(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMV7_DEBHA

ID   Q6BMV7_DEBHA            Unreviewed;       572 AA.
AC   Q6BMV7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   10-APR-2019, entry version 92.
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   OrderedLocusNames=DEHA2F02244g {ECO:0000313|EMBL:CAG88770.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88770.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88770.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC         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; CR382138; CAG88770.2; -; Genomic_DNA.
DR   RefSeq; XP_460463.2; XM_460463.1.
DR   STRING; 4959.XP_460463.2; -.
DR   EnsemblFungi; CAG88770; CAG88770; DEHA2F02244g.
DR   GeneID; 2903966; -.
DR   KEGG; dha:DEHA2F02244g; -.
DR   HOGENOM; HOG000046975; -.
DR   InParanoid; Q6BMV7; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   OrthoDB; 906802at2759; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1020.10; -; 1.
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; Q6BMV7.
DR   SWISS-2DPAGE; Q6BMV7.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU362012};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
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:UP000000599}.
FT   DOMAIN      390    462       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      490    562       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   572 AA;  63519 MW;  171C4B0E087028D0 CRC64;
     MMIARNLLKG IHKPVNRRVC IPKIGSLTSA KFYSTQSTVQ QFPELQEADF TPEGEPDYIK
     LILTSRVYDV VDEGGSPLTH AVNLSQKCNT NIFLKREDLL PVFSFKLRGA YNMIAHLHSN
     SKSPVSGVIA CSAGNHAQGV AFSASKLKIQ STIVMPTATP SIKYKNVSRL GSQVVLYGDD
     FDSAKKECDR LSSLNGLTNI PPFNHPYVIA GQGTIALEIT RQLRLDKLDA LFVPVGGGGL
     IAGIAVYLKK IAPHVKIIGV ETFDADALYQ SLQNHQSKTL DQVGVFADGT AVKVLGDETW
     KLCHKYVDEV VRVSTDELCA AIKDIFEDTR SIVEPSGALS VAGLKRYLSD NSEIDHRNKN
     YVPILSGANM NFDRLRFVSE RAVLGEGKEV SLAVTIPERP GEFAILQNII DPRAITEFSY
     RFNNSGPANI FVSFNVTNKD KELAPIVESM KSNDYEVIDI SENELAKTHG RYLVGGKSTT
     ANCNKISKER LFRFEFPERP GALTKFLQTL KYDWDITLFH YRNHGHDVGK ILCGFVLPEG
     TSDEDFQDFL KKIGYNFVDE TDNVVYKKFL QS
//

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