ID   COBQ_SINFN              Reviewed;         484 AA.
AC   C3MDR9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=NGR_c18240;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP25588.1; -; Genomic_DNA.
DR   RefSeq; WP_012708353.1; NC_012587.1.
DR   RefSeq; YP_002826341.1; NC_012587.1.
DR   AlphaFoldDB; C3MDR9; -.
DR   SMR; C3MDR9; -.
DR   STRING; 394.NGR_c18240; -.
DR   EnsemblBacteria; ACP25588; ACP25588; NGR_c18240.
DR   KEGG; rhi:NGR_c18240; -.
DR   PATRIC; fig|394.7.peg.4651; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001054; 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; 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   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000116911"
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;  51019 MW;  29B7119113C8F429 CRC64;
     MTRAIMLQGT GSDVGKSVLV AGLCRLAANR GLKVRPFKPQ NMSNNAAVSD DGGEIGRAQW
     LQSLAARVPS SVHMNPVLLK PQSDVGSQVI LQGKVAGQAK GREYQALKPK LLGAVMESFG
     RVSAGADLVV VEGAGSPAEI NLRAGDIANM GFATHANVPV VLVGDIDRGG VIASLVGTHA
     ILPEEDRRMV AGYLINKFRG DVSLFDDGIA AVGRFTGWPC FGVVPWLKSA ARLPAEDSVV
     LEKLARGSGK ALKVAVPVLS RIANFDDLDP LAAEPEVELV FVRPGMSLPQ DAGLVVIPGS
     KSTISDLKNF RAQGWDRDLE RHVRRGGRVI GICGGYQILG TRVADPLGIE GSEREIAGLG
     LLSVETEMAP EKTVRNSRAW SLEHDVGLEG YEIHLGKTTG ADCERAPVTI DGRPDGAMSA
     DGRVMGTYLH GLFGSDAYRA ALLKSLGIEG GGANYRQSVD SALDEIAAEL EGVLDGAWLN
     RLLG