ID A0A073IR51_9BACT Unreviewed; 568 AA.
AC A0A073IR51;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EH55_06080 {ECO:0000313|EMBL:KEJ91951.1};
OS Synergistes jonesii.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Synergistes.
OX NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91951.1, ECO:0000313|Proteomes:UP000027665};
RN [1] {ECO:0000313|EMBL:KEJ91951.1, ECO:0000313|Proteomes:UP000027665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=78-1 {ECO:0000313|EMBL:KEJ91951.1,
RC ECO:0000313|Proteomes:UP000027665};
RA Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT "Draft Genome Sequence of Synergistes jonesii.";
RL Submitted (APR-2014) 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:KEJ91951.1}.
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DR EMBL; JMKI01000036; KEJ91951.1; -; Genomic_DNA.
DR RefSeq; WP_037976650.1; NZ_JQEL01000036.1.
DR AlphaFoldDB; A0A073IR51; -.
DR STRING; 2754.EH55_06080; -.
DR PATRIC; fig|2754.20.peg.1476; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000027665; 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; 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:UP000027665};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 61503 MW; 292F27B9F936D31C CRC64;
MTVSEFIAEY LYSQGVDCIF EMIGGMTVRL LDAIYRHGGI KIISMHHEQA AAFAACGWAQ
VKGVPGVALA TSGPGATNLV TGIGTAYFDS IPAVFITGQV NQNELSTGTK CRQIGFQETD
IVSIAGPITK MSVQLQKAQD ITTLLPDAFK TALGGRPGPV LLDVPMNLQK EEIDCSCFDF
SPVEVNNPLP PAEALDGFID KLNAELSEAR RPLMLLGTGV IRSHTEKEAR RFAEEKQIPA
VYSWHGKGII SSECKWSVGL TGTNGNRWAN RALAHCDLLI ILGSRTDVRQ IGANTDVFSQ
NKTIFHIDID EAELNNRLKN TNTLCADLKN ILPLLIERTN KSSASAEWLA GIIKDKEENP
DTKELSHISG INPNAFVYKI SSSENNGASG YVSGVGTNRT WVSQSLWLKE GQYYITTPCM
GSMGFALPAA VGASIADAGA EIIVVAGDGG MQCNIQELEV INRLALPLKI VVMKNNALAT
VRQFQKEICG GRLPGSDWTF GAPDFVKVGK AYGLRSDRLE RPEEMDEKIK EFLAGGGPAL
LEVAVDKEAG AYPKMQFGHN LDDMFPFK
//