WECB_METJA
ID WECB_METJA Reviewed; 366 AA.
AC Q58899;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase;
DE EC=5.1.3.14;
DE AltName: Full=UDP-GlcNAc-2-epimerase;
GN Name=wecB; OrderedLocusNames=MJ1504;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) to produce UDP-N-acetylmannosamine (UDP-
CC ManNAc), the activated donor of ManNAc residues. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; L77117; AAB99517.1; -; Genomic_DNA.
DR PIR; G64487; G64487.
DR RefSeq; WP_010871027.1; NC_000909.1.
DR PDB; 4NEQ; X-ray; 2.85 A; A=1-366.
DR PDB; 4NES; X-ray; 1.42 A; A=1-366.
DR PDBsum; 4NEQ; -.
DR PDBsum; 4NES; -.
DR AlphaFoldDB; Q58899; -.
DR SMR; Q58899; -.
DR STRING; 243232.MJ_1504; -.
DR EnsemblBacteria; AAB99517; AAB99517; MJ_1504.
DR GeneID; 1452411; -.
DR KEGG; mja:MJ_1504; -.
DR eggNOG; arCOG01392; Archaea.
DR HOGENOM; CLU_041674_0_1_2; -.
DR InParanoid; Q58899; -.
DR OMA; RYNTERP; -.
DR OrthoDB; 18594at2157; -.
DR PhylomeDB; Q58899; -.
DR BRENDA; 5.1.3.14; 3260.
DR Proteomes; UP000000805; 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 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..366
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /id="PRO_0000208535"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:4NES"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:4NES"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:4NES"
SQ SEQUENCE 366 AA; 41726 MW; E40DA8E87B835416 CRC64;
MKLSIILGTR PEIIKLSPII RALEKTNIDW HIIHTNQHYS ENMDKIFFEE LNLPNPKYNL
NIGSGTHGEQ TGKMLIEIEK VLLKEKPDVV VVQGDTNTVL AGALVASKLK IDVAHVEAGL
RSFDRNMPEE INRVLTDHIS SYLFAPTEIA KNNLLREGIE ENKIFVVGNT IVDATLQNLK
IAEKNENVRA FFNSVVIDDD YFLLTLHRAE NVDNKERLKN IVEGIFEIIE IYDKAIIFSI
HPRTKKRLKE FNLFDKLKSN KKIKIIEPVG YLEFLMLEKN AELILTDSGG VQEEACILKV
PCITLRDNTE RPETVEVGAN ILVGDNKEKL IKAVEIMLNK KRNWKNPFGN GKSGERIVRI
LTYGKY
