ID A0A0A2L6V3_PENIT Unreviewed; 285 AA.
AC A0A0A2L6V3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyruvate/Phosphoenolpyruvate kinase {ECO:0000313|EMBL:KGO74906.1};
GN ORFNames=PITC_031440 {ECO:0000313|EMBL:KGO74906.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO74906.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO74906.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO74906.1,
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 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:KGO74906.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQGA01000558; KGO74906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L6V3; -.
DR STRING; 40296.A0A0A2L6V3; -.
DR HOGENOM; CLU_059964_4_0_1; -.
DR OMA; PAPLMVE; -.
DR OrthoDB; 1822991at2759; -.
DR PhylomeDB; A0A0A2L6V3; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KGO74906.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyruvate {ECO:0000313|EMBL:KGO74906.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000313|EMBL:KGO74906.1}.
FT DOMAIN 39..226
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 285 AA; 29969 MW; 0CB6028A3A9D8296 CRC64;
MGSVAIDTVE PIMADCQNIL LTKAGTGRFC KAMGIRLVTN PLVVQLARNA GYDALFIDLE
HSTLSLAEAS AIACAGILSG VTPFVRLPHQ CGMGFVQQVL DGGAMGIIFP HVISKADAQR
AVATCKFPPF GLRSMWAQQP AVGLRPMALP DLIEVCNSQA SSVVVMIEAA ESLFNLDEIA
SVKGVDMLLV GCLDLSTDMG IPGSFDDKGF HAALEAVSVA CKRHGKVFGI AGLYNNPKLQ
GWAINELGVR FMLCQQDSNL LGIGATQCAE ALSAVDGTNG IILPH
//