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Database: UniProt
Entry: A0A0A2ILW8_PENEN
LinkDB: A0A0A2ILW8_PENEN
Original site: A0A0A2ILW8_PENEN 
ID   A0A0A2ILW8_PENEN        Unreviewed;       356 AA.
AC   A0A0A2ILW8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Fumarylacetoacetase, C-terminal-like protein {ECO:0000313|EMBL:KGO57625.1};
GN   ORFNames=PEX2_020670 {ECO:0000313|EMBL:KGO57625.1};
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:KGO57625.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO57625.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO57625.1,
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 FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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:KGO57625.1}.
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DR   EMBL; JQFZ01000139; KGO57625.1; -; Genomic_DNA.
DR   RefSeq; XP_016599281.1; XM_016739342.1.
DR   AlphaFoldDB; A0A0A2ILW8; -.
DR   STRING; 27334.A0A0A2ILW8; -.
DR   GeneID; 27674761; -.
DR   HOGENOM; CLU_787785_0_0_1; -.
DR   OrthoDB; 9433at2759; -.
DR   PhylomeDB; A0A0A2ILW8; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF7; ACYLPYRUVASE FAHD1, MITOCHONDRIAL; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          10..204
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   356 AA;  39063 MW;  4A2FE1BB3CFEF4CC CRC64;
     MASIRANCRK IMCIGRNYAD HITELNNTAP KQPFFFLKPA SSILTPGSGP VLRPKGVSLH
     YEVELGLVIG KTVRDLDPND EQAALDAIQS YVLAIDMTAR NVQDEAKKKG LPWSIAKGFD
     TFLPISQEIA KSRIPNPHDA FLRLSVGQNE RQADSTSLML YRIPQQLAQI SRVMTLEKGD
     IVLTGTPKGV GQVKAGDVMR ASIEVGGKEI EEGRIEVEVQ DREGRFPVCQ DIAMFASDFK
     DQMFSSTQTS LDLSTCKSQR FSQTSIPSAS AMAQGHNEAL ALVNVHKNIT GSDSTESGSA
     LADKSPADDK ADLRRAKELV ELHYEVKARH ANGTVDEELS QARQDVRRVL RELSTV
//
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