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P07953

- F261_RAT

UniProt

P07953 - F261_RAT

Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

Pfkfb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Synthesis and degradation of fructose 2,6-bisphosphate.

    Catalytic activityi

    Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
    ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

    Enzyme regulationi

    Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Fructose 6-phosphateBy similarity
    Binding sitei105 – 1051Fructose 6-phosphateBy similarity
    Active sitei131 – 1311Sequence Analysis
    Binding sitei133 – 1331Fructose 6-phosphateBy similarity
    Binding sitei139 – 1391Fructose 6-phosphateBy similarity
    Active sitei161 – 1611Sequence Analysis
    Binding sitei175 – 1751Fructose 6-phosphateBy similarity
    Binding sitei196 – 1961Fructose 6-phosphateBy similarity
    Binding sitei200 – 2001Fructose 6-phosphateBy similarity
    Binding sitei258 – 2581Fructose 2,6-bisphosphateBy similarity
    Active sitei259 – 2591Tele-phosphohistidine intermediate1 Publication
    Binding sitei265 – 2651Fructose 2,6-bisphosphateBy similarity
    Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogen
    Binding sitei308 – 3081Fructose 2,6-bisphosphateBy similarity
    Active sitei328 – 3281Proton donor/acceptor1 Publication
    Binding sitei339 – 3391Fructose 2,6-bisphosphate
    Binding sitei353 – 3531Fructose 2,6-bisphosphate
    Binding sitei357 – 3571Fructose 2,6-bisphosphate
    Binding sitei368 – 3681Fructose 2,6-bisphosphate
    Active sitei393 – 3931Proton donor/acceptor1 Publication
    Binding sitei394 – 3941Fructose 2,6-bisphosphate
    Binding sitei398 – 3981Fructose 2,6-bisphosphate
    Binding sitei430 – 4301ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi49 – 579ATPBy similarity
    Nucleotide bindingi170 – 1756ATPBy similarity
    Nucleotide bindingi350 – 3534ATP
    Nucleotide bindingi394 – 3985ATP

    GO - Molecular functioni

    1. 6-phosphofructo-2-kinase activity Source: RGD
    2. ATP binding Source: RGD
    3. fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB
    4. fructose-6-phosphate binding Source: RGD
    5. identical protein binding Source: IntAct
    6. kinase binding Source: RGD

    GO - Biological processi

    1. carbohydrate phosphorylation Source: RGD
    2. dephosphorylation Source: GOC
    3. fructose 2,6-bisphosphate metabolic process Source: UniProtKB
    4. fructose metabolic process Source: InterPro
    5. organ regeneration Source: RGD
    6. positive regulation of glucokinase activity Source: RGD
    7. response to cAMP Source: RGD
    8. response to glucagon Source: RGD
    9. response to glucocorticoid Source: RGD
    10. response to insulin Source: RGD
    11. response to starvation Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.46. 5301.
    ReactomeiREACT_217998. Gluconeogenesis.
    REACT_225694. Glycolysis.
    SABIO-RKP07953.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
    Short name:
    6PF-2-K/Fru-2,6-P2ase 1
    Short name:
    PFK/FBPase 1
    Alternative name(s):
    6PF-2-K/Fru-2,6-P2ase liver isozyme
    Including the following 2 domains:
    Fructose-2,6-bisphosphatase (EC:3.1.3.46)
    Gene namesi
    Name:Pfkfb1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome X

    Organism-specific databases

    RGDi3307. Pfkfb1.

    Subcellular locationi

    GO - Cellular componenti

    1. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex Source: UniProtKB
    2. cytosol Source: Reactome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1PRO_0000179962Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei33 – 331Phosphoserine; by PKA1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP07953.

    PTM databases

    PhosphoSiteiP07953.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    GenevestigatoriP07953.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-709873,EBI-709873

    Protein-protein interaction databases

    IntActiP07953. 2 interactions.
    MINTiMINT-8147404.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi253 – 2586
    Helixi263 – 2675
    Helixi278 – 29215
    Beta strandi300 – 3067
    Helixi307 – 3148
    Turni315 – 3173
    Beta strandi321 – 3233
    Helixi324 – 3263
    Helixi332 – 3343
    Helixi339 – 3457
    Helixi347 – 3559
    Turni357 – 3593
    Helixi368 – 3747
    Helixi376 – 3838
    Beta strandi386 – 3927
    Helixi394 – 40411
    Turni409 – 4113
    Helixi412 – 4143
    Beta strandi421 – 4288
    Beta strandi431 – 4388

