Reviewed, UniProtKB/Swiss-Prot O08333 (K6PF1_STRCO)

Names and origin

Protein names

Recommended name:
    6-phosphofructokinase 1
    EC=2.7.1.11
Alternative name(s):
    Phosphofructokinase 1
    Phosphohexokinase 1
    ATP-PFK

Gene names

Name:	pfkA1
Synonyms:	pfk1, pfkA
Ordered Locus Names:	SCO2119
ORF Names:	SC6E10.13c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP MF_00339
Enzyme regulation	Allosterically inhibited by phosphoenolpyruvate. HAMAP MF_00339
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP MF_00339
Subunit structure	Homotetramer By similarity.
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
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 magnesium 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 – 342	342	6-phosphofructokinase 1 HAMAP MF_00339		PRO_0000111986
Regions
	Nucleotide binding	20 – 24	5	ATP By similarity
	Nucleotide binding	155 – 159	5	ATP By similarity
	Nucleotide binding	172 – 188	17	ATP By similarity
Sites
	Active site	128	1	Proton acceptor By similarity
	Metal binding	186	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	266	1	Substrate By similarity
	Binding site	272	1	Substrate By similarity
	Binding site	275	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O08333-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: CEEFC7B74092AB34	FASTA	342	36,664
	10 20 30 40 50 60 MKVGVLTGGG DCPGLNAVIR AVVRKGVQEY GYDFTGFRDG WRGPLEGDTV PLDIPAVRGI 70 80 90 100 110 120 LPRGGTVLGS SRTNPLKQRD GIRRIKDNLA ALGVEALITI GGEDTLGVAT RLADEYGVPC 130 140 150 160 170 180 VGVPKTIDND LSATDYTFGF DTAVGIATEA IDRLHTTAES HMRVLVVEVM GRHAGWIALH 190 200 210 220 230 240 SGLAGGANVI LIPEQRFDVE QVCSWVTSRF RASYAPIVVV AEGAMPRDGD MVLKDESLDS 250 260 270 280 290 300 YGHVRLSGVG EWLAKQIEKR TGNEARTTVL GHVQRGGTPS AFDRWLATRF GLHAVDCVHD 310 320 330 340 GDFGKMVALR GTDIVRVPIA EATARLKTVD PALYEEVGVF FG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)." Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L. Appl. Environ. Microbiol. 63:956-961(1997) [PubMed: 9055413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: A3(2) / 1109.
[2]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U51728 Genomic DNA. Translation: AAC45135.1. AL939111 Genomic DNA. Translation: CAB51967.1.
PIR	T35500.
RefSeq	NP_626376.1.
3D structure databases
HSSP	HSSP built from PDB template 3PFK based on UniProtKB P00512.
ModBase	Search...
Genome annotation databases
GeneID	1097553.
GenomeReviews	Gene locus SCO2119 in contig AL645882_GR.
KEGG	sco:SCO2119.
NMPDR	fig|100226.1.peg.2085.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O08333.
OMA	ESHHRIM.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO2119-MON.
BRENDA	2.7.1.11. 1084.
Family and domain databases
HAMAP	MF_00339. [Tree]
InterPro	IPR012003. ATP_PFK_prok. IPR012829. PFK. IPR000023. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. [Graphical view]
Pfam	PF00365. PFK. 1 hit. [Graphical view]
PIRSF	PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
ProDom	PD000707. Ppfruckinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02483. PFK_mixed. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

K6PF1_STRCO

Accession

Primary (citable) accession number: O08333

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)