ID   COBQ_SINSX              Reviewed;         485 AA.
AC   P29932;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cobyric acid synthase;
GN   Name=cobQ;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1655697; DOI=10.1128/jb.173.19.6074-6087.1991;
RA   Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S.,
RA   Rouyez M.-C., Blanche F., Debussche L., Thibaut D.;
RT   "Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair
RT   Pseudomonas denitrificans DNA fragment containing five cob genes and
RT   identification of structural genes encoding Cob(I)alamin
RT   adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide
RT   kinase-cobinamide phosphate guanylyltransferase.";
RL   J. Bacteriol. 173:6074-6087(1991).
RN   [2]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 2-17.
RX   PubMed=1917839; DOI=10.1128/jb.173.19.6046-6051.1991;
RA   Blanche F., Couderc M., Debussche L., Thibaut D., Cameron B., Crouzet J.;
RT   "Biosynthesis of vitamin B12: stepwise amidation of carboxyl groups b, d,
RT   e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in
RT   Pseudomonas denitrificans.";
RL   J. Bacteriol. 173:6046-6051(1991).
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   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M62866; AAA25777.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29932; -.
DR   SMR; P29932; -.
DR   PRIDE; P29932; -.
DR   KEGG; ag:AAA25777; -.
DR   BioCyc; MetaCyc:MON-124; -.
DR   UniPathway; UPA00148; -.
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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Direct protein sequencing;
KW   Glutamine amidotransferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1917839"
FT   CHAIN           2..485
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141321"
FT   DOMAIN          251..438
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  51982 MW;  FC2E5E15657016A9 CRC64;
     MTRRIMLQGT GSDVGKSVLV AGLCRLAANQ GLKVRPFKPQ NMSNNAAVSD DGGEIGRAQW
     LQALAARVPS SVHMNPVLLK PQSDVGSQIV VQGKVAGQAR GREYQALKPK LLGAVMESFE
     QISAGADLVV VEGAGSPAEI NLRPGDIANM GFATRANVPV VLVGDIDRGG VIASLVGTHA
     ILPEEDRRMV TGYLINKFRG DVTLFDDGIA AVNRYTGWPC FGVVPWLKAA ARLPAEDSVV
     LEKLTRGEGR ALKVAVPVLS RIANFDDLDP LAAEPEIDLV FVRPGSPIPV DAGLVVIPGS
     KSTIGDLIDF RAQGWDRDLE RHVRRGGRVI GICGGYQMLG RRVTDPLGIE GGERAVEGLG
     LLEVETEMAP EKTVRNSRAW SLEHDVVLEG YEIHLGKTQG ADCGRPSVRI DNRADGALSA
     DGRVMGTYLH GLFTSDAYRG ALLKSFGIEG GANNYRQSVD AALDDVANEL EAVLDRRWLD
     ELLRH