ID C1CV78_DEIDV Unreviewed; 378 AA.
AC C1CV78;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Deide_11860 {ECO:0000313|EMBL:ACO46095.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46095.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO46095.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO46095.1; -; Genomic_DNA.
DR RefSeq; WP_012693218.1; NC_012526.1.
DR AlphaFoldDB; C1CV78; -.
DR STRING; 546414.Deide_11860; -.
DR PaxDb; 546414-Deide_11860; -.
DR KEGG; ddr:Deide_11860; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_0; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000002208; 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:UP000002208}.
FT DOMAIN 25..364
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 378 AA; 41134 MW; 8A17CC19A507A3B9 CRC64;
MTSKRIVLAF GTRPEATKMA PVYRAVEQTC GLQPLILSTG QQRQMLDGAL SVFDLTPDHD
LNVMTDRQTL ADLTARIVPQ AGRTLREMGA DMVLVHGDTS TSFCVALSAF YEGIPVGHVE
AGLRSGNLRE PFPEEANRRL TGVLSTLDFA PTGGSKANLL REGKSETGIF VTGQTAVDAV
REVAGRVPLR PPWRQRLEAG QRLVTVTMHR RENQPMMREM AEALGRVARA HPELHFIYPV
HLSPAVQEAV RPALGSLENF ELIEPLDYSE MAPLMAASVL LATDSGGLQE EGAALGVPVA
VLRNVTERPE GVEAGVLRLA GNDPQQLEAT LLELLGDERQ LEAMRSARNP YGDGKAAGRI
AQAIAWHFGL TQRPDDWQ
//
