ID H6SSM6_PARPM Unreviewed; 213 AA.
AC H6SSM6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=RSPPHO_01279 {ECO:0000313|EMBL:CCG07905.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07905.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG07905.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000673};
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 -!- SUBUNIT: Dimer of large and small chains.
CC {ECO:0000256|ARBA:ARBA00011744}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|ARBA:ARBA00006341}.
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DR EMBL; HE663493; CCG07905.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SSM6; -.
DR STRING; 1150469.RSPPHO_01279; -.
DR KEGG; rpm:RSPPHO_01279; -.
DR PATRIC; fig|1150469.3.peg.1441; -.
DR eggNOG; COG0440; Bacteria.
DR HOGENOM; CLU_055003_1_2_5; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000033220; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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; PTHR30239; ACETOLACTATE SYNTHASE SMALL SUBUNIT; 1.
DR PANTHER; PTHR30239:SF0; ACETOLACTATE SYNTHASE SMALL SUBUNIT 2, CHLOROPLASTIC; 1.
DR Pfam; PF13710; ACT_5; 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:UP000033220};
KW Transferase {ECO:0000313|EMBL:CCG07905.1}.
FT DOMAIN 54..129
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 22902 MW; 003B73F2AD74E8E6 CRC64;
MPSSFDPQRR MPRSGVRRPR AIPAARPRGG APRGGNRPVP ILSQASDQDI ACHTISVLVD
NEAGVLARVI GLFSGRGYNI ESLTVAEVNA QEHLSRITLV TSGTPMIIEQ IKAQLGRLVP
VHKVSDLTVE GPHVSRELAL VKVAGTGEKR VESLRIADIF RARVVDSTNE SFVFEIVGKT
EKINAFIALM EPLGLTDVTR TGVAAIARGC DPI
//