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
//