ID A0A0A2JNI7_PENEN Unreviewed; 541 AA.
AC A0A0A2JNI7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP-binding {ECO:0000313|EMBL:KGO56997.1};
GN ORFNames=PEX2_003510 {ECO:0000313|EMBL:KGO56997.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO56997.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO56997.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO56997.1,
RC ECO:0000313|Proteomes:UP000030143};
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:KGO56997.1}.
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DR EMBL; JQFZ01000155; KGO56997.1; -; Genomic_DNA.
DR RefSeq; XP_016598685.1; XM_016737629.1.
DR AlphaFoldDB; A0A0A2JNI7; -.
DR STRING; 27334.A0A0A2JNI7; -.
DR GeneID; 27673048; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR PhylomeDB; A0A0A2JNI7; -.
DR Proteomes; UP000030143; 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: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:UP000030143};
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 154..258
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 364..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 541 AA; 57959 MW; 0C5BEAA0BFEF654D CRC64;
MVALSMADGY ARLTGKPQAV IVHVDVGTQG LGAAVHNASC GRAPVLIFAG LSPYTIEGEM
RGSRTEYIHW IQDVPDQKQI VSQYCRYTGE IKSGKNVKQI VNRALQFATS DPQGPVYLAG
AREVMEEDIE PYQLNQAVWG PVAPAALPTS GVELIASELA AAKSPLIITG YSGRKSQAVA
ELVSLADSFK GIRVLDTGGS DMCFPADHPA WLGLRYPGHE AVGTSDLILV VDCDVPWVPT
QFKPSASAKI IHIDVDPLKQ QIPVFYIHSM ASFRADASTA VKQINDHVAS QESLQQFIGT
QENITMGQRR DEEHSKRRQE ISDLAVVPEG GSEAFLNINY LMAQVRQGVP IDTIWAIESV
TMTHFVADQV SATQPKSWIN CGGGGLGWSG GGALGIKLAS DMQHGGRGKG KFVCQVVGDG
TFLFSVPGSV YWIARRYGIP ILTIVLNNKG WNAPRRSMLL VHPEGDGSRA TNEDLNISFA
PTPDYAGIAK AAAGGELWAG RASTVAELAQ QLPEAIQSVL NGKAAVLEVQ LDGTTGKYVE
N
//
