ID A0A0A2KZT9_PENIT Unreviewed; 601 AA.
AC A0A0A2KZT9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP-binding {ECO:0000313|EMBL:KGO72453.1};
GN ORFNames=PITC_076300 {ECO:0000313|EMBL:KGO72453.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO72453.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO72453.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO72453.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO72453.1}.
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DR EMBL; JQGA01000881; KGO72453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KZT9; -.
DR STRING; 40296.A0A0A2KZT9; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OMA; DCGTLAM; -.
DR OrthoDB; 2291769at2759; -.
DR PhylomeDB; A0A0A2KZT9; -.
DR Proteomes; UP000030104; 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; 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:UP000030104};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 31..162
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 236..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 441..592
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 601 AA; 64944 MW; 28C70E492D80F205 CRC64;
MKSTNAVPHK RKKVNSDDEE EIVKDHSLTS AAENFFEALS EAGITHCFVN LGSDHPAMLE
AMIKAKQENK TNFPNIITCP SELVALSAAL GYAQATGVPQ CVIVHVDCGT LAMGQSIHNA
SVSRVPVLCF AGLSPFTQNG ELLGSRTEFI HWLQDVPDQA AIVRQYCRYT GEIKTGRNIK
QMVSRALQFA TSDPKGPAYL MAAREVLEEH VGKEDLDGEI LSSITPSALP EQEVKLIAKS
LLGAKRPLVI TSYLGRNLKA PALLAELCDK LPITVVEMVG SDVSLRSDHE AYRGVTVTTH
PEVLEADVIL ILDCDVPWIP TAGKPQKGTK VFHLDVDPLK QQMPLFSISA TRKLKVGCGI
ALGQINAFLD KQDIDRAEYT AAFEVRSKNY KTWRRTLQTL ESPSEDGVVS VPFLASRLRD
SLPQDTIYVL EAVTNAGPLI HHLNLTKPGS LIASGAGGLG WGGGAALGVK LGKPGSFICA
IVGDGVYLFS QMESVYWIAR RYDIPFLLVV LNNGGWNAPK VSALLVHKDG LSSKSNRRDL
NISFDPSPDY PGIAAAAGKA WGKTVTTQSE LDPAIKEATE VVQGGKCAVI EVSVPSMWKE
N
//
