ID D1PXX4_9BACT Unreviewed; 597 AA.
AC D1PXX4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
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 {ECO:0000313|EMBL:EFA43795.1};
GN ORFNames=HMPREF0645_1809 {ECO:0000313|EMBL:EFA43795.1};
OS Hallella bergensis DSM 17361.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA43795.1, ECO:0000313|Proteomes:UP000003160};
RN [1] {ECO:0000313|EMBL:EFA43795.1, ECO:0000313|Proteomes:UP000003160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA43795.1,
RC ECO:0000313|Proteomes:UP000003160};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2009) 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|ARBA:ARBA00000673,
CC 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:EFA43795.1}.
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DR EMBL; ACKS01000072; EFA43795.1; -; Genomic_DNA.
DR AlphaFoldDB; D1PXX4; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_10; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000003160; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Reference proteome {ECO:0000313|Proteomes:UP000003160};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:EFA43795.1}.
FT DOMAIN 33..153
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 227..361
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 423..570
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65331 MW; 1D1284CB3F36D1C3 CRC64;
MDSKKKEYAT QSDNRLQETE SPWAGIQIGE ECSGAEILMR ALYQENVKTI FGYPGGAIIP
VFDRLYTYTH KREPWFHHVL VRHEQAAAHA AEGYARVSGE VGVALVTSGP GATNTLTGVA
DAMMDSIPIV VIAGQVGIND LGTDAFQEVD LVGMTQPITK WSYQIRHAED VAWAVNRAFY
IARSGRPGPV VLDFAKNAQV SKAKWMPGKT NAVRSYLPYP KIDREAVRAA AELINNASKP
MALVGHGVEI ADAQNELKDF IEKANIPAAR TLLGLSALPT DHALNMGMLG MHGNYAPNVK
QQEADVIIAV GMRFSDRDTG RLNDYAKQAK IVHLDIDPAE INKNVRADVA VVGNCKESLP
AITALLQKAD HGEWIESFAP LYEEEKREVI DGATRPESGP LLMGEVVRAV TNAVGADGVL
VNDVGLNQMI SSRYFNYTKK RSIVTSGGLG TMGFGLPAAI GAAFGTLDRT ICCFMGDGGF
QMSIQELGTI MEQQTPVKMI VMNNNYLGNV RQWQDLMFDH RHSFTRMLNP RYDAIAEGYG
IPYDVAINRE DLKDKIAKML ATDGPYILEC AVMEEENVVP MITPGSAVDE MKLHLDI
//