ID D8MKS6_ERWBE Unreviewed; 376 AA.
AC D8MKS6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:CAX57732.1};
GN Synonyms=wecE {ECO:0000256|HAMAP-Rule:MF_02026};
GN OrderedLocusNames=EbC_02010 {ECO:0000313|EMBL:CAX57732.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX57732.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57732.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(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; FP236843; CAX57732.1; -; Genomic_DNA.
DR RefSeq; WP_013200239.1; NC_014306.1.
DR AlphaFoldDB; D8MKS6; -.
DR STRING; 634500.EbC_02010; -.
DR KEGG; ebi:EbC_02010; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_2_6; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000008793; 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:CAX57732.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02026, ECO:0000313|EMBL:CAX57732.1}.
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; 41836 MW; FAA00731933134A6 CRC64;
MIPFNAPPIV GTELDYMKSA MGSGKLCGDG GFTRRCQQWM ENKFGSKKVL LTPSCTASLE
MAAILIDIQP GDEVIMPSYT FVSTANAFVL RGATIVFVDI RPDTLNMDET LIEAAITDKT
KAIVPVHYAG VSCDMDVIMA LAAKHHLFVI EDAAQGVMST WKGKALGTIG HIGCFSFHET
KNYTAGGEGG ATLINDPALV ERAEIIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMADLQA
AYLWAQLEAA SAINAQRLRL WQNYYSALQP IAASGRITLP TIPSTCQHNA HMFYIKLHDI
DDRTALINWL KEAEILAVFH YIPLHSSPAG QRFGRFHGED RYTQSESERL LRMPLFYNLT
DNNQQTVINS LLSYFS
//
