ID A4U0T3_9PROT Unreviewed; 170 AA.
AC A4U0T3;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Acetolactate synthase small subunit {ECO:0000256|RuleBase:RU368092};
DE Short=AHAS {ECO:0000256|RuleBase:RU368092};
DE Short=ALS {ECO:0000256|RuleBase:RU368092};
DE EC=2.2.1.6 {ECO:0000256|RuleBase:RU368092};
DE AltName: Full=Acetohydroxy-acid synthase small subunit {ECO:0000256|RuleBase:RU368092};
GN Name=ilvH {ECO:0000313|EMBL:CAM76490.1};
GN ORFNames=MGR_3217 {ECO:0000313|EMBL:CAM76490.1};
OS Magnetospirillum gryphiswaldense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM76490.1};
RN [1] {ECO:0000313|EMBL:CAM76490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM76490.1};
RX PubMed=17449609; DOI=10.1128/JB.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
CC -!- FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into
CC acetolactate in the first common step of the biosynthetic pathway of
CC the branched-amino acids such as leucine, isoleucine, and valine.
CC {ECO:0000256|RuleBase:RU368092}.
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 ECO:0000256|RuleBase:RU368092};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU368092}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU368092}.
CC -!- SUBUNIT: Dimer of large and small chains.
CC {ECO:0000256|ARBA:ARBA00011744, ECO:0000256|RuleBase:RU368092}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|ARBA:ARBA00006341, ECO:0000256|RuleBase:RU368092}.
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DR EMBL; CU459003; CAM76490.1; -; Genomic_DNA.
DR AlphaFoldDB; A4U0T3; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
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 1, CHLOROPLASTIC; 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 ECO:0000256|RuleBase:RU368092};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU368092};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:CAM76490.1}.
FT DOMAIN 11..89
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 170 AA; 18490 MW; A51AC08F4CB88E9A CRC64;
MSKEQEIQRH TIAVLVANES GVLARVIGLF SGRGYNIESL TVAEVDTKEA LSRITIVTSG
TQMIVEQIKN QLRRLVPIYK VADLTTDGPH VSRELALVKV SSTGEKRVES LRIADIFRAN
VIDSTNESFV FEVVGATEKV DAFIKLMEPL GLIDVSRTGV AAIARGANPL
//
