ID D6IG26_ECOLX Unreviewed; 376 AA.
AC D6IG26;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=ECDG_04574 {ECO:0000313|EMBL:EFF04020.2};
OS Escherichia coli B185.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=550676 {ECO:0000313|EMBL:EFF04020.2, ECO:0000313|Proteomes:UP000004669};
RN [1] {ECO:0000313|EMBL:EFF04020.2, ECO:0000313|Proteomes:UP000004669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B185 {ECO:0000313|EMBL:EFF04020.2,
RC ECO:0000313|Proteomes:UP000004669};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli B185.";
RL Submitted (JAN-2010) 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 ---------------------------------------------------------------------------
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; GG749187; EFF04020.2; -; Genomic_DNA.
DR RefSeq; WP_000612033.1; NZ_GG749187.1.
DR AlphaFoldDB; D6IG26; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000004669; 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 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 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; 41950 MW; BB936BCB1611E61C CRC64;
MIPFNAPPVV GTELDYMQSA MGSGKLCGDG GFTRRCQQWL EQRFGSAKVL LTPSCTASLE
MAALLLDIQP GDEVIMPSYT FVSTANAFVL RGAKIVFVDV RPDTMNIDEM LIEAAITDKT
RVIVPVHYAG VACEMDTIMA LAKKHNLFVV EDAAQGVMST YKGRALGTIG HIGCFSFHET
KNYTAGGEGG ATLINDKALI ERAEIIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMSDLQA
AYLWAQLEAA DRINQQRLAL WQNYYDALAP LAKAGRIELP SIPDGCVQNA HMFYIKLRDI
DDRSALINFL KEAEIMAVFH YIPLHGCPAG ERFGEFHGED RYTTKESERL LRLPLFYNLS
PVNQRTVIAT LLNYFS
//