GenomeNet

Database: UniProt
Entry: A0A085JMA5_9GAMM
LinkDB: A0A085JMA5_9GAMM
Original site: A0A085JMA5_9GAMM 
ID   A0A085JMA5_9GAMM        Unreviewed;       376 AA.
AC   A0A085JMA5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   ECO:0000313|EMBL:KFD21601.1};
GN   ORFNames=GTPT_0792 {ECO:0000313|EMBL:KFD21601.1};
OS   Tatumella ptyseos ATCC 33301.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD21601.1, ECO:0000313|Proteomes:UP000028602};
RN   [1] {ECO:0000313|EMBL:KFD21601.1, ECO:0000313|Proteomes:UP000028602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD21601.1,
RC   ECO:0000313|Proteomes:UP000028602};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KFD21601.1}.
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; JMPR01000014; KFD21601.1; -; Genomic_DNA.
DR   RefSeq; WP_025904153.1; NZ_JMPR01000014.1.
DR   AlphaFoldDB; A0A085JMA5; -.
DR   eggNOG; COG0399; Bacteria.
DR   OrthoDB; 9804264at2; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000028602; 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   Aminotransferase {ECO:0000313|EMBL:KFD21601.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02026, ECO:0000313|EMBL:KFD21601.1}.
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;  42333 MW;  14582B37D682CE03 CRC64;
     MIPFNSPPVT GSEIDYMRSA MESGKLSGDG GFTRRCQQWM EQQSGSHKVL LTPSCTASLE
     MAALLINIVP GDEVIMPSYT FVSTANAFVL RGARIVFVDI RPDTLNIDET RVEAAITDKT
     RAIVVVHYAG VPCEMDALVR LTEKHKLYLI EDAAQGVMSA YQGRPLGSIG HIGCFSFHET
     KNYTAGGEGG ATLINDPELV ARAEIIREKG TNRSQFFRGQ TDKYTWRDLG SSYLMSDLQA
     AYLWAQLESA EQINQRRLAL WNNYYSALQP LARQGRLTLP VVPEGCTHNA HMFYILLEDN
     DTRERLIAWM KEAEILAVFH YIPLHSSPAG EQFGRFHGED RYTTLQSERL LRLPLFYNLT
     DNNQKTVISS LMSFFR
//
DBGET integrated database retrieval system