(data stored in ACNUC7421 zone)

SWISSPROT: Q8XA80_ECO57

ID   Q8XA80_ECO57            Unreviewed;       428 AA.
AC   Q8XA80; A0A0H3JF64; Q7AHU9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 122.
DE   SubName: Full=L-threonine synthase {ECO:0000313|EMBL:BAB33427.1};
GN   Name=thrC {ECO:0000313|EMBL:BAB33427.1};
GN   ORFNames=ECs_0004 {ECO:0000313|EMBL:BAB33427.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33427.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33427.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604450-51};
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DR   EMBL; BA000007; BAB33427.1; -; Genomic_DNA.
DR   RefSeq; NP_308031.1; NC_002695.1.
DR   RefSeq; WP_000781063.1; NZ_SDVX01000001.1.
DR   SMR; Q8XA80; -.
DR   STRING; 155864.EDL933_0004; -.
DR   EnsemblBacteria; AAG54304; AAG54304; Z0004.
DR   EnsemblBacteria; BAB33427; BAB33427; BAB33427.
DR   GeneID; 913393; -.
DR   KEGG; ecs:ECs0004; -.
DR   PATRIC; fig|386585.9.peg.101; -.
DR   eggNOG; ENOG4105D98; Bacteria.
DR   eggNOG; COG0498; LUCA.
DR   KO; K01733; -.
DR   BioCyc; ECOO157:THRC-MONOMER; -.
DR   Proteomes; UP000000558; 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; Q8XA80.
DR   SWISS-2DPAGE; Q8XA80.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
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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