ID   COBQ_POLNA              Reviewed;         485 AA.
AC   A1VP76;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Pnap_2146;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM37454.1; -; Genomic_DNA.
DR   RefSeq; WP_011801532.1; NC_008781.1.
DR   AlphaFoldDB; A1VP76; -.
DR   SMR; A1VP76; -.
DR   STRING; 365044.Pnap_2146; -.
DR   EnsemblBacteria; ABM37454; ABM37454; Pnap_2146.
DR   KEGG; pna:Pnap_2146; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_1_4; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000644; 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; Reference proteome.
FT   CHAIN           1..485
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332359"
FT   DOMAIN          250..448
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        334
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   485 AA;  51459 MW;  3F23C46B200FB4D3 CRC64;
     MTAKSVMVLG TTSNAGKSWL TTALCRYYAR QGLKVAPYKS QNMSNNARVV VGGEIGSAQY
     FQALAARAVP DVRMNPLLLK PEKDTQSQVV LMGQVNAELS RMEWRGRSLS VWPVVARALD
     ELLAENDVVV IEGAGSPAEI NLKSCDIVNM RVALHANAAC LLVTDIDRGG AFAHLYGTWA
     MLDKTEQQLI RGFVLNKFRG DASLLAPGPQ MLQELTGVPT VATLPMWWQH GLPEEDGVFD
     DRSTAAGAVT QTVAVIAYPR ISNLDEFQPL KNVPGVRLKW VRSPSELAGL GPADWVILPG
     SKATSADLAW LRAQGLDQAI AAHAGRGGAV LGICGGLQML GEALIDPHGI DGNGPGLGLL
     PVVTVFDEAK TVQHRQAAFA SVGGPWAGLS GVEVQGYEIH HGQTARHSAM AAAGDIACPV
     MPDGLAWQNA AGNVLGLYLH GMFEDPRVLQ ALFGAATPTL ESVFDGLADY IGQHFEPGVL
     QSLIA