ID A0A1R1XML3_9FUNG Unreviewed; 304 AA.
AC A0A1R1XML3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetolactate synthase small subunit, mitochondrial {ECO:0000313|EMBL:OMJ15839.1};
GN ORFNames=AYI70_g11270 {ECO:0000313|EMBL:OMJ08866.1}, AYI70_g6993
GN {ECO:0000313|EMBL:OMJ15839.1}, AYI70_g9187
GN {ECO:0000313|EMBL:OMJ12334.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ15839.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ15839.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ15839.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OMJ15839.1}.
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DR EMBL; LSSN01005660; OMJ08866.1; -; Genomic_DNA.
DR EMBL; LSSN01004018; OMJ12334.1; -; Genomic_DNA.
DR EMBL; LSSN01002538; OMJ15839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1XML3; -.
DR STRING; 133412.A0A1R1XML3; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000187283; 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:UP000187283}.
FT DOMAIN 93..167
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 25..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 32792 MW; D003726C75CE9991 CRC64;
MFPARLLSKR AFSLNPSILV SRSVSSSSAN NSNSNVPNVN TSSTTGLEYK GKSSQGKIQP
IPGVLDTLTV EQAVSNIIKS TPLAPRVAEE RYLIDCLAQD EPGVLSNVTG IMAARGFSID
TLVASKTEVP GLSRMTIGLK GPRKSMEQAK KQLESLVPVW AVLDYSHTKI VERETLLVKV
SLDGLKNFRE TLSNAEPSQQ QTHPHASKFT SAMDRLSAIK NLAGLFRASV VDVGPNSIIV
EMSAKSERID AFLKLVRPFG ILEAVRSGVM VMARSIQESR QFGSNSTAED APQVVEDLSN
LPPS
//
