COBQ_KLEP7
ID COBQ_KLEP7 Reviewed; 507 AA.
AC A6TDB1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=KPN78578_31210; ORFNames=KPN_03184;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR78582.1; -; Genomic_DNA.
DR RefSeq; WP_004174595.1; NC_009648.1.
DR AlphaFoldDB; A6TDB1; -.
DR STRING; 272620.KPN_03184; -.
DR EnsemblBacteria; ABR78582; ABR78582; KPN_03184.
DR KEGG; kpn:KPN_03184; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000265; 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..507
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002361"
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; 55098 MW; 49CE819EA0D8523D 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 GAQPGLGVLK
TVTHFAQHKT TTQVQATLGS ALPDWLADAA GLRVSGYEIH MGETRREAGC PPLLQLHKAG
QAVDDGAISD DGLAFGTYLH GLFDSDAFTR ALLNGLRQRK GLAPLDSALE YARYKTRQFD
RLAEAMREHI AIDKIYAIMR QHQEPLC
