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Database: UniProt
Entry: J9DSV0_9RHOB
LinkDB: J9DSV0_9RHOB
Original site: J9DSV0_9RHOB 
ID   J9DSV0_9RHOB            Unreviewed;       376 AA.
AC   J9DSV0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=A33M_1258 {ECO:0000313|EMBL:EJW09487.1};
OS   Rhodovulum sp. PH10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW09487.1, ECO:0000313|Proteomes:UP000002930};
RN   [1] {ECO:0000313|EMBL:EJW09487.1, ECO:0000313|Proteomes:UP000002930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH10 {ECO:0000313|EMBL:EJW09487.1,
RC   ECO:0000313|Proteomes:UP000002930};
RX   PubMed=23105089; DOI=10.1128/JB.01695-12;
RA   Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT   "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT   Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT   India.";
RL   J. Bacteriol. 194:6363-6363(2012).
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:EJW09487.1}.
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DR   EMBL; AKZI01000169; EJW09487.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9DSV0; -.
DR   STRING; 1187851.A33M_1258; -.
DR   PATRIC; fig|1187851.3.peg.4293; -.
DR   eggNOG; COG0381; Bacteria.
DR   Proteomes; UP000002930; 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:UP000002930}.
FT   DOMAIN          20..366
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   376 AA;  41417 MW;  6C1C1734E921623E CRC64;
     MLLVFGTRPE AIKMLPVAQA LMRKSNADVR ICVTAQHRQM LDQVLDLFDV WPDYDLDIMK
     QGQGLEHVTT AVLQGLGDVL DDAKPDRVLV HGDTTTTMAA SLAAFYRKVP VAHVEAGLRS
     GDPAQPWPEE MNRRVTDVIA DRFFAPTTRA RDNLLKENAS PAAIHVTGNT VIDALLAVVD
     RIDRSPDLKE TLAAQFAFLA PDRPILLVTG HRRENFGKPF DSLCSAIRDL ARAHQIQVVY
     PVHLNPNVQS AVRRFLGDVP HVHLVPPLDY LPFVYLMMRA HVVLTDSGGI QEEAPSLGKP
     VFVMRNVTER PEAVEAGTVK LVGTDRDRIF TAVGEVIEDA DAHARMSQAH NPYGDGQAAR
     RIADILTIGS TDEFSP
//
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