(data stored in ACNUC10821 zone)

SWISSPROT: C8U179_ECO10

ID   C8U179_ECO10            Unreviewed;       428 AA.
AC   C8U179;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 49.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:BAI28887.1};
GN   Name=thrC {ECO:0000313|EMBL:BAI28887.1};
GN   OrderedLocusNames=ECO103_0004 {ECO:0000313|EMBL:BAI28887.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28887.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28887.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI28887.1; -; Genomic_DNA.
DR   RefSeq; WP_000781067.1; NC_013353.1.
DR   EnsemblBacteria; BAI28887; BAI28887; ECO103_0004.
DR   KEGG; eoh:ECO103_0004; -.
DR   HOGENOM; HOG000230743; -.
DR   KO; K01733; -.
DR   OMA; YNIKHPE; -.
DR   BioCyc; ECOL585395:ECO103_RS00020-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U179.
DR   SWISS-2DPAGE; C8U179.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  47100 MW;  15B69AC96DC42B9B 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 KFKESVESIL GETLDLPKEL AERADLPLLS HNLPADFAAL
     RKLMMNHQ
//

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