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Database: UniProt
Entry: A0A433RU19_9BACL
LinkDB: A0A433RU19_9BACL
Original site: A0A433RU19_9BACL 
ID   A0A433RU19_9BACL        Unreviewed;       368 AA.
AC   A0A433RU19;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
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=QI30_12100 {ECO:0000313|EMBL:RUS55650.1};
OS   Kurthia sp. 3B1D.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS55650.1, ECO:0000313|Proteomes:UP000288623};
RN   [1] {ECO:0000313|EMBL:RUS55650.1, ECO:0000313|Proteomes:UP000288623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B1D {ECO:0000313|EMBL:RUS55650.1,
RC   ECO:0000313|Proteomes:UP000288623};
RA   Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA   Trudeau A., Shah S., Reiman D.;
RT   "Genome sequence and analysis of novel Kurthia sp.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUS55650.1}.
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DR   EMBL; JTFC01000031; RUS55650.1; -; Genomic_DNA.
DR   RefSeq; WP_020189099.1; NZ_JTFC01000031.1.
DR   AlphaFoldDB; A0A433RU19; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000288623; Unassembled WGS sequence.
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:UP000288623}.
FT   DOMAIN          25..363
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   368 AA;  41071 MW;  62D938B53FECF62A CRC64;
     MSKLKVMTVF GTRPEAIKMA PLVLELKKHE EIETIVTVTA QHREMLDQVL ETFKITPDYD
     LNIMKARQTL IDVTTRGLEG LDAVMKEARP DIVLVHGDTS TTFVASLAAF YNQIPVGHVE
     AGLRTGNKYS PYPEEMNRQL TGVMADIHFA PTEQAKENLL RENKQEDAIV VTGNTAIDAL
     KTTVDDSYTH PILEKLVGER MILLTAHRRE NLGEPMRHIF GAIKRLLQDH EDVEVVYPIH
     LNPVVREIAT DVLGGESRVH LIEPLDVFDF HNFAAKSFMI MTDSGGVQEE APSLGKPVLV
     LRDTTERPEG ISAGTLKLAG TDEEQIYRLA TELLTDEQAY KKMAHASNPY GDGHASERIV
     KALITFLQ
//
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