C5W020 (C5W020_STRSE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
6-phosphofructokinase HAMAP-Rule MF_00339
Short name=Phosphofructokinase HAMAP-Rule MF_00339
EC=2.7.1.11 HAMAP-Rule MF_00339

Alternative name(s):
Phosphohexokinase HAMAP-Rule MF_00339

Gene names

Name:	pfk EMBL CAR45106.1
Synonyms:	pfkA HAMAP-Rule MF_00339
Ordered Locus Names:	SSU0494

Organism

Streptococcus suis (strain P1/7) [Complete proteome] [HAMAP] EMBL CAR45106.1

Taxonomic identifier

218494 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus suis

Protein attributes

Sequence length	336 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 SAAS SAAS000023
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339 SAAS SAAS000023
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00339 SAAS SAAS000023.
Sequence similarities	Belongs to the phosphofructokinase family. HAMAP-Rule MF_00339

Ontologies

Keywords
Biological process	Glycolysis HAMAP-Rule MF_00339 SAAS SAAS000023
Cellular component	Cytoplasm HAMAP-Rule MF_00339 SAAS SAAS000023
Ligand	ATP-binding HAMAP-Rule MF_00339 SAAS SAAS015912 RuleBase RU004092 Magnesium HAMAP-Rule MF_00339 SAAS SAAS000023 Metal-binding HAMAP-Rule MF_00339 SAAS SAAS000023 Nucleotide-binding
Molecular function	Kinase HAMAP-Rule MF_00339 SAAS SAAS015912 RuleBase RU004092 EMBL CAR45106.1 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 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
Regions
	Nucleotide binding	21 – 25	5	ATP By similarity HAMAP-Rule MF_00339
	Nucleotide binding	154 – 158	5	ATP By similarity HAMAP-Rule MF_00339
	Nucleotide binding	171 – 187	17	ATP By similarity HAMAP-Rule MF_00339
Sites
	Active site	127	1	Proton acceptor By similarity HAMAP-Rule MF_00339
	Metal binding	185	1	Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_00339
	Metal binding	187	1	Magnesium By similarity HAMAP-Rule MF_00339
	Binding site	162	1	Substrate By similarity HAMAP-Rule MF_00339
	Binding site	244	1	Substrate By similarity HAMAP-Rule MF_00339
	Binding site	250	1	Substrate By similarity HAMAP-Rule MF_00339
	Binding site	253	1	Substrate By similarity HAMAP-Rule MF_00339

Sequences

	Sequence		Length	Mass (Da)
	C5W020 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: E17587F515A638AA	FASTA	336	35,491
	10 20 30 40 50 60 MKRIAVLTSG GDAPGMNAAI RAVVRQAISE GMEVYGINEG YAGMVAGDIH ELSARSVGDI 70 80 90 100 110 120 ISRGGTFLCS ARYPEFAKLE GQLKGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAI 130 140 150 160 170 180 GVPGTIDNDI VGTDFTIGFD TAVTTAMDAI DKIRDTSSSH RRTFVVEVMG RHAGDIALWA 190 200 210 220 230 240 GIASGADVIV VPEEDFNIND VVDRIKAGYD KGKKHSIIVL AEGVMPAAQF AEELKAAGDT 250 260 270 280 290 300 SDLRVTELGH IQRGGSPTAR DRVLASRMGA HAVKLLKEGR GGLAVGIRNE QMVENPILGT 310 320 330 AEEGALFSLT TDGKIVVNNP HKADLELADL NRNLSI

References

[1]

"Rapid evolution of virulence and drug resistance in the emerging zoonotic pathogen Streptococcus suis." Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., Cronin A., Goodhead I., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H., Diep T.S., Chinh N.T., Kehoe M. , Leigh J.A., Ward P.N., Dowson C.G., Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D., Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S.D., Barrell B.G., Schultsz C., Maskell D.J., Parkhill J. PLoS ONE 4:e6072-e6072(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: P1/7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM946016 Genomic DNA. Translation: CAR45106.1.
RefSeq	YP_003026420.1. NC_012925.1.
3D structure databases
ProteinModelPortal	C5W020.
SMR	C5W020. Positions 1-297.
ModBase	Search...
Protein-protein interaction databases
STRING	218494.SSU0494.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR45106; CAR45106; SSU0494.
GeneID	8151156.
KEGG	ssi:SSU0494.
PATRIC	19785940. VBIStrSui84581_0479.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0205.
HOGENOM	HOG000248870.
KO	K00850.
OMA	PETINGC.
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

C5W020_STRSE

Accession

Primary (citable) accession number: C5W020

Entry history

Integrated into UniProtKB/TrEMBL:	September 1, 2009
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)