ID U1FK07_TRESO Unreviewed; 582 AA.
AC U1FK07;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=ilvB_1 {ECO:0000313|EMBL:ERF59681.1};
GN ORFNames=HMPREF1325_1099 {ECO:0000313|EMBL:ERF59681.1};
OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF59681.1, ECO:0000313|Proteomes:UP000016412};
RN [1] {ECO:0000313|EMBL:ERF59681.1, ECO:0000313|Proteomes:UP000016412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF59681.1,
RC ECO:0000313|Proteomes:UP000016412};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERF59681.1}.
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DR EMBL; AUZJ01000064; ERF59681.1; -; Genomic_DNA.
DR AlphaFoldDB; U1FK07; -.
DR STRING; 1125725.HMPREF1325_1099; -.
DR PATRIC; fig|1125725.3.peg.2399; -.
DR eggNOG; COG0028; Bacteria.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000016412; Unassembled WGS sequence.
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:SF171; ACETOLACTATE SYNTHASE ISOZYME 1 LARGE SUBUNIT; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:ERF59681.1}.
FT DOMAIN 6..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 62666 MW; BD124C51FF2F2E57 CRC64;
MFMKKTGSEI IVKLLEMEGI TVVSGIPGGS VLPLYDALAK SSIRHVLARH EQGAGFIAQG
MARSTGKVAV CFATSGPGAM NLLTAVADAR SDSVPIVAIT GQVNTSLIGT DAFQEADTFG
LSFPIAKHSI MVKSPEELLR AIPQAFAIAA NGRPGPVLVD VPRDVQLSSC EFDSWPDIAS
VTIHDIRFHT PPSEYASSMD RITDALAEAK RPVLFCGGGC NSEGAAKELQ KFLKTYRLPV
VTSLMGIGCV PFSFEMFAGM VGMHGSYAAN VAMHDADLVI AAGVRFDDRA TGVVSKFCPK
ARVVHIDVDA AEVDKIIDAD ISVVADVGSV FPILVQLASR KQELFASNWQ NAEARAVWLE
KIIKLKTETF SPLCGAAKKS SYGNPRELIA SIPLFAEKAG MRRDKLIVTT DVGQHQMWTA
QYYPVEKPRT FLTSGSLGTM GFGLPAAIGA SLAHPECRVV CVSGDGSILM NIQELATLSE
QNLAVTVIVF DNGTLGMVYQ QQKYLFGGTY AASEFSRRVD FVEIARGFGI DAVDAAEDEK
WYEKAFSPKR ERKPFLVRIE IDSAEDVLPF VLPGKANIDA LR
//
