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Database: UniProt
Entry: I3PVS2_NYCPV
LinkDB: I3PVS2_NYCPV
Original site: I3PVS2_NYCPV 
ID   I3PVS2_NYCPV            Unreviewed;       724 AA.
AC   I3PVS2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=6-phosphofructokinase type A {ECO:0000256|ARBA:ARBA00041249};
DE   AltName: Full=Phosphofructo-1-kinase isozyme A {ECO:0000256|ARBA:ARBA00041366};
DE   Flags: Fragment;
OS   Nyctalus plancyi velutinus (Fine-haired noctule) (Nyctalus velutinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Nyctalus.
OX   NCBI_TaxID=187011 {ECO:0000313|EMBL:AFH77898.1};
RN   [1] {ECO:0000313|EMBL:AFH77898.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pan X.W., Shen Y.Y., Zhang Y.P.;
RT   "Adaptive evolution of a speed-limited glycolytic gene PFKM in bats.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679}.
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DR   EMBL; JF911721; AFH77898.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3PVS2; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00764; Eukaryotic_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR041914; PFK_vert-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF59; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFH77898.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..294
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   DOMAIN          374..657
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFH77898.1"
FT   NON_TER         724
FT                   /evidence="ECO:0000313|EMBL:AFH77898.1"
SQ   SEQUENCE   724 AA;  79321 MW;  4D40F19CA27000EA CRC64;
     MNAAVRAVVR VGIFTGARVF FVHEGYQGLV DGGEHIREAT WESVSMMLQL GGTVIGSARC
     KDFREREGRL RAAHNLVKRG ITNLCVIGGD GSLTGADTFR SEWSGLLNDL QKEGKITAEE
     AKKSSYLNIV GLVGSIDNDF CGTDMTIGTD SALHRIIEIV DAITTTAQSH QRTFVLEVMG
     RHCGYLALVT SLSCGADWVF IPECPPDDDW EEHLCRRLSE TRTRGSRLNI IIVAEGAIDK
     HGKPITSEDV KNLVVKRLGY DTRVTVLGHV QRGGTPSAFD RILGSRMGVE AVMALLEGTP
     DTPACVVSLS GNQAVRLPLM ECVQVTKDVT KAMSEKKFDE ALKLRGRSFM NNWEVYKLLA
     HVRPPVSKTG LHTVAVMNVG APAAGMNAAV RSTVRIGLIQ GNRVLVVHDG FEGLAKGQIE
     EAGWSYVGGW TGQGGSKLGT KRTLPKKNLE QISANITKFN IQGLVIIGGF EAYTGGLELM
     EGRKQYDELC IPFVIIPATV SNNVPGSDFS VGADTALNTI CTTCDRIKQS AAGTKRRVFI
     IETMGGYCGY LATMAGLAAG ADAAYIFEEP FTIRDLQANV EHLVQKMKTT VKRGLVLRNE
     KCNENYTTDF IFNLYSEEGK GIFDSRKNVL GHMQQGGSPT PFDRNFATKM GAKAMNWMTG
     KIKESYRNGR IFANTPDSGC VLGMRKRALV FQPVTELKDQ TDFEHRIPKE QWWLKLRPIL
     KILA
//
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