NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 277-295.
STRAIN=cv. Kennebec;
PubMed=2170409 [NCBI, ExPASy, EBI, Israel, Japan]
Carlisle S.M., Blakeley S.D., Hemmingsen S.M., Trevanion S.J., Hiyoshi T., Kruger N.J., Dennis D.T.;
"Pyrophosphate-dependent phosphofructokinase. Conservation of protein sequence between the alpha- and beta-subunits and with the ATP-dependent phosphofructokinase.";
J. Biol. Chem. 265:18366-18371(1990).

Comments

FUNCTION: The alpha subunit may be involved in the regulation of PFP by Fru-2,6-P.
CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate.
ENZYME REGULATION: Fru-2,6-P is an activator of the plant enzyme.
SUBUNIT: Tetramer of two alpha and two beta chains.
MISCELLANEOUS: The active site might be on the beta subunit.
SIMILARITY: Belongs to the pyrophosphate-dependent phosphofructokinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55190; AAA63451.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36094; A36094.

3D structure databases

HSSP

P70826; 1KZH. [HSSP ENTRY / PDB]

ModBase

P21342.

Ontologies

GO:0005945;	Cellular component: 6-phosphofructokinase complex (inferred from electronic annotation from InterPro).
GO:0003872;	Molecular function: 6-phosphofructokinase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0047334;	Molecular function: diphosphate-fructose-6-phosphate 1-phosphotransferase activity (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR011183; PfpB_PPi_PFK.
IPR000023; Ppfruckinase.
Graphical view of domain structure.

PANTHER

PTHR13697; Ppfruckinase; 1.

Pfam

PF00365; PFK; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005677; PPi_PFK_PfpB; 1.

PRINTS

PR00476; PHFRCTKINASE.

ProDom

PD000707; Ppfruckinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02477; PFKA_PPi; 1.

ProtoNet

P21342.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; ATP-binding; Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 616`	`616`		`Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha.`	`PRO_0000112048`

Sequence information

Length: 616 AA [This is the length of the unprocessed precursor]

Molecular weight: 67157 Da [This is the MW of the unprocessed precursor]

CRC64: 2D33EF2ADF3AA0AF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDADYGIPRE LSDLQKLRSH YHPELPPCLQ GTTVRVELRD ATTAADPAGE HTIKRFFPHT 

        70         80         90        100        110        120 
YGQPLAHFLR ATAKVPDAQI ITEHPAIRVG VLFCGRQSPG GHNVIWGLHD ALKVHNPKNI 

       130        140        150        160        170        180 
LLGFLGGSEG LFAQKTLEIT DDVLATYKNQ GGYDMLGRTK DQIRTTEQVN AAMAACKALK 

       190        200        210        220        230        240 
LDGLVIIGGV TSNTDAAHLA EKFAETKCLT KVVGVPVTLN GDLKNQFVEA NVGFDTICKV 

       250        260        270        280        290        300 
NSQLISNVCT DALSAEKYYY FIRLMGRKAS HVALDCTLQS HPNMVILGEE VAASKLTIFD 

       310        320        330        340        350        360 
ITQQICDAVQ ARAEHDKNHG VILLPEGLIE SIPEVYSLLQ EIHGLLRQGV SADKISSQLS 

       370        380        390        400        410        420 
PWASALFEFL PHFIRKQLLL HPESDDSAQL SQIETEKLIA HLVETEMNKR LKEGTYKGKK 

       430        440        450        460        470        480 
FNAICHFFGY QARGSLPSKF DCDYAYVLGH VCYHILAAGL NGYMATITNL KNPANKWHCG 

       490        500        510        520        530        540 
ASPISAMMTV KRYGRGPGKA SIGVPALHPA TVDLRGKSYE LLSQNATKFL LDDVYRNPGP 

       550        560        570        580        590        600 
LQFDGPGADA KAGSLVVEDA DYIGAIKKLQ EYLDKVRTIV KPGCSQDVLK AALSAMASVT 

       610 
DILSVISSPS SVSTPF

P21342 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools