ID A0A1S2P435_9ACTN Unreviewed; 564 AA.
AC A0A1S2P435;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BIV24_22980 {ECO:0000313|EMBL:OIJ88417.1};
OS Streptomyces colonosanans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ88417.1, ECO:0000313|Proteomes:UP000179935};
RN [1] {ECO:0000313|EMBL:OIJ88417.1, ECO:0000313|Proteomes:UP000179935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ88417.1,
RC ECO:0000313|Proteomes:UP000179935};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 93.";
RL Submitted (OCT-2016) 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:OIJ88417.1}.
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DR EMBL; MLYP01000058; OIJ88417.1; -; Genomic_DNA.
DR RefSeq; WP_071368280.1; NZ_MLYP01000058.1.
DR AlphaFoldDB; A0A1S2P435; -.
DR STRING; 1428652.BIV24_22980; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000179935; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000179935};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 59437 MW; C3B474704336527E CRC64;
MTLSQPRATV TADATVRRHG GHVVAQVLEE HGITEIFGQD SPELLFAVLD HSRFRVTTMR
DERSAGFAAD AVARLTGRPA VATGIHGPGA LNLTTALFEA REASSPVIAL ISGIETTTKG
TGAFQEADHV AAARPLVKWA ARVERPDRVR STLERAIRVA TSGRPGPVLV ELPNDVLTVE
QPAEEYAAPP VTLTATPADA RVVTELSGAT APVLLLGSGA LQTACEDLVA LAERLDAAVC
VTHTGRGAFP ERHHLFAGVC GFMSDREDGS GAVANAMLAA ADVVLALGTG MDGVTTDGGR
LPAARATLVR VDVDAGTLAL DTRAAHTVLA DITSYVPALT AALPGASVRG TREALARKWA
VVRDAQRDRI AAGSPVIRPS FLMGALQQAL RPDDLLVCDA AYSSVWALSY LTQGEHFHRI
TYGRAAGTLG FGFPGAIGAS VAYPDRRVVA LVGDGGFGFT WGELETAARI GANITCVVLN
NSMFAYQVLW HELNGTHARN LEFVDVHHDV LASAVGGHGV RVESRDALLP VLRTSLDHDG
LSVVDVVLDP HELPPFRKER HVGH
//
