COBQ_KLEP3
ID COBQ_KLEP3 Reviewed; 507 AA.
AC B5XUV5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=KPK_0932;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI06774.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XUV5; -.
DR SMR; B5XUV5; -.
DR EnsemblBacteria; ACI06774; ACI06774; KPK_0932.
DR KEGG; kpe:KPK_0932; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001734; 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..507
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090230"
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 507 AA; 55180 MW; 616E24A2E86FCA17 CRC64;
MTLAVMLQGT ASDVGKSVLV AGLCRIFHQD GLRTAPFKSQ NMALNSGITP DGKEMGRAQI
FQAEAAGIAP DVRMNPILLK PTSDRQAQVV LMGQVATSMD AVSYHQYKPR LREQILAVYQ
SLAGEYEALV LEGAGSPAEI NLRDRDIVNM GMAEMAQCPV ILVADIDRGG VFAAIYGTLA
LLQPQERARV KGVIINKFRG DVALLRSGIE QIEALTGVPV LGVMPWLDVD LEDEDGVALQ
AGKYHRTDRR DIDIAVVHLP HIANFTDFNA LAAQPDVRVR YVRDPQALAD ADLVILPGSK
NTLGDLCWLR ESGMAHAVEQ ARQRKVPLLG ICGGYQMLGE TIIDEVESGL GTQPGLGVLK
TVTHFAQHKT TTQVQATLGT NLPEWLADAA GLHVSGYEIH MGETRREAGS PPLLQLHKAG
QSVEDGAISD DGLAFGTYLH GLFDSDAFTR ALLNGLRQRK GLAPLDSALE YARYKTRQFD
RLADAMREHI AIDKIYAIMR QHQEPLC