Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00511

- PFKAM_RABIT

UniProt

P00511 - PFKAM_RABIT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

Magnesium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251ATP; via amide nitrogenUniRule annotation
Metal bindingi119 – 1191Magnesium; catalyticUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei201 – 2011Substrate; shared with dimeric partnerUniRule annotation
Binding sitei264 – 2641SubstrateUniRule annotation
Binding sitei292 – 2921Substrate; shared with dimeric partnerUniRule annotation
Binding sitei471 – 4711Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei566 – 5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei629 – 6291Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei735 – 7351Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892ATPUniRule annotation
Nucleotide bindingi118 – 1214ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: UniProtKB-UniPathway
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

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
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typePRO_0000112019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Glycosylationi530 – 5301O-linked (GlcNAc)By similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei775 – 7751Phosphoserine; by PKA1 Publication

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP00511.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014991.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 134
Beta strandi17 – 215
Helixi30 – 4314
Beta strandi47 – 493
Helixi54 – 596
Helixi62 – 643
Helixi71 – 733
Helixi91 – 933
Helixi95 – 10814
Beta strandi112 – 1176
Helixi119 – 13012
Helixi133 – 1386
Turni139 – 1435
Turni146 – 1483
Helixi149 – 1513
Beta strandi157 – 1637
Helixi178 – 19316
Beta strandi202 – 2076
Helixi214 – 22310
Helixi240 – 25213
Beta strandi256 – 2605
Beta strandi269 – 2713
Helixi276 – 28611
Beta strandi291 – 2944
Helixi307 – 32519
Beta strandi334 – 3396
Beta strandi342 – 3476
Helixi348 – 36316
Helixi367 – 3748
Helixi377 – 38913
Beta strandi402 – 4109
Helixi415 – 42814
Beta strandi432 – 4387
Helixi441 – 4455
Beta strandi448 – 4503
Turni453 – 4564
Helixi475 – 4773
Helixi478 – 48710
Beta strandi493 – 4986
Helixi499 – 51416
Beta strandi522 – 5276
Helixi542 – 55615
Turni557 – 5604
Beta strandi562 – 5643
Beta strandi566 – 5727
Helixi579 – 5879
Beta strandi591 – 5944
Beta strandi596 – 5983
Helixi602 – 61615
Beta strandi621 – 6288
Beta strandi633 – 6353
Helixi637 – 64711
Turni648 – 6514
Beta strandi653 – 6586
Helixi670 – 69223
Beta strandi697 – 7004
Beta strandi708 – 7147
Beta strandi717 – 7226
Helixi723 – 7264
Helixi727 – 7293
Turni732 – 7354
Beta strandi736 – 7394
Helixi741 – 7444
Helixi746 – 7516
Turni752 – 7543

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O8LX-ray3.20A/B1-762[»]
3O8NX-ray3.20A/B1-762[»]
ProteinModelPortaliP00511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00511.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 390389N-terminal catalytic PFK domain 1Add
BLAST
Regioni164 – 1663Substrate bindingUniRule annotation
Regioni208 – 2103Substrate bindingUniRule annotation
Regioni298 – 3014Substrate bindingUniRule annotation
Regioni391 – 40111Interdomain linkerAdd
BLAST
Regioni402 – 780379C-terminal regulatory PFK domain 2Add
BLAST
Regioni528 – 5325Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni573 – 5753Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni661 – 6644Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

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

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP00511.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691R → S AA sequence (PubMed:6233492)Curated
Sequence conflicti480 – 50829Missing AA sequence (PubMed:6233492)CuratedAdd
BLAST
Sequence conflicti559 – 5591S → I AA sequence (PubMed:6233492)Curated
Sequence conflicti566 – 5661Missing AA sequence (PubMed:6233492)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A26550. KIRBF.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O8L X-ray 3.20 A/B 1-762 [» ]
3O8N X-ray 3.20 A/B 1-762 [» ]
ProteinModelPortali P00511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000014991.

Chemistry

ChEMBLi CHEMBL1075312.

Proteomic databases

PRIDEi P00511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi P00511.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P00511.

Miscellaneous databases

EvolutionaryTracei P00511.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The rabbit muscle phosphofructokinase gene. Implications for protein structure, function, and tissue specificity."
    Lee C.P., Kao M.C., French B.A., Putney S.D., Chang S.H.
    J. Biol. Chem. 262:4195-4199(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Muscle.
  2. "Evolution of phosphofructokinase -- gene duplication and creation of new effector sites."
    Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.
    Nature 309:467-469(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-780, ACETYLATION AT THR-2.
  3. "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase."
    Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.
    Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 768-780, PHOSPHORYLATION AT SER-775.
  4. "The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
    Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
    J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959.

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: October 29, 2014
This is version 121 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

External Data

Dasty 3