ID A0A317WII2_9EURO Unreviewed; 328 AA.
AC A0A317WII2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PWY86183.1};
GN ORFNames=BO70DRAFT_386453 {ECO:0000313|EMBL:PWY86183.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY86183.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY86183.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY86183.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|ARBA:ARBA00006341}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY86183.1}.
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DR EMBL; MSFL01000008; PWY86183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WII2; -.
DR STRING; 1448321.A0A317WII2; -.
DR VEuPathDB; FungiDB:BO70DRAFT_386453; -.
DR OrthoDB; 1361624at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; 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; cd04878; ACT_AHAS; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.70.1150; ACT-like. Chain A, domain 2; 1.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR NCBIfam; TIGR00119; acolac_sm; 1.
DR PANTHER; PTHR31242; ACETOLACTATE SYNTHASE SMALL SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR31242:SF2; ACETOLACTATE SYNTHASE SMALL SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF10369; ALS_ss_C; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT DOMAIN 97..174
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 203..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 328 AA; 35805 MW; 30CDDD475C0DDD6E CRC64;
MAFRRPVMLS SSTASAPFLS VASRTSRLAA TLPRFSNTTI RASSSSTSAL AYKALHRRSP
LPLPVSDASP QWDAPTAVSS ILYETPTTPT NPPKRHILNC LVQNEPGVLS RVSGILAARG
FNIDSLVVCN TEVEDLSRMT IVLQGQDGVV EQARRQLDDL VPVWAVLDYT ESALVQRELL
LAKVSILGPE FFEELLQHHR EITTPGELAD GQKDKPAQGK VAKPEYHPRN LPQSQALRHK
HEHLDAITRL THQFGGKVLD ISTNNCIVEV SAKPSRIDSF MKLIGPFGVL ESTRTGLMAL
PRSPLFEPSE EIEKDAADVV DASTLPPG
//
