NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 393-404.
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).

[2]

SEQUENCE REVISION TO N-TERMINUS.
DOI=10.1016/0378-1119(94)00646-A; PubMed=7835697 [NCBI, ExPASy, EBI, Israel, Japan]
Todd J.F., Blakeley S.D., Dennis D.T.;
"Structure of the genes encoding the alpha- and beta-subunits of castor pyrophosphate-dependent phosphofructokinase.";
Gene 152:181-186(1995).

Comments

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.
SEQUENCE CAUTION:
- Sequence=AAA63452.1; Type=Miscellaneous discrepancy; Note=Sequencing errors. Its N-terminal part is probably wrong

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

M55191; AAA63452.1; ALT_SEQ; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B36094; B36094.

3D structure databases

HSSP

P70826; 1KZH. [HSSP ENTRY / PDB]

ModBase

P21343.

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

P21343.

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`	`1 552`	`552`	`Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta.`	`PRO_0000112050`
`ACT_SITE`	`214 214`		`Proton acceptor (By similarity).`

Sequence information

Length: 552 AA [This is the length of the unprocessed precursor]

Molecular weight: 60394 Da [This is the MW of the unprocessed precursor]

CRC64: 1AF685A66C023C8E [This is a checksum on the sequence]

        10         20         30         40         50         60 
XQVSGHRRYA AVYSEVQNSR LDHPLPLPSV LGSPFKVVDG PPSSAAGHPE EIAKLFPSLY 

        70         80         90        100        110        120 
GQPHVSLVPD DSGDVAMNQI LKIGVVLSGG QAPGGHNVIS GIFDYLQTHC KGSTMYGFRG 

       130        140        150        160        170        180 
GPAGVMKGKY VVLTPEFIYP YRNQGGFDMI CSGRDKIETP EQFKQAEETA KKLDLDGLVV 

       190        200        210        220        230        240 
IGGDDSNTNA CLLAENFRSK NLKTRVIGCP KTIDGDLKSK EVPTSFGFDT ACKIYAEMIG 

       250        260        270        280        290        300 
NVMIDARSTG KYYHFVRLMG RAASHITLEC ALQTHPNVTL IGEEVFAKKL TLKNVTDYIA 

       310        320        330        340        350        360 
DVVCKRAESG YNYGVILIPE GLIDFIPEVQ QLIAELNEIL AHDVVDEAGV WKKKLTPQCL 

       370        380        390        400        410        420 
ELFELLPLAI QEQLLLERDP HGNVQVAKIE TEKMLIQMVE TELDQRKQKG AYNAQFKGQF 

       430        440        450        460        470        480 
HFFGYEGRCG LPSNFDSTYC YALGYGAGSL LQSGKTGLIS SVGNLAAPVE ELTVGGTALT 

       490        500        510        520        530        540 
ALMDVERRHG KFKPVIKKAM VELEGAPFKK FASKREEWAL NNRYINPGPI QFVGPVANKV 

       550 
NHTLLLELGV DA

P21343 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