ID A0A0F8UKE2_9EURO Unreviewed; 326 AA.
AC A0A0F8UKE2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Mitochondrial acetolactate synthase small subunit {ECO:0000313|EMBL:KKK20023.1};
GN ORFNames=ARAM_004061 {ECO:0000313|EMBL:KKK20023.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK20023.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK20023.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK20023.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:KKK20023.1}.
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DR EMBL; JZBS01002132; KKK20023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8UKE2; -.
DR STRING; 308745.A0A0F8UKE2; -.
DR OrthoDB; 1361624at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000034291; 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:UP000034291}.
FT DOMAIN 94..171
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 207..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 35697 MW; 65CC098A2FF6B54D CRC64;
MAFRRPLMLS STASMPLLSA SGRVTRLTAS LPRFTPSRAT SSSTSALAYK ALHRRSPLTL
PVADISPQWD APTAVSSILY ETPVRPTNPP KRHILNCLVQ NEPGVLSRVS GILAARGFNI
DSLVVCNTEV EDLSRMTIVL QGQDGVVEQA RRQLDDLVPV WAVLDYTDSA LVQRELLLAK
VSILGPEFFE ELLQHHREIT TPADVVEGQK GKKGGAEPAK TTEFHPRNLP SSQALRHKHE
HLDAITRLTH QFGGKVLDIS TNNCIVEVSA KPNRIDSFMK LIAPFGILES TRTGLMALPR
SPLFEPREEI EKDAADVVDA STLPPG
//
