ID S7ZA48_PENO1 Unreviewed; 698 AA.
AC S7ZA48;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN ORFNames=PDE_02408 {ECO:0000313|EMBL:EPS27465.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS27465.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS27465.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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DR EMBL; KB644410; EPS27465.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZA48; -.
DR STRING; 933388.S7ZA48; -.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_006383_3_1_1; -.
DR OrthoDB; 2013830at2759; -.
DR PhylomeDB; S7ZA48; -.
DR Proteomes; UP000019376; 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:SF32; 6-PHOSPHOFRUCTO-2-KINASE 1; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 120..174
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 283..449
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 632
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 698 AA; 77222 MW; 2758B33911283B41 CRC64;
MTSANSPVHA NQGDQGVKNS GPNGVTSSGA SIGSGKEGAL MPPGPKTVVS RALGSDLHSD
AHRGSQGGVG TALTDTPIST APSSPQINGL SAASTPSRVR ATTLDIPGLT RSKVSPDGRI
AQRDVGSKLV IVMVGLPARG KSYITKKLAR YLNWLQHDTE IFNVGERRRV AAGKSPSPAH
IGRPLEKRVS SVHKDLVDSV RRLSVSVGTA NQDATSPPEA SSPPNDTSLP PPAIPTKILI
NGKEPDSSIS QNGSTVVSSD DAGNHTADIP ADAIKEASPE PMDQSANFFD PSNQIALKLR
EQVALDTLDE LLEYILEEGG SVGILDATNS TMERRKAIVD HIRKRAGPEL GILFLESSCV
DKDLLEANMR LKLSGPDYKG QDPTAALEDF RKRVALYEKS YVPLGEYEEK NDMAYIQMID
VGRKIVSHQT HGFLSSQVVY YLLNFNLSPR QIWITRHGES VDDQAGRLGG DSDLSENGQR
YAKALAKFID HQRKKWELYQ RQKNLIKHFP PRPGDSTPPN PSYIPRDRPR NFCVWSSMMK
RAIQTVEYFN EDDFDVKQMR MLDELHAGKM EGMTYKEIQE QFPEEYAHRK KDKLFYRYPG
PGGESYLDII NRLRAVIVEV ERTTDHVLLV SHRSTARVLL SYFRGLKRDM VADLDVPMGM
LYMLEPKPYG VDFKAYQYNP DSDWFDEVPN YELHQVGA
//
