ID A0A1I1P691_9BURK Unreviewed; 559 AA.
AC A0A1I1P691;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SFD05196.1};
GN ORFNames=SAMN05216321_110144 {ECO:0000313|EMBL:SFD05196.1};
OS Cupriavidus sp. OV038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1855313 {ECO:0000313|EMBL:SFD05196.1, ECO:0000313|Proteomes:UP000199583};
RN [1] {ECO:0000313|EMBL:SFD05196.1, ECO:0000313|Proteomes:UP000199583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV038 {ECO:0000313|EMBL:SFD05196.1,
RC ECO:0000313|Proteomes:UP000199583};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOKX01000010; SFD05196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1P691; -.
DR Proteomes; UP000199583; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 559 AA; 59702 MW; B5E2AAC7132433D7 CRC64;
MTAQTPSFQA RTGGRVLVDQ LRLHGTERIF CVPGESFLDV LDALHDQPAI DLVVTKHEGA
AANMAEADGK LTGRPGICFV TRGPGATHAS IGVHIAQQDS TPMILFVGQI SRAHKGREAF
QEVDYAAVFG TMAKWAAEID DPARIPEMVA RAFQVATSGR PGPVVLALPE DVLDDLVDCA
DAEPYRTVAA APRAEDARAL AAALAEARQP LVIAGGAGWT DAAVRDFAAF VKAWNLPVAC
AFRRQDVIDN RDPHYIGHLS LGVSPKLAER VRTADLIVAV GTRLGDIATD GYTLLEVPRP
KQKLVHIHAD SGELGRVYQS ALPIHSGVVP AAAMLAALPA PASIGWKDWT SGARAEHEAF
VTPPKPHAEL TGVDMAAAMS HLNAVLPEDA ILSNGAGNYT VWLHRFYAYK RPRTELAPTC
GAMGYGLPAA IAAKLRAPEK TVVCLAGDGC FLMYPQEIAT AAAHGANLIV ILVNNRMYGT
IRMHQEKRYP GRQSGTTIAN PDFVAMARAC GAWAERVEKT EDFAAAFERA RNAGQPAVLE
LMTDPLQITP AMRVTELPA
//
