Q8Y6W0 (K6PF_LISMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphofructokinase
Short name=Phosphofructokinase
EC=2.7.1.11

Alternative name(s):
Phosphohexokinase

Gene names

Name:	pfkA
Synonyms:	pfk
Ordered Locus Names:	lmo1571

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphofructokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	6-phosphofructokinase activity Inferred from electronic annotation. Source: HAMAP ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	6-phosphofructokinase HAMAP-Rule MF_00339		PRO_0000111962
Regions
	Nucleotide binding	21 – 25	5	ATP By similarity
	Nucleotide binding	154 – 158	5	ATP By similarity
	Nucleotide binding	171 – 187	17	ATP By similarity
Sites
	Active site	127	1	Proton acceptor By similarity
	Metal binding	185	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	187	1	Magnesium By similarity
	Binding site	162	1	Substrate By similarity
	Binding site	243	1	Substrate By similarity
	Binding site	249	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y6W0 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: AE15D577691BA74F	FASTA	319	34,420
	10 20 30 40 50 60 MKRIAILTSG GDAPGMNAAT RAVVRKAIYE GLEVYGINYG FLGLVNGDIR KLELGSVGDL 70 80 90 100 110 120 LHRGGTFLYS ARYPEFATEE GQLKGIEQLK KHQIDGLVVI GGDGSYHGAE ALTKRGFPTI 130 140 150 160 170 180 GIPGTIDNDI SGTDFTIGFD TALNTVLDAL DKIRDTATSH ERTFIIEVMG RDAGDIALWS 190 200 210 220 230 240 GLAGGAEAII VPEESFNMDD VVDRLNKGRE RGKKHSIIVV AEGVMSGNEF AKQLAEYGDY 250 260 270 280 290 300 HARVTVLGHV QRGGSPTAFD RVLASRLGAR SVELLLENRG GLAVGIRENR IVENDISEIL 310 KEKHTLDQKL FDLASILSI

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591979 Genomic DNA. Translation: CAC99649.1.
PIR	AC1271.
RefSeq	NP_465096.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y6W0.
SMR	Q8Y6W0. Positions 1-319.
ModBase	Search...
Protein-protein interaction databases
STRING	169963.lmo1571.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC99649; CAC99649; CAC99649.
GeneID	986951.
KEGG	lmo:lmo1571.
PATRIC	20312271. VBILisMon69206_1612.
Organism-specific databases
GenoList	LMO1571.
Phylogenomic databases
eggNOG	COG0205.
HOGENOM	HOG000248870.
KO	K00850.
OMA	DFDARAN.
ProtClustDB	PRK03202.
Enzyme and pathway databases
UniPathway	UPA00109; UER00182.
Family and domain databases
HAMAP	MF_00339. Phosphofructokinase.
InterPro	IPR012003. ATP_PFK_prok. IPR012828. PFKA_ATP. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view]
Pfam	PF00365. PFK. 1 hit. [Graphical view]
PIRSF	PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
SUPFAM	SSF53784. Ppfruckinase. 1 hit.
TIGRFAMs	TIGR02482. PFKA_ATP. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

K6PF_LISMO

Accession

Primary (citable) accession number: Q8Y6W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program