ID A0A0R1YJ12_9LACO Unreviewed; 381 AA.
AC A0A0R1YJ12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=FD40_GL000285 {ECO:0000313|EMBL:KRM42494.1}, LA20533_06310
GN {ECO:0000313|EMBL:APT18884.1};
OS Amylolactobacillus amylophilus DSM 20533 = JCM 1125.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Amylolactobacillus.
OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM42494.1, ECO:0000313|Proteomes:UP000051230};
RN [1] {ECO:0000313|EMBL:KRM42494.1, ECO:0000313|Proteomes:UP000051230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM42494.1,
RC ECO:0000313|Proteomes:UP000051230};
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).
RN [2] {ECO:0000313|EMBL:APT18884.1, ECO:0000313|Proteomes:UP000185499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:APT18884.1,
RC ECO:0000313|Proteomes:UP000185499};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Lactobacillus amylophilus DSM
RT 20533T strain.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; CP018888; APT18884.1; -; Genomic_DNA.
DR EMBL; AYYS01000009; KRM42494.1; -; Genomic_DNA.
DR RefSeq; WP_054745835.1; NZ_CP018888.1.
DR AlphaFoldDB; A0A0R1YJ12; -.
DR STRING; 1423721.LA20533_06310; -.
DR KEGG; lah:LA20533_06310; -.
DR PATRIC; fig|1423721.4.peg.287; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000051230; Unassembled WGS sequence.
DR Proteomes; UP000185499; 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:UP000051230}.
FT DOMAIN 26..365
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 381 AA; 42952 MW; 6F7C3393965931C2 CRC64;
MADKIKVMTV FGTRPEAIKM APLVLELQQD ERFTEITVVT AQHREMLDQV LEIFHIKPDY
DFNIMKKNQS LAEITSKVML DLGHVIQSEK PDIVLVHGDT TTSFAAGLAT FYEQTVLGHV
EAGLRTWDKY SPFPEEMNRQ LTDVLTDLYF APTAKSKANL LQENHPEKEI YITGNTAIDA
LQQTVKEEYH HDVLDSIKPG NRVVLVTMHR RENQGEPMRR VFKVMKEVVD AHDDVEIIYP
VHLSPAVQEV AHAVLDNDPR IHLIAPLDVV DFHNLAKRSY LIMTDSGGVQ EEAPSLGKPV
LVLRDTTERP EGVAAGTLRL VGTDEQPVKD AMIELLDSKE SYDKMAKAKN PYGDGQAAKR
IVAAIAHHFD EQHNPRPQDF E
//