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Database: UniProt
Entry: G2FYX8_9FIRM
LinkDB: G2FYX8_9FIRM
Original site: G2FYX8_9FIRM 
ID   G2FYX8_9FIRM            Unreviewed;       380 AA.
AC   G2FYX8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=DOT_4944 {ECO:0000313|EMBL:EGW37132.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW37132.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW37132.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW37132.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
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:EGW37132.1}.
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DR   EMBL; AGAF01000231; EGW37132.1; -; Genomic_DNA.
DR   RefSeq; WP_009623529.1; NZ_AGAF01000231.1.
DR   AlphaFoldDB; G2FYX8; -.
DR   PATRIC; fig|913865.3.peg.4549; -.
DR   eggNOG; COG0381; Bacteria.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
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}.
FT   DOMAIN          32..364
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   380 AA;  43465 MW;  A979505F76AD2C41 CRC64;
     MEKIRCLTVF GTRLEAIKMA PLVKEFQKFP DRIDNKVCVT AQHRDMLDQV LSIFQIEPEF
     DLNIMQHGQT LTQITSRALE KSEKVIVETK PHIVLVHGDT STTFMAALAA FYQRITIGHV
     EAGLRTYDKY SPFPEEINRQ LTGNIADLHF APTWISANNL LKEGKKQQNI FMTGNTVIDA
     MKTTVRSNFN HPIFDNFGKD YRLIFMTVNS RENIGQPMEN IFRAVLRIVD DHNDVVVVYP
     MHRNPAVREL AVRILGNRLR IHLIEPLDVI EAHNFMARSY LILTDSGGVQ EEALSLGVPV
     LDLRNTTERP EEIKARTLRL VGTNEEDIYN LSYGLLNHSF VYRTMTSVNN PYGDGHASER
     IREAVLYYFG LGERPDNFEG
//
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