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Database: UniProt
Entry: H6SSM6_PARPM
LinkDB: H6SSM6_PARPM
Original site: H6SSM6_PARPM 
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
//
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