ID   COBQ_CLOBB              Reviewed;         501 AA.
AC   B2TPE7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CLL_A2917;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
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 sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-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; CP001056; ACD22172.1; -; Genomic_DNA.
DR   RefSeq; WP_012423046.1; NC_018648.1.
DR   AlphaFoldDB; B2TPE7; -.
DR   SMR; B2TPE7; -.
DR   EnsemblBacteria; ACD22172; ACD22172; CLL_A2917.
DR   KEGG; cbk:CLL_A2917; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001195; 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..501
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090224"
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;  55679 MW;  D7ADC8D2D3EEFB1C CRC64;
     MNKKNIMFLG TASSVGKSTL VAALCRVLKN EEFKVAPFKA MNISLNSYVT KDGAEMGRAQ
     VVQAEACKLE PNALMNPILL KPSGGHTQVI VNGKVYDNIE PYKYKELNKK LKGIVKESYD
     KLSNKYELIV LEGSGGCAEI NLKDSDIANM NMAESVDAPV ILVADIDRGG VFASIVGTLE
     LLSKNERSRV KGVIINKFRG EKQHFEAGVK QLEEIIKIPV LGVMPYEYFD IEDEDAVTEK
     ICNKESEDEN SIDVAIIRLS HMSNFTDFNV LSRINGVNVR YVESTKYLKN PDVIIIPGTK
     NTIEDLRILK ESKLADEIIK LHDSGTLVLG ICGGYQMLGK ILLDQQGVEG NTLQEEGLGL
     LDIKTRFNER KITKQVEAQV VSNLKDINEI ENKSLVGYEI HNGISKVGKN VKPFIKDSKG
     KIIGVCDIEG SVAGTYLHGI FDSEEFTNAF INALKKNNNF DLLEDDELNK ISDYKNEQYE
     KLAKIFSENV DVDKIKEIIG I