ID Q47SH6_THEFY Unreviewed; 553 AA.
AC Q47SH6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AAZ54591.1};
GN OrderedLocusNames=Tfu_0553 {ECO:0000313|EMBL:AAZ54591.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54591.1};
RN [1] {ECO:0000313|EMBL:AAZ54591.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ54591.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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}.
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DR EMBL; CP000088; AAZ54591.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47SH6; -.
DR STRING; 269800.Tfu_0553; -.
DR KEGG; tfu:Tfu_0553; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_11; -.
DR OrthoDB; 4959782at2; -.
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; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 58142 MW; EDC5CAEFB904B37E CRC64;
MGSPSFSGKL TGHGGNHAVE VARHHGVDTL FTLSGGHIFP IYDGAVKADP PMRLLDVRHE
QTAVFAAEAV GKLTRRAGWA ALTAGPGVTN GVSGIATAHF NGSPLVVVGG RAPDNRWGQG
LLQELDQSPL FTTITKRAWT VHDTAQIGPA LDEAFTLANT AHRGPVFLDI PMDRLYDQAE
ITVTGQAAAE DRSPDPDAVA AVARLLSEAE RPVLVYGSDV WLDHAEQAAL EAAEELGVPV
VTNGQGRGVL PAGHPLLATR ARGLALGRAD LVIVVGTPLD FRLNHGLFGG RDGAPLARTV
HITDSPAQLA THLTLAGAVS GDLSAILRAL AEQAKPKREV AQWRTEVAEA AAATAAKDRE
VLDSDASPIH PARIYGELNR ILDDDAVVIG DGGDFVSYAG KYIQPRRPGN WLDPGPFGCL
GTGMGYAIAA RLVRPSSQVV ALFGDGALGF SLADVDTLVR HNLPVVMVCG NNGIWGLEKA
PMQLVYGYDV LADLAPQTRY DQVVTALGGG GELVTDPAEI GPALRRAFDS GVPYLVNIVT
DPENVYPRKT MGV
//
