(data stored in ACNUC7421 zone)

SWISSPROT: B7UI49_ECO27

ID   B7UI49_ECO27            Unreviewed;       428 AA.
AC   B7UI49;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:CAS07552.1};
GN   Name=thrC {ECO:0000313|EMBL:CAS07552.1};
GN   OrderedLocusNames=E2348C_0004 {ECO:0000313|EMBL:CAS07552.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07552.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07552.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604450-51};
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DR   EMBL; FM180568; CAS07552.1; -; Genomic_DNA.
DR   RefSeq; WP_000781063.1; NC_011601.1.
DR   SMR; B7UI49; -.
DR   EnsemblBacteria; CAS07552; CAS07552; E2348C_0004.
DR   KEGG; ecg:E2348C_0004; -.
DR   HOGENOM; HOG000230743; -.
DR   KO; K01733; -.
DR   OMA; YNIKHPE; -.
DR   BioCyc; ECOL574521:E2348C_RS00020-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1380.10; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00260; thrC; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
DR   PRODOM; B7UI49.
DR   SWISS-2DPAGE; B7UI49.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR604450-51}.
FT   DOMAIN        8     80       Thr_synth_N. {ECO:0000259|Pfam:PF14821}.
FT   DOMAIN       99    369       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES     107    107       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR604450-51}.
SQ   SEQUENCE   428 AA;  47084 MW;  020041B36DC42B9B CRC64;
     MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD FVTRSAKILS
     AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH GPTLAFKDFG GRFMAQMLTH
     IAGDKPVTIL TATSGDTGAA VAHAFYGLPN VKVVILYPRG KISPLQEKLF CTLGGNIETV
     AIDGDFDACQ ALVKQAFDDE ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQEARNQ
     LVVSVPSGNF GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA
     MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS EPHAAVAYRA
     LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL AERADLPLLS HNLPADFAAL
     RKLMMNHQ
//

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