ID A0ZA79_NODSP Unreviewed; 632 AA.
AC A0ZA79;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN ORFNames=NSP_1450 {ECO:0000313|EMBL:AHJ26501.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ26501.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ26501.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ26501.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
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:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; CP007203; AHJ26501.1; -; Genomic_DNA.
DR RefSeq; WP_006194312.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZA79; -.
DR STRING; 313624.NSP_1450; -.
DR PATRIC; fig|313624.11.peg.142; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_3; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000019325; Chromosome.
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:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR026870; Zinc_ribbon_dom.
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 Pfam; PF13240; zinc_ribbon_2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:AHJ26501.1}.
FT DOMAIN 34..151
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 228..362
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 425..573
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 611..632
FT /note="Zinc-ribbon"
FT /evidence="ECO:0000259|Pfam:PF13240"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68707 MW; 0AD0B6D44E784454 CRC64;
MTVRLPSLTN PPQTENHNQS GVTQSPVVAP KRETGGFALL DSLVRHEVEY IFGYPGGAIL
PIYDDLYKVE STGAIKHILV RHEQGAAHAA DGYARATGKV GVCFGTSGPG ATNLVTGIAT
AYMDSIPMIV VTGQVPRASI GTDAFQETDI YGITLPIVKH SYVVRDPKDM ARIVAEAFHI
ASTGRPGPVL IDVPKDVALE ECDYVPVARG TVKLPGYRPT VKGNPRQINA AIKLIRNSHR
PLLYVGGGAI ASNAHAEIKE LAELFNIPVT TTLMGIGAFD EHHPLSVGML GMHGTAYANF
AVTDCDLLIC VGARFDDRVT GKLDEFASHA KVIHIDIDPA EVGKNRVPEV PIVGDVRQVL
VDLLRRCQET GIKNIPHKNQ EWLHLINRWR QDYPLEVPQH PDSISPQEVI VEVGRQAPHA
FYTTDVGQHQ MWAAQFLKNG PRRWISSAGL GTMGFGVPAA MGAKVAFPDE EVICISGDAS
FQMCLQELGT LAQYGINVKT VILNNGWQGM VRQWQQAFYG ERYSCSNMEV GMPDIEHLTK
AYGIKGMVVQ TREELQGAIA EMLAHNGPVV MDVRVTKDEN CYPMVAPGKS NAQMIGLPIQ
QPKVVVEPVS CNHCGTTNPP THNFCSECGT KL
//
