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P65691 (PFKA_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:Mb3035c
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length343 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_01976

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_01976

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01976

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_01976

Subunit structure

Homodimer or homotetramer By similarity. HAMAP-Rule MF_01976

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01976.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_01976
PRO_0000111969

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region273 – 2764Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site101ATP; via amide nitrogen By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2231Substrate By similarity
Binding site2671Substrate; shared with dimeric partner By similarity
Site1051Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P65691 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 826E5FF16A6ECABA

FASTA34336,880
        10         20         30         40         50         60 
MRIGVLTGGG DCPGLNAVIR AVVRTCHARY GSSVVGFQNG FRGLLENRRV QLHNDDRNDR 

        70         80         90        100        110        120 
LLAKGGTMLG TARVHPDKLR AGLPQIMQTL DDNGIDVLIP IGGEGTLTAA SWLSEENVPV 

       130        140        150        160        170        180 
VGVPKTIDND IDCTDVTFGH DTALTVATEA IDRLHSTAES HERVMLVEVM GRHAGWIALN 

       190        200        210        220        230        240 
AGLASGAHMT LIPEQPFDIE EVCRLVKGRF QRGDSHFICV VAEGAKPAPG TIMLREGGLD 

       250        260        270        280        290        300 
EFGHERFTGV AAQLAVEVEK RINKDVRVTV LGHIQRGGTP TAYDRVLATR FGVNAADAAH 

       310        320        330        340 
AGEYGQMVTL RGQDIGRVPL ADAVRKLKLV PQSRYDDAAA FFG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44303.1.
RefSeqNP_856680.1. NC_002945.3.

3D structure databases

ProteinModelPortalP65691.
SMRP65691. Positions 2-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb3035c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96722; CAD96722; Mb3035c.
GeneID1093228.
KEGGmbo:Mb3035c.
PATRIC18008410. VBIMycBov88188_3335.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMARGDFGRM.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_01976. Phosphofructokinase_III.
InterProIPR012003. ATP_PFK_prok.
IPR012829. PFK.
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.
TIGRFAMsTIGR02483. PFK_mixed. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_MYCBO
AccessionPrimary (citable) accession number: P65691
Secondary accession number(s): O53257, X2BMF7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways