ILVB_SCHPO
ID ILVB_SCHPO Reviewed; 669 AA.
AC P36620; Q9P796;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Acetolactate synthase, mitochondrial;
DE EC=2.2.1.6;
DE AltName: Full=AHAS;
DE AltName: Full=ALS;
DE AltName: Full=Acetohydroxy-acid synthase;
DE Flags: Precursor;
GN Name=ilv1; ORFNames=SPBP35G2.07;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8299177; DOI=10.1007/bf00351720;
RA Bekkaoui F., Nadin-Davis S.A., Crosby W.L.;
RT "Isolation and structure of an acetolactate synthase gene from
RT Schizosaccharomyces pombe and complementation of the ilv2 mutation in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 24:544-547(1993).
RN [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; L11293; AAA35315.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB87369.1; -; Genomic_DNA.
DR PIR; S39111; S39111.
DR RefSeq; NP_595382.1; NM_001021289.2.
DR AlphaFoldDB; P36620; -.
DR SMR; P36620; -.
DR BioGRID; 277856; 58.
DR STRING; 4896.SPBP35G2.07.1; -.
DR iPTMnet; P36620; -.
DR MaxQB; P36620; -.
DR PaxDb; P36620; -.
DR PRIDE; P36620; -.
DR EnsemblFungi; SPBP35G2.07.1; SPBP35G2.07.1:pep; SPBP35G2.07.
DR GeneID; 2541345; -.
DR KEGG; spo:SPBP35G2.07; -.
DR PomBase; SPBP35G2.07; ilv1.
DR VEuPathDB; FungiDB:SPBP35G2.07; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_1_2_1; -.
DR InParanoid; P36620; -.
DR OMA; CFGTSGP; -.
DR PhylomeDB; P36620; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P36620; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005948; C:acetolactate synthase complex; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IGI:PomBase.
DR GO; GO:0009098; P:leucine biosynthetic process; IC:PomBase.
DR GO; GO:0009099; P:valine biosynthetic process; IDA:PomBase.
DR CDD; cd02015; TPP_AHAS; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00118; acolac_lg; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW Flavoprotein; Magnesium; Metal-binding; Mitochondrion; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Transit peptide.
FT TRANSIT 1..140
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 141..669
FT /note="Acetolactate synthase, mitochondrial"
FT /id="PRO_0000035663"
FT REGION 497..577
FT /note="Thiamine pyrophosphate binding"
FT BINDING 134
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 351..372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 403..422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="A -> V (in Ref. 1; AAA35315)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="H -> D (in Ref. 1; AAA35315)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="A -> G (in Ref. 1; AAA35315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73194 MW; 822CEED9B8414D73 CRC64;
MTVLAPLRRL HTRAAFSSYG REIALQKRFL NLNSCSAVRR YGTGFSNNLR IKKLKNAFGV
VRANSTKSTS TVTTASPIKY DSSFVGKTGG EIFHDMMLKH NVKHVFGYPG GAILPVFDAI
YRSPHFEFIL PRHEQAAGHA AQAYSRVTKK PGVVLVTSGP GATNVITPIA DALADGTPLV
VFSGQVATSA IGSDAFQEAD MVGISRSCTK WNVMVKDVAD LPRRIDEAFE IATSGRPGPV
LVDLPKDVTA SVLKEPIPIL SSVPSMNRRM KEVLEEGSKN VTAKIDRVAN LLKLAKKPVI
FCGHGVLANP ECPTLLRKFS ERLQIPVTTS LLGLGAVDER SDLSLHMLGM HGSGYANMAM
QEADLILALG VRFDDRVTGN VSLFAPQARL AAAEERGGII HFDISPKNIG KVVQPTEAIE
GDVYESLKLL DSATKNIKIP SRFDWLSQIQ TWKERFPFTF TRSAPGELVK PQEVIQELDK
QTSDIKDKVT ITTGVGAHQM WAATFYRWTK PSSLVTSGGL GTMGFGLPAA IGASVAAPKD
IVIDIDGDAS FSMTGMELAT VRQFDIPVKI LILNNEEQGM VTQWQNLFYE KRYSHTHQKN
PNFVKLADAM GIKALRVEKR EDLAKKMKEF LSTKGPVLME VLVAQKEHVY PFVPGGKALH
QFILHESLS
