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Database: UniProt
Entry: A0A2N5H022_9BACI
LinkDB: A0A2N5H022_9BACI
Original site: A0A2N5H022_9BACI 
ID   A0A2N5H022_9BACI        Unreviewed;       382 AA.
AC   A0A2N5H022;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=CVD19_11600 {ECO:0000313|EMBL:PLR96622.1};
OS   Bacillus sp. T33-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2054168 {ECO:0000313|EMBL:PLR96622.1, ECO:0000313|Proteomes:UP000235118};
RN   [1] {ECO:0000313|EMBL:PLR96622.1, ECO:0000313|Proteomes:UP000235118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T33-2 {ECO:0000313|EMBL:PLR96622.1,
RC   ECO:0000313|Proteomes:UP000235118};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) 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:PLR96622.1}.
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DR   EMBL; PGVB01000013; PLR96622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5H022; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000235118; 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:UP000235118}.
FT   DOMAIN          28..365
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   382 AA;  43161 MW;  97E87D0BB6EDEC56 CRC64;
     MKQPIKVMTI FGTRPEAIKM APLVLELQKQ PEHFESIVTV TAQHRQMLDQ VLDIFKITPD
     YDLNIMKDRQ TLVDVTTRGL EGLDRVMKEV KPDIVLVHGD TTTTFVASLA ALYNQITVGH
     VEAGLRTWNK YSPFPEEMNR QLTGVMADLH FAPTAMAADN LLRENKSQEN IFITGNTAID
     ALKTTVKETY HHEVLDKVGD DRLILLTAHR RENLGDPMRN MFRAIKRIVD EQPDVQVVYP
     VHLNPVVREI ASEILGNDPR IHLIEPLDVI DFHNFASRAF LILTDSGGVQ EEAPSLGVPV
     LVLRDTTERP EGIEAGTLKL AGNQEEPIYE MATELLNSRE AYEKMAGAVN PYGDGLASKR
     IADAIRYYFK QLDDRPREYQ PK
//
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