ID   COBQ_ROSDO              Reviewed;         481 AA.
AC   Q167R8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=RD1_2180;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG31775.1; -; Genomic_DNA.
DR   RefSeq; WP_011568392.1; NZ_FOOO01000003.1.
DR   AlphaFoldDB; Q167R8; -.
DR   SMR; Q167R8; -.
DR   STRING; 375451.RD1_2180; -.
DR   PRIDE; Q167R8; -.
DR   EnsemblBacteria; ABG31775; ABG31775; RD1_2180.
DR   KEGG; rde:RD1_2180; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_0_5; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000007029; 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..481
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002374"
FT   DOMAIN          249..436
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   481 AA;  51074 MW;  1A6A1E2A5CC5E69C CRC64;
     MGRAIMLQGT GSDVGKSLLV AGLCRAAKRR GISVAPFKPQ NMSNNAAATT NGGEIGRAQA
     LQAFACGLDP TVDMNPILLK PETETGSQVI VQGQRMTSVA AGDYAKLKPT LLGPVLDSFN
     RLKAQYDLII VEGAGSPAEV NLRSNDIANM GFAEAAQVPV LLCGDINRGG VIAQVVGTQA
     VISPADAGMI KGFLINKFRG DPKLFDEGYE IIKNHTGWPG FGVLPWFTDA WKLPAEDAYD
     IKTPPRKGGL HIVCLHLSRI ANFDDMDPLS HEPGVQMTML RAGEVLPADA DIVILPGSKS
     TRGDLAFLRA QGWDIDLAAH LRRGGHVLGL CGGYQMLGQS IADPDGIEGP PGTTEGLGFL
     DITTVMTPQK RVARITAKHA QSGAMFPAYE IHVGRTDGPD CARPFAYVHG QPDGAISQNA
     QVTGTYLHGM FTDDAFRAQW LAQFDVTQNA SYTATVETTL DALATHLEAH ADVDGILALA
     R