ID E7G485_9HELI Unreviewed; 459 AA.
AC E7G485;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000313|EMBL:EFX41807.1};
GN Name=wecB {ECO:0000313|EMBL:EFX41807.1};
GN ORFNames=HSUHS5_0784 {ECO:0000313|EMBL:EFX41807.1};
OS Helicobacter suis HS5.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX41807.1, ECO:0000313|Proteomes:UP000054093};
RN [1] {ECO:0000313|EMBL:EFX41807.1, ECO:0000313|Proteomes:UP000054093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS5 {ECO:0000313|EMBL:EFX41807.1,
RC ECO:0000313|Proteomes:UP000054093};
RX PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT "Genome sequence of Helicobacter suis supports its role in gastric
RT pathology.";
RL Vet. Res. 42:51-51(2011).
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {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:EFX41807.1}.
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DR EMBL; ADHO01000126; EFX41807.1; -; Genomic_DNA.
DR AlphaFoldDB; E7G485; -.
DR Proteomes; UP000054093; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF3; 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|RuleBase:RU003513};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054093};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..445
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 459 AA; 52128 MW; EBB94B60FCEBB7C5 CRC64;
MNPGMVCIIS MSTGHRLISA LMVCVYPPFL IIFSISSMLA KPLSGKQALM PRMEICLLEM
ARFAWLYQNR ALTHVLKLST SIKLVKLYTI LGARPQFIKA RALSATLKQN PYIHSPHATY
QLQEFYIHTN QHSQANMSMD FFKELHLDSP THTLPKAPNH LSRLEHVGFM FAKLKTICTQ
ERPDFILVYG DTNSTLAGSL IAHFLNIPLI HIEAGLRSDN FNMPEEYNRI ATDKLSTLLF
CPTKQVYHTF KPKPHQKLYF SGDVMLDNVL FYQNHAHPPQ GFEAKNFLFA TLHRASNIDN
QDCLHAIISA LEELAQQIPV FLALHPRTAM ALEKYNLFLK HTHILPPLSY LETLYMLKHA
RLVLTDSGGL QKEAYFCKTP VLILREQSEY QVLIEEGAGV LVGHDKARII QIAMQSLKEQ
PKLSFASMHP FGEGHSASLI LQAIKEHVCY LESLVLEDL
//
