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A1SUH6 (A1SUH6_PSYIN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 64. 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:Ping_1316 EMBL ABM03141.1
OrganismPsychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP] EMBL ABM03141.1
Taxonomic identifier357804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPsychromonadaceaePsychromonas

Protein attributes

Sequence length320 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. SAAS SAAS012828 HAMAP-Rule MF_00339

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
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner 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
Region250 – 2534Substrate 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 site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2441Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
A1SUH6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2825057520B21815

FASTA32034,922
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNSA IRAVVRCALA NDIEVYGIYD GYAGLHKGNL KQLTRHSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFKEE SVRQEAIKNL EKHGIEALVV IGGDGSYMGA KKLSEMGYPC 

       130        140        150        160        170        180 
IGIPGTIDND IAGTDYTIGF MTCLNTIVDA VDRLRDTSSS HNRISIVEVM GRYCGDLTLW 

       190        200        210        220        230        240 
SAIAGGSEYV VLPEIGFDEA ELFEHIETGE ASGKKHAIIM ITEHVTDVTE LAKRIEAKTG 

       250        260        270        280        290        300 
RETRATILGH IQRGGSPMAF DRVLASRMGA RAVELLIDGK SARCIGLQYG KMVDHDIIEC 

       310        320 
LEEMERPFRE DLYNLSNVLF 

« Hide

References

[1]"Complete sequence of Psychromonas ingrahamii 37."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 37 EMBL ABM03141.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000510 Genomic DNA. Translation: ABM03141.1.
RefSeqYP_942740.1. NC_008709.1.

3D structure databases

ProteinModelPortalA1SUH6.
SMRA1SUH6. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357804.Ping_1316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM03141; ABM03141; Ping_1316.
GeneID4625848.
KEGGpin:Ping_1316.
PATRIC23067671. VBIPsyIng103130_1445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAMELREGH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycPING357804:GJBJ-1392-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 nameA1SUH6_PSYIN
AccessionPrimary (citable) accession number: A1SUH6
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)