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Database: UniProt
Entry: A0A087BZI0_9BIFI
LinkDB: A0A087BZI0_9BIFI
Original site: A0A087BZI0_9BIFI 
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
//
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