ID   ILVB_NEOYE              Reviewed;         590 AA.
AC   Q1XDF6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Acetolactate synthase large subunit;
DE            Short=AHAS;
DE            EC=2.2.1.6;
DE   AltName: Full=Acetohydroxy-acid synthase large subunit;
DE            Short=ALS;
GN   Name=ilvB;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4.
CC   -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AP006715; BAE92455.1; -; Genomic_DNA.
DR   RefSeq; YP_537012.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDF6; -.
DR   SMR; Q1XDF6; -.
DR   PRIDE; Q1XDF6; -.
DR   GeneID; 3978889; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; FAD; Flavoprotein; Magnesium; Metal-binding; Plastid;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..590
FT                   /note="Acetolactate synthase large subunit"
FT                   /id="PRO_0000277306"
FT   REGION          405..484
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         61
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         314..333
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  64684 MW;  A2688F3D9B575511 CRC64;
     MPLKQRVSSE KTGAFALLDS IVRHGVKHIF GYPGGAILPI YDELYAWEEA SLIKHILVRH
     EQGAAHAADS YSRSTGEVGV CFATSGPGAT NLVSGIATAH IDSVPILAIT GQVGRAFIGT
     DAFQEVDIFG ITLPIVKHSY VVRDPRDMSR IVAEAFFICK HGRPGPVLID VPKDVGLEKF
     NYFSVEPGKV NIPGCRPITS LKSRQILMAA KMIQQSSQPL LYIGGGAIIS DSHQIIKELV
     DFYKIPVTTT LMGKGIFNED SDYCLGMLGM HGTAYANFAV SECDLLIALG ARFDDRVTGK
     LDEFACNAQV IHVDIDPAEV GKNRIPQVAI VGDVAEVVSE ILNLLKTSFP PYPEQIISWQ
     ERINRWRQQY PLLVPRKSTS ISPQVILVAT NKLAQNAYFT TDVGQHQMWS AQFLKVKAKH
     WLSSAGLGTM GYGLPAAIGA QVAHPNDVVI CISGDSSFQM NMQELGTIAQ YQLPVKIIII
     NNRWQGMVRQ WQQAFYGERY SHSRMTEGAP DFQKLAEAFG IKAFTINNRQ NMQSALQVAI
     DYPGPVLLDC QVTENENCYP MVAPGKSNAQ MIGIAKPQRG TASNYINNSV