ID A0A411YI82_9ACTN Unreviewed; 553 AA.
AC A0A411YI82;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:QBI20806.1};
GN ORFNames=ER308_15345 {ECO:0000313|EMBL:QBI20806.1};
OS Egibacter rhizosphaerae.
OC Bacteria; Actinomycetota; Nitriliruptoria; Egibacterales; Egibacteraceae;
OC Egibacter.
OX NCBI_TaxID=1670831 {ECO:0000313|EMBL:QBI20806.1, ECO:0000313|Proteomes:UP000291469};
RN [1] {ECO:0000313|EMBL:QBI20806.1, ECO:0000313|Proteomes:UP000291469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGI 80759 {ECO:0000313|EMBL:QBI20806.1,
RC ECO:0000313|Proteomes:UP000291469};
RA Chen D.-D., Tian Y., Jiao J.-Y., Zhang X.-T., Zhang Y.-G., Zhang Y.,
RA Xiao M., Shu W.-S., Li W.-J.;
RT "Egibacter rhizosphaerae EGI 80759T.";
RL Submitted (JAN-2019) 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; CP036402; QBI20806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411YI82; -.
DR KEGG; erz:ER308_15345; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000291469; Chromosome.
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; cd00568; TPP_enzymes; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000291469};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 57185 MW; 72D25525BB337371 CRC64;
MTAAIDAAVA QLVAAGVRRA YTVPGESFLP LLDALDAHPA VQVLSTRHES GAGFMAEAEA
KVTGAPAVVL ATRGVGASNL SIAVHTARQD STPMVVLLGQ VSTQALGREA FQEIDLPTYY
GEVTKGAWTV EQSERLPEQI ARAVLTAISG RPGPTMLALP EDVLDSDPPV ADGWRPGVEQ
ASRPTLDAAT ARAVADLLGP ASSPVLIAGG GAGGAREALV AFAEAFGVGV YAAFRRQDVF
PNEHPNYLGH LTLGAPAETL ATLHEADVVL VVGSRLSEVT TQAYTLPTSG QTVVQIDIDP
SVVGAVRPVA IGAVADAEAA LRALLAHAPE SSASRGTRTS SLERGHEAFL AASTPSEPSD
GPIHPAEVMA ALGRVFPPTT IVTNDAGNFS VFAHRYWRFA EPGTQVGPTS GAMGYGVPAA
IGAQLARPEG EVVALAGDGG FLMTGQELET AVRYELPITV VVFRNGLYGT IALHQGRKLG
RTAAVGIGQV DLAAVARGYG ATAWQVNERA ELEDALWQAR RSGRPALVDV VVDSDVLTPA
ASLSDLLGTE RAR
//
