ID   COBQ_POLSJ              Reviewed;         507 AA.
AC   Q129W6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Bpro_2760;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE44676.1; -; Genomic_DNA.
DR   RefSeq; WP_011483674.1; NC_007948.1.
DR   AlphaFoldDB; Q129W6; -.
DR   SMR; Q129W6; -.
DR   STRING; 296591.Bpro_2760; -.
DR   PRIDE; Q129W6; -.
DR   EnsemblBacteria; ABE44676; ABE44676; Bpro_2760.
DR   KEGG; pol:Bpro_2760; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_1_4; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001983; 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   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..507
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332360"
FT   DOMAIN          273..468
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        354
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   507 AA;  53760 MW;  366160EBB407B2A7 CRC64;
     MSGTLARSVM VLGTTSGAGK SWLTTALCRY YARQGLKVAP FKAQNMSNNA RVVAGGEIGS
     AQYFQALAAR AEPDVRMNPL LLKPEKDTQS QVILMGQVDA ELSRMPWRGR SASVWPVIAR
     ALDELLAEND VVVIEGAGSP AEINLKSSDI VNMRVAQHTG ASCLLVTDID RGGAFAHLYG
     TWAMLDEAER QLIKGFVLNK FRGDASLLAP GPQMLQEMTG VPTVATLPMW WQHGLPEEDG
     VFDMAPTLGT GVSTLPPEGA ELARGGPSLR SPRPVIAVIA YPRISNLDEF QPLKNVPGVH
     LKWVRSPGEL AGVDWIILPG SKHTSGDLAW LRAQGLDRAV AAHAEQGGAV LGVCGGLQML
     GEALIDPHGI DGNAPGLGLL PVVTVFEEGK TVQRRQARFG ELAGAWAALS GVGLQGYEIH
     HGQTAPHTAM AAAGDIAHGV MAEGLAWQNT RGNVLGLYLH GMFEDPAVLQ ALFGATVPTL
     DAVFDGLADY IEQHFEPGVL QSLIATP