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Database: UniProt
Entry: A0A0M2SXE1_9BACI
LinkDB: A0A0M2SXE1_9BACI
Original site: A0A0M2SXE1_9BACI 
ID   A0A0M2SXE1_9BACI        Unreviewed;       374 AA.
AC   A0A0M2SXE1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=WQ57_07295 {ECO:0000313|EMBL:KKK38823.1};
OS   Mesobacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK38823.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK38823.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK38823.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT   a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) 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:KKK38823.1}.
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DR   EMBL; LAYY01000006; KKK38823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2SXE1; -.
DR   PATRIC; fig|1408103.3.peg.1642; -.
DR   Proteomes; UP000034166; 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:UP000034166}.
FT   DOMAIN          25..358
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   374 AA;  42235 MW;  BF696A99B2BC958D CRC64;
     MTIFGTRPEA IKMAPLVLEL EKYPEKIESI VTVTAQHRQM LDQVLEIFNI EPDHDLNVMK
     DRQTLTDVTV RALEGLDKTM KEVKPDIVLV HGDTTTTFVA SLAAFYNQIT VGHVEAGLRT
     WNKYSPYPEE INRQVTGVIA DLHFSPTSKS YDNLVQENKK PETIFITGNT AIDALQTTVT
     DSYNHEVLDK VEGSRMILLT AHRRENLGEP MRNMFKAIKR LVEEHDDVQV VYPVHMNPAV
     REVASEILGE DDRIHLIEPL GVLDFHNFAS RAFIILTDSG GVQEEAPSLG VPVLVLRDTT
     ERPEGIEAGT LKLAGTDEET IYNMAYELLN NKEEYERMSK ASNPYGDGKA SYRIVQAILH
     HFDNDHKKPK PFLS
//
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