ID   COBQ_CLOBM              Reviewed;         493 AA.
AC   B1KY08;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLK_0351;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
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; CP000962; ACA55921.1; -; Genomic_DNA.
DR   RefSeq; WP_012343842.1; NC_010520.1.
DR   AlphaFoldDB; B1KY08; -.
DR   SMR; B1KY08; -.
DR   EnsemblBacteria; ACA55921; ACA55921; CLK_0351.
DR   KEGG; cbl:CLK_0351; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000722; 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_1000090226"
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;  55132 MW;  9953F20F0DF219DF CRC64;
     MAKIMIQGTA SSVGKSLIVA ALCRIFKQDG YSVCPFKSQN MSLNSYITLD GKEMGRAQVL
     QAYAAGLEPE VYMNPILLKP TSDKKSQIIV NGKVYGNSTA MEYHNLKIKF KDMLKEQFKK
     LEENFDIVVM EGAGSPAEIN LRDRDIVNMG MAELVDAPVL LVGDIDKGGV FASLAGTMLL
     LNEGEKERVK GTIINKFRGD VEILKPGLDM LEDIIHIPCL GVVPYTRLQL EDEDGAVEFN
     KKTYAPIDIA VIKMPHISNF TDLDALKSEE DVSIRFVTSK EELKKPDLLI IPGSKNTIED
     LLYLRQCGLE ESIKEYSNDG RIIGICGGYQ VLGSKIKDPH NVETDLGEID GLNLLDMKTI
     FEKEKVTTRV SAKLLNEEAE NTVYGYEIHM GISKYGQNIN PLFKIYDKNG EKVGYFDGAI
     NDKGNVMGTY IHGVFDGVAF REKIINELRV KKGLKKKKSQ VYEHMREKEL DKLADIVRQS
     LDMKKIYSII GMK