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Q9SLP5

- Q9SLP5_MAIZE

UniProt

Q9SLP5 - Q9SLP5_MAIZE

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Protein
Submitted name:

Ferredoxin

Gene

L-FNRII

Organism
Zea mays (Maize)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei174 – 1741FADImported
Binding sitei368 – 3681FADImported

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi147 – 1504FADImported
Nucleotide bindingi168 – 1703FADImported
Nucleotide bindingi185 – 1873FADImported

GO - Molecular functioni

  1. nucleotide binding Source: UniProtKB-KW
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

FADImported, Flavoprotein, Nucleotide-bindingImported

Names & Taxonomyi

Protein namesi
Submitted name:
FerredoxinImported
Gene namesi
Name:L-FNRIIImported
OrganismiZea mays (Maize)Imported
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiQ9SLP5.

PTM / Processingi

Proteomic databases

PRIDEiQ9SLP5.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VO1X-ray2.00A/B56-368[»]
ProteinModelPortaliQ9SLP5.
SMRiQ9SLP5. Positions 74-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

KOiK02641.
OMAiEHEDYKY.

Family and domain databases

InterProiIPR017927. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSiPR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SLP5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVTAAAVS LPSSSSSPAA AKAKASASAS PSSPCGHLQF PRRHGGPRAV
60 70 80 90 100
RLRVQVSTTE TAEAEPVKKL EKVSKKQEEG LVTNKYKPKE PYVGRCLLNT
110 120 130 140 150
RITGDQAPGE TWHMVFSTEG EVPYREGQSI GVIADGEDKN GKPHKLRLYS
160 170 180 190 200
IASSALGDFG DSKTVSLCVK RLVYTNDQGE VVKGVCSNFL CDLKPGAEVK
210 220 230 240 250
ITGPVGKEML MPKDPNATII MLATGTGIAP FRSFLWKMFF EEHEDYKYTG
260 270 280 290 300
LAWLFLGVPT SDTLLYKEEL EKMKEMAPDN FRLDFAVSRE QTNAAGEKMY
310 320 330 340 350
IQTRMAEYKE ELWELLKKDN TYVYMCGLKG MEKGIDDIML DLAAKDGINW
360
LDYKKQLKKS EQWNVEVY
Length:368
Mass (Da):40,864
Last modified:May 1, 2000 - v1
Checksum:i6F9DEBD77DC6C338
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB035645 mRNA. Translation: BAA88237.1.
RefSeqiNP_001104851.1. NM_001111381.1.
UniGeneiZm.93707.

Genome annotation databases

GeneIDi541626.
KEGGizma:541626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB035645 mRNA. Translation: BAA88237.1 .
RefSeqi NP_001104851.1. NM_001111381.1.
UniGenei Zm.93707.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VO1 X-ray 2.00 A/B 56-368 [» ]
ProteinModelPortali Q9SLP5.
SMRi Q9SLP5. Positions 74-368.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9SLP5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 541626.
KEGGi zma:541626.

Organism-specific databases

Gramenei Q9SLP5.

Phylogenomic databases

KOi K02641.
OMAi EHEDYKY.

Family and domain databases

InterProi 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 PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSi PR00371. FPNCR.
SUPFAMi SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins."
    Onda Y., Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T., Hase T.
    Plant Physiol. 123:1037-1045(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: LeafImported.
  2. "N-terminal structure of maize ferredoxin:NADP+ reductase determines recruitment into different thylakoid membrane complexes."
    Twachtmann M., Altmann B., Muraki N., Voss I., Okutani S., Kurisu G., Hase T., Hanke G.T.
    Plant Cell 24:2979-2991(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 56-368 IN COMPLEX WITH FAD.

Entry informationi

Entry nameiQ9SLP5_MAIZE
AccessioniPrimary (citable) accession number: Q9SLP5
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3