ILV3_SCHPO
ID ILV3_SCHPO Reviewed; 598 AA.
AC Q10318; P78903;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dihydroxy-acid dehydratase, mitochondrial {ECO:0000250|UniProtKB:P39522};
DE Short=DAD {ECO:0000250|UniProtKB:P39522};
DE EC=4.2.1.9 {ECO:0000250|UniProtKB:P39522};
DE Flags: Precursor;
GN ORFNames=SPAC17G8.06c;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-598.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: Dihydroxyacid dehydratase that catalyzes the third step in
CC the common pathway leading to biosynthesis of branched-chain amino
CC acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-
CC methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-
CC methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-
CC methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate
CC (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-
CC valine, respectively. {ECO:0000250|UniProtKB:P39522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:49072; EC=4.2.1.9;
CC Evidence={ECO:0000250|UniProtKB:P39522};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC Evidence={ECO:0000250|UniProtKB:P39522};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-
CC oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9;
CC Evidence={ECO:0000250|UniProtKB:P05791};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695;
CC Evidence={ECO:0000250|UniProtKB:P05791};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P39522};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P39522};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKJ5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000305}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 3/4. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P39522}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93689.1; -; Genomic_DNA.
DR EMBL; D89254; BAA13915.1; -; mRNA.
DR PIR; T37858; T37858.
DR PIR; T43179; T43179.
DR RefSeq; NP_593729.1; NM_001019160.2.
DR AlphaFoldDB; Q10318; -.
DR SMR; Q10318; -.
DR BioGRID; 278631; 3.
DR STRING; 4896.SPAC17G8.06c.1; -.
DR MaxQB; Q10318; -.
DR PaxDb; Q10318; -.
DR PRIDE; Q10318; -.
DR EnsemblFungi; SPAC17G8.06c.1; SPAC17G8.06c.1:pep; SPAC17G8.06c.
DR GeneID; 2542155; -.
DR KEGG; spo:SPAC17G8.06c; -.
DR PomBase; SPAC17G8.06c; -.
DR VEuPathDB; FungiDB:SPAC17G8.06c; -.
DR eggNOG; KOG2448; Eukaryota.
DR HOGENOM; CLU_014271_4_2_1; -.
DR InParanoid; Q10318; -.
DR OMA; TQGRNMA; -.
DR PhylomeDB; Q10318; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR PRO; PR:Q10318; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; ISS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; ISS:PomBase.
DR GO; GO:0006551; P:leucine metabolic process; ISS:PomBase.
DR GO; GO:0009099; P:valine biosynthetic process; ISS:PomBase.
DR Gene3D; 3.50.30.80; -; 1.
DR HAMAP; MF_00012; IlvD; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR004404; DihydroxyA_deHydtase.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; SSF143975; 1.
DR TIGRFAMs; TIGR00110; ilvD; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..598
FT /note="Dihydroxy-acid dehydratase, mitochondrial"
FT /id="PRO_0000015635"
FT ACT_SITE 511
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 157
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 232
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKJ5"
FT CONFLICT 196
FT /note="I -> V (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Y -> F (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> A (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="K -> E (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="M -> L (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> F (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> T (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="G -> D (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="L -> V (in Ref. 2; BAA13915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 63927 MW; DF9E5544F0B87393 CRC64;
MMFCKLLRCQ NGIASKRAAL SLKGFKTSSI NLVEKKLNKY SETITGPKSQ GASQAMLYAT
GLNEEDMKKP QVGIASCWYE GNPCNMHLLD LGRRVKEGVK KAGLTGFQFN TIGVSDGISM
GTTGMRYSLQ SREIIADSIE TVMQGQWYDA NVSIPGCDKN MPGCLIAMGR FNRPSIMVYG
GSIRAGHSPC QNNAPIDIVS AFQSYGEFIT GKIDEPTRHD IIRHACPGGG ACGGMYTANT
MASCAEAMGM TLPGSSSYLA GSPEKFAECE AAGSAIKRLL VDDIKPRDIM TRSAFENAMV
LTMTLGGSTN SVLHLIAIAK SVGITLTLDD FQAVSNRTPF IADMKPSGKY VMEDLFAIGG
IPSVLKYLHA EGLIDGSNIT VTGKTLAENL RGFKDLAEGQ KIIRPLSNPI KTEGHLRVLR
GSLAPEGSVA KITGKEGLNF TGKARVFDAE NDFIAALERG EFKKGEKTVV IIRFEGPKGG
PGMPEMLKPS SAIMGAGLGK DVALLTDGRF SGGSHGFLIG HVDPEAQVGG PIALVQDGDV
IEINAVKNTL DLMVDEKEMA RRRSVWKAPP LKYQQGTLLK YARNVSTASK GAVTDSLE
