; UPA00148; UER00220.
DR   Proteomes; UP000006023; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR   GO; GO:0043802; F:hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) 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   CDD; cd05388; CobB_N; 1.
DR   CDD; cd03130; GATase1_CobB; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00027; CobB_CbiA; 1.
DR   InterPro; IPR004484; CbiA/CobB_synth.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00379; cobB; 1.
DR   PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR   PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00027}; Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00027};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00027}; Reference proteome {ECO:0000313|Proteomes:UP000006023}.
FT   DOMAIN          6..200
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          264..446
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        345
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT   SITE            442
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   463 AA;  47425 MW;  C1AF8357C5846329 CRC64;
     MTIPTIVVAA PASGSGKTTV TTGLIGALRA AGHRVAPFKV GPDFIDPGYH AVAAGRPGRN
     LDPNLVGIEL VARLFAAGSA GADIAVVEGV MGLFDGRILS DSTGSAIADA DPVAYGSTAH
     VAALIGAPVV LVVDGSGHSQ SLAALLHGFL TYESSVRIAG VILNRVGSAR HEEVLRHACA
     RVGVPVFGVL RRDPSLVVPS RHLGLIPAAE RSVEAVAAVE SMSAELAAAL DLPAIVAAAA
     GRTPLTVTPW SADDGIEPAG NPVIAVAGGP AFTFFYTELG EMLTAAGARI AVFDPLTDPL
     PDGTAGVIVG GGFPEEHAAE LSANRTLRGQ LAEHAGAGRP IWAECAGLLY LTRELDGHPM
     AGVIDAVGRF SPSLTLGYRD AVAVADSVLF GEGARVTGHE FHRSVVVEDR PGANPAWTWR
     DADGRPARHG YTHRGVHASY LHLHPAAHPD AVTRFVAAAA GRP
//
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