ID G7MBC3_9CLOT Unreviewed; 386 AA.
AC G7MBC3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=CDLVIII_0725 {ECO:0000313|EMBL:EHI97450.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97450.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI97450.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97450.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001240; EHI97450.1; -; Genomic_DNA.
DR RefSeq; WP_009168132.1; NZ_CM001240.1.
DR AlphaFoldDB; G7MBC3; -.
DR STRING; 641107.CDLVIII_0725; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_9; -.
DR Proteomes; UP000005106; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT DOMAIN 24..366
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 386 AA; 43796 MW; FAABFBE5E62B91AF CRC64;
MSTKKIITIF GTRPEAIKMA PLVKELEKRE EIESKVCVTA QHREMLDQVL ELFDIKPDFD
LNIMKTKQSL TGITSRVLEG LEEVFKEEKP DMILVHGDTT TTFAGSLAAF YQQIKVGHVE
AGLRTFNKYF PFPEEMNRKL TGSLADLHFA PTKGSKNNLL REGIKENEIY VTGNTVIDAM
KHTVEENYVF ENEELNNIDF NKKVIMITAH RRENWGEGIQ NICIALNKIV EQNSDVELIY
LVHLNPVVKD VVFERLGGKE RIHLLSPLDT KETHNLMNKS FMVMTDSGGL QEEAPHLGKP
VLVLRDVTER PEAVEAGTVK LVGTDVDRIV SEANELLRND EAYSKMSKSI NPYGDGIASR
RIVDAILKYF DLNSRNVEEF DTDSIR
//
