ID A0A0D2FKP0_9EURO Unreviewed; 537 AA.
AC A0A0D2FKP0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.6, whole genome shotgun sequence {ECO:0000313|EMBL:KIX02487.1};
GN ORFNames=Z518_08428 {ECO:0000313|EMBL:KIX02487.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX02487.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX02487.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX02487.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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; KN847480; KIX02487.1; -; Genomic_DNA.
DR RefSeq; XP_013269623.1; XM_013414169.1.
DR AlphaFoldDB; A0A0D2FKP0; -.
DR STRING; 1442369.A0A0D2FKP0; -.
DR GeneID; 25296499; -.
DR VEuPathDB; FungiDB:Z518_08428; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..80
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 153..257
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 360..515
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 537 AA; 58082 MW; 2A543E889964A03D CRC64;
MVALSMADGY ARLTGKPQCV IVHVDVGTQS LGAGVHNASA GRSPVLIFAG LSPYTVEGEL
CGSRTEYIHW IQDVPDQKQI VAQYCRYSGE IKTGRNVKQM VHRALQFATN DPPGPVYLVG
ARETMAEEIE PYWLDQSVWK TVGPAALPPQ GVESIAKQLI DAERPLLITG YSGRNHAAVP
ELIALADTMK GLRVLVTDGS DLCFPFSHRA SLGMKYGVDD DIPQADFILV VDCDVPWIPT
QCRPNDKCKI VHVDIDPLKN MMPVFYLPAV ERYKADATTA FKQLHTCLSR QYGNVLDSEK
FDIRWMKLGE SHAKRLEVIQ SLAAPPEGGA LSSSYVCAEA RKLCPDDTIW TVEAVTETIF
VADQIQAEAP GSWINQGGGG LGWSGGASLG IKLASDAGAG GPGKGKFVCQ IVGDGSYLFS
FPGSVYWIAQ RYNIPTLTVV LNNKGWNAPR RSLLLVHADG EGSRSTNEEL NLSFEPSPDY
AGIAKAASGG KMWAGRATSV DEFSELLPEA IKSVKEGTGA VLEVRLKDKD TVPKQKS
//
