ID A0A0A2K9Z9_PENIT Unreviewed; 544 AA.
AC A0A0A2K9Z9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Bifunctional 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphate 2-phosphatase {ECO:0000313|EMBL:KGO63748.1};
GN ORFNames=PITC_072000 {ECO:0000313|EMBL:KGO63748.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO63748.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO63748.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO63748.1,
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 -!- 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:KGO63748.1}.
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; JQGA01001621; KGO63748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2K9Z9; -.
DR STRING; 40296.A0A0A2K9Z9; -.
DR HOGENOM; CLU_006383_0_2_1; -.
DR OMA; VKTHVFH; -.
DR OrthoDB; 2013830at2759; -.
DR PhylomeDB; A0A0A2K9Z9; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR PANTHER; PTHR10606:SF39; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE YLR345W-RELATED; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KGO63748.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000313|EMBL:KGO63748.1}.
FT DOMAIN 45..269
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 492..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 62565 MW; 1C724CF022167E22 CRC64;
MDTLLTAEIV ANSPRFRRKS SIFVDAIHDL PEKADLAPAQ LYSTESGRLF HSGRIVIITV
GLPARGKTYD AFYINLIALA RYLRWLGVKT RIFHLGDYRR ATIPFGEDMP DDYFYVNATA
KSVLLRQKIV RKCREDIYHF LNHENGQIAI YDAVNPLASG RRSLAKEFAK HDIETLFIES
WCDDEHIIEE NVRRVKISSP DYVSWKSEDA VKHYLNRISS RIPQFQTMEE KDLNYIKMIN
AGERLIVNNR SFGYLSNRIV FYLLNLHIKS RRTYFARAGV SLDADSYKAD ASLSEQGEDY
AKKMTARLLA HREEEKQAMI ERGETGYESR PLKVWTSTRR RTVETAKYLH ENGYKIRQRS
QLSQLNPGVC EKMSENRIRA EFGDEVAKHE LDPYHHRYPR AESYHDLAVR LEPIILELER
EQTDLLIIAH ESVLRVLYGY LMACNAADIP FLEFPRDEII EIVPESYQNE AQRIHIPDLP
VEMIPASPED LKIPVPPSGV VSPTQGLGSP EGQVTPQSGH RTPSGIRTPR EGERISQQHV
EDVV
//
