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Database: UniProt
Entry: A0A0A7EBR6_9GAMM
LinkDB: A0A0A7EBR6_9GAMM
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ID   A0A0A7EBR6_9GAMM        Unreviewed;       549 AA.
AC   A0A0A7EBR6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=OM33_01730 {ECO:0000313|EMBL:AIY64014.1};
OS   Pseudoalteromonas piratica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY64014.1, ECO:0000313|Proteomes:UP000030341};
RN   [1] {ECO:0000313|EMBL:AIY64014.1, ECO:0000313|Proteomes:UP000030341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OCN003 {ECO:0000313|EMBL:AIY64014.1,
RC   ECO:0000313|Proteomes:UP000030341};
RA   Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA   Belcaid M.;
RT   "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT   from Kaneohe Bay, Oahu, Hawaii.";
RL   Submitted (NOV-2014) 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         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; CP009888; AIY64014.1; -; Genomic_DNA.
DR   RefSeq; WP_038637931.1; NZ_CP009888.1.
DR   AlphaFoldDB; A0A0A7EBR6; -.
DR   STRING; 1348114.OM33_01730; -.
DR   KEGG; pseo:OM33_01730; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_6; -.
DR   OrthoDB; 9785953at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000030341; Chromosome 1.
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:SF142; ACETOLACTATE SYNTHASE; 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:UP000030341};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:AIY64014.1}.
FT   DOMAIN          1..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          374..521
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   549 AA;  59181 MW;  3E77343E1294662D CRC64;
     MTGAELTIDL LAKHGVKEVF GYPGGAIMPI YDALYGSPVK HYLTRHEQGA GFAAVGYARS
     TGKLGVCFAT SGPGATNLIT ALADAMMDSV PLLAITGQVP TAAIGSDAFQ EVDVLGMSLS
     CTKHSYMVER AEDLAEILQE AMHLAQSGRP GPVLVDIPKD IQMGAVTYQP WLAADDYKPE
     FKQSELAKAN ELLSDAKQPL AYIGGGVQMA DAQDELMQFL KSTNMPAVST LKALGSVTPD
     YPYDLGMLGM HGGQAANLAV QECDLLVCIG ARFDDRVTGN LAKFASKAKV IHLDVDAAEV
     GKRKPVDASL VADLKDSLPH LATHKTHAEW LAHISNMQQQ HAWRYDYPGE KVYAPYLLNR
     LSQLMPSNGV VCCDVGQHQM WVAQHMKFSH PSNHLSSGGA GTMGFGLPAA IGAQIARPND
     FVLTVSGDGS IMMNIQELAT IRRNNLPVKL LILDNQRLGM VRQWQQLFFD GRYSETNLSD
     NPDFVQLAAV FGIPGETITH ADQVDAAIDK LVASEGPYIL HACIDDKENV WPLVPPGAAN
     DQMLTEVTK
//
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