ID   W4P7N5_9BACE            Unreviewed;       429 AA.
AC   W4P7N5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:GAE15149.1};
GN   ORFNames=JCM6292_1385 {ECO:0000313|EMBL:GAE15149.1};
OS   Bacteroides pyogenes JCM 6292.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1235809 {ECO:0000313|EMBL:GAE15149.1, ECO:0000313|Proteomes:UP000018861};
RN   [1] {ECO:0000313|EMBL:GAE15149.1, ECO:0000313|Proteomes:UP000018861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6292 {ECO:0000313|EMBL:GAE15149.1,
RC   ECO:0000313|Proteomes:UP000018861};
RA   Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Strains of Bacteroides pyogenes Isolated
RT   from a Cat and Swine.";
RL   Genome Announc. 2:e01242-13(2014).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:GAE15149.1}.
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DR   EMBL; BAIQ01000012; GAE15149.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4P7N5; -.
DR   Proteomes; UP000018861; 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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 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;
FT   DOMAIN          105..239
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          301..416
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   429 AA;  47171 MW;  2B0D172F7FB7058D CRC64;
     MIDSCPLVVI AGQVGTGFLG TDAFQEVDLV GITQPISKWS YQIRRAEDVA WAVARAFYIA
     RSGRPGPVVL DFAKNAQVEK IHYEPVAIDF VRSYVPVPDT DEASVKEAAE LINAAERPFV
     LVGQGVELAN AQKELIAFIE KADLPAGCTL HGLSVLPTEH PLNKGMLGMH GNLGPNMNTN
     KCDVLIAVGM RFDDRVTGNV ATYAKQAKVI HFDIDPGEIN KNVRADVAVL GDCRETLPAV
     ARLLKKKKHA EWIDSFGEYE QVEEERVIRP ELYPASEELS MGEVVRAVSE ATLHRAVLVT
     DVGQNQMMAA RYFKYTQERS IVTSGGLGTM GFSLPAAIGA TFGRPDRTVC AFMGDGGLQM
     NIQELGTIME QQAPVKIICM NNNFLGNVRQ WQAMFFNGRY SFTPMQNPDY MKIAEATAFL
     PEECLHVKN
//