ID A0A087DHA2_9BIFI Unreviewed; 588 AA.
AC A0A087DHA2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KFI94902.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KFI94902.1};
GN ORFNames=BSTEL_1566 {ECO:0000313|EMBL:KFI94902.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI94902.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFI94902.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI94902.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-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:KFI94902.1}.
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DR EMBL; JGZP01000019; KFI94902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087DHA2; -.
DR STRING; 762211.BSTEL_1566; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000029004; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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:UP000029004};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KFI94902.1}.
FT DOMAIN 39..152
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 226..360
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 420..558
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 64079 MW; 30C5863A7E8C952B CRC64;
MCPSAQWCCY TFPTVNAPDA TASPATEPQE QSKKTHIRTV ADLFVECLVN EGVETMYGIP
GEENIPLMEA IERDGRIRFV LTRHEQGAGF MAATQGHLTG KPGVCLATLG PGALNLTLPV
AQANASTTPL VAICAQGNVT RLYKESHQIV DLVSVFRPLT QWTSMVMEPA SVPEMVRKAF
SIAQRNRPGA TCLILPEDVA EMPAPEDAHP LPLPNPMSFA PTPDTIERAV SIIRGAKHPI
ILAGNGVARG HAENRLLALA EQLNVPVATT FEGKGVISDR IPLALGVVGF MRHDYENFAF
DEADLIIAVG FSIQQFDPKK INPNDDKTII HINTFIEDTD AHYSTALNIM GSIDATLSAL
VDALKRHHVT FGVSHPKIHE LLTDEYESYA QDDSFPLKPQ RIVADTRRAM ETDTDIALVD
TGALKMWMAR LYPTYYSNTC VIDNSLSTMA WTLPGAVAAS LENPGRPVLA VMGDGSFMMN
VQEIETAVRV GARIVILVWV DEAYGLIKWK MDLHDGSHEY VDFNNPDVVA LGMSFGAKGH
LIESADELYP TLRSALRSGS GIDIIACPVD YSENMKLIDK LGEVDFSA
//
