(data stored in SCRATCH zone)

SWISSPROT: C5BBC2_EDWI9

ID   C5BBC2_EDWI9            Unreviewed;       376 AA.
AC   C5BBC2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   OrderedLocusNames=NT01EI_0097 {ECO:0000313|EMBL:ACR67357.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67357.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67357.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67357.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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-D-galactose =
CC         dTDP-4-dehydro-6-deoxy-D-galactose + L-glutamate;
CC         Xref=Rhea:RHEA:10368, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57596, ChEBI:CHEBI:57837; 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
CC       common antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02026}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_02026, ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP001600; ACR67357.1; -; Genomic_DNA.
DR   RefSeq; WP_015869576.1; NC_012779.2.
DR   EnsemblBacteria; ACR67357; ACR67357; NT01EI_0097.
DR   GeneID; 7959816; -.
DR   KEGG; eic:NT01EI_0097; -.
DR   PATRIC; fig|634503.3.peg.91; -.
DR   eggNOG; ENOG4105CF4; Bacteria.
DR   eggNOG; COG0399; LUCA.
DR   HOGENOM; HOG000230162; -.
DR   KO; K02805; -.
DR   OMA; IVNHGMY; -.
DR   OrthoDB; 1722208at2; -.
DR   BioCyc; EICT634503:G1GVC-90-MONOMER; -.
DR   UniPathway; UPA00566; -.
DR   Proteomes; UP000001485; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_02026; WecE_RffA; 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR032894; WecE.
DR   InterPro; IPR012749; WecE-like.
DR   PANTHER; PTHR30244; PTHR30244; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02379; ECA_wecE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BBC2.
DR   SWISS-2DPAGE; C5BBC2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02026,
KW   ECO:0000256|PIRSR:PIRSR000390-2, ECO:0000256|RuleBase:RU004508,
KW   ECO:0000256|SAAS:SAAS01096425};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02026}.
FT   MOD_RES     181    181       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02026,
FT                                ECO:0000256|PIRSR:PIRSR000390-2}.
SQ   SEQUENCE   376 AA;  42084 MW;  138485774BC988FB CRC64;
     MIPFNAPPVT GSESDYMQAA MASGKLCGDG GFTRRCQQWM EQRFGSAKVL LTPSCTASLE
     MAALLLDIQP GDEVIMPSFT FVSTANAFVL RGARIVFVDV RPDTMNIDET LIEAAITEKT
     RAIVPVHYAG VACEMDTIMA LAQQYGLYVV EDAAQGVMAT YKGRALGTIG HIGCYSFHET
     KNYTAGGEGG ATLINDAALI ERAEIIREKG TNRSQFFRGQ VDKYTWRDIG SSYLMSDLQA
     AYLWAQLEVA DRINQRRLQL WRQYHEALAP LAGAGRLALP TMPTHCGHNA HMFYLKLRDM
     RERSAFIDFL KEAEIMAVFH YIPLHCSPAG ARFGRFVGED RYTTRESERL VRLPLFYNLP
     DVNQRTVINS IQSFFR
//

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