(data stored in ACNUC7421 zone)

SWISSPROT: Q75BN9_ASHGO

ID   Q75BN9_ASHGO            Unreviewed;       560 AA.
AC   Q75BN9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE            EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE   AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
GN   ORFNames=AGOS_ACR232C {ECO:0000313|EMBL:AAS51458.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51458.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51458.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|RuleBase:RU362012}.
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DR   EMBL; AE016816; AAS51458.1; -; Genomic_DNA.
DR   RefSeq; NP_983634.1; NM_208987.1.
DR   STRING; 33169.AAS51458; -.
DR   EnsemblFungi; AAS51458; AAS51458; AGOS_ACR232C.
DR   GeneID; 4619766; -.
DR   KEGG; ago:AGOS_ACR232C; -.
DR   HOGENOM; HOG000046975; -.
DR   InParanoid; Q75BN9; -.
DR   KO; K01754; -.
DR   OMA; SDNEMAK; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   GO; GO:0006566; P:threonine metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.1020.10; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BN9.
DR   SWISS-2DPAGE; Q75BN9.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          377..457
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
FT   DOMAIN          479..550
FT                   /note="ACT-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51672"
SQ   SEQUENCE   560 AA;  61222 MW;  89CF836EA4AAAC06 CRC64;
     MVFNACGRRS GNLVSSALRT GRRYSGTLHK LYTQLKPQEL LPDNTPDYVR MILRSSVYDV
     IEESPMSEAK LLSAKLDTNV CLKREDLLPV FSFKLRGAYN MISNLDEYQK SAGVIACSAG
     NHAQGVAFSA RELGIRAMIV MPTSTPSIKY NSVAAMGAEV VLYGKDFDEA KAECARLAQL
     HKLTDIPPFD HPYVIAGQGT IATEILRQVH NASQIGAVFC GVGGGGLIAG IGSYLKRIAP
     HIKIIGVETH DAPTLHTALK QGRRTMLPAV GCFADGTSVR MMGEETFRVA RDVVDEVVLV
     NTDELCAAIK DIFEDTRAIV EPSGALGVAG LKKYIASHQD AENSRHTYVP VLSGANMNFD
     RLRFVSERAV LGEGKEVFLA VTIPDVPGSF KRMNQIIHPR AVTEFSYRYN EHARRNQDGT
     ARACIYTSFS VADPAAEVPD VLTRLRALGF DARDISANEL AKSHARYLVG GAARVPNERL
     FAFEFPERPG ALTNFLAGLD SSWNITLFHY RNHGADVGRV LVGIAVPSDE YSAFDAFLSG
     LGYAYQEETG NPVYREFLLC
//

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