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P21890

- FENR_NOSSO

UniProt

P21890 - FENR_NOSSO

Protein

Ferredoxin--NADP reductase

Gene

petH

Organism
Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171NADPBy similarity
    Binding sitei237 – 2371NADP
    Binding sitei241 – 2411FAD
    Binding sitei294 – 2941FAD
    Binding sitei294 – 2941NADP; via amide nitrogen
    Binding sitei438 – 4381NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi214 – 2174FAD
    Nucleotide bindingi235 – 2373FAD
    Nucleotide bindingi253 – 2553FAD
    Nucleotide bindingi330 – 3312NADPBy similarity
    Nucleotide bindingi360 – 3612NADP
    Nucleotide bindingi370 – 3745NADP
    Nucleotide bindingi399 – 4002NADPBy similarity

    GO - Molecular functioni

    1. ferredoxin-NADP+ reductase activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. NADP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferredoxin--NADP reductase (EC:1.18.1.2)
    Short name:
    FNR
    Gene namesi
    Name:petH
    OrganismiNostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
    Taxonomic identifieri1168 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

    Subcellular locationi

    Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side
    Note: May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.

    GO - Cellular componenti

    1. phycobilisome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane, Phycobilisome, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Ferredoxin--NADP reductasePRO_0000167632Add
    BLAST

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    isiBP0A3E05EBI-593915,EBI-593907
    petFP0A3C85EBI-593915,EBI-637080

    Protein-protein interaction databases

    IntActiP21890. 3 interactions.

    Structurei

    Secondary structure

    1
    440
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi144 – 1474
    Beta strandi151 – 1533
    Beta strandi158 – 16710
    Beta strandi173 – 1753
    Beta strandi177 – 1837
    Turni185 – 1873
    Beta strandi196 – 2005
    Beta strandi202 – 2043
    Beta strandi208 – 2103
    Beta strandi214 – 2185
    Turni222 – 2276
    Beta strandi228 – 23710
    Beta strandi240 – 2423
    Beta strandi243 – 2486
    Beta strandi249 – 2513
    Helixi253 – 2597
    Beta strandi266 – 2738
    Beta strandi275 – 2773
    Beta strandi286 – 2927
    Helixi293 – 2953
    Helixi296 – 30712
    Helixi309 – 3146
    Beta strandi324 – 3329
    Helixi333 – 3353
    Helixi339 – 34810
    Turni350 – 3523
    Beta strandi353 – 3597
    Turni360 – 3623
    Beta strandi368 – 3703
    Helixi373 – 3797
    Helixi381 – 3888
    Beta strandi393 – 3997
    Helixi403 – 41614
    Turni417 – 4193
    Helixi422 – 43110
    Beta strandi435 – 4395

