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D3V6X6 (D3V6X6_XENBS) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 28. 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 EMBL CBJ83405.1
Ordered Locus Names:XBJ1_4302 EMBL CBJ83405.1
OrganismXenorhabdus bovienii (strain SS-2004) [Complete proteome] [HAMAP] EMBL CBJ83405.1
Taxonomic identifier406818 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeXenorhabdus

Protein attributes

Sequence length325 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 binding76 – 772ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding106 – 1094ATP By similarity HAMAP-Rule MF_00339
Region25 – 295Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region129 – 1313Substrate binding By similarity HAMAP-Rule MF_00339
Region173 – 1753Substrate binding By similarity HAMAP-Rule MF_00339
Region189 – 1913Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region219 – 2213Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region255 – 2584Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1311Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1071Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site151ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1581Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1661Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2171Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2281Substrate By similarity HAMAP-Rule MF_00339
Binding site2491Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
D3V6X6 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: E3A82561775ADB5D

FASTA32535,775
        10         20         30         40         50         60 
MINKIKRIGV LTSGGDAPGM NAAIRGVVRV ALTEGLEVYG IYDGYLGLYE NRMKKLDRFS 

        70         80         90        100        110        120 
VSDMINRGGT FLGSARFPEF RDDKVREIAI ENMRKNDIDA LVVIGGDGSY LGAKKLTEAG 

       130        140        150        160        170        180 
FPCIGLPGTI DNDVAGTDYT IGYFTALETV VEAIDRLRDT STSHKRISIV EVMGRYCGDL 

       190        200        210        220        230        240 
TLSAAIAGGC EFIVLPENEI PFDREELLAE IKAGIQKGKR HAIVAITEHV CNVDELAKYI 

       250        260        270        280        290        300 
EAETRHETRA TVLGHIQRGG APVAYDRILA SRMGAYSVQL LMEGFGGRCV GIQNEKLVHH 

       310        320 
DIIDAVQNMQ RVFKKDWLET AKQLY 

« Hide

References

[1]"Complete genome sequence of Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."
Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., Suen G.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS-2004.
[2]"The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus: convergent lifestyles from divergent genomes."
Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E., Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J. expand/collapse author list , Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.
PLoS ONE 6:e27909-e27909(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS-2004 EMBL CBJ83405.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN667741 Genomic DNA. Translation: CBJ83405.1.
RefSeqYP_003470163.1. NC_013892.1.

3D structure databases

ProteinModelPortalD3V6X6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBJ83405; CBJ83405; XBJ1_4302.
GeneID8833935.
KEGGxbo:XBJ1_4302.
PATRIC35303161. VBIXenBov95754_3872.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.

Enzyme and pathway databases

BioCycXBOV406818:GHLH-4305-MONOMER.
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 nameD3V6X6_XENBS
AccessionPrimary (citable) accession number: D3V6X6
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)