ID   COBQ_SINMW              Reviewed;         484 AA.
AC   A6UAC0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Smed_1765;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR60600.1; -; Genomic_DNA.
DR   RefSeq; WP_011975903.1; NC_009636.1.
DR   RefSeq; YP_001327435.1; NC_009636.1.
DR   AlphaFoldDB; A6UAC0; -.
DR   SMR; A6UAC0; -.
DR   STRING; 366394.Smed_1765; -.
DR   EnsemblBacteria; ABR60600; ABR60600; Smed_1765.
DR   GeneID; 61613583; -.
DR   KEGG; smd:Smed_1765; -.
DR   PATRIC; fig|366394.8.peg.4906; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001108; 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..484
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002378"
FT   DOMAIN          251..438
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        430
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   484 AA;  51486 MW;  EAB28B75AD2BA143 CRC64;
     MTRKIMLQGT GSDVGKSVLV AGLCRLASNR GLSVKPFKPQ NMSNNAAVSD DGGEIGRAQW
     LQALAARVPS SVHMNPVLLK PQSDVGSQVV VQGRVAGQAR GKEYQALKPG LLGSVMESFE
     LVSAGADLVI VEGAGSPAEI NLRAGDIANM GFATRAGVPV VLVGDIDRGG VIASLVGTHA
     ILSDEDRRMV TGYLINKFRG DVTLFDDGIA SIRTFTGWPC FGVVPWLKSA GRLPAEDSVV
     LERLARGGGK ALKVAVPVLS RIANFDDLDP LAAEPDVEIV FVRPGTPLPD DAALVVIPGS
     KSTIADLEDF RRQGWDRDLD RHIRRGGRVI GICGGYQMLG TRVIDPLGIE GGKREIEGLG
     LLSVETEMAP EKTVRNSRAW SREYGVLLEG YEIHLGRTAG IDCGRAPVEI DGRRDGAMSA
     DGRVMGTYLH GLFGSDPYRA ELLRSFGIEG GGGNYRQSVD AALDEIAAEL DAVLDRVWLE
     TLLG