ID   COBQ_CLOBL              Reviewed;         493 AA.
AC   A7GBV6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLI_1000;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000728; ABS42184.1; -; Genomic_DNA.
DR   RefSeq; WP_011987838.1; NC_009699.1.
DR   AlphaFoldDB; A7GBV6; -.
DR   SMR; A7GBV6; -.
DR   EnsemblBacteria; ABS42184; ABS42184; CLI_1000.
DR   KEGG; cbf:CLI_1000; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002410; 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_0000332331"
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;  55212 MW;  C263CA31160EBC8A CRC64;
     MAKIMIQGTA SSVGKSLIVA ALCRIFKQDG YSVCPFKSQN MSLNSYITLD GKEMGRAQVV
     QAYAAGLEPE AYMNPILLKP TSDKKCQIIV NGKVYGNSTA MGYHNLKLRF KDMLKEHFNK
     LEEDFDIVVM EGAGSPAEIN LRDRDIVNMG MAELVDAPVL LVGDIDKGGV FASLAGTMLL
     LKDGEKERVK GTIINKFRGD VEILKPGLDM LEDIVHIPCL GVVPYTRLQL EDEDGAVEFN
     KKAYAPIDIA VIKMPHISNF TDLDALKSEE DVSIRFITSK EEFKEPDLLV IPGSKNTIED
     LLYLRKCGLE ESIKEYSKDG KIVGICGGYQ VLGSKIKDPY KVETDLGEID GLNLLDMETT
     FEKEKVTTRV SAKLIDEKIE NTVYGYEIHM GISEYSENVK PLFKIYDKNG EKVDYFDGAI
     NEKGNVMGTY IHGVFDGVSF REKIINELRV KKGLKKKKSQ VYEHMREKEL DKLADIVRQS
     LDMKKIYSII GMK