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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM)
  4. Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei25ATP; via amide nitrogenUniRule annotation1
Metal bindingi119Magnesium; catalyticUniRule annotation1
Active sitei166Proton acceptorUniRule annotation1
Binding sitei201Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Binding sitei292Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei471Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei566Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei629Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei655Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei735Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 89ATPUniRule annotation2
Nucleotide bindingi118 – 121ATPUniRule annotation4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.11. 1749.
SABIO-RKP00511.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKM
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001120192 – 780ATP-dependent 6-phosphofructokinase, muscle typeAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1
Modified residuei133PhosphoserineBy similarity1
Modified residuei377PhosphoserineBy similarity1
Glycosylationi530O-linked (GlcNAc)By similarity1
Modified residuei667PhosphoserineBy similarity1
Modified residuei775Phosphoserine; by PKA1 Publication1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiP00511.

Interactioni

Subunit structurei

Homo- and heterotetramers. Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).By similarity

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014991.

Structurei

Secondary structure

1780
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 13Combined sources4
Beta strandi17 – 21Combined sources5
Helixi30 – 43Combined sources14
Beta strandi47 – 49Combined sources3
Helixi54 – 59Combined sources6
Helixi62 – 64Combined sources3
Helixi71 – 73Combined sources3
Helixi91 – 93Combined sources3
Helixi95 – 108Combined sources14
Beta strandi112 – 117Combined sources6
Helixi119 – 130Combined sources12
Helixi133 – 138Combined sources6
Turni139 – 143Combined sources5
Turni146 – 148Combined sources3
Helixi149 – 151Combined sources3
Beta strandi157 – 163Combined sources7
Helixi178 – 193Combined sources16
Beta strandi202 – 207Combined sources6
Helixi214 – 223Combined sources10
Helixi240 – 252Combined sources13
Beta strandi256 – 260Combined sources5
Beta strandi269 – 271Combined sources3
Helixi276 – 286Combined sources11
Beta strandi291 – 294Combined sources4
Helixi307 – 325Combined sources19
Beta strandi334 – 339Combined sources6
Beta strandi342 – 347Combined sources6
Helixi348 – 363Combined sources16
Helixi367 – 374Combined sources8
Helixi377 – 389Combined sources13
Beta strandi402 – 410Combined sources9
Helixi415 – 428Combined sources14
Beta strandi432 – 438Combined sources7
Helixi441 – 445Combined sources5
Beta strandi448 – 450Combined sources3
Turni453 – 456Combined sources4
Helixi475 – 477Combined sources3
Helixi478 – 487Combined sources10
Beta strandi493 – 498Combined sources6
Helixi499 – 514Combined sources16
Beta strandi522 – 527Combined sources6
Helixi542 – 556Combined sources15
Turni557 – 560Combined sources4
Beta strandi562 – 564Combined sources3
Beta strandi566 – 572Combined sources7
Helixi579 – 587Combined sources9
Beta strandi591 – 594Combined sources4
Beta strandi596 – 598Combined sources3
Helixi602 – 616Combined sources15
Beta strandi621 – 628Combined sources8
Beta strandi633 – 635Combined sources3
Helixi637 – 647Combined sources11
Turni648 – 651Combined sources4
Beta strandi653 – 658Combined sources6
Helixi670 – 692Combined sources23
Beta strandi697 – 700Combined sources4
Beta strandi708 – 714Combined sources7
Beta strandi717 – 722Combined sources6
Helixi723 – 726Combined sources4
Helixi727 – 729Combined sources3
Turni732 – 735Combined sources4
Beta strandi736 – 739Combined sources4
Helixi741 – 744Combined sources4
Helixi746 – 751Combined sources6
Turni752 – 754Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O8LX-ray3.20A/B1-762[»]
3O8NX-ray3.20A/B1-762[»]
ProteinModelPortaliP00511.
SMRiP00511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00511.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 390N-terminal catalytic PFK domain 1UniRule annotation1 PublicationAdd BLAST389
Regioni164 – 166Substrate bindingUniRule annotation3
Regioni208 – 210Substrate bindingUniRule annotation3
Regioni298 – 301Substrate bindingUniRule annotation4
Regioni391 – 401Interdomain linkerUniRule annotation1 PublicationAdd BLAST11
Regioni402 – 780C-terminal regulatory PFK domain 2UniRule annotation1 PublicationAdd BLAST379
Regioni528 – 532Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni573 – 575Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni661 – 664Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP00511.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHEEHHAAR TLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF
60 70 80 90 100
VHEGYQGLVD GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITAEEA
160 170 180 190 200
TRSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRITEIVD AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDNWE DHLCRRLSET
260 270 280 290 300
RTRGSRLNII IVAEGAIDRN GKPITSEGVK DLVVRRLGYD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME
360 370 380 390 400
CVQVTKDVTK AMDEKRFDEA MKLRGRSFMN NWEVYKLLAH IRPPAPKSGS
410 420 430 440 450
YTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGPAKGQIEE
460 470 480 490 500
AGWSYVGGWT GQGGSKLGSK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE
510 520 530 540 550
AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC
560 570 580 590 600
TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
610 620 630 640 650
TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG
660 670 680 690 700
IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMAGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVTELQNQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSEHAHLEHI SRKRSGEATV
Length:780
Mass (Da):85,203
Last modified:January 23, 2007 - v3
Checksum:iACDDF38C36F48EDB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti269R → S AA sequence (PubMed:6233492).Curated1
Sequence conflicti480 – 508Missing AA sequence (PubMed:6233492).CuratedAdd BLAST29
Sequence conflicti559S → I AA sequence (PubMed:6233492).Curated1
Sequence conflicti566Missing AA sequence (PubMed:6233492).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14477
, M14456, M14457, M14458, M14459, M14460, M14461, M14462, M14463, M14464, M14465, M14466, M14467, M14468, M14469, M14470, M14471, M14472, M14473, M14474, M14475, M14476 Genomic DNA. Translation: AAA31441.1.
PIRiA26550. KIRBF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14477
, M14456, M14457, M14458, M14459, M14460, M14461, M14462, M14463, M14464, M14465, M14466, M14467, M14468, M14469, M14470, M14471, M14472, M14473, M14474, M14475, M14476 Genomic DNA. Translation: AAA31441.1.
PIRiA26550. KIRBF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O8LX-ray3.20A/B1-762[»]
3O8NX-ray3.20A/B1-762[»]
ProteinModelPortaliP00511.
SMRiP00511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014991.

Chemistry databases

ChEMBLiCHEMBL1075312.

PTM databases

iPTMnetiP00511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP00511.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BRENDAi2.7.1.11. 1749.
SABIO-RKP00511.

Miscellaneous databases

EvolutionaryTraceiP00511.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKAM_RABIT
AccessioniPrimary (citable) accession number: P00511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.