THDH_SCHPO
ID THDH_SCHPO Reviewed; 600 AA.
AC O94634;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Threonine dehydratase, mitochondrial;
DE EC=4.3.1.19;
DE AltName: Full=Threonine deaminase;
DE Flags: Precursor;
GN ORFNames=SPBC1677.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB37622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:P00927};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P00927};
CC -!- ACTIVITY REGULATION: Isoleucine allosterically inhibits while valine
CC allosterically activates this enzyme. {ECO:0000250|UniProtKB:P00927}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000250|UniProtKB:P00927}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00927}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P00927}.
CC Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAB37622.1; -; Genomic_DNA.
DR PIR; T39516; T39516.
DR RefSeq; NP_596641.1; NM_001022563.2.
DR AlphaFoldDB; O94634; -.
DR SMR; O94634; -.
DR BioGRID; 276697; 1.
DR STRING; 4896.SPBC1677.03c.1; -.
DR iPTMnet; O94634; -.
DR MaxQB; O94634; -.
DR PaxDb; O94634; -.
DR PRIDE; O94634; -.
DR EnsemblFungi; SPBC1677.03c.1; SPBC1677.03c.1:pep; SPBC1677.03c.
DR GeneID; 2540162; -.
DR KEGG; spo:SPBC1677.03c; -.
DR PomBase; SPBC1677.03c; -.
DR VEuPathDB; FungiDB:SPBC1677.03c; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_6_0_1; -.
DR InParanoid; O94634; -.
DR OMA; VNFPQRA; -.
DR PhylomeDB; O94634; -.
DR UniPathway; UPA00047; UER00054.
DR PRO; PR:O94634; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:PomBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IDA:PomBase.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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 SUPFAM; SSF55021; SSF55021; 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;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Isoleucine biosynthesis;
KW Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00927, ECO:0000255"
FT CHAIN ?..600
FT /note="Threonine dehydratase, mitochondrial"
FT /id="PRO_0000314633"
FT DOMAIN 425..497
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 519..590
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT MOD_RES 144
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 66544 MW; 8D8F4E169ED5D0F9 CRC64;
MTGTSFYTSV LRLGRLAQQG LKFQSVKHIR PSCFSSFGLQ AKRWNSTQQN DSSIDCLEPK
LQGIIEDNIS PSTAQKEISD IKFNIPKEML LPDGTPDYLR LTLTSNVYEV IKETPLTKGV
VISESTGVPV YLKREDLTPV FSFKIRGAHN KMASLDKQSL KNGVIACSAG NHAQGVAYSA
RTLGVKATIV MPQNTPEIKW RNVKRLGANV LLHGANFDIA KAECARLAKE QNLEVIHPFD
DPYVIAGQGT IGLEILHQID LRKLDAIYCA VGGGGLIAGI ATYVKRIAPH VKVIGVETFD
ADALKKSLKD KKRVTLKEVG LFADGTAVKL VGEETFRLVS KNIDDVVLVD KDEICAAIKD
VFLDTRSVVE PSGAMAVAGM KRYVAKHKPK NPNAAQVCIL SGANMDFDRL RFIAERADLG
LNKEVFLSVT IPERPGSFEA LHNIITPRSI TEFSYRYDND DYANIYTSFV VKDRATELPL
ILQQISEQNM VAEDISDNEL AKTHARYLIG GKSSVSKERL YRLDFPERPG ALCKFLRSIK
EVCSISLFHY RNCGGDIASV LAGLRVFDGQ VEKLHSVLEE IGYNWVDETN NPVYLRYLRK
