[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0006-291X(91)90429-B; PubMed=1828151 [NCBI, ExPASy, EBI, Israel, Japan] Xu J., Seki M., Denda K., Yoshida M.; "Molecular cloning of phosphofructokinase 1 gene from a thermophilic bacterium, Thermus thermophilus."; Biochem. Biophys. Res. Commun. 176:1313-1318(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; "Complete genome sequence of Thermus thermophilus HB8."; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 1-25. PubMed=1830879 [NCBI, ExPASy, EBI, Israel, Japan] Xu J., Oshima T., Yoshida M.; "Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus thermophilus HB8."; J. Biochem. 109:199-203(1991).

Comments

CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
ENZYME REGULATION: Allosterically inhibited by phosphoenolpyruvate which induces the dissociation of the active tetramer into an inactive two-subunit forms.
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the 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

M71213; AAA27501.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008226; BAD71785.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_145228.1; -.

3D structure databases

HSSP

P00512; 6PFK. [HSSP ENTRY / PDB]

ModBase

P21777.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1962-MON; -.

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 HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006002;	Biological process: fructose 6-phosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00339; -; 1.
PBIL [Tree]

InterPro

IPR012003; ATP_PFK_prok.
IPR012828; PFKA_ATP.
IPR015912; Phosphofructokinase_CS.
IPR000023; Ppfruckinase.
Graphical view of domain structure.

PANTHER

PTHR13697; Ppfruckinase; 1.

Pfam

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

PIRSF

PIRSF000532; ATP_PFK_prok; 1.

PRINTS

PR00476; PHFRCTKINASE.

ProDom

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

TIGRFAMs

TIGR02482; PFKA_ATP; 1.

PROSITE

PS00433; PHOSPHOFRUCTOKINASE; 1.

ProtoNet

P21777.

Genome annotation databases

GeneID

3169721; -.

GenomeReviews

AP008226_GR; TTHA1962.

KEGG

ttj:TTHA1962; -.

Phylogenomic databases

HOGENOM

P21777; -.

Genome annotation databases

CMR

P21777; TTHA1962.

Other

UniRef

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

Keywords

Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 322`	`322`	`6-phosphofructokinase isozyme 1.`	`PRO_0000112001`
`NP_BIND`	`21 25`	`5`	`ATP (By similarity).`
`NP_BIND`	`155 159`	`5`	`ATP (By similarity).`
`NP_BIND`	`172 188`	`17`	`ATP (By similarity).`
`ACT_SITE`	`128 128`		`Proton acceptor (By similarity).`
`METAL`	`186 186`		`Magnesium; via carbonyl oxygen (By similarity).`
`METAL`	`188 188`		`Magnesium (By similarity).`
`BINDING`	`163 163`		`Substrate (By similarity).`
`BINDING`	`246 246`		`Substrate (By similarity).`
`BINDING`	`252 252`		`Substrate (By similarity).`
`BINDING`	`255 255`		`Substrate (By similarity).`
`CONFLICT`	`111 111`		`C -> F (in Ref. 1; AAA27501).`
`CONFLICT`	`273 273`		`A -> P (in Ref. 1; AAA27501).`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 33537 Da [This is the MW of the unprocessed precursor]

CRC64: 608CD4053E6ACEA3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV PLGVRDVANI 

        70         80         90        100        110        120 
IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI GGDGTFRGAL CLVEEHGMPV 

       130        140        150        160        170        180 
VGVPGTIDND LYGTDYTIGF DTAVNTALEA IDRIRDTAAS HERVFFIEVM GRHAGFIALD 

       190        200        210        220        230        240 
VGLAGGAEVI AVPEEPVDPK AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH 

       250        260        270        280        290        300 
LQVEARVTVL GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK 

       310        320 
EAVERRKDIN RALLRLSQVL AL

P21777 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