ID   K6PF2_ASPOR             Reviewed;         775 AA.
AC   Q9HGZ0; Q2TWS2;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   30-NOV-2010, entry version 59.
DE   RecName: Full=6-phosphofructokinase subunit beta;
DE            EC=2.7.1.11;
DE   AltName: Full=6PF-1-K subunit beta;
DE   AltName: Full=Phosphofructokinase 2;
DE   AltName: Full=Phosphohexokinase;
GN   Name=pfkB; ORFNames=AO090010000444;
OS   Aspergillus oryzae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5062;
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   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- ENZYME REGULATION: Allosterically inhibited by ATP and activated
CC       by AMP and fructose 2,6-bisphosphate (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC       subfamily.
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DR   EMBL; AB032271; BAB12231.1; -; mRNA.
DR   EMBL; AP007175; BAE66301.1; -; Genomic_DNA.
DR   RefSeq; XP_001827434.1; XM_001827382.1.
DR   ProteinModelPortal; Q9HGZ0; -.
DR   SMR; Q9HGZ0; 16-356, 405-760.
DR   EnsemblFungi; CADAORAT00004509; CADAORAP00004429; CADAORAG00004509.
DR   GeneID; 5999568; -.
DR   GenomeReviews; AP007175_GR; pfkB.
DR   KEGG; aor:AO090010000444; -.
DR   OrthoDB; EOG902Z9M; -.
DR   PhylomeDB; Q9HGZ0; -.
DR   BRENDA; 2.7.1.11; 2240.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA: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:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR009161; 6-phosphofructokinase_euk.
DR   InterPro; IPR022953; Phosphofructokinase.
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; Ppfruckinase; 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   Repeat; Transferase.
FT   CHAIN         1    775       6-phosphofructokinase subunit beta.
FT                                /FTId=PRO_0000112037.
FT   NP_BIND      35     39       ATP (By similarity).
FT   NP_BIND     193    197       ATP (By similarity).
FT   NP_BIND     210    226       ATP (By similarity).
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   METAL       224    224       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
FT   BINDING     298    298       Substrate (By similarity).
FT   BINDING     301    301       Substrate (By similarity).
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
//