ID A0A086ZQA5_9BIFI Unreviewed; 591 AA.
AC A0A086ZQA5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KFI48705.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KFI48705.1};
GN ORFNames=BBIA_2243 {ECO:0000313|EMBL:KFI48705.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI48705.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI48705.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI48705.1,
RC ECO:0000313|Proteomes:UP000029108};
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:KFI48705.1}.
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DR EMBL; JGYN01000029; KFI48705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086ZQA5; -.
DR STRING; 1437608.GCA_000771645_00009; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000029108; 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; cd02010; TPP_ALS; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029108};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KFI48705.1}.
FT DOMAIN 43..157
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 230..364
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 423..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64946 MW; 95810BE8BC4E5083 CRC64;
MTEQQHHSLI SRLESRLHEN AAHHPQPQQA ASPKPTEPRH ERNVADLMVQ CLVQEGVEVI
FGIPGEENIP FIEALERDGR IRFVVTRHEQ GAGFMALTYA HLTGKPGVCL ATLGPGALNL
TLPVACANAS NTPLVALCAQ GSVRRLHKES HQIIDLVSVF RPITRWTNMI LSPEAVTETM
RKGFALAQRK RPAATCIILP EDIAEQPAPA DAEPLSRALQ VHTVPTPADI DAAADIIAKA
KHPIILAGNG VSRAHADYQL RILSEQLNLP VATTFEGKGV FSDRHDNALG VVGFMRHDYE
NFAFDDADLI IAIGFSIQQF DPVKINPKND KKIIHINTFV EDTDAHYTTT LNIMADIDAT
LTQLIDALRE RDVRFDDMES DIRRLLTDEF TSRKDDDSFP MKPQRVVYDT RRALGDSDVA
LVDTGALKMW MARLYPTYLP NTCIIDNSLS TMGWTLPGAV GASLARHGRP VLAVMGDGSF
MMNMQEIETA VRLGCHIVIL VWVDRAYGLI KWKMDLHAGH HDDVDFGNPD FVKLAESFGA
TGTLIQAANE LGPAIEAAMT ADGGVHVIAC PVDYSENMKL TDKLGELELP G
//
