ID A0A0D2CRM9_9EURO Unreviewed; 560 AA.
AC A0A0D2CRM9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW32595.1};
GN ORFNames=PV07_04125 {ECO:0000313|EMBL:KIW32595.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW32595.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW32595.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW32595.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847041; KIW32595.1; -; Genomic_DNA.
DR RefSeq; XP_016252811.1; XM_016390909.1.
DR AlphaFoldDB; A0A0D2CRM9; -.
DR STRING; 569365.A0A0D2CRM9; -.
DR GeneID; 27343319; -.
DR VEuPathDB; FungiDB:PV07_04125; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000054466; 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:UP000054466};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 11..103
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 176..282
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 60260 MW; 7FDA728C7826FBF6 CRC64;
MEAIAKKEKM ENPNLPKIIT CPSEMVALSM ADGYARVTGK AQAVIVHVDV GTQALGCALH
NAHIARTPVL IFAGLCPSTL EGEERGTRTE FVNYLQDIPD QAAIVRQYCR YTNEIRSSNN
VKQVVARALQ IASSAPKGPV YLYAARETLE RESKPPRLEP KFWKPIGPAA LPDEAVQEIS
EALVSSKDPL IITGYTGRNE KAPSELVKLA DAIPGLRVLD TSMGDMCFPA NHPGWLSGKY
SSHPSIPKAD CILVLDCDVP YVPVKCRPSS AAKVYHIDID PLKKSMAMYH IDAVGLWQAD
SYTAIKQINA HLSRPEYVTT LEGLLESDSA VSRAQSHNQL LSDIAQAGMP ASGSPTPLTA
ALIAAELKRS LPNSTTYAVE AVTNTASIYD QLRCTVPGSY LSSGATGLGW VGGASLGIKL
ATMDKDGDAE NAIVTQIVGD GTYLFSAPSS VYWLSSRYRI PILTIILNNK GWNAPRVSMQ
LVHPTGEGSR MSNRDLHISF DPSPDYAGIA KAAGGAMVWT GYAETAGDFA AVIKEAIREI
MSGRTAVVEC KIRGMDPKME
//
