ID   WECB_METMP              Reviewed;         366 AA.
AC   Q6LZC4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase;
DE            EC=5.1.3.14;
DE   AltName: Full=UDP-GlcNAc-2-epimerase;
GN   Name=wecB; Synonyms=wbpI; OrderedLocusNames=MMP0705;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=900;
RX   PubMed=18263721; DOI=10.1128/jb.01970-07;
RA   Namboori S.C., Graham D.E.;
RT   "Acetamido sugar biosynthesis in the Euryarchaea.";
RL   J. Bacteriol. 190:2987-2996(2008).
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.
CC       {ECO:0000269|PubMed:18263721}.
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         Evidence={ECO:0000269|PubMed:18263721};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.36 mM for UDP-GlcNAc {ECO:0000269|PubMed:18263721};
CC       pH dependence:
CC         Active from pH 6 to 10. {ECO:0000269|PubMed:18263721};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:18263721};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18263721}.
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; BX950229; CAF30261.1; -; Genomic_DNA.
DR   RefSeq; WP_011170649.1; NC_005791.1.
DR   AlphaFoldDB; Q6LZC4; -.
DR   SMR; Q6LZC4; -.
DR   STRING; 267377.MMP0705; -.
DR   EnsemblBacteria; CAF30261; CAF30261; MMP0705.
DR   GeneID; 2761897; -.
DR   KEGG; mmp:MMP0705; -.
DR   PATRIC; fig|267377.15.peg.722; -.
DR   eggNOG; arCOG01392; Archaea.
DR   HOGENOM; CLU_041674_0_1_2; -.
DR   OMA; RYNTERP; -.
DR   OrthoDB; 18594at2157; -.
DR   BioCyc; MMAR267377:MMP_RS03690-MON; -.
DR   BRENDA; 5.1.3.14; 3262.
DR   SABIO-RK; Q6LZC4; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IDA:CACAO.
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   Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..366
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /id="PRO_0000337833"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  41356 MW;  F0DE241FAEA54139 CRC64;
     MYKIGIILGT RPEIIKMSPV IRELTTKKFF LIHTNQHYSE NMDKIFFEEL NLKKPDYNLN
     IGSGSHGDQT GRMLMEIEKV LLKEKPDFVL VQGDTNTVLA GALAASKLGI KIGHIEAGLR
     SFDRKMPEET NRVLTDHISE FLFAPTKTAA NNILKEGISD EKIHIVGNTI VDATIQNLKI
     AEKNEKVCKF ISKITKNEKY FLLTLHRAEN TDNFEILSKL VTSINNISKK YEKNIIFPIH
     PRTHKKLNEF GLINKLENNH LIKIIEPVGY LEFLGLEKNA ELIITDSGGL QEEACILNVP
     CVTLRENTER PETLDVNSNI LAGSDPENIL NCVEKMLKSN RHWNNPFGDG NSGKIIVNIV
     FGEKKP