ILVB_CRYNJ
ID ILVB_CRYNJ Reviewed; 718 AA.
AC Q5KPJ5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=ILV2; OrderedLocusNames=CNA02570;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017341; AAW40825.1; -; Genomic_DNA.
DR RefSeq; XP_566644.1; XM_566644.1.
DR AlphaFoldDB; Q5KPJ5; -.
DR SMR; Q5KPJ5; -.
DR STRING; 5207.AAW40825; -.
DR PaxDb; Q5KPJ5; -.
DR PRIDE; Q5KPJ5; -.
DR EnsemblFungi; AAW40825; AAW40825; CNA02570.
DR GeneID; 3253594; -.
DR KEGG; cne:CNA02570; -.
DR VEuPathDB; FungiDB:CNA02570; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_1_2_1; -.
DR InParanoid; Q5KPJ5; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..718
FT /note="Acetolactate synthase, mitochondrial"
FT /id="PRO_0000035661"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..621
FT /note="Thiamine pyrophosphate binding"
FT BINDING 173
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 397..418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 449..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 718 AA; 78381 MW; A7729BFA0A4F8943 CRC64;
MLTRQSRLLR RIPPPNAVLQ SGLQRRHRST DRYSNNIHTS STQNAPAPVY DAPIREKGMT
IEAKERVRAH ARKIQSSAST AAASPAVRPQ PAQHFQAAPQ PMPANTPRFE SDGQVKNGLD
YSFIGLSGGQ IFQEMMLRHD VKQVFGYPGG AILPVFDAIY NSPHFDFVLP RHEQGAGHMA
EGYARVSGKP GVVLVTSGPG ATNVITPMQD ALSDGVPMVV FCGQVATNLI GSDAFQEADV
VGISRSCTKW NVMVKDIAEL PRRINEAFKI ATTGRPGPVL VDLPKDVTAA ILRTPIPAKS
AQPGHSPYLP SNPLNPSSQP SDPLPGDADL ITEAAQMINK AKRPIIFAGN GVLSSPEGPK
LLKELSDKGR IPVTTTLQGL GAFDERDEKS LHMIGMHGSA YANFAMQEAD VLIALGVRFD
DRVTGKVDTF APAAKAAAAE GRGGIIHFEI QPKNINKIVE AQIPVLGDVV ASLAELVPQI
EAVDRSAWIG RCKATKERYP FTYTPSQEGQ KLKPQEVVQE LDRQAEALGK EKFIISTGVG
QHQMWACQYY RWTEPRSWVS SGGLGTMGFG LPSAIGAKVA APEKYVIDID GDASFSMTAM
ELATASQYDI GVKVLLFNNE FQGMVEQWQD LFYENRYSHT RMTNPDFVKL SESMGTKGLR
CTKLEDLPRM MKEFLEYDGK RPIVLECLVS SEHVYPMIPA GKALHEQLLH PLLRNGSE
