ID A0A024FGU5_9FLAO Unreviewed; 578 AA.
AC A0A024FGU5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=WPG_1874 {ECO:0000313|EMBL:BAO76104.1};
OS Winogradskyella sp. PG-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO76104.1, ECO:0000313|Proteomes:UP000031636};
RN [1] {ECO:0000313|EMBL:BAO76104.1, ECO:0000313|Proteomes:UP000031636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2 {ECO:0000313|EMBL:BAO76104.1,
RC ECO:0000313|Proteomes:UP000031636};
RX PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT Proteorhodopsin-Containing Marine Flavobacterium.";
RL Genome Announc. 2:e00490-14(2014).
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; AP014583; BAO76104.1; -; Genomic_DNA.
DR RefSeq; WP_045471598.1; NZ_AP014583.1.
DR AlphaFoldDB; A0A024FGU5; -.
DR STRING; 754409.WPG_1874; -.
DR KEGG; win:WPG_1874; -.
DR HOGENOM; CLU_013748_1_2_10; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000031636; 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 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000031636};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 22..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 212..346
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..554
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 63386 MW; 5FE45CB14F8B8E72 CRC64;
MKETQTIQNE VEDTKTTERI PGSEAVVRCL LEEGVEVLYG YPGGAIMPVY DELFKYQDKI
HHVLSRHEQG AAHAAQGYAR ISDKVGVAIA TSGPGATNLI TGIADAQIDS TPMVCITGQV
GSHLLGSDAF QETDIVGIST PVTKWNHQIT KASEIPEVFA KAFYIAKSGR PGPVLIDITK
DAQFEEFDFK YEKCKGVRSY KPVPSTEENS LKTAAELINN AKKPLIVWGQ GVILGKAEEE
FKAVIEKAGI PSAWTILGAS AIPTSHPLNV GMVGMHGNYA PNVLTNECDV LIAIGMRFDD
RVTGNLATYA KQAKIVHFEI DPAEVDKNVK TDVAVLGDAK ASLKDLLPLL NANSHNEWHQ
KFKDLYKIEY DKVIKNDLHP TKEGLTMGEV LKEINIQTKG EAAIVSDVGQ HQMIACRYAE
FNKTKSNITS GGLGTMGFAL PAAIGAKMAA PDREVVMIAG DGGYQMNIQE LGTIFQQKVP
VKIVVLNNEF LGMVRQWQQL FFDKRYASTE MVNPDFVAIA KGYHIDAKKV SERKDLKAAI
KEMIDCNDPY FLEVRVEKED NVFPMIPTGA SVSDIRLE
//
