ID   COBQ_CLOK1              Reviewed;         499 AA.
AC   B9DZL9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CKR_0643;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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; AP009049; BAH05694.1; -; Genomic_DNA.
DR   RefSeq; WP_011989289.1; NC_011837.1.
DR   AlphaFoldDB; B9DZL9; -.
DR   EnsemblBacteria; BAH05694; BAH05694; CKR_0643.
DR   KEGG; ckr:CKR_0643; -.
DR   HOGENOM; CLU_019250_2_2_9; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000007969; 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..499
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000116903"
FT   DOMAIN          246..441
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   499 AA;  55646 MW;  279E18D7D7743312 CRC64;
     MPKIMIQGTA SSVGKSIIVA ALCRIFKQDG FKVCPYKSQN MSLNSYITLD GREMGRAQVL
     QAYASGLEPE VYMNPILLKP TTDKNCQVII RGEVYCNSSA REYYNMKKEF VPMLKKDFEI
     LEDKFDIVVI EGAGSPAEIN LRDNDIVNMG LAEMVDSPVI LVGDIDKGGV FASLLGTIML
     LTEKEKSRVK GTIINKFRGD VDILKPGLSM IEEKIKVPSI GVIPYFRLAL EDEDSAVDFN
     TKISAPIDIA IIKLPHISNF TDMDPLKIEE DVSLRYVTSA DDFGNPDLLI IPGSKNTIED
     LLYIRKVGIE DKIKKYSSRD GFIFGICGGY QMLGTYIEDP LGVETKVKAV EGMNILDVST
     VFAKEKITTR VKGKVCGLTE NIDIYGYEIH MGSCNYGKKA KPLVEITDKN GCSCNFKEGA
     INPGRNVMGT YIHGIFDGAE LRQYIMNTLR SRRGIKHKNS KVYENLRDGE IDKLADIVRS
     SLDMKKVYEI LNVKSKFME