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Database: UniProt
Entry: A0A0A2JQJ9_PENEN
LinkDB: A0A0A2JQJ9_PENEN
Original site: A0A0A2JQJ9_PENEN 
ID   A0A0A2JQJ9_PENEN        Unreviewed;       202 AA.
AC   A0A0A2JQJ9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Pyruvate/Phosphoenolpyruvate kinase {ECO:0000313|EMBL:KGO56938.1};
GN   ORFNames=PEX2_002920 {ECO:0000313|EMBL:KGO56938.1};
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:KGO56938.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO56938.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO56938.1,
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 HpcH/HpaI aldolase family.
CC       {ECO:0000256|ARBA:ARBA00005568}.
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:KGO56938.1}.
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DR   EMBL; JQFZ01000155; KGO56938.1; -; Genomic_DNA.
DR   RefSeq; XP_016598626.1; XM_016737570.1.
DR   AlphaFoldDB; A0A0A2JQJ9; -.
DR   STRING; 27334.A0A0A2JQJ9; -.
DR   GeneID; 27672989; -.
DR   HOGENOM; CLU_059964_4_0_1; -.
DR   OrthoDB; 1822991at2759; -.
DR   PhylomeDB; A0A0A2JQJ9; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KGO56938.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyruvate {ECO:0000313|EMBL:KGO56938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Transferase {ECO:0000313|EMBL:KGO56938.1}.
FT   DOMAIN          14..90
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   DOMAIN          95..148
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   202 AA;  21630 MW;  A865DCD43CECA06B CRC64;
     MGLSIKALGI RLVTNPAVVQ LAKNGGFDAL FVDLEHSTLS VNDASQICTA ALQIDITPFV
     RVPYQCGNGF VQRVLDSGAM GVVFPHIHNK GEPLDSIENV DDIAAVDGVD VLLIGSNDLA
     IELGVPGQFE STEFRNALEK VSQSCHKHRK IFGLAGIYDA PEIQDWALNT LGARFILAQQ
     DSGLIAGAGK KCADVLSRIY KQ
//
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