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
//