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
//