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Database: UniProt
Entry: A0A0M9DBS0_9LACO
LinkDB: A0A0M9DBS0_9LACO
Original site: A0A0M9DBS0_9LACO 
ID   A0A0M9DBS0_9LACO        Unreviewed;       382 AA.
AC   A0A0M9DBS0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=RZ71_00140 {ECO:0000313|EMBL:KOY75596.1};
OS   Apilactobacillus kunkeei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Apilactobacillus.
OX   NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY75596.1, ECO:0000313|Proteomes:UP000037778};
RN   [1] {ECO:0000313|EMBL:KOY75596.1, ECO:0000313|Proteomes:UP000037778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAko {ECO:0000313|EMBL:KOY75596.1,
RC   ECO:0000313|Proteomes:UP000037778};
RX   PubMed=25953738; DOI=10.1093/gbe/evv079;
RA   Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA   Andersson S.G.;
RT   "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT   Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL   Genome Biol. Evol. 7:1455-1473(2015).
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:KOY75596.1}.
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DR   EMBL; JXCY01000007; KOY75596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9DBS0; -.
DR   PATRIC; fig|148814.15.peg.951; -.
DR   Proteomes; UP000037778; 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:UP000037778}.
FT   DOMAIN          32..367
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   382 AA;  42963 MW;  B8CEC25FB6AEF61D CRC64;
     MKKPIKVMTI FGTRPEAIKM APIILEMKNN LDEFQPITVL TGQHKEMLDQ VMDIFHIEAD
     YNLHVMKAQQ TLSSITTTVI NKLDSIINEA KPDIILVHGD TTTTFAAAVS AFYHQIPLGH
     VEAGLRTWDK YSPYPEEMNR QMTDILSDVY FAPTELSKEN LLKQNLKEDR IYITGNTAID
     ALKQTVDRNY HHSVLDDIDK THKIILLTMH RRENQGEPMR RTFETIKNEV LNRKDIEVVY
     PVHLSPAVQS VAHSVFDGVN RVHLIEPLDV VDFHNMAARS HFIMTDSGGV QEEAPSLGKP
     VLVLREATER PEGVDAGTLK LVGTDPEKIS ASIDQLLDDS EEYKKMATAK NPYGDGTASK
     QILEAIKEVF ATNKLSGDHN EA
//
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