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Protein
Submitted name:

Ferredoxin

Gene

L-FNRII

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

Functioni

Sites

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

Regions

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
FerredoxinImported
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:L-FNRIIImported
OrganismiZea mays (Maize)Imported
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Chromosome 3

Interactioni

Protein-protein interaction databases

STRINGi4577.GRMZM2G059083_P01.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VO1X-ray2.00A/B56-368[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

KOiK02641.
OMAiWLDYKKQ.

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.

Q9SLP5-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
BT038551 Genomic DNA. No translation available.
EU963527 Genomic DNA. No translation available.
AB035645 mRNA. Translation: BAA88237.1.
RefSeqiNP_001104851.1. NM_001111381.1.
UniGeneiZm.93707.

Genome annotation databases

EnsemblPlantsiGRMZM2G059083_T01; GRMZM2G059083_P01; GRMZM2G059083.
GRMZM2G059083_T04; GRMZM2G059083_P04; GRMZM2G059083.
GeneIDi541626.
KEGGizma:541626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT038551 Genomic DNA. No translation available.
EU963527 Genomic DNA. No translation available.
AB035645 mRNA. Translation: BAA88237.1.
RefSeqiNP_001104851.1. NM_001111381.1.
UniGeneiZm.93707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VO1X-ray2.00A/B56-368[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G059083_P01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGRMZM2G059083_T01; GRMZM2G059083_P01; GRMZM2G059083.
GRMZM2G059083_T04; GRMZM2G059083_P04; GRMZM2G059083.
GeneIDi541626.
KEGGizma:541626.

Phylogenomic databases

KOiK02641.
OMAiWLDYKKQ.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "The B73 maize genome: complexity, diversity, and dynamics."
    Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., Fronick C.
    , Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.
    Science 326:1112-1115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. B73Imported.
  3. "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.
  4. EnsemblPlants
    Submitted (OCT-2014) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: cv. B73Imported.
  5. EnsemblPlants
    Submitted (FEB-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: cv. B73.

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: June 24, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.