GenomeNet

Database: UniProt
Entry: G5NKB0_SALET
LinkDB: G5NKB0_SALET
Original site: G5NKB0_SALET 
ID   G5NKB0_SALET            Unreviewed;       376 AA.
AC   G5NKB0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000256|HAMAP-Rule:MF_02026};
DE            EC=2.6.1.59 {ECO:0000256|HAMAP-Rule:MF_02026};
GN   Name=wecE {ECO:0000256|HAMAP-Rule:MF_02026};
GN   ORFNames=LTSEINV_5566 {ECO:0000313|EMBL:EHC49742.1};
OS   Salmonella enterica subsp. enterica serovar Inverness str. R8-3668.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913075 {ECO:0000313|EMBL:EHC49742.1, ECO:0000313|Proteomes:UP000003532};
RN   [1] {ECO:0000313|EMBL:EHC49742.1, ECO:0000313|Proteomes:UP000003532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R8-3668 {ECO:0000313|EMBL:EHC49742.1,
RC   ECO:0000313|Proteomes:UP000003532};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- FUNCTION: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-
CC       galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-
CC       Glc4O) and L-glutamate. {ECO:0000256|HAMAP-Rule:MF_02026}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose =
CC         dTDP-4-dehydro-6-deoxy-alpha-D-glucose + L-glutamate;
CC         Xref=Rhea:RHEA:10368, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57649, ChEBI:CHEBI:68492; EC=2.6.1.59;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02026};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02026};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC       antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02026}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_02026, ECO:0000256|RuleBase:RU004508}.
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:EHC49742.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFCO01001821; EHC49742.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5NKB0; -.
DR   PATRIC; fig|913075.3.peg.4353; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000003532; Unassembled WGS sequence.
DR   GO; GO:0019180; F:dTDP-4-amino-4,6-dideoxygalactose transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_02026; WecE_RffA; 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR032894; WecE.
DR   InterPro; IPR012749; WecE-like.
DR   NCBIfam; TIGR02379; ECA_wecE; 1.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02026}.
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         181
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02026,
FT                   ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   376 AA;  41956 MW;  21C587BC6C8421C1 CRC64;
     MIPFNAPPVV GTELEYMQSA MSSGKLCGDG GFTRRCQQWL EQHFGSAKVL LTPSCTASLE
     MAALLLDIQP GDEVIMPSFT FVSTANAFVL RGAKIVFVDI RPDTMNIDET LIEAAITDKT
     RAIVPVHYAG VACEMDVIMA LADKYNLFVV EDAAQGVMST YKGRALGTIG HIGCFSFHET
     KNYTAGGEGG ATLINDRTLI ERAEIIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMSDLQA
     AYLWAQLEAA DRINQQRLSL WQTYYDALTP LAHAGRIELP SIPENCGHNA HMFYIKLRDI
     ADRSALINFL KEAEIMAVFH YIPLHDCPAG DKFGEFIGDD VYTTKESERL LRLPLFYNLA
     PVDQRTVITT LLNYFS
//
DBGET integrated database retrieval system