ID K0JWB6_SACES Unreviewed; 385 AA.
AC K0JWB6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=wecB {ECO:0000313|EMBL:CCH28483.1};
GN OrderedLocusNames=BN6_11570 {ECO:0000313|EMBL:CCH28483.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH28483.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH28483.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(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}.
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DR EMBL; HE804045; CCH28483.1; -; Genomic_DNA.
DR RefSeq; WP_015098596.1; NC_019673.1.
DR AlphaFoldDB; K0JWB6; -.
DR STRING; 1179773.BN6_11570; -.
DR KEGG; sesp:BN6_11570; -.
DR PATRIC; fig|1179773.3.peg.1162; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_11; -.
DR OrthoDB; 9803238at2; -.
DR BioCyc; SESP1179773:BN6_RS05690-MONOMER; -.
DR Proteomes; UP000006281; 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:UP000006281}.
FT DOMAIN 24..366
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 385 AA; 40470 MW; 4AB7042E78FE7541 CRC64;
MKEVLLLAGT RPEAVKIAPV ALALADHPVL RPLIVHSGQH EGLVEQALGA FDLKPDIVLT
TPRVTGSQAE LVAALVPALD QVLRVRDPAV VLVQGDTTTA LAGALAAFWR GIPVAHLEAG
LRTGDLAGPF PEEGTRQMIA RIAALHLAPT DDAATALVGE ALPAAEIVVT GNTVVDAVRR
VAAAALPVRD PALAALEADL DATGDRLVLV TVHRRESWGA PLERVLHAVR ALVDRHPDVR
VLLPAHPNPA LRATARQVLG GHARIVVGEP LDYPDLVRAL RRSALVLTDS GGIQEEAPSF
GVPVLVLRSA TERMSAVDAG CAWLVGTDTT RILAEAGWIL GSRLRLPPGR NPFGDGRAAI
RVRGALERLV GSPALLAPLP VRARR
//
