ID A0A0X8HD79_9GAMM Unreviewed; 223 AA.
AC A0A0X8HD79;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:AMD00466.1};
GN ORFNames=LOKO_01398 {ECO:0000313|EMBL:AMD00466.1};
OS Halomonas chromatireducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=507626 {ECO:0000313|EMBL:AMD00466.1, ECO:0000313|Proteomes:UP000063387};
RN [1] {ECO:0000313|EMBL:AMD00466.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00466.1,
RC ECO:0000313|Proteomes:UP000063387};
RX PubMed=26988058;
RA Sharko F.S., Shapovalova A.A., Tsygankova S.V., Komova A.V.,
RA Boulygina E.S., Teslyuk A.B., Gotovtsev P.M., Namsaraev Z.B.,
RA Khijniak T.V., Nedoluzhko A.V., Vasilov R.G.;
RT "Draft Genome Sequence of 'Halomonas chromatireducens' Strain AGD 8-3, a
RT Haloalkaliphilic Chromate- and Selenite-Reducing Gammaproteobacterium.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|EMBL:AMD00466.1, ECO:0000313|Proteomes:UP000063387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMD00466.1,
RC ECO:0000313|Proteomes:UP000063387};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014226; AMD00466.1; -; Genomic_DNA.
DR STRING; 507626.LOKO_01398; -.
DR KEGG; hco:LOKO_01398; -.
DR PATRIC; fig|507626.3.peg.1384; -.
DR Proteomes; UP000063387; Chromosome.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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:UP000063387}.
FT DOMAIN 24..190
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT REGION 196..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 223 AA; 24114 MW; 274C77B94B1ECC60 CRC64;
MPIKTLCVFG TRPEAIKMAP LALALATDER FDAKVCVTGQ HREMLDQVLD LFELVPDHDL
NIMKPGQDLT DVTTAILQGM KEVLEEVKPD IVLVHGDTST TLSTTLAAYY QQIPVGHVEA
GLRTGNIYSP WPEEANRKLT GALAELHFAP TDRSRQNLLE EGVAPTKVYV TGNTVIDALV
DVVRKIDTSP VXALAAAQQQ AEQDDEAASE AEADADAGQE AKS
//
