ID   COBQ_CLOBA              Reviewed;         501 AA.
AC   B2UXD4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLH_2659;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-2008) 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; CP001078; ACD53442.1; -; Genomic_DNA.
DR   RefSeq; WP_012451340.1; NC_010723.1.
DR   AlphaFoldDB; B2UXD4; -.
DR   SMR; B2UXD4; -.
DR   KEGG; cbt:CLH_2659; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
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..501
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090223"
FT   DOMAIN          251..446
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   501 AA;  55803 MW;  70EE9AE4656A7B5B CRC64;
     MNKKNIMFLG TASSVGKSTL VAALCRVLKN EDFKVSPFKA MNISLNSYVT KDGAEMGRAQ
     VVQAEASKIE PSALMNPILL KPSGGHTQVI VNGKVYDNIE PYEYKELNKK LKGIVKESYD
     RISNEYDLIV LEGSGGCAEI NLKDTDIANM NMAECVDAPV ILVADIDRGG VFASIVGTLN
     LLSENERKRV KGVIINKFRG KKEYFEPGVK QLEDIIKIPV LGVMPYEYFD IDDEDSVTEK
     ISNKESTEAK NIDIAIIRLS HMSNFTDFNV LNRINGVNIR YVESTKYLKN PDVIIIPGTK
     NTIEDLRILK ESKLANEIIK LHESGTLVFG ICGGYQMLGK LLLDQQGVEG STFQEEGLGL
     LDIKTRFNER KVTKQVEAQV VSNLKHINEI ENKSLVGYEI HNGISKVGKN AKPFIKDSKG
     KIIGVCDMEG SVAGTYLHGI FDSEEFTNSF INALKKNNNF ELLENDELDK VSDYKNEQYE
     KLAKVFSDNI DVSKIKEIMG I