ID A0A0B5EYH0_STRA4 Unreviewed; 583 AA.
AC A0A0B5EYH0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AJE83152.1};
GN ORFNames=SLNWT_2776 {ECO:0000313|EMBL:AJE83152.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE83152.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE83152.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) 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; CP010519; AJE83152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5EYH0; -.
DR KEGG; sals:SLNWT_2776; -.
DR Proteomes; UP000031523; Chromosome.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000031523};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 583 AA; 59776 MW; 8C2E6866CD052274 CRC64;
MRKGPPRVAD YVISSLAAQG TDHVFGVGGA NIEDLYDAAH LSGGRVTAVV AKHEFSAATM
AEGYHRTSGR LGVAMATSGA GAMNLVPGLA EAYAARIPTL ALVGQPPRSL EGRGAFQDSS
GLAGTFDAVD LFTPLSRFCA RVDDPADIGK LLAEAVAATR GPCRGPAVLL LPKDVQQATV
EQLPPLEQLL AEPDGPAAAA GNRAAAARML TGAAASGAEV LVIAGDGVGR GGARAELAEL
ARLLGASVAV TPEAKDAFDN GDPRYAGVAG TVGHPTVRRR LERASLCVLV GTRLPVMARA
GLEAALDATP LVCFDPEPPY TGPPRADAPV VHVDGDLRTE LRAAAEALAA LPARGAGTPP
PGGPEYLVAP RPDSPGVRLD DAVRAIESAL PDGATVVSDA GNASSAVIHH LSVPPEGQFV
LALGMGGMGH SFGAGIGAAF GTGRRAYVLS GDGGFYAHGM ELHTAVEHQL PITFVVFNNN
AHAMCVTREQ LLYEADYSYN TFRPADLAAG AGAMFPSLRT ATATTAEELR RALLAANERT
GPALVCVEAD PDELPPFLPF LKLIDDRATP SGAHDDDRVT PVG
//
