ID   COBQ_VIBVY              Reviewed;         480 AA.
AC   Q7ME60;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VVA0824;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC       and one molecule of ATP is hydrogenolyzed for each amidation.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR   EMBL; BA000038; BAC96850.1; -; Genomic_DNA.
DR   RefSeq; WP_011152137.1; NC_005140.1.
DR   AlphaFoldDB; Q7ME60; -.
DR   SMR; Q7ME60; -.
DR   STRING; 672.VV93_v1c38310; -.
DR   EnsemblBacteria; BAC96850; BAC96850; BAC96850.
DR   KEGG; vvy:VVA0824; -.
DR   PATRIC; fig|196600.6.peg.4008; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002675; Chromosome II.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..480
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141342"
FT   DOMAIN          249..436
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   480 AA;  52582 MW;  F932218CB84A576F CRC64;
     MKKLLMVQGT TSDAGKSVLV AGLCRVLARK GVKVAPFKPQ NMALNSAVTK EGGEIGRAQA
     VQAQACRIEP SVHMNPVLIK PNSDTGAQII LQGKALTNMD AYGFHNYKKV AMDTVMDSFA
     RLKDEYQAIM IEGAGSPAEI NLRQNDIANM GFAEEADVPV IIVADIDRGG VFAHLYGTLA
     LLSPSEQARV KGFVINRFRG DIKLLESGLD WLEEKTGKPV IGVLPFLHGL NLEAEDAITS
     QQALSDEVKL KVVVPVLTRI SNHTDFDVLR LHPQIDLRYV GKGERLEHAD LIILPGSKSV
     RDDLRYLREQ GWDKDILRHL RFGGKVLGIC GGYQMLGESI RDPFGVEGEP GESVGLGLLK
     TRTELTQDKC LINTKGQLSL NGKHVNVTGY EIHVGRSQVN EYQPITKDDG QLEGALSECG
     QIMGSYLHGF LDSEAALELI CEWVNGVRIK AQNHQQLKEQ AIDRIADAIE EHLDLSQLGI