ID Q0C833_ASPTN Unreviewed; 689 AA.
AC Q0C833;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=6-phosphofructo-2-kinase 1 {ECO:0000313|EMBL:EAU29600.1};
GN ORFNames=ATEG_10151 {ECO:0000313|EMBL:EAU29600.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU29600.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476609; EAU29600.1; -; Genomic_DNA.
DR RefSeq; XP_001209453.1; XM_001209453.1.
DR AlphaFoldDB; Q0C833; -.
DR STRING; 341663.Q0C833; -.
DR EnsemblFungi; EAU29600; EAU29600; ATEG_10151.
DR GeneID; 4319428; -.
DR VEuPathDB; FungiDB:ATEG_10151; -.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_006383_3_1_1; -.
DR OMA; HAYRYNE; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000007963; 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 InterPro; IPR001345; PG/BPGM_mutase_AS.
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; 2.
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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EAU29600.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Transferase {ECO:0000313|EMBL:EAU29600.1}.
FT DOMAIN 110..164
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 269..439
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 531
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 689 AA; 77491 MW; C0331C7DED912C3D CRC64;
MSSADSLRER PNGVTSNPSA KGKDASLMPP TKSLVGRALG NELHADGHKG ATASKDGVGF
ALTDTPVSTA PSSPQFSANT TQPSTPSRVR ATTLDIPGLT KSKVSPDGRI AQRDVGSKLV
IVMVGLPARG KSYITKKLAR YLNWLQHDTE IFNVGERRRV AAGKSPSPPG RHRSARTSSI
HKDLVDSVRR LSVSVGGAFG SPAHRDSAHL EPATSPPELD NHLPPPAVPT KILINGREED
DSYHNGSTIV PPFHASPEDQ RAMEEAESNE PLDQSASFFD PKNQLAVKLR EQVALDTLDE
LLNYILEEGG SVGILDATNS TMERRKAIVD HIRQRAGPEL NILFLESSCV DQELLEANMR
LKLSGPDYKD QDPVKALEDF KKRVALYEKS YVPLGEYEER NNMAYIQMID VGRKVVSHQT
HGFLSSQVVY YLLNFNLSPR QIWITRHGES KDNQSGRIGG DSDLSENGHR YAKALARFID
EQRKLWESLQ RQKDIMQQFP PRPGDSTPPN PSYVPRDRPR NFCVWSSMMK RSIQTVDYYN
EEDYDVKQMK MLDELHAGKM EGMTYEEIRE KYPDDYATRK KDKLYYRYPG PGGEGYLDVI
NRLRAVIVEV ERMTDHVLLV THRAVARVLL AYFLGLKRNE VADLDVPLGM LYMLEPKPYG
VEFKAYRYNP ETDWFDHIPD FKLRQATMN
//
