ID A0A0P9GVT0_9BACL Unreviewed; 547 AA.
AC A0A0P9GVT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN477_02480 {ECO:0000313|EMBL:KPV45388.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV45388.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV45388.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV45388.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KPV45388.1}.
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DR EMBL; LJCO01000011; KPV45388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9GVT0; -.
DR STRING; 471514.AN477_02480; -.
DR PATRIC; fig|471514.4.peg.2836; -.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 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; 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 PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE 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 Reference proteome {ECO:0000313|Proteomes:UP000050482};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 59015 MW; 09030CC579804F80 CRC64;
MTGGQVVTQV LASEGVKHVF CVPGESYLEV LDGLYEHPEI ELISTRHESG AAFMAEAYAK
ASGQVGVCMA TRAVGLSNLS IGLHTARQDS TPLVAIVGHV PQDHQEKEAF QEVPLSEWFR
PVCKWTVEIR DVKRIPELLH RAFYVASTGR KGPVLVVMPQ DVLEAVTEPP VRDALPYHAS
LPQPDLSMVR NVHQELIRAA RPVVIVGGGV TASAATNPLL AVAKRYELPL VSAFRRYDAV
PNEDVYFAGW LGFGPNRGLV EEIGQADLVL TIGTRLSQVT TQDYTLLSPE TKVIVVDVDP
LAGVTAHPPA YVISSDAAAF CEALLAVSED SGDLSTSNRT MRRDRIDRLH RAYLQFSEPR
HIEGDGAVNL EGMMYDFART VPEDTIITSD AGNFFGWLAR YYRFNKPGTY VGPTSGAMGY
GLPAALGVKL AKPSATVVAF AGDGGFMMTM SEMATAALYE IPVVAVVVNN SLYGTIRAHQ
ERKHQGRPVG TSLFNPSFAE VARSFGGFGI RVTTNEEFKA GLAQALSAGR FALVEVLSDP
KILSAGS
//