ID A0A1H0Q6M2_9ACTN Unreviewed; 557 AA.
AC A0A1H0Q6M2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SDP12685.1};
GN ORFNames=SAMN05660199_03225 {ECO:0000313|EMBL:SDP12685.1};
OS Klenkia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=1052260 {ECO:0000313|EMBL:SDP12685.1, ECO:0000313|Proteomes:UP000199088};
RN [1] {ECO:0000313|EMBL:SDP12685.1, ECO:0000313|Proteomes:UP000199088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45843 {ECO:0000313|EMBL:SDP12685.1,
RC ECO:0000313|Proteomes:UP000199088};
RA de Groot N.N.;
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}.
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DR EMBL; FNIR01000010; SDP12685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Q6M2; -.
DR STRING; 1052260.SAMN05660199_03225; -.
DR Proteomes; UP000199088; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 557 AA; 58611 MW; 3EA8204EFE99F57F CRC64;
MPEQHPPRTG SDLVVECLHT EGVDLVAGVP GTTVMDLIDS LARQSDIRFV HTRHEQVAGF
LADGVSRAGG LGVALVSRGP GAANAAIAVH NAYDESVPFL LLVGQVPGSI TERRSFEEMD
VVATFTPMSK WAVEVHRADR IPELLQRAIR TAVTGRPGPV VVSLPLDVLQ AEVPPDVVPA
RRVRTFPPGP APDAVAAAVR VLGEAERPAL LVGGGGAGRS AELTRLADRL GAPLVTTWLR
QSTVSHEDPA FLGALGYGAH DVTEEVVRAA DVLLAVGCRF SEFSTKRWTL VQPGTRIVHV
DVDPVELGRV HLPAVGLVAD AGLAAAALAD ALPEPPVGRR DRVAELRQRY LAATSLDSPA
LAGDDPAGKV SSTAVVQALQ AVVDREGTLL VQDAPSFGPW SHRYLRLPRP GSFSGSAGGA
MAWGFPAGLG MALARPDLRV VTVSGDGSFW MVAQDLETAV RERIPTVNVV VNNDAYGNTR
DRQRSAHGGR YLGVFYGNPD FAGFARSLGA FGARATTDDE VGPAIQAALD QDLPAVVEVV
QDQMYGLPPG LLPPAAR
//
