ID   K6P2_ASPOR     STANDARD;      PRT;   775 AA.
AC   Q9HGZ0;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   6-phosphofructokinase beta subunit (EC 2.7.1.11) (Phosphofructokinase
DE   2) (Phosphohexokinase) (6PF-1-K beta subunit).
GN   Name=PFKB;
OS   Aspergillus oryzae.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5062;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=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.
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: Key control step of glycolysis.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC       subfamily.
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DR   EMBL; AB032271; BAB12231.1; -.
DR   HSSP; P06998; 2PFK.
DR   InterPro; IPR009161; PFK_euk.
DR   InterPro; IPR000023; Ppfruckinase.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   ProDom; PD000707; Ppfruckinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; Repeat;
KW   Transferase.
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   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
//