ID   COBQ_CLOBK              Reviewed;         493 AA.
AC   B1IHC4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLD_3646;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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; CP000939; ACA46412.1; -; Genomic_DNA.
DR   RefSeq; WP_015958067.1; NC_010516.1.
DR   AlphaFoldDB; B1IHC4; -.
DR   SMR; B1IHC4; -.
DR   EnsemblBacteria; ACA46412; ACA46412; CLD_3646.
DR   KEGG; cbb:CLD_3646; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008541; 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.
FT   CHAIN           1..493
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090225"
FT   DOMAIN          246..440
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        326
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   493 AA;  55279 MW;  6870102D760BD802 CRC64;
     MAKIMIQGTA SSVGKSLIVA ALCRIFKQDG YSVCPFKSQN MSLNSYITLD GKEMGRAQVL
     QAYATGLEPE VYMNPILLKP TSDRKCQIIV NGKVYGNSTA MGYHNLKLKF KDMLKEHFNK
     LEEEFDIVVM EGAGSPAEIN LRDRDIVNMG MAELVDAPVL LVGDIDKGGV FASLAGTMLL
     LKDGEKERVK GTIINKFRGD VEILKPGLDM LEDIVHIPCL GVVPYTRLQL EDEDGAVEFN
     KKAYAPIDIA VIKMPHISNF TDLDALKSEE DVSIRFITSK EEFKEPDLLI IPGSKNTIED
     LLYLRQCGLE ESIKEYSKDG KIIGICGGYQ VLGSKIKDPH NVETDLGEID GLNLLDMKTI
     FEKEKITTRV SAKLLNEEIE NTVYGYEIHM GISEYSENVK PLFKIYNKNG EKVGYFDGAI
     NEKGNVMGTY IHGVFDGVVF REKIINELRV KKGLKKKKSQ IYEHMREKEL DKLADIVRQS
     LDMEKIYSII GMK