ID E0SKQ2_DICD3 Unreviewed; 376 AA.
AC E0SKQ2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=rffA {ECO:0000313|EMBL:ADN00455.1};
GN Synonyms=wecE {ECO:0000256|HAMAP-Rule:MF_02026};
GN OrderedLocusNames=Dda3937_00273 {ECO:0000313|EMBL:ADN00455.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00455.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADN00455.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADN00455.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(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}.
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DR EMBL; CP002038; ADN00455.1; -; Genomic_DNA.
DR RefSeq; WP_013319853.1; NC_014500.1.
DR AlphaFoldDB; E0SKQ2; -.
DR STRING; 198628.Dda3937_00273; -.
DR GeneID; 9735748; -.
DR KEGG; ddd:Dda3937_00273; -.
DR PATRIC; fig|198628.6.peg.4202; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_2_6; -.
DR OrthoDB; 9804264at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000006859; 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 Aminotransferase {ECO:0000313|EMBL:ADN00455.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02026, ECO:0000313|EMBL:ADN00455.1}.
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; 41906 MW; 7A45E8B311F30B01 CRC64;
MIPFNSPPVV GSELEYMQAA MRSGKLSGDG AFTRRCQQWL EHYSGSCKVL LTPSCTASLE
MAALLLNIQP GDEVIMPSYT FVSTANAFVL RGATIVFVDI RPDTLNLDEN RIEAAITNKT
RAIVVVHYAG VGCDMNAVMA LAQQHGLFVV EDAAQGMMSR YQERPLGAIG HIGCFSFHET
KNYTAGGEGG ATLINAPELA ERAEIIREKG TNRSQFFRGQ ADKYTWRDIG SSYLMADIQA
AYLWGQLEAA QRIHERRLTL WQHYARAFAP LAAAGRVTLP VIPADCRHNG HLFFLRLRDA
AERSAFISHM KEAEILTVFH YIPLHSSPAG RQFGRFVGED RHTTRESERL VRLPLFYNLS
DLDQRTVINS ALSFFS
//
