ID   Y1034_THEMA             Reviewed;         378 AA.
AC   Q9X0C4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Putative UDP-N-acetylglucosamine 2-epimerase;
DE            EC=5.1.3.14;
DE   AltName: Full=UDP-GlcNAc-2-epimerase;
GN   OrderedLocusNames=TM_1034;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000512; AAD36111.1; -; Genomic_DNA.
DR   PIR; A72304; A72304.
DR   RefSeq; NP_228840.1; NC_000853.1.
DR   RefSeq; WP_004080488.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X0C4; -.
DR   SMR; Q9X0C4; -.
DR   STRING; 243274.THEMA_09190; -.
DR   EnsemblBacteria; AAD36111; AAD36111; TM_1034.
DR   KEGG; tma:TM1034; -.
DR   eggNOG; COG0381; Bacteria.
DR   InParanoid; Q9X0C4; -.
DR   OMA; RYNTERP; -.
DR   OrthoDB; 1117971at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
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; Lipopolysaccharide biosynthesis; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Putative UDP-N-acetylglucosamine 2-epimerase"
FT                   /id="PRO_0000208534"
SQ   SEQUENCE   378 AA;  42846 MW;  0EF1F9F9A0BC4B80 CRC64;
     MIRVLSVFGT RPEAIKMAPL VKKLEEEQNV ESLVCVTAQH RQMLDQVLEV FDIKPDFDLN
     IMKERQNLSD ITVNALSGLY DLIGELKPDI VLVQGDTTTT FAGALAAFYH RIPVGHVEAG
     LRTNDRYSPF PEEINRRLTG VLSTLHFAPT KRNRENLLKE NVMGKIYVTG NTVIDALRYT
     VKENHVFEDP ILRNMDFSDG RYILLTSHRR ENIGKPLENI CRAVRRIVEG FEDVKVIYPV
     HMNPAVREIV FPMLENVERV FLIDPVNVID MHNLMARSYL IMTDSGGIQE EAPALGKPVI
     VLRKETERPE AIEAGVAVLG GVEEERIFEL AKKLLVDREE YEKMAKAVNP FGDGRASERI
     VKAILHEFGL SDPPEEFC