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WECB_YERPE
ID   WECB_YERPE              Reviewed;         376 AA.
AC   Q8ZAE3; Q0WAE6;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
DE            EC=5.1.3.14 {ECO:0000255|HAMAP-Rule:MF_02028};
DE   AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000255|HAMAP-Rule:MF_02028};
GN   Name=wecB {ECO:0000255|HAMAP-Rule:MF_02028}; Synonyms=rffE;
GN   OrderedLocusNames=YPO3864, y0364, YP_3181;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC       acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-
CC       N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc
CC       residues. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC         mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:68623; EC=5.1.3.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02028};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC       antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02028}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02028}.
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02028}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM83953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS63349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL590842; CAL22451.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM83953.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS63349.1; ALT_INIT; Genomic_DNA.
DR   PIR; AH0470; AH0470.
DR   RefSeq; WP_002211986.1; NZ_WHLN01000069.1.
DR   RefSeq; YP_002348742.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZAE3; -.
DR   SMR; Q8ZAE3; -.
DR   STRING; 214092.YPO3864; -.
DR   PaxDb; Q8ZAE3; -.
DR   DNASU; 1145311; -.
DR   EnsemblBacteria; AAM83953; AAM83953; y0364.
DR   EnsemblBacteria; AAS63349; AAS63349; YP_3181.
DR   GeneID; 57974839; -.
DR   KEGG; ype:YPO3864; -.
DR   KEGG; ypk:y0364; -.
DR   KEGG; ypm:YP_3181; -.
DR   PATRIC; fig|214092.21.peg.4390; -.
DR   eggNOG; COG0381; Bacteria.
DR   HOGENOM; CLU_041674_1_0_6; -.
DR   OMA; RYNTERP; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02028; WecB_RffE; 1.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   InterPro; IPR032892; WecB.
DR   InterPro; IPR029767; WecB-like.
DR   PANTHER; PTHR43174; PTHR43174; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   TIGRFAMs; TIGR00236; wecB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..376
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /id="PRO_0000208531"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         290..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02028"
SQ   SEQUENCE   376 AA;  42379 MW;  0F9BE03C292DDD02 CRC64;
     MKVLTVFGTR PEAIKMAPLV HALAQDDAFE SRVCVTAQHR EMLDQVLRLF EIQPDYDLDI
     MRPGQGLTEI TCRILEGLKP VLEEFKPDVI LVHGDTTTTL SASLAGFYHR IPVGHVEAGL
     RTGDLYSPWP EEANRQLTGH LAMYHFAPTE NSRQNLLREW VPENRIFVTG NTVIDALFWV
     RDRVMNTPDL RANLAQRYAF LDTNKKMILV TGHRRESFGG GFERICSALA EIARKHPEVQ
     VVYPVHLNPN VSEPVNRILK GIDNIILIDP QDYLPFVYLM NHAYLILTDS GGIQEEAPSL
     GKPVLVMRDT TERPEAVDSG TVLLVGTNIN KIVDAVTRLL TDETAYHQMT RAHNPYGDGY
     ACQRILKALK NHQVTL
 
 
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