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C7ZX-ray2.60A/B252-441[»]
    1C80X-ray2.20A/B252-441[»]
    1C81X-ray2.50A252-441[»]
    1FBTX-ray2.00A/B252-441[»]
    1TIPX-ray2.20A/B252-441[»]
    ProteinModelPortaliP07953.
    SMRiP07953. Positions 7-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07953.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2502496-phosphofructo-2-kinaseAdd
    BLAST
    Regioni251 – 471221Fructose-2,6-bisphosphataseAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG0406.
    GeneTreeiENSGT00390000018751.
    HOGENOMiHOG000181112.
    HOVERGENiHBG005628.
    InParanoidiP07953.
    KOiK01103.
    OMAiNIRGRIG.
    OrthoDBiEOG7M3J03.
    PhylomeDBiP07953.
    TreeFamiTF313541.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view]
    PANTHERiPTHR10606. PTHR10606. 1 hit.
    PfamiPF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSiPR00991. 6PFRUCTKNASE.
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P07953-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSREMGELTQ TRLQKIWIPH SSSSSVLQRR RGSSIPQFTN SPTMVIMVGL    50
    PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNTE 100
    AQLIRKQCAL AALKDVHKYL SREEGHVAVF DATNTTRERR SLILQFAKEH 150
    GYKVFFIESI CNDPEIIAEN IKQVKLGSPD YIDCDQEKVL EDFLKRIECY 200
    EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT AYYLMNIHVT 250
    PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQGISSLK 300
    VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF 350
    ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL 400
    LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCRVESIYLN VEAVNTHRDK 450
    PENVDITREA EEALDTVPAH Y 471
    Length:471
    Mass (Da):54,763
    Last modified:January 23, 2007 - v3
    Checksum:iE307AF13945E0FCD
    GO
    Isoform 2 (identifier: P07953-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGS → MEEKASKRTA

    Show »
    Length:448
    Mass (Da):52,070
    Checksum:i3DCD00D54929917D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351T → Y(PubMed:2547611)Curated
    Sequence conflicti135 – 1351T → Y(PubMed:2848802)Curated
    Sequence conflicti135 – 1351T → Y(PubMed:2826464)Curated
    Sequence conflicti138 – 1381E → F(PubMed:2547611)Curated
    Sequence conflicti257 – 2571Missing AA sequence (PubMed:3040762)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333MSREM…RRRGS → MEEKASKRTA in isoform 2. 1 PublicationVSP_004674Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00702 mRNA. Translation: CAA68694.1.
    X15579 mRNA. Translation: CAA33606.1.
    X15580 mRNA. Translation: CAA33607.1.
    M26215 Genomic DNA. Translation: AAA02888.2.
    M26216 Genomic DNA. Translation: AAA02889.1.
    J04197 mRNA. Translation: AAA79008.1.
    M27886 Genomic DNA. Translation: AAA58780.1.
    PIRiS11761. KIRTFB.
    RefSeqiNP_036753.4. NM_012621.4. [P07953-1]
    UniGeneiRn.10115.

    Genome annotation databases

    EnsembliENSRNOT00000000178; ENSRNOP00000000178; ENSRNOG00000000165. [P07953-2]
    ENSRNOT00000033656; ENSRNOP00000035212; ENSRNOG00000000165. [P07953-1]
    GeneIDi24638.
    KEGGirno:24638.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00702 mRNA. Translation: CAA68694.1 .
    X15579 mRNA. Translation: CAA33606.1 .
    X15580 mRNA. Translation: CAA33607.1 .
    M26215 Genomic DNA. Translation: AAA02888.2 .
    M26216 Genomic DNA. Translation: AAA02889.1 .
    J04197 mRNA. Translation: AAA79008.1 .
    M27886 Genomic DNA. Translation: AAA58780.1 .
    PIRi S11761. KIRTFB.
    RefSeqi NP_036753.4. NM_012621.4. [P07953-1 ]
    UniGenei Rn.10115.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C7Z X-ray 2.60 A/B 252-441 [» ]
    1C80 X-ray 2.20 A/B 252-441 [» ]
    1C81 X-ray 2.50 A 252-441 [» ]
    1FBT X-ray 2.00 A/B 252-441 [» ]
    1TIP X-ray 2.20 A/B 252-441 [» ]
    ProteinModelPortali P07953.
    SMRi P07953. Positions 7-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07953. 2 interactions.
    MINTi MINT-8147404.

    PTM databases

    PhosphoSitei P07953.

    Proteomic databases

    PRIDEi P07953.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000000178 ; ENSRNOP00000000178 ; ENSRNOG00000000165 . [P07953-2 ]
    ENSRNOT00000033656 ; ENSRNOP00000035212 ; ENSRNOG00000000165 . [P07953-1 ]
    GeneIDi 24638.
    KEGGi rno:24638.

    Organism-specific databases

    CTDi 5207.
    RGDi 3307. Pfkfb1.

