ID Q6CAI4_YARLI Unreviewed; 529 AA.
AC Q6CAI4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
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=YALI0_D02497g {ECO:0000313|EMBL:CAG80516.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG80516.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG80516.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., 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(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00001274,
CC ECO:0000256|RuleBase:RU362012};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR EMBL; CR382130; CAG80516.1; -; Genomic_DNA.
DR RefSeq; XP_502328.1; XM_502328.1.
DR AlphaFoldDB; Q6CAI4; -.
DR STRING; 284591.Q6CAI4; -.
DR EnsemblFungi; CAG80516; CAG80516; YALI0_D02497g.
DR GeneID; 2910530; -.
DR KEGG; yli:YALI0D02497g; -.
DR VEuPathDB; FungiDB:YALI0_D02497g; -.
DR HOGENOM; CLU_021152_6_0_1; -.
DR InParanoid; Q6CAI4; -.
DR OMA; TRFEYTK; -.
DR OrthoDB; 5476420at2759; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
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:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR CDD; cd04906; ACT_ThrD-I_1; 1.
DR CDD; cd04907; ACT_ThrD-I_2; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU362012};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU362012}; Lyase {ECO:0000256|RuleBase:RU362012};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 352..427
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
FT DOMAIN 449..520
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 529 AA; 58110 MW; 42348BBC6CD7B41B CRC64;
MSEPDYLKLI LKSRVYDVCK ETPVTSAHGL SEKLGCKVLL KREDLQPVFS FKLRGAYNMI
SQLSDEEKWK GVIACSAGNH AQGVAFSANY LNIPATIVMP LATPSIKHSN VSRLGGKVVL
HGDDFDSAKA HCKQLCEKYG LTDIPPFDHP HVIAGQGTIG MEILRQASDN LKAVFICVGG
GGLIAGVGAY IKRIQPDVKI IAVETYDACA LKQSLIKGER VTLPEVGLFA DGAAVKLCGE
ETFRLCRKYV DGVVLVNTDE ICAAIKDVFE ATRSVVEPAG ALSVAGLKKY CSDPSAIWWS
PESDSAKANG IPTNVAISET DEYLSILSGA NMNFDRLRFV AERAMLGEGT EVFMVVTIPD
IPGAFEKLHE IILPRAVTEF SYRKKSTAEN EDANIFVSFS VKNRQEEIAD VLEKLQAAGM
SGVDVSDNEL AKTHARYLVG GQPDVPNERL FRFEFPERPN ALKNFLGGVQ TKWNITLFHY
RNNGSDIGKI LTALDVPESD NEALKEFLEK LKYPFVEETD NVVYKQFMK
//
