ID   COBQ_SALSV              Reviewed;         506 AA.
AC   B4TZP8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=SeSA_A2188;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
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; CP001127; ACF91336.1; -; Genomic_DNA.
DR   RefSeq; WP_000189661.1; NC_011094.1.
DR   AlphaFoldDB; B4TZP8; -.
DR   EnsemblBacteria; ACF91336; ACF91336; SeSA_A2188.
DR   KEGG; sew:SeSA_A2188; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001865; 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_1000090249"
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;  55065 MW;  4DA7F3FB05D36D37 CRC64;
     MTQAVMLQGT ASDVGKSVLA AGLCRIFYQD GLRTAPFKSQ NMALNSGITP DGKEMGRAQI
     FQAEAAGITP DVRMNPVLLK PTSDRQAQVV LMGKVATNMD AVSYHDYKPR LREQILAVYN
     SLAQEYDVIV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFAAIYGTLA
     LLHKQERDRV KGVIINKFRG DVALLYSGIE QIESLTGVPV LGVMPWLDVD LEDEDGVALQ
     NDKYRGNAPR DITIAIVQLP HISNFTDFNA LAAQPDVRIR YIRRPEALTD VDLVILPGSK
     NTLSDLAWLR ESGMADAVLQ THRQGVPVMG ICGGYQMLGD TIVDEVESGL GTQPGLGLLN
     TITRFAQDKT TTQVNATMSD ELPGWLAAAA GLPVRGYEIH MGETVLQEGC CTAMTLQKNG
     CSVADGAVTA DGLAFGTYLH GLFDSDAFTR AVVNGLRARK GLAPWETTFC YAEHKARQFD
     LLAEAMRQHI DIDKIYTIMQ QYQEPV