ID A0A1A9ETX5_9GAMM Unreviewed; 573 AA.
AC A0A1A9ETX5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=A8C75_00645 {ECO:0000313|EMBL:ANG61108.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG61108.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG61108.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG61108.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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; CP015839; ANG61108.1; -; Genomic_DNA.
DR RefSeq; WP_067376650.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9ETX5; -.
DR STRING; 1821621.A8C75_00645; -.
DR KEGG; mars:A8C75_00645; -.
DR OrthoDB; 9785953at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000078070; 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; 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 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:UP000078070};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 573 AA; 63422 MW; 1F0556BFE0B107FC CRC64;
MELLSGAEMV VRALHDEGVK YIYGYPGGAL LHVYDALFRQ EDVQHILVRH EQAATHMADA
YARATGKAGV ALVTSGPGAT NAVTGIATAY MDSIPMVVIT GQVMSHLIGE DAFQETDMMG
ISRPIVKHSF SVSRAEDIPA IIKKAFHIAQ TGRPGPVVVD IPKDMTSPTE RYEYEHPKTV
KLRSYSPVTR GHSGQIKKAT DLLLAAKRPV LYTGGGVIMG NASAELLQLA RMLNYPVTNT
LMGLGGFPGT DRQFIGMLGM HGSYEANMTM HHSDLILAVG ARFDDRVTNG LDKFCPTAKI
IHIDIDPASI SKTVKADIPI VGPAQAVLAE MIELVAASKK QPDAAALKTW WEQIDEWRTR
HGGRYRTDDS DKMKPQQVIE MLSKVTNGDA YVCSDVGQHQ MFAAQYYKFN KPNRWINSGG
LGTMGFGLPA AMGVQMNFPD ADVACVTGEG SIQMNIQELS TCKQYDLPVK IINLNNQSLG
MVRQWQDMNY ESRHSHSYMK SLPDFVKLAE AYGHVGMKVE KYSDLEAAMR EAFAMKDRLV
FMDIYVDQFE HVYPMQVPRG SMRDMWLTKT ERT
//
