ID Q0K9J3_CUPNH Unreviewed; 577 AA.
AC Q0K9J3;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:CAJ93328.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAJ93328.1};
GN OrderedLocusNames=H16_A2231 {ECO:0000313|EMBL:CAJ93328.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93328.1, ECO:0000313|Proteomes:UP000008210};
RN [1] {ECO:0000313|EMBL:CAJ93328.1, ECO:0000313|Proteomes:UP000008210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC 337 {ECO:0000313|Proteomes:UP000008210};
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AM260479; CAJ93328.1; -; Genomic_DNA.
DR RefSeq; WP_011615565.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K9J3; -.
DR STRING; 381666.H16_A2231; -.
DR GeneID; 57644360; -.
DR KEGG; reh:H16_A2231; -.
DR PATRIC; fig|381666.6.peg.2635; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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:UP000008210};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAJ93328.1}.
FT DOMAIN 20..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..551
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 577 AA; 61904 MW; D8710FD6DC6BC7B0 CRC64;
MTPANTTQPD DPEHGTPLPG GHILVDALLA HGAELAFGVP GESYLAVLDG FHRRRDQLRF
IICRQEGGAA VMAEAYGKLT GRPGLAFCTR GPGATNASIG VHTAFQDSTP MILFIGQVGT
DFMDREAFQE IDYRRMFGQM AKWVAQIDRV ERIPEYIARA YQTATSGRPG PVVLALPEDM
LAQTAVVPQL QAYQRVMSWP GEADLARLAE MLDAAERPFV LAGGSGWTPQ ACADLQAFAE
RFALPVGCAF RGQDLFDNCH PNYAGDVGIG INPALAERVR NADLVLAIGP RLGEMTTGGY
ALIAAPRPAQ KLIHVHAGAE ELGSVYQADL MVQASMPAIA ARLAGLQPTA EPRWQAWTEA
AHADYERYLQ PPPFTGQGVD MAEVIRTLDQ LLPADAVVTN GAGNYAGWLH RYFHYRPFTS
GGRGQLAPTS GAMGYGVPAA VGAKIAFPQR TVVALAGDGC FLMNGQELAT SMQYQAPVIF
IVVNNGMYGT IRMHQEREYP THVSGTELHN PDFAALARAY GARGATVTTT EAFAPALREA
LAAPVSTLIE IQVDPDVITP RTTLSAIRAQ ALASQQQ
//
