ID A0A0D2FNZ1_9EURO Unreviewed; 608 AA.
AC A0A0D2FNZ1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW69958.1};
GN ORFNames=PV04_02270 {ECO:0000313|EMBL:KIW69958.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW69958.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW69958.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW69958.1,
RC ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
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; KN846957; KIW69958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FNZ1; -.
DR STRING; 5601.A0A0D2FNZ1; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2692099at2759; -.
DR Proteomes; UP000054266; 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; 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:SF13; 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 27..149
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..368
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 441..588
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 66350 MW; 45352C10C8A7216E CRC64;
MSLPVRLSPH DTPNLQNGDS SPKPGWGSDY IARQLAKVHI PYFVLVPGSS YRGLHDSLVN
LNGNTAPEMV VCLHEEHSIA IAHGYAKVTE KPLACGLHAN VGLMHASMAI FNAFIDRVPM
VIFGAAGPFD TTKRRPWIDS THTAVDQAAL VRNYTKWDDQ PASVNSAIRS VIKATAVASV
KPCAPTYVVL DVGLQEAPYD EKDVRYPDTE RYLTQQSAGA SQGDIKKVAQ ALRESKKALI
MFGRMNRTQK GWDERIRLAE MFDAKVITDI KQPVAFPTTH RLHPAAPALF LAPEAASMIR
EADLIISFDW VDLVGFFTAA HGELIEPTAK VIEVSVDSQL HNGWSKDHFE TPPADISIFA
DPDKFITDLV AELESSKLTG FPNSAWPATQ PSSSQKPQNL DGEDIFQADL ASALYATISP
DDMCIIRLPL SFRGIDLLAT HPLAYLGMDG GAGIGSGPGQ AVGSALALKG TKYVPVAILG
DGDFLMGNSA IWTAARYRIP VLIIVSNNGS FYNDEVHQER VANTRSRPVE NKWIGMRLDD
PLPDIGKMSE GFGLKTLGGQ ISKRSELKGK LEEAIKLVRD DKQAVVLDIR VRPDDYLKNW
GAGNIVKK
//
