ID B3T1Z8_9ZZZZ Unreviewed; 590 AA.
AC B3T1Z8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=ALOHA_HF4000133G03ctg1g12 {ECO:0000313|EMBL:ABZ06607.1};
OS uncultured marine microorganism HF4000_133G03.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=455521 {ECO:0000313|EMBL:ABZ06607.1};
RN [1] {ECO:0000313|EMBL:ABZ06607.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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 TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; EU016580; ABZ06607.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T1Z8; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; cd02015; TPP_AHAS; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 65171 MW; 1A9F6E9A8B4D0889 CRC64;
MGKLMTGAEM VFKALEDQGV RHIFGYPGGA VLPIYDELKN HKKIKHILVR HEQGAGHAAE
GYARSSGKPG VILVTSGPGA TNTVTALTDA YMDSVPLVCI TGQVPTHLIG TDAFQECDTT
GITRPCTKHN WLVKDIEKLS SILHKAFEVA TSGRPGPVLV DIPKDIQFAK GKYVRPKKSK
KNSGRADVKF NGKNKDIEAA VELFKKSSKP ILYTGGGVIN SGPKATQLLR ELVSLTGFPI
TSTLQGLGAF PGYDQQFLGM LGMHGTFEAN NAMHDCDLMI NIGARFDDRI TGKIDEFSPK
SKKIHIDIDP SSINKNIAVD LALVGDVKII LEKLILALKK KNPNFINSNK QRIAAWWNQI
EKWRKKNSLS FVNSKEIIKP QFAVQRLYEL TKAQDVFITT EVGQHQMWAA QHYKLDKPNR
WMTSGGLGTM GYGLPAAVGV QVAHPGKLVI DIAGEASVLM TMQEMSTAVQ YKLPIKIFIL
NNEYMGMVRQ WQEILHDKNY SESYTAALPD FVKLAEAYGC VGIRANKPEE LDEKIKHMIT
VNKPVIFDCV VDKTENCYPM IPSGKPHNQM LLGSKDKAEE EISEEGKILV
//
