Reviewed, UniProtKB/Swiss-Prot Q633J8 (K6PF_BACCZ)

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
Ordered Locus Names:	BCE33L4340

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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 MF_00339
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP MF_00339
Subcellular location	Cytoplasm By similarity HAMAP MF_00339.
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	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 – 319	319	6-phosphofructokinase HAMAP MF_00339		PRO_1000059742
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)
	Q633J8-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: F655330A5044C628	FASTA	319	34,308
	10 20 30 40 50 60 MKRIGVLTSG GDSPGMNAAI RAVVRKAIFH DIEVYGIYHG YAGLISGHIE KLELGSVGDI 70 80 90 100 110 120 IHRGGTKLYT ARCPEFKDPE VRLKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEQGFPCV 130 140 150 160 170 180 GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA 190 200 210 220 230 240 GLADGAETIL IPEEEYDMED VIARLKRGSE RGKKHSIIVV AEGVGSAIDI GKHIEEATNF 250 260 270 280 290 300 DTRVTVLGHV QRGGSPSAQD RVLASRLGAR AVELLIAGKG GRCVGIQDNK LVDHDIIEAL 310 AQKHTIDKDM YQLSKELSI

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU15928.1.
RefSeq	YP_085919.1.
3D structure databases
HSSP	HSSP built from PDB template 6PFK based on UniProtKB P00512.
SMR	Q633J8. Positions 1-319.
ModBase	Search...
Protein-protein interaction databases
STRING	Q633J8.
Genome annotation databases
GeneID	3023636.
GenomeReviews	Gene locus BCE33L4340 in contig CP000001_GR.
KEGG	bcz:BCZK4340.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0205.
HOGENOM	HBG405044.
OMA	DTCLNTV.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L4340-MONOMER.
Family and domain databases
HAMAP	MF_00339. Phosphofructokinase. [Tree]
InterPro	IPR012003. ATP_PFK_prok. IPR012828. PFKA_ATP. IPR000023. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. [Graphical view]
Pfam	PF00365. PFK. 1 hit. [Graphical view]
PIRSF	PIRSF000532. ATP_PFK_prok. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
TIGRFAMs	TIGR02482. PFKA_ATP. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

K6PF_BACCZ

Accession

Primary (citable) accession number: Q633J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 25, 2004
Last modified:	February 9, 2010
This is version 43 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)