PFKA2_ASPOR
ID PFKA2_ASPOR Reviewed; 775 AA.
AC Q9HGZ0; Q2TWS2;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=pfkB; ORFNames=AO090010000444;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.;
RT "Molecular cloning and characterization of glycolytic gene from Aspergillus
RT oryzae.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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DR EMBL; AB032271; BAB12231.1; -; mRNA.
DR EMBL; AP007175; BAE66301.1; -; Genomic_DNA.
DR RefSeq; XP_001827434.1; XM_001827382.2.
DR AlphaFoldDB; Q9HGZ0; -.
DR SMR; Q9HGZ0; -.
DR STRING; 510516.Q9HGZ0; -.
DR EnsemblFungi; BAE66301; BAE66301; AO090010000444.
DR GeneID; 5999568; -.
DR KEGG; aor:AO090010000444; -.
DR VEuPathDB; FungiDB:AO090010000444; -.
DR HOGENOM; CLU_011053_0_0_1; -.
DR OMA; SRYAVKC; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..775
FT /note="ATP-dependent 6-phosphofructokinase 2"
FT /id="PRO_0000112037"
FT REGION 1..390
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 391..404
FT /note="Interdomain linker"
FT REGION 405..775
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 88..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 118..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 164..166
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 201
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 208..210
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 292
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 298..301
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 537..541
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 582..584
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 640
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 672..675
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
SQ SEQUENCE 775 AA; 84727 MW; B5A78C4F7EE43848 CRC64;
MTNTILDTYS SRRKPRRIGI LTSGGDAPGM NGAIRAVVRT AIQNGCEAWA IHEGYEGLIQ
GGAMMHPLYW EDVRGFLSRG GTLIGSVRCD RFREREGRLQ AARNMVLFGI DALVVCGGDG
SLTGADLFRS EWPELLNELV STGVLTVAQV APHQNLNIVG LLGSIDNDFS GTDATIGCYS
ALTRICEAVD AVFDTASSHR RGFVVEVMGR HCGWLALMAA IATGADWLFI PERPPRDGWE
DDMCSIITKN RNRGKRRTIV ILAEGAQDSN LDRISSSAVK DVLSKRLGLD TRVTVLGHIQ
RGGSPCAYDR WLSTLQGIHA VKAVLSMTPE SPSPVVIIQE NRIRTSSLAE TVALTKEANA
SMHAKEFEKA ATLRDPEFME YHSAYRHLNT SDHPKMVLPE DKRMRVAIIH VGAPAAGMNP
ATRAVVAYCL TRGHTPIAIH NGFPGLCRHH DDTPGSVREM HWLESGDWIN DGGSDIGTNA
GLPLDDIETT AQCFERYKFD ALFVIGGFEA FTAVSQLRKA RKQYLAFRIP LVLLPASMSN
NVPGTEYSLG SDTSLNTLVY FCDVVRQSAS SSGHSVFVVE AQGAEYQATA AALAAGAMTV
YTPERGITLQ SLSNDIEYLR QQFSKDHGAN RSGKLIIRND QTSTIYSTTE IANIIKHEAK
NRFDAQGVVP GHFQQGGKVS PIDRIRAFRL AVKCMEHLET FAGQSPEEIM NDENSATVIS
IKQSRILLLP MGGPTGVEAT DTDWKRQRPK TQNWLEIQEA VDSLSGRSSL YAIPN
