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Database: UniProt
Entry: D6IG26_ECOLX
LinkDB: D6IG26_ECOLX
Original site: D6IG26_ECOLX 
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}.
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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
//
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