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Database: UniProt
Entry: W0RMQ9_9BACT
LinkDB: W0RMQ9_9BACT
Original site: W0RMQ9_9BACT 
ID   W0RMQ9_9BACT            Unreviewed;       383 AA.
AC   W0RMQ9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing) {ECO:0000256|ARBA:ARBA00038858};
DE            EC=5.1.3.14 {ECO:0000256|ARBA:ARBA00038858};
GN   ORFNames=J421_4215 {ECO:0000313|EMBL:AHG91752.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91752.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG91752.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG91752.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
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:0000256|ARBA:ARBA00036080};
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00038209, ECO:0000256|RuleBase:RU003513}.
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DR   EMBL; CP007128; AHG91752.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RMQ9; -.
DR   STRING; 861299.J421_4215; -.
DR   KEGG; gba:J421_4215; -.
DR   PATRIC; fig|861299.3.peg.4272; -.
DR   eggNOG; COG0381; Bacteria.
DR   HOGENOM; CLU_041674_1_0_0; -.
DR   InParanoid; W0RMQ9; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000019151; Chromosome.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
DR   CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   InterPro; IPR029767; WecB-like.
DR   NCBIfam; TIGR00236; wecB; 1.
DR   PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   PANTHER; PTHR43174:SF2; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003513};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT   DOMAIN          28..366
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   383 AA;  41861 MW;  B4D456EA62530C13 CRC64;
     MRHRVCVVVG TRPEAIKLAP VIRALHDRRH AVECVVLATS QHREMLRQAL DAFGLRADVD
     LDLMVDGQDH RQFTSRAMRA LHESFESLQP AAVMVQGDTS TVAAAALIAR ACGILLVHVE
     AGLRSGSLSD PYPEELNRRI ATWAADLHFA PTERARCQLL AEGIDPESVI VTGNTVVDAL
     GSFPADGPLG NARLDALPWD TQPVLLATVH RRENYGARLG QICAALRTIV ERHPAAHVVM
     PVHRNPQVRQ RVHDALDGVA RVHLTEPLSY PLLLRVLRRC RLVLSDSGGL QEEVPSFHKP
     ILILRDRTER PEVLDAGFGR LVGASTETIV RETSRLLTDA RLYAEMCSGR NPFGDGQAAG
     RIADALIARL GARRVAIAAS RPA
//
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