ID A0A1I7G2R8_9FIRM Unreviewed; 578 AA.
AC A0A1I7G2R8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SFU42754.1};
GN ORFNames=SAMN05216508_104121 {ECO:0000313|EMBL:SFU42754.1};
OS Eubacterium pyruvativorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=155865 {ECO:0000313|EMBL:SFU42754.1, ECO:0000313|Proteomes:UP000198817};
RN [1] {ECO:0000313|EMBL:SFU42754.1, ECO:0000313|Proteomes:UP000198817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHGC13 {ECO:0000313|EMBL:SFU42754.1,
RC ECO:0000313|Proteomes:UP000198817};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FPBT01000004; SFU42754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7G2R8; -.
DR STRING; 155865.SAMN05216515_10410; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000198817; 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:SF142; 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:UP000198817};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 63905 MW; 57DC2E6587352681 CRC64;
MKTSDYIAEF LADHGIRHCY GYQGTMIAHL VDSLCRHPRL TNHVCLNEQG AAFAAVGEAK
VTGRCAFAYS TSGPGAANLL NGVADAYYDS VPVLFITGQL NSYEYYDLPE LKQHGFQEMD
VVDMAKPVTK YCVQVRNAHD LPRILHEAYE TAVSGRPGPV LIDLPMDMQR MEIDPEDYCF
ASSSGQAEPV FEMTPEACAD EILEALRAAK RPVLAVGKGI DPALRKTLRD LVRTLEIPTV
TSMPARDLLE YDDPLNFGHM GSGYGHRAVN MIVNKKTDLI VALGVSLCKR QTGMKTENFA
RDAQIIRVDI DSTELSRRIH EHEKSYLQDA SDVMTALAAK AEGAVTDPAW LAVCRRIREE
LTAFDDSRPE REPNQITKLI SEYTKDAKTV CLDVGQHMMW GSQSYALRGD QRMICSGGHG
AMGFSLPAAI GAAISTGGPV ITLTGDGSMQ MNIQELEWMH REQLPITVFV MNNHSLGLIQ
QQQDSIFQGR YYSSVAEGGY TAPDFAKVAA AYGIHSARAE NREELEQILK DLDLGKPNVI
DVQLDVHSRA YPKTSFGEEM QNQQPYMPAE LMKELLAL
//
