ILVB_CRYNH
ID ILVB_CRYNH Reviewed; 718 AA.
AC Q6SSJ3; J9VGF8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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; ORFNames=CNAG_00268;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=15133116; DOI=10.1099/mic.0.26928-0;
RA Kingsbury J.M., Yang Z., Ganous T.M., Cox G.M., McCusker J.H.;
RT "Cryptococcus neoformans Ilv2p confers resistance to sulfometuron methyl
RT and is required for survival at 37 degrees C and in vivo.";
RL Microbiology 150:1547-1558(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
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DR EMBL; AY450850; AAR29084.1; -; Genomic_DNA.
DR EMBL; CP003820; AFR92401.1; -; Genomic_DNA.
DR RefSeq; XP_012046625.1; XM_012191235.1.
DR AlphaFoldDB; Q6SSJ3; -.
DR SMR; Q6SSJ3; -.
DR SwissPalm; Q6SSJ3; -.
DR EnsemblFungi; AFR92401; AFR92401; CNAG_00268.
DR GeneID; 23884092; -.
DR VEuPathDB; FungiDB:CNAG_00268; -.
DR HOGENOM; CLU_013748_1_2_1; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PHI-base; PHI:358; -.
DR Proteomes; UP000010091; Chromosome 1.
DR GO; GO:0005948; C:acetolactate synthase complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:EnsemblFungi.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
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_0000035662"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..621
FT /note="Thiamine pyrophosphate binding"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 78497 MW; 4A0B0F1F0BF7BAFD CRC64;
MLTRQARLLR RIPPPNAVLQ SGLQRRHRST DRYSNNIHTS STQNAPAPVY DTPIREKGMT
LEAKERVRAH VRKIQSSAST AAASPAVRPQ PAQHFQAAPQ PMPTNMPRFE SDSQVKNGLD
YSFIGLSGGQ IFQEMMLRHD VKQVFGYPGG AILPVFDAIY NSPHFEFVLP RHEQGAGHMA
EGYARVSGKP GVVLVTSGPG ATNVITPMQD ALSDGVPMVV FCGQVATNLI GSDAFQEADV
VGISRSCTKW NVMVKDIAEL PRRINEAFKI ATTGRPGPVL VDLPKDVTAA ILRTPIPAKS
VQPGHSPYLP SNPLNPSSQP SDPLPGDADL ITEAAQMINK AKRPIIFAGN GVLSSPEGPK
LLKELSDKGR IPVTTTLQGL GAFDERDEKS LHMIGMHGSA YANFAMQEAD VLIALGVRFD
DRVTGKVDTF APAAKAAAAE GRGGIIHFEI QPKNINKIVE AQIPVLGDVV ASLGELVPQI
EAVDRSAWIG RCKATKERYP FTYTPSQEGQ KLKPQEVVQE LDRQAEALGK EKFVISTGVG
QHQMWACQYY RWTEPRSWVS SGGLGTMGFG LPSAIGAKVA APEKYVIDID GDASFSMTAM
ELATASQYDI GVKVLLFNNE FQGMVEQWQD LFYENRYSHT RMTNPDFVKL SESMGAKGLR
CTKLEDLPRM MKEFLEYDGK RPIVLECLVS SEHVYPMIPA GKALHEQLLH PLLRNGSE
