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Database: UniProt
Entry: A0A0W0SDI0_9GAMM
LinkDB: A0A0W0SDI0_9GAMM
Original site: A0A0W0SDI0_9GAMM 
ID   A0A0W0SDI0_9GAMM        Unreviewed;       401 AA.
AC   A0A0W0SDI0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:KTC81440.1};
GN   ORFNames=Lbru_1960 {ECO:0000313|EMBL:KTC81440.1};
OS   Legionella brunensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC81440.1, ECO:0000313|Proteomes:UP000054742};
RN   [1] {ECO:0000313|EMBL:KTC81440.1, ECO:0000313|Proteomes:UP000054742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC81440.1,
RC   ECO:0000313|Proteomes:UP000054742};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
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:KTC81440.1}.
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DR   EMBL; LNXV01000029; KTC81440.1; -; Genomic_DNA.
DR   RefSeq; WP_065235454.1; NZ_LNXV01000029.1.
DR   AlphaFoldDB; A0A0W0SDI0; -.
DR   STRING; 29422.Lbru_1960; -.
DR   PATRIC; fig|29422.6.peg.2090; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000054742; 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}.
FT   DOMAIN          22..370
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   401 AA;  44536 MW;  F76D7AB03107037C CRC64;
     MINTLTVFGT RPEAIKLAPV IRELKAHSQV NNKICVTGQH QQMLQPVLDL FNIKPDFNLN
     VMSKNQGLTT LTTKILTGLE ELFNNFKPHL VLVHGDTTTT FAASLSAYYH QIPVAHIEAG
     LRTGNINSPW PEEANRKLAG ALAAIHFAPT ELARDNLLRE GVLPEKIYVT GNTVIDALFE
     MTRKIDAELE FDIQLAKSFP FLTANRKVIL VTGHRRENFG VGFEQICHAI KQIAISFPEV
     DIVYPVHLNP NVQQPVNSML GGIPNIYLIE PVNYLPFIYL MKRSYLILTD SGGIQEEAPS
     LGKPVLVMRD TTERLEAIIA GTVKLVGSNI ENIVNGVKEL LTDEQVYLGM SEANNPYGDG
     LASSRIMRII SQVTLKPDSH EDVVSKEIEK NKITPKEESL V
//
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