ID A0A0Q4FYM2_9BURK Unreviewed; 377 AA.
AC A0A0Q4FYM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=ASE76_10340 {ECO:0000313|EMBL:KQM70195.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM70195.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM70195.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM70195.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM70195.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM70195.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQM70195.1}.
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DR EMBL; LMKO01000023; KQM70195.1; -; Genomic_DNA.
DR RefSeq; WP_055841014.1; NZ_LMKO01000023.1.
DR AlphaFoldDB; A0A0Q4FYM2; -.
DR STRING; 1735686.ASE76_10340; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000051325; Unassembled WGS sequence.
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:UP000051325}.
FT DOMAIN 22..367
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 377 AA; 41490 MW; CF4391B23778BA5F CRC64;
MHVLSIFGTR PEAIKMAPLV AALRAEPQVR STVCITGQHR EMLAQVMALF DLKADHDLDV
MRPDQTLNGL HARVVAGVDG LLQTARPDCV LVHGDTTTAA ACALAAFHRQ IPVGHVEAGL
RSGDIRSPFP EEMNRRFVDS VSTWLFAPTP SSRDALLREN LPGRIWVTGN TVIDALAATV
ARLQADAALA RTLAERYDWV DAGRRLVLVT GHRRENFGEG FRNICTALHT LAQRSDVQIV
YPVHLNPQVR DVVTAELSGL SNVHLVAPLE YLDFVWFMQR AHLILTDSGG VQEEAPYLGK
PVLVMRDVTE RPEAVTAGTV RLVGTSRERI VGETNRLLDD PATYADFCRR SNPYGDGHAS
RRIVDALCTR PFTEFAG
//
