ID A0A087BZI0_9BIFI Unreviewed; 584 AA.
AC A0A087BZI0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KFI76430.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KFI76430.1};
GN ORFNames=BMON_1730 {ECO:0000313|EMBL:KFI76430.1};
OS Bifidobacterium mongoliense DSM 21395.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI76430.1, ECO:0000313|Proteomes:UP000029082};
RN [1] {ECO:0000313|EMBL:KFI76430.1, ECO:0000313|Proteomes:UP000029082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI76430.1,
RC ECO:0000313|Proteomes:UP000029082};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KFI76430.1}.
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DR EMBL; JGZE01000016; KFI76430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BZI0; -.
DR STRING; 1437603.GCA_000771525_00521; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000029082; 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:UP000029082};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KFI76430.1}.
FT DOMAIN 36..148
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..357
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 416..555
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 63670 MW; 65049337A70EE95A CRC64;
MHNGNIDHQT AATTGGVPGN REVEVQAEPE AQQPRNVSDL FVQCLVNEGV EVIFGIPGEE
NIPLMEAIKR DGRIKFVLTR HEQGAGFMAA TYAHETGKPG VCLSTLGPGA LNLVLPVAQA
NASTTPLVAI CAQGNVNRLY KESHQIVDLV SVFRPITQWA AMVLDAAAVP EMIRKAFSVA
QRKRPGASCL VLPEDISQLA APVQAEPLPL PRPVHTIPAP DTIVEAANLI GAAKHPVILA
GNGVARSHAE QQLKEITELL NVPVATTFEG KGVFSDKHPN ALGVVGFMKH DYENFAFDTA
DLILAVGFSI QQFDPIKINP NNDKVIIHIN TFTEDTDAHY PASLNIRADI KNTLVALEAE
LRKRTISFEP SHPQIRGLLQ REYESCKADM SFPMKPQRVV YDTRRAVQGD WPVLVDTGAL
KMWMARLYPT YEPSTCVIDN SLSTMGWSLP GAVGASLSAP GVPILAVMGD GSFMMNLQEI
ETAVRYGCRI VILVWIDNAY GLIKWKMDMH TKDHEFVDFN NPDFLDLAAS FGAKGHEITS
ADELYPVLRS ALRSGSGVDL IACPVDYREN MKLISKLGDI DFAS
//