O42938 (K6PF_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
6PF-1-K
Phosphohexokinase

Gene names

Name:	pfk1
ORF Names:	SPBC16H5.02

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May also have a role in cell cycle regulation. Ref.3
Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphofructokinase family. Two domains subfamily.
Sequence caution	The sequence BAA13773.1 differs from that shown. Reason: Frameshift at position 836.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
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 sequence orthology. Source: PomBase
Cellular_component	6-phosphofructokinase complex Inferred from direct assay PubMed 17643314. Source: PomBase
Molecular_function	6-phosphofructokinase activity Inferred from sequence orthology. Source: PomBase ATP binding Inferred from direct assay PubMed 17643314. Source: PomBase fructose-6-phosphate binding Inferred from direct assay PubMed 17643314. Source: PomBase 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 – 942	942	6-phosphofructokinase		PRO_0000112043
Regions
	Nucleotide binding	214 – 218	5	ATP By similarity
	Nucleotide binding	372 – 376	5	ATP By similarity
	Nucleotide binding	389 – 405	17	ATP By similarity
Sites
	Active site	345	1	Proton acceptor By similarity
	Metal binding	403	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	380	1	Substrate By similarity
	Binding site	472	1	Substrate By similarity
	Binding site	478	1	Substrate By similarity
	Binding site	481	1	Substrate By similarity
Amino acid modifications
	Modified residue	43	1	Phosphoserine Ref.4
	Modified residue	45	1	Phosphoserine Ref.4
	Modified residue	85	1	Phosphoserine Ref.4
	Modified residue	160	1	Phosphoserine Ref.4
	Modified residue	163	1	Phosphoserine Ref.4
	Modified residue	167	1	Phosphoserine Ref.4
	Modified residue	171	1	Phosphoserine Ref.4
	Modified residue	175	1	Phosphothreonine Ref.4
	Modified residue	600	1	Phosphoserine Ref.4
	Modified residue	602	1	Phosphothreonine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O42938 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: C6052AF7C1DB75B4	FASTA	942	102,555
	10 20 30 40 50 60 MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV CNESLREDWM 70 80 90 100 110 120 HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL VFYYPNLLDL LKQLSADAIK 130 140 150 160 170 180 YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN PFAHANLKKS EESGAASNLE SGLATPVVET 190 200 210 220 230 240 LKKATTSDKP AGVKKKIAVM TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG 250 260 270 280 290 300 GDMIKQLQWG DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS 310 320 330 340 350 360 LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS TDVTIGAFSS 370 380 390 400 410 420 LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL ATGADFVFIP ERPAEVGKWQ 430 440 450 460 470 480 DELCNSLSSV RKLGKRKSIV IVAEGAIDSE LNHISPEDIK NLLVERLHLD TRVTTLGHVQ 490 500 510 520 530 540 RGGIPCAYDR MLATLQGVDA VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD 550 560 570 580 590 600 AIEKKQFAHA MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS 610 620 630 640 650 660 ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE IGTNRDTPDL 670 680 690 700 710 720 DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP SFRIPMAIIP ATISNNVPGT 730 740 750 760 770 780 EFSLGCDTCL NAVMEYCDTI KQSASASRRR VFVCEVQGGR SGYIATVGGL ITGASAIYTP 790 800 810 820 830 840 EDGISLDMLR KDIDHLKATF ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF 850 860 870 880 890 900 SARTAVPGHV QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV 910 920 930 940 SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-942. Strain: PR745.
[3]	"Genome-wide search of Schizosaccharomyces pombe genes causing overexpression-mediated cell cycle defects." Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J. Yeast 19:1139-1151(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL CYCLE REGULATION.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-85; SER-160; SER-163; SER-167; SER-171; THR-175; SER-600 AND THR-602, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17900.1. D89110 mRNA. Translation: BAA13773.1. Frameshift.
PIR	T39624. T42087.
RefSeq	NP_595946.1. NM_001021854.2.
3D structure databases
ProteinModelPortal	O42938.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC16H5.02-1.
Proteomic databases
PaxDb	O42938.
PRIDE	O42938.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
GeneID	2539972.
KEGG	spo:SPBC16H5.02.
Organism-specific databases
PomBase	SPBC16H5.02.
Phylogenomic databases
eggNOG	COG0205.
HOGENOM	HOG000200154.
KO	K00850.
OMA	VYHMASK.
OrthoDB	EOG418FWH.
Enzyme and pathway databases
SABIO-RK	O42938.
UniPathway	UPA00109; UER00182.
Family and domain databases
InterPro	IPR009161. 6-phosphofructokinase_euk. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view]
Pfam	PF00365. PFK. 2 hits. [Graphical view]
PIRSF	PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
SUPFAM	SSF53784. Ppfruckinase. 2 hits.
TIGRFAMs	TIGR02478. 6PF1K_euk. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801115.

Entry information

Entry name

K6PF_SCHPO

Accession

Primary (citable) accession number: O42938
Secondary accession number(s): P78762

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program