ID   COBQ_SALDC              Reviewed;         506 AA.
AC   B5FLY7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SeD_A2354;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001144; ACH75170.1; -; Genomic_DNA.
DR   RefSeq; WP_000189667.1; NC_011205.1.
DR   AlphaFoldDB; B5FLY7; -.
DR   SMR; B5FLY7; -.
DR   KEGG; sed:SeD_A2354; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008322; 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..506
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090244"
FT   DOMAIN          251..448
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        440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   506 AA;  54999 MW;  ED2E5998DEFC2AC9 CRC64;
     MTQAVMLQGT ASDVGKSVLA AGLCRIFYQD GLRTAPFKSQ NMALNSGITS DGKEMGRAQI
     FQAEAAGITP DVRMNPVLLK PTSDRQAQVV LMGKVATNMD AVSYHDYKPR LREQILAVYN
     SLAQEYDVIV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFAAIYGTLA
     LLHKQERDRV KGVIINKFRG DVALLYSGIE QIESLTGVPV LGVMPWLDVD LEDEDGVALQ
     NDKYRGNAPR DITIAIVQLP HISNFTDFNA LAAQPDVRIR YIRRPEALTD ADLVILPGSK
     NTLSDLAWLR ESGMADALLQ THRQGVPVMG ICGGYQMLGD TIVDEVESGL GTQPGLGLLN
     TITRFAQDKI TTQVNATMSG ELPSWLAAAA GLPVRGYEIH MGETVLQEGC CTAMTLQKNG
     CSVADGAVTA DGLAFGTYLH GLFDSDAFTR AVVNGLRARK GLAPWETTFC YAEHKARQFD
     LLAEAMRQHI DIDKIYTIMQ QHQEPV