ID E1SK76_PANVC Unreviewed; 391 AA.
AC E1SK76;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:ADO11525.1};
GN OrderedLocusNames=Pvag_3389 {ECO:0000313|EMBL:ADO11525.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO11525.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO11525.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO11525.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
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}.
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DR EMBL; CP002206; ADO11525.1; -; Genomic_DNA.
DR AlphaFoldDB; E1SK76; -.
DR KEGG; pva:Pvag_3389; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_2_6; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000006631; Chromosome.
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 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02026,
FT ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 391 AA; 43693 MW; 77E5FBE499FF9BF7 CRC64;
MPGSTAPPTG FTGKVMIPFN APPIVGTEIE YMQSAMNSGK LCGDGGFTRR CQQWMEQRFG
SKKVLLTPSC TASLEMAALL IDLQPGDEVI MPSYTFVSTA NAFVLRGARI VFVDVRPDTM
NIDETLIEAA ITEKTRAIVP VHYAGVACEM DTIMALAAKH KLFVIEDAAQ GVMSRYKGRA
LGTIGHIGCF SFHETKNYTA GGEGGATLIN DASLVERAEI VREKGTNRSQ FFRGQVDKYT
WRDMGSSYLM ADLQAAYLWA QLEAAERINQ QRLRIWHRYY DALQPLAAQG RISLPVIPAS
CEHNAHMFYI KLRDQDDRQA LINWMKEAEI LTVFHYIPLH SSPAGERFSQ FVGDDRFTTL
ESERLLRLPL FYNLSDNNQS TVISSLLSFF S
//
