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Database: UniProt
Entry: A0A0R1P0V5_9LACO
LinkDB: A0A0R1P0V5_9LACO
Original site: A0A0R1P0V5_9LACO 
ID   A0A0R1P0V5_9LACO        Unreviewed;       368 AA.
AC   A0A0R1P0V5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=FD27_GL001297 {ECO:0000313|EMBL:KRL26160.1};
OS   Limosilactobacillus frumenti DSM 13145.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL26160.1, ECO:0000313|Proteomes:UP000051445};
RN   [1] {ECO:0000313|EMBL:KRL26160.1, ECO:0000313|Proteomes:UP000051445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL26160.1,
RC   ECO:0000313|Proteomes:UP000051445};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(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:KRL26160.1}.
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DR   EMBL; AZER01000024; KRL26160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1P0V5; -.
DR   STRING; 1423746.FD27_GL001297; -.
DR   PATRIC; fig|1423746.3.peg.1322; -.
DR   Proteomes; UP000051445; 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:UP000051445}.
FT   DOMAIN          26..361
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   368 AA;  41422 MW;  7208383BAD8144C5 CRC64;
     MLLFGTRAEA LKLAPIIEQM KKDPTTWQPS IVVAAQERRS LLQQTMKFLN VKSDFDLDTS
     EISHVNAAEK LSQLLHNFNN VINASQPDMM LVVGDAATSL AASLVSFYHH LPLGHVEAGL
     RTYDKFSPFP DEMHRRLTDD LADLYFAPTT GARDNLLSEH HPAEQIYVTG NTSIDAVRER
     LTADFHNEVL DQIPDDHRLI ILTMQRPESI GAPMERVFHT MKDVVETNPD VDVIYPVYPN
     SEVISMADDV LSNQDRVHLI EPLNHSDFLN LVARSDFLIT DSGSIQEEAP ALHKPVLLLR
     EKTERQEAVE EGSVKIVGTN PTSIQQAVFE LLHKPKIYRK MAEAPNPFGD GHASEKILQI
     IQDYLTHK
//
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