ID   COBQ_YERE8              Reviewed;         512 AA.
AC   A1JTQ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=YE2711;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12744.1; -; Genomic_DNA.
DR   RefSeq; WP_005168494.1; NC_008800.1.
DR   RefSeq; YP_001006901.1; NC_008800.1.
DR   AlphaFoldDB; A1JTQ2; -.
DR   SMR; A1JTQ2; -.
DR   STRING; 393305.YE2711; -.
DR   EnsemblBacteria; CAL12744; CAL12744; YE2711.
DR   KEGG; yen:YE2711; -.
DR   PATRIC; fig|393305.7.peg.2880; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000642; Chromosome.
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.
FT   CHAIN           1..512
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002381"
FT   DOMAIN          251..451
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        443
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   512 AA;  55935 MW;  0D9D8EFEAC77A90B CRC64;
     MNLSIMVQGT ASDVGKSVLV AGLCRIFMQD GYRCAPFKSQ NMALNSGITP QGEEMGRAQI
     FQAEAAGIAP DVRMNPVLLK PTSDRKAQVV LMGKVACNMD AVEYHQYKPQ LQQQISEVYH
     SLAREYDVMV LEGAGSPAEI NLRDRDIVNM GMAEMADAPV LLVADIDRGG VFASIYGTLA
     LLHPHEKARV KGVIINKFRG DIALLTPGLE QIEALTNVPV LGVMPWLDID LEDEDGVALQ
     NGKYQDTAEK ALDIAVIRLP HIANFTDFNA LAAQPDVRLR YVSQLSALGQ PDLIILPGSK
     NTLGDLQWLH HSGLAAALLT LHQRNVPVIG ICGGYQMLGK RIIDGVESGL EQMDGLGLLD
     VETEFAPDKV TTRVSGYCQI GLPGILKNCC DHPLEGYEIH MGVSHLGSAA IPFAQLTLRN
     GQAEQWVDGA VNGDGSVLGS YIHGLFDSHH FTRALLDSLR QRKGLAAFDG VTVNYAEHKQ
     QQFDILASQM REHIDIDRIL KLMKQHQQER AQ