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   07-JUN-2017, entry version 99.
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.
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
RT   Aspergillus 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.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., 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
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- ENZYME REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" 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   ProteinModelPortal; Q9HGZ0; -.
DR   SMR; Q9HGZ0; -.
DR   EnsemblFungi; BAE66301; BAE66301; AO090010000444.
DR   GeneID; 5999568; -.
DR   KEGG; aor:AOR_1_724024; -.
DR   HOGENOM; HOG000200154; -.
DR   KO; K00850; -.
DR   OrthoDB; EOG092C0LOE; -.
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-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   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   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; Complete proteome; Cytoplasm;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    775       ATP-dependent 6-phosphofructokinase 2.
FT                                /FTId=PRO_0000112037.
FT   NP_BIND      88     89       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     118    121       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    390       N-terminal catalytic PFK domain 1.
FT   REGION      164    166       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      208    210       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      298    301       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      391    404       Interdomain linker.
FT   REGION      405    775       C-terminal regulatory PFK domain 2.
FT   REGION      537    541       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      582    584       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      672    675       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       119    119       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      25     25       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     201    201       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     292    292       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     640    640       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                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
//