    Phylogenomic databases

    eggNOGi COG0406.
    GeneTreei ENSGT00390000018751.
    HOGENOMi HOG000181112.
    HOVERGENi HBG005628.
    InParanoidi P07953.
    KOi K01103.
    OMAi NIRGRIG.
    OrthoDBi EOG7M3J03.
    PhylomeDBi P07953.
    TreeFami TF313541.

    Enzyme and pathway databases

    BRENDAi 3.1.3.46. 5301.
    Reactomei REACT_217998. Gluconeogenesis.
    REACT_225694. Glycolysis.
    SABIO-RK P07953.

    Miscellaneous databases

    EvolutionaryTracei P07953.
    NextBioi 603924.
    PROi P07953.

    Gene expression databases

    Genevestigatori P07953.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view ]
    PANTHERi PTHR10606. PTHR10606. 1 hit.
    Pfami PF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSi PR00991. 6PFRUCTKNASE.
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence coding for rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase derived from a cDNA clone."
      Darville M.I., Crepin K.M., Vandekerckhove J., van Damme J., Octave J.-N., Rider M.H., Marchand M.J., Hue L., Rousseau G.G.
      FEBS Lett. 224:317-321(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), PROTEIN SEQUENCE OF 16-29; 65-74; 90-105; 123-137; 189-195; 240-252; 259-266 AND 309-324 (ISOFORM 1).
      Strain: Wistar.
      Tissue: Liver.
    2. "Isolation of a cDNA clone for rat liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase."
      Colosa A.D., Lively M.O., El-Maghrabi M.R., Pilkis S.J.
      Biochem. Biophys. Res. Commun. 143:1092-1098(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
      Strain: Sprague-Dawley.
    3. "Characterization of distinct mRNAs coding for putative isozymes of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Crepin K.M., Darville M.I., Hue L., Rousseau G.G.
      Eur. J. Biochem. 183:433-440(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: Wistar.
      Tissue: Liver.
    4. "Induction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase mRNA by refeeding and insulin."
      Colosia A.D., Marker A.J., Lange A.J., El-Maghrabi M.R., Granner D.K., Tauler A., Pilkis J., Pilkis S.J.
      J. Biol. Chem. 263:18669-18677(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. "Complete amino acid sequence of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Lively M.O., El-Maghrabi M.R., Pilkis J., D'Angelo G., Colosia A.D., Ciavola J.A., Fraser B.A., Pilkis S.J.
      J. Biol. Chem. 263:839-849(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT SER-2.
      Tissue: Liver.
    6. "Cloning and expression in Escherichia coli of a rat hepatoma cell cDNA coding for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Crepin K.M., Darville M.I., Michel A., Hue L., Rousseau G.G.
      Biochem. J. 264:151-160(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
      Strain: Wistar.
      Tissue: Liver.
    7. "Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in primary structure with phosphoglycerate mutase."
      Pilkis S.J., Lively M.O., El-Maghrabi M.R.
      J. Biol. Chem. 262:12672-12675(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 220-267.
      Tissue: Liver.
    8. "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Darville M.I., Crepin K.M., Hue L., Rousseau G.G.
      Proc. Natl. Acad. Sci. U.S.A. 86:6543-6547(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32 (ISOFORM 1), PROTEIN SEQUENCE OF 2-10 (ISOFORM 2).
    9. "Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site."
      Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.
      J. Biol. Chem. 264:6344-6348(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 106-114, REGION.
    10. "Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Bazan J.F., Fletterick R.J., Pilkis S.J.
      Proc. Natl. Acad. Sci. U.S.A. 86:9642-9646(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    11. "Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme."
      Kurland I.J., Pilkis S.J.
      Protein Sci. 4:1023-1037(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-33, ENZYME REGULATION.
    12. "Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases."
      Lee Y.-H., Ogata C., Pflugrath J.W., Levitt D.G., Sarma R., Banaszak L.J., Pilkis S.J.
      Biochemistry 35:6010-6019(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Tissue: Liver.
    13. "Crystal structure of a trapped phosphoenzyme during a catalytic reaction."
      Lee Y.-H., Olson T.W., Ogata C.M., Levitt D.G., Banaszak L.J., Lange A.J.
      Nat. Struct. Biol. 4:615-618(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 251-441 IN COMPLEX WITH FRUCTOSE 6-PHOSPHATE, ACTIVE SITE.
    14. "Reaction mechanism of fructose-2,6-bisphosphatase suggested by the crystal structures of a pseudo-Michaelis complex and metabolite complexes."
      Lee Y.-H., Olson T.W., McClard R.W., Witte J.F., McFarlan S.C., Banaszak L.J., Levitt D.G., Lange A.J.
      Submitted (APR-2000) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 252-440 IN COMPLEXES WITH SUBSTRATE ANALOG AND WITH GTP.

    Entry informationi

    Entry nameiF261_RAT
    AccessioniPrimary (citable) accession number: P07953
    Secondary accession number(s): P16119
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 158 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, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3