ID A4FL93_SACEN Unreviewed; 547 AA.
AC A4FL93;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:CAM04818.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAM04818.1};
GN Name=ilvB4 {ECO:0000313|EMBL:CAM04818.1};
GN OrderedLocusNames=SACE_5632 {ECO:0000313|EMBL:CAM04818.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM04818.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM04818.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AM420293; CAM04818.1; -; Genomic_DNA.
DR RefSeq; WP_011874786.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FL93; -.
DR STRING; 405948.SACE_5632; -.
DR KEGG; sen:SACE_5632; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OMA; GKGAFPW; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000006728; Chromosome.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAM04818.1}.
FT DOMAIN 7..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 547 AA; 56398 MW; 9FE2D0DE6D3273B6 CRC64;
MTEARIGGDL VVETLRALGA RTVFGLPGQH ALGLFEALRR APDLRLVSSR VENNLAFAAD
GHARAKLAEG GPVPVTPMIV STGPGALLTL ASLQESRASS VPVLGISSQV PAAGLGGGRR
GYLHELPDQQ ASFRDVVKSV HVARTASQIP GALRAAWESA ATAPYGPTWV EIPQDVLLGP
AGLPPITGVS ASPPPLAPQP ELIAEAADLL AAAENPVVLA GGGVARAGAA GPLRELAEAL
RAPVLSTFGG KGVFGWDHPL SGQSWMEDWH STEFLAAADV LLVLGSGLGE LSSNYHRFAP
RGRIVQVEAD AGKLESNHPA LGIHADAGLA LSALLERLPR RRADGRAERA VAELLAKVHD
RLAGQDLERE QHVLADVRAA LPEGTPTFWD MTILGYWAWS AWNADGAPMH SAQGAGGLGF
GFPAALGAAA ATGGPVLAVS GDGGAMYGIA ELATAVQHGL DVTWLIVDDG GYGILREYLT
GTFGQTTSTE LSRPDFVALA GAFGVPAVRS GLGTLRADLA HALQTPGPSV VVLPALLRMF
APTHLPV
//