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C5J703 (C5J703_MYCCR) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339

Short name=ATP-PFK 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:pfkA HAMAP-Rule MF_00339
Ordered Locus Names:MCJ_005670 EMBL CAT05266.1
OrganismMycoplasma conjunctivae (strain ATCC 25834 / HRC/581 / NCTC 10147) [Complete proteome] [HAMAP]
Taxonomic identifier572263 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 SAAS SAAS022953

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. 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 SAAS SAAS012828

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339 SAAS SAAS022953.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding73 – 742ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding103 – 1064ATP By similarity HAMAP-Rule MF_00339
Region126 – 1283Substrate binding By similarity HAMAP-Rule MF_00339
Region170 – 1723Substrate binding By similarity HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region251 – 2544Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1281Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1041Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site121ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1551Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2121Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2451Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
C5J703 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: B8C74ED7174B86CE

FASTA32235,081
        10         20         30         40         50         60 
MVRKIGILTS GGDSPGMNSA LKAVAKAAIS YNIEPYFIFN GYSGIINKNI KSAKEFGYDT 

        70         80         90        100        110        120 
IGSLGGTVIG STRFVEFREL EVQKKAKEIL DELGIESLVV IGGDGTYKGG YKLHKLGVKV 

       130        140        150        160        170        180 
IGLPGTIDND IQFTDYTIGF DTALNTIVES IDKLRDTAAS HKRVFLVEVM GRHCQDLALY 

       190        200        210        220        230        240 
SGIATGSEII ITNTFRPSDE EIVEIVKQQF AKGKSNVIIN VSEYVIDDLK ALAKYIESST 

       250        260        270        280        290        300 
GFVTKHVELA HLQRGGRPSA FERILAAQMG VYAVELIVNG ESGFAVGHLN GKIEKVPLKE 

       310        320 
VFTTKNANSS FLVEKYNKIN QT 

« Hide

References

[1]"The Mycoplasma conjunctivae genome sequencing, annotation and analysis."
Calderon-Copete S.P., Wigger G., Wunderlin C., Schmidheini T., Frey J., Quail M.A., Falquet L.
BMC Bioinformatics 10:S7-S7(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25834 / HRC/581 / NCTC 10147.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM864216 Genomic DNA. Translation: CAT05266.1.
RefSeqYP_002961069.1. NC_012806.1.

3D structure databases

ProteinModelPortalC5J703.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING45361.MCJ_005670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAT05266; CAT05266; MCJ_005670.
GeneID7989360.
KEGGmco:MCJ_005670.
PATRIC20007335. VBIMycCon56923_0543.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAGIYRGYK.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC5J703_MYCCR
AccessionPrimary (citable) accession number: C5J703
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)