ID   COBQ_CLOD6              Reviewed;         504 AA.
AC   Q180T4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CD630_34350;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ70338.1; -; Genomic_DNA.
DR   RefSeq; WP_003437761.1; NZ_CP010905.2.
DR   RefSeq; YP_001089955.1; NC_009089.1.
DR   AlphaFoldDB; Q180T4; -.
DR   SMR; Q180T4; -.
DR   STRING; 272563.CD630_34350; -.
DR   EnsemblBacteria; CAJ70338; CAJ70338; CD630_34350.
DR   KEGG; cdf:CD630_34350; -.
DR   KEGG; pdc:CDIF630_03743; -.
DR   PATRIC; fig|272563.120.peg.3629; -.
DR   eggNOG; COG1492; Bacteria.
DR   OMA; EIHHGVA; -.
DR   PhylomeDB; Q180T4; -.
DR   BioCyc; PDIF272563:G12WB-3612-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001978; 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..504
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000332332"
FT   DOMAIN          249..451
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        443
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   504 AA;  56522 MW;  897366A8F5DDBC70 CRC64;
     MGKKIMLQGT ASNVGKSVLV AGLCRIFKQD GYTVAPFKSQ NMALNSFITK EGLEMGRAQV
     FQAEAAKIEP IADMNPVLLK PSGNNKSQVI VRGKVVGEMP SSKYHDYKLE LVDVLKETFN
     SLNSRYDIVV MEGAGSNAEI NLKDRDISNM GMAEIADAPV IIVGDIDRGG VFASLAGTML
     LLNEDEKRRV KGVIINKFRG KKELLQDGVK MLEDIIKVPV IGVVPYTDIK IEDEDSVTTR
     FKKKMNKSDI HIEIIRTPHM SNFTDFNIFE TQEDVSIRYV DYGESLGNPD ILIIPGTKST
     IDDLTYIRKS GLESQIKNLH SQGKLIFGIC GGYQMLGKKL KDPYHVESEI EEVDGIGLLD
     TETTFEKEKT TTQVEATIVE CISEYMNNLK GKKVKGYEIH MGITKRGNDV RSLDLITKKL
     DKEVNYTEGS VNKEGNVIGT YLHGIFDEIS FTRAILNNIR KKKGLGELES KVNSFNEFKD
     KEYDKLADFL REHLDIEKIY EIMK