ID A0A0N0SM99_9ACTN Unreviewed; 546 AA.
AC A0A0N0SM99;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KOU72290.1};
GN ORFNames=ADK57_10070 {ECO:0000313|EMBL:KOU72290.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU72290.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOU72290.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDG01000063; KOU72290.1; -; Genomic_DNA.
DR RefSeq; WP_053749035.1; NZ_LGDG01000063.1.
DR AlphaFoldDB; A0A0N0SM99; -.
DR STRING; 1415546.ADK57_10070; -.
DR PATRIC; fig|1415546.3.peg.2199; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000037741; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF169; 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:UP000037741};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 185..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 56861 MW; 78567E204F3642CE CRC64;
MKVAEAVGRA VTAAGVGRVF GVVGSGNFHL TNAMVAAGAR FVAARHEGGA ATMADAYARM
SGRPAALSVH QGPGLTNALT GVTEAAKSRT PLLVLAAEVT EPRSNFHVDQ EALGRAVGAI
TLRVTSAENA VGQTLDAVRL ALHERRTVLL NLPLAVQALD VPDGVLAQAA PPPQRAAVEP
TAADVAALAR ALDRARRPVF VAGRGSRSPG ARDALAALAE RHGALLATSA VARGLFHGNP
WSLDVSGGFA SPLTAELIGA ADTIVGWGCA LNMWTMRHGN LIGSDTTVVQ VDDDASALGA
HRDVHVGVTG DVERTARRVL ETGGAKRQGY RTADVAAGIA ARVRLRDVPY EDTGSRERID
PRTLSIALDD ILPAERVIGV DSGNFMGYPS MYLSVPDENG FCFTQAFQSI GLGLATAIGA
ALAQPDRLPV AALGDGGALM GAAELDTVRR LGLPMVVVVY NDDGYGAEVH HFGPDGHPLD
TVEFPSTDIA DVARGYGFEA VTVRTRADLK AVADWVAGPR SAPVLIDAKV VKDRGSWWLE
EAFRGH
//