(data stored in SCRATCH zone)

SWISSPROT: C5BBB7_EDWI9

ID   C5BBB7_EDWI9            Unreviewed;       376 AA.
AC   C5BBB7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000256|HAMAP-Rule:MF_02028};
DE            EC=5.1.3.14 {ECO:0000256|HAMAP-Rule:MF_02028};
DE   AltName: Full=UDP-GlcNAc-2-epimerase {ECO:0000256|HAMAP-Rule:MF_02028};
GN   Name=wecB {ECO:0000256|HAMAP-Rule:MF_02028};
GN   OrderedLocusNames=NT01EI_0092 {ECO:0000313|EMBL:ACR67352.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67352.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC       acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with
CC       UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of
CC       ManNAc residues. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine = UDP-N-
CC       acetyl-alpha-D-mannosamine. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial
CC       common antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02028}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02028}.
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02028,
CC       ECO:0000256|RuleBase:RU003513}.
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DR   EMBL; CP001600; ACR67352.2; -; Genomic_DNA.
DR   RefSeq; WP_015869571.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0092; -.
DR   EnsemblBacteria; ACR67352; ACR67352; NT01EI_0092.
DR   GeneID; 7959811; -.
DR   KEGG; eic:NT01EI_0092; -.
DR   PATRIC; fig|634503.3.peg.86; -.
DR   eggNOG; ENOG4105EAG; Bacteria.
DR   eggNOG; COG0381; LUCA.
DR   HOGENOM; HOG000076048; -.
DR   KO; K01791; -.
DR   OrthoDB; POG091H02IH; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd03786; GT1_UDP-GlcNAc_2-Epimerase; 1.
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;
DR   PRODOM; C5BBB7.
DR   SWISS-2DPAGE; C5BBB7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02028};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_02028,
KW   ECO:0000256|RuleBase:RU003513, ECO:0000313|EMBL:ACR67352.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       22    370       Epimerase_2. {ECO:0000259|Pfam:PF02350}.
FT   REGION      290    292       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02028}.
FT   BINDING      95     95       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     117    117       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     213    213       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     271    271       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     276    276       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     296    296       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
FT   BINDING     313    313       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02028}.
SQ   SEQUENCE   376 AA;  41250 MW;  A03ACA865789D863 CRC64;
     MKVLTVFGTR PEAIKMAPLV HALAADAAFD ARVCVTAQHR EMLDQVLGLF QIEPDYDLNI
     MRPGQDLSDI TCRILEGLKP ILAEFRPDVV LVHGDTTTTL AASLAAFYQR IPVGHVEAGL
     RTGDLYSPWP EEANRTLTGH LASLHFAPTL TARANLLREG IGEQTIHLTG NSVVDALLWV
     RDRICADTAL QAHLAAAYPF LDADKPLLLV TGHRRESFGG GFERICGALA QIARSHPQVQ
     VVYPVHLNPN VSEPVNRILR DIENVFLIPP QDYLPFVYLM GRAQLILTDS GGIQEEAPSL
     GKPVLVMRET TERPEAVQAG TVRLVGTDTA TIVAQVSLLL ENEQQYRAMS HATNPYGDGY
     ACQRILSALK NYRATL
//

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