ID   COBQ_CITK8              Reviewed;         506 AA.
AC   A8AEQ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-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=CKO_00819;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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; CP000822; ABV11971.1; -; Genomic_DNA.
DR   RefSeq; WP_012131792.1; NC_009792.1.
DR   AlphaFoldDB; A8AEQ8; -.
DR   SMR; A8AEQ8; -.
DR   STRING; 290338.CKO_00819; -.
DR   EnsemblBacteria; ABV11971; ABV11971; CKO_00819.
DR   GeneID; 45135016; -.
DR   KEGG; cko:CKO_00819; -.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000008148; 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; Reference proteome.
FT   CHAIN           1..506
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002351"
FT   DOMAIN          251..448
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        440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   506 AA;  55021 MW;  538EC61B4F1188DD CRC64;
     MTQAVMLQGT ASDVGKSVLV AGLCRIFYQD GLRTAPFKSQ NMALNSGITP DGKEMGRAQI
     FQAEAAGIAP DVRMNPVLLK PTSDRKAQVV LMGKVATDMD AVSYHEYKPR LREQILTVYN
     SLAQEYDVLV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFASIYGTLA
     LLHDSERARV KGVIINKFRG DVTLLYSGIE QIEALTGVPV LGVMPWLEVD LEDEDGVALQ
     KGKYLRTDKR DIDIAVVQVP HISNFTDFNA LAAQPDVRVR YVRHPEELAG ADLIILPGSK
     NTLGDLVWLR ESAMAHGVLQ AHRQGVPVAG ICGGYQMLGD TIIDEVESGL GTLPGLGLLN
     TVTHFAQDKT TTQVEGQMAS ALPGWLAAAS GLAVRGYEIH MGETTLNAQC QPAMTLRKGE
     NAIADGAVTD DGLVFGTYLH GLFDSDAFTR ALVNGLRVRK GLTPLDHAFH YAQYKSQQFD
     LLADAMRQHI DIEKIYTIMQ QHREPV