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A4SGR6 (A4SGR6_PROVI) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length359 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 binding107 – 1082ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding137 – 1404ATP By similarity HAMAP-Rule MF_00339
Region56 – 605Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region161 – 1633Substrate binding By similarity HAMAP-Rule MF_00339
Region205 – 2073Substrate binding By similarity HAMAP-Rule MF_00339
Region221 – 2233Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region288 – 2914Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1631Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1381Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site461ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1901Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1981Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2581Substrate By similarity HAMAP-Rule MF_00339
Binding site2821Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
A4SGR6 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 9F7F93EA3913ECE8

FASTA35938,658
        10         20         30         40         50         60 
MKGQPRLRES RTLHPPMATM TRKSDNDQLS FTSGRIKKIG ILTSGGDAPG MNAAIRAATR 

        70         80         90        100        110        120 
SAIAAGREAV GILRGYQGMI DGDFIPLQST DVSGILQLGG TMLKTARCKE FRTPEGRRRA 

       130        140        150        160        170        180 
KEQLTAAAID AVIVIGGDGS FTGAWVMSQE CDIPFVGIPA TIDNDMYGTD YTIGYETALN 

       190        200        210        220        230        240 
SVVCAVDKIK DTARSHGRIF FIEVMGHEAG LLALNSGIAC GAEVILIPES KAQHEELQKF 

       250        260        270        280        290        300 
LEKGYRDKES SGIVMVAEGD EAGGALHIAE QIRRDHPDLD VRISILGHIQ RGGSPVARDR 

       310        320        330        340        350 
INATRMGIAA VDALLNDQKS IMIGLDNNRI VHVTFNKAVK MNHSIDTGLL EVHNLLNGM 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265 EMBL ABP37675.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37675.1.
RefSeqYP_001131177.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SGR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37675; ABP37675; Cvib_1665.
GeneID4970059.
KEGGpvi:Cvib_1665.
PATRIC21397866. VBIChlPha132153_1750.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1713-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 nameA4SGR6_PROVI
AccessionPrimary (citable) accession number: A4SGR6
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)