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Database: UniProt
Entry: A0A0N0SM99_9ACTN
LinkDB: A0A0N0SM99_9ACTN
Original site: A0A0N0SM99_9ACTN 
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}.
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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
//
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