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F9Z4U8 (F9Z4U8_ODOSD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 18. 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:Odosp_0362 EMBL ADY31457.1
OrganismOdoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus) [Complete proteome] [HAMAP] EMBL ADY31457.1
Taxonomic identifier709991 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeOdoribacter

Protein attributes

Sequence length326 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 SAAS SAAS022953 HAMAP-Rule MF_00339.

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 binding75 – 762ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding105 – 1084ATP By similarity HAMAP-Rule MF_00339
Region24 – 285Allosteric 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
Region256 – 2594Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1311Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1061Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site141ATP; 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 site2261Substrate By similarity HAMAP-Rule MF_00339
Binding site2501Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
F9Z4U8 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 3022F3FB43993F2D

FASTA32634,929
        10         20         30         40         50         60 
MGRIKRIGVL TSGGDAPGMN AAIRAVVRTA IFNGCEAYGI FGGYQGLIEG DIKRLKSNDV 

        70         80         90        100        110        120 
SNIIQRGGTI LKSARSMEFR TPEGRTKAAQ MLAEHKIDAL VVIGGDGSFT GAKLLIQEHD 

       130        140        150        160        170        180 
IPVVGIPGTI DNDLYGTDST IGYDTAVNTA VEAVDKIKDT ASAHNRLFFV EVMGRDAGFI 

       190        200        210        220        230        240 
ALRTAIATGA EAVLVPEVET DLTDLEHFIE KDYNPKTSSG IVIVAEGEKS GGAYSIAEKV 

       250        260        270        280        290        300 
AQKHPEYDIR VSVLGHMQRG GSPSQFDRVL ASQLGAAAVD ALMDDQKSIM LGIMNKEIVH 

       310        320 
VPFNKTIKHT KNLNPELLNL VRILSI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002544 Genomic DNA. Translation: ADY31457.1.
RefSeqYP_004251637.1. NC_015160.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY31457; ADY31457; Odosp_0362.
GeneID10252068.
KEGGosp:Odosp_0362.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.
OMAAKLERGH.

Enzyme and pathway databases

BioCycOSPL709991:GI68-365-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 nameF9Z4U8_ODOSD
AccessionPrimary (citable) accession number: F9Z4U8
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)