ID   COBQ_VIBPA              Reviewed;         483 AA.
AC   Q87HN1;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VPA0932;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000032; BAC62275.1; -; Genomic_DNA.
DR   RefSeq; NP_800442.1; NC_004605.1.
DR   RefSeq; WP_005479326.1; NC_004605.1.
DR   AlphaFoldDB; Q87HN1; -.
DR   SMR; Q87HN1; -.
DR   STRING; 223926.28809233; -.
DR   EnsemblBacteria; BAC62275; BAC62275; BAC62275.
DR   GeneID; 1191621; -.
DR   KEGG; vpa:VPA0932; -.
DR   PATRIC; fig|223926.6.peg.3863; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002493; Chromosome 2.
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; 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; 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..483
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141340"
FT   DOMAIN          252..439
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   483 AA;  52356 MW;  968A8F9A84F0A9F6 CRC64;
     MKSAIPSLMV QGTTSDAGKS VLVAGLCRVL ARKGINVAPF KPQNMALNSA VTKDGGEIGR
     AQAVQAQACN IEPTVHMNPV LIKPNSDTGA QIILQGKALS NMDAASFHDY KKVAMNTVLD
     SFSKLTKEFD SIMIEGAGSP AEINLREGDI ANMGFAEAAD VPVIIVADID RGGVFAHLYG
     TLALLSESEQ TRVKGFVINR FRGDIRLLQS GLDWLEEKTG KPVLGVLPYL HGLNLEAEDA
     ITAQQELNSE VKLNVVVPVL TRISNHTDFD VLRLNPDINL SYVGKGEKID KADLIILPGT
     KSVRDDLAYL KSQGWDKDIL RHIRLGGKVM GICGGYQMLG KTIDDPDGVE GEPGSSEGLG
     LLNVHTVLTG SKQLTKTEAV LNLNNQKAKV KGYEIHVGRS QVLDEQPLEL DNGECDGAIS
     ECGQIMGTYL HGFFDEAEAL NLITEWVNGT QVKQQDFEVL KEQGINRIAD AIEQHMNLDF
     LFK