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Database: UniProt
Entry: D3CYF6_9ACTN
LinkDB: D3CYF6_9ACTN
Original site: D3CYF6_9ACTN 
ID   D3CYF6_9ACTN            Unreviewed;       562 AA.
AC   D3CYF6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:EFC84276.1};
GN   ORFNames=FrEUN1fDRAFT_2576 {ECO:0000313|EMBL:EFC84276.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC84276.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC84276.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC84276.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:EFC84276.1}.
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DR   EMBL; ADGX01000033; EFC84276.1; -; Genomic_DNA.
DR   RefSeq; WP_006540418.1; NZ_ADGX01000033.1.
DR   AlphaFoldDB; D3CYF6; -.
DR   Proteomes; UP000004777; 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:SF169; 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   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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          12..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          215..343
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..558
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   562 AA;  59666 MW;  73ADE1319B282D3E CRC64;
     MTDLTDEKDQ KDGGEAILEA CRNLGVDVIF SSPGSEWAPV WEALARQEKN GTPGPRYLDL
     LHETLAVAMA TGYGLVTGRP QMVLLHAVPG LLQGACGIHG ALLANVGMVV CSSESITYGE
     TETDPGSQWY RNLSIVGGTQ AVAAPFVKWS TQVGSVSTLY GSVVRAAEIA RRGPAGPVYL
     NVPVEVLLEP WKPAATAIRP VALPGSRVST ERDLAEAARR LVAAEHPVIV TESAGRHPDG
     FAALVDLAEL LSIPVIEPQS AVCANFPRTS ELHRGGDGGA LFAEADLIVL VCCRAPWYPP
     SNRPADAEVL VVDDVPHRPY SDYQVLVADQ YLEGDVGPTL RALVSGVKEL GVDDERVAAR
     RAVLAAPRPA RAAAGDGLDA AAVVRELRDL IDPRAAVVDE TITHSRAIAQ HLRAEEPGRY
     SYVQGGLGQG LGVALGVKLA DPDREVVLTI GDGSFLYNPI VQSLAASRAL GLPLLVVVFN
     NRQYRSMKLN HLRFYPQGTA VTEGDFRGVD LTDQPDLASL VTPFEMAGHT VTNPDDLRPV
     LEAALASVRA GVTALVDVHL PL
//
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