ID   COBQ_CHLAA              Reviewed;         489 AA.
AC   A9WIN9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Caur_2560;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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; CP000909; ABY35766.1; -; Genomic_DNA.
DR   RefSeq; WP_012258419.1; NC_010175.1.
DR   RefSeq; YP_001636155.1; NC_010175.1.
DR   AlphaFoldDB; A9WIN9; -.
DR   STRING; 324602.Caur_2560; -.
DR   EnsemblBacteria; ABY35766; ABY35766; Caur_2560.
DR   KEGG; cau:Caur_2560; -.
DR   PATRIC; fig|324602.8.peg.2886; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_0; -.
DR   InParanoid; A9WIN9; -.
DR   OMA; DVRMNPL; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002008; 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..489
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332328"
FT   DOMAIN          251..444
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        436
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   489 AA;  52814 MW;  3D1CC9C3D349B75E CRC64;
     MQAPVLMVVG TASSVGKSTL VTALCRLAYR RGLRVAPFKA QNMSNNAAVT ADGKEIARST
     AVQAAAAGIA PTVAMNPILI KPEGQRRSQI IVEGRPWQSL TATDFWQRKA QLWSVVTRNL
     DHLRATYDLV IAEGAGSPVE LNLKPGDIVN MRVARYAQAQ TILVGDIDRG GIFAQLLGTL
     MLLEPEERQL ITGCIVNRFR GDPSLFADGV TILEERSGLP VLGVIPWLDD LGLPEEDAVA
     LEQPPVAPAH GLIIAVIRLP TIANFDDFDP LAREPGVVVR YIDHPLELTG AAAVILPGVK
     HTLAARHWLH ERGFDNALRE FTGAIVGICG GYQLLGERIS DPLAVEGSGG EAAGLGLLPI
     ETIFTTAKQT TQTIACAQVP WAGNEPLQGY EIHMGQSYRR GEAPAFLRII QRGNTPTSAD
     DGCISSDGRV WGCYLHGIFA NDTFRRGWLR RLGWQPPTTP VARADPFDRL ADHVAAALGP
     AVLDRLMRR