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B2RX-ray1.80A137-440[»]
    1BJKX-ray2.30A146-440[»]
    1BQEX-ray2.45A146-440[»]
    1E62X-ray2.30A137-440[»]
    1E63X-ray2.30A137-440[»]
    1E64X-ray2.30A137-440[»]
    1EWYX-ray2.38A/B138-440[»]
    1GJRX-ray2.10A137-440[»]
    1GO2X-ray1.70A137-440[»]
    1GR1X-ray2.50A138-440[»]
    1H42X-ray2.15A137-440[»]
    1H85X-ray2.30A146-440[»]
    1OGIX-ray1.64A138-440[»]
    1OGJX-ray1.64A138-440[»]
    1QGYX-ray1.70A146-440[»]
    1QGZX-ray2.30A146-440[»]
    1QH0X-ray1.93A146-440[»]
    1QUEX-ray1.80A138-440[»]
    1QUFX-ray2.25A137-440[»]
    1W34X-ray1.73A137-440[»]
    1W35X-ray1.90A137-440[»]
    1W87X-ray3.00A/B137-440[»]
    2BMWX-ray1.50A137-440[»]
    2BSAX-ray1.92A138-440[»]
    2VYQX-ray1.90A137-440[»]
    2VZLX-ray1.93A137-440[»]
    2X3UX-ray1.93A138-440[»]
    3ZBTX-ray1.92A138-440[»]
    3ZBUX-ray1.89A138-440[»]
    3ZC3X-ray2.30A/B138-440[»]
    4BPRX-ray2.00A138-440[»]
    4C43X-ray1.70A138-440[»]
    ProteinModelPortaliP21890.
    SMRiP21890. Positions 138-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21890.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 7559CpcD-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini155 – 279125FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 cpcD-like domain.PROSITE-ProRule annotation
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR008213. CpcD-like_dom.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR015701. FNR.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF01383. CpcD. 1 hit.
    PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000361. Frd-NADP+_RD. 1 hit.
    PRINTSiPR00371. FPNCR.
    SMARTiSM01094. CpcD. 1 hit.
    [Graphical view]
    SUPFAMiSSF63380. SSF63380. 1 hit.
    PROSITEiPS51441. CPCD_LIKE. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21890-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV    50
    PYNRMNQEMQ RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS 100
    EGNGKATPVK TDSGAKAFAK PPAEEQLKKK DNKGNTMTQA KAKHADVPVN 150
    LYRPNAPFIG KVISNEPLVK EGGIGIVQHI KFDLTGGNLK YIEGQSIGII 200
    PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE YKHPESGETV 250
    YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR 300
    TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP 350
    DNFRLTYAIS REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL 400
    RGMEEGIDAA LSAAAAKEGV TWSDYQKDLK KAGRWHVETY 440
    Length:440
    Mass (Da):48,865
    Last modified:October 1, 1994 - v2
    Checksum:i8E1F61D0F09338B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801I → L AA sequence (PubMed:3124746)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72394 Genomic DNA. Translation: CAA51088.1.
    X54039 Genomic DNA. Translation: CAA37973.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72394 Genomic DNA. Translation: CAA51088.1 .
    X54039 Genomic DNA. Translation: CAA37973.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B2R X-ray 1.80 A 137-440 [» ]
    1BJK X-ray 2.30 A 146-440 [» ]
    1BQE X-ray 2.45 A 146-440 [» ]
    1E62 X-ray 2.30 A 137-440 [» ]
    1E63 X-ray 2.30 A 137-440 [» ]
    1E64 X-ray 2.30 A 137-440 [» ]
    1EWY X-ray 2.38 A/B 138-440 [» ]
    1GJR X-ray 2.10 A 137-440 [» ]
    1GO2 X-ray 1.70 A 137-440 [» ]
    1GR1 X-ray 2.50 A 138-440 [» ]
    1H42 X-ray 2.15 A 137-440 [» ]
    1H85 X-ray 2.30 A 146-440 [» ]
    1OGI X-ray 1.64 A 138-440 [» ]
    1OGJ X-ray 1.64 A 138-440 [» ]
    1QGY X-ray 1.70 A 146-440 [» ]
    1QGZ X-ray 2.30 A 146-440 [» ]
    1QH0 X-ray 1.93 A 146-440 [» ]
    1QUE X-ray 1.80 A 138-440 [» ]
    1QUF X-ray 2.25 A 137-440 [» ]
    1W34 X-ray 1.73 A 137-440 [» ]
    1W35 X-ray 1.90 A 137-440 [» ]
    1W87 X-ray 3.00 A/B 137-440 [» ]
    2BMW X-ray 1.50 A 137-440 [» ]
    2BSA X-ray 1.92 A 138-440 [» ]
    2VYQ X-ray 1.90 A 137-440 [» ]
    2VZL X-ray 1.93 A 137-440 [» ]
    2X3U X-ray 1.93 A 138-440 [» ]
    3ZBT X-ray 1.92 A 138-440 [» ]
    3ZBU X-ray 1.89 A 138-440 [» ]
    3ZC3 X-ray 2.30 A/B 138-440 [» ]
    4BPR X-ray 2.00 A 138-440 [» ]
    4C43 X-ray 1.70 A 138-440 [» ]
    ProteinModelPortali P21890.
    SMRi P21890. Positions 138-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21890. 3 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P21890.

    Family and domain databases

    InterProi IPR008213. CpcD-like_dom.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR015701. FNR.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF01383. CpcD. 1 hit.
    PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000361. Frd-NADP+_RD. 1 hit.
    PRINTSi PR00371. FPNCR.
    SMARTi SM01094. CpcD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63380. SSF63380. 1 hit.
    PROSITEi PS51441. CPCD_LIKE. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homology of the N-terminal domain of the petH gene product from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker polypeptide."
      Fillat M.F., Flores E., Gomez-Moreno C.
      Plant Mol. Biol. 22:725-729(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence of the ferredoxin-NADP(+)-reductase gene from Anabaena PCC 7119."
      Fillat M.F., Bakker H.A.C., Weisbeek P.J.
      Nucleic Acids Res. 18:7161-7161(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-440.
    3. "Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis."
      Sancho J., Peleato M.L., Gomez-Moreno C., Edmondson D.E.
      Arch. Biochem. Biophys. 260:200-207(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-183.
      Strain: 1403.46.
    4. "X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8-A resolution, and crystallographic studies of NADP+ binding at 2.25-A resolution."
      Serre L., Vellieux F.M.D., Medina M., Gomez-Moreno C., Fontecilla-Camps J.-C., Frey M.
      J. Mol. Biol. 263:20-39(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
    5. "Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer."
      Martinez-Julvez M., Hermoso J., Hurley J.K., Mayoral T., Sanz-Aparicio J., Tollin G., Gomez-Moreno C., Medina M.
      Biochemistry 37:17680-17691(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-440.
    6. "Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by X-ray crystallography."
      Mayoral T., Medina M., Sanz-Aparicio J., Gomez-Moreno C., Hermoso J.A.
      Proteins 38:60-69(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
    7. "Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule."
      Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M.
      Acta Crystallogr. D 56:1408-1412(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).

    Entry informationi

    Entry nameiFENR_NOSSO
    AccessioniPrimary (citable) accession number: P21890
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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