Skip Header

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

Ferredoxin

Gene

L-FNRI

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 sitei161 – 1611FADCombined sources
Binding sitei213 – 2131FADCombined sources
Binding sitei355 – 3551FADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi134 – 1374FADCombined sources
Nucleotide bindingi155 – 1573FADCombined sources
Nucleotide bindingi171 – 1744FADCombined sources

GO - Molecular functioni

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

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BRENDAi1.18.1.2. 6752.

Names & Taxonomyi

Protein namesi
Submitted name:
FerredoxinImported
Submitted name:
Ferredoxin--NADP reductase, leaf isozymeImported
Submitted name:
FerredoxinFerredoxin--NADP reductase, leaf isozymeImported
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:L-FNRIImported
ORF Names:ZEAMMB73_116832Imported
OrganismiZea mays (Maize)Imported
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Chromosome 9

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GAQX-ray2.59A/C42-355[»]
1GAWX-ray2.20A/B42-355[»]
3W5UX-ray2.70A/C/E/G42-355[»]
3W5VX-ray3.81A/C42-355[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000220125.
KOiK02641.
OMAiFPATSCA.

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.

Q9SLP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVMAAAVS SFPSSSAVVA KASPASPCAA PHFRPRAVRA AIRAQASAVE
60 70 80 90 100
APATAKAKKE SKKQEEGVVT NLYKPKEPYV GRCLLNTKIT GDDAPGETWH
110 120 130 140 150
MVFSTEGKIP YREGQSIGVI ADGVDKNGKP HKVRLYSIAS SAIGDFGDSK
160 170 180 190 200
TVSLCVKRLI YTNDAGEIVK GVCSNFLCDL QPGDNVQITG PVGKEMLMPK
210 220 230 240 250
DPNATIIMLA TGTGIAPFRS FLWKMFFEKH DDYKFNGLGW LFLGVPTSSS
260 270 280 290 300
LLYKEEFGKM KERAPENFRV DYAVSREQTN AAGERMYIQT RMAEYKEELW
310 320 330 340 350
ELLKKDNTYV YMCGLKGMEK GIDDIMVSLA EKDGIDWFDY KKQLKRGDQW

NVEVY
Length:355
Mass (Da):39,323
Last modified:May 1, 2000 - v1
Checksum:iAE56B6A6BF471267
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU959484 mRNA. Translation: ACG31602.1.
BT055002 mRNA. Translation: ACL53609.1.
CM000785 Genomic DNA. Translation: AFW86197.1.
AB035644 mRNA. Translation: BAA88236.1.
RefSeqiNP_001105568.1. NM_001112098.1.
XP_008659023.1. XM_008660801.1.
UniGeneiZm.94506.

Genome annotation databases

EnsemblPlantsiGRMZM2G168143_T01; GRMZM2G168143_P01; GRMZM2G168143.
GeneIDi542558.
KEGGizma:542558.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU959484 mRNA. Translation: ACG31602.1.
BT055002 mRNA. Translation: ACL53609.1.
CM000785 Genomic DNA. Translation: AFW86197.1.
AB035644 mRNA. Translation: BAA88236.1.
RefSeqiNP_001105568.1. NM_001112098.1.
XP_008659023.1. XM_008660801.1.
UniGeneiZm.94506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GAQX-ray2.59A/C42-355[»]
1GAWX-ray2.20A/B42-355[»]
3W5UX-ray2.70A/C/E/G42-355[»]
3W5VX-ray3.81A/C42-355[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGRMZM2G168143_T01; GRMZM2G168143_P01; GRMZM2G168143.
GeneIDi542558.
KEGGizma:542558.

Phylogenomic databases

HOGENOMiHOG000220125.
KOiK02641.
OMAiFPATSCA.

Enzyme and pathway databases

BRENDAi1.18.1.2. 6752.

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. "Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase."
    Kurisu G., Kusunoki M., Katoh E., Yamazaki T., Teshima K., Onda Y., Kimata-Ariga Y., Hase T.
    Nat. Struct. Biol. 8:117-121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-355 IN COMPLEX WITH FAD.
  3. Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: B73Imported.
  5. "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.
  6. "Concentration-dependent oligomerization of cross-linked complexes between ferredoxin and ferredoxin-NADP+ reductase."
    Kimata-Ariga Y., Kubota-Kawai H., Lee Y.H., Muraki N., Ikegami T., Kurisu G., Hase T.
    Biochem. Biophys. Res. Commun. 434:867-872(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 42-355 IN COMPLEX WITH FAD.
  7. Maize Genome Sequencing Project
    Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  8. EnsemblPlants
    Submitted (FEB-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: cv. B73Imported.

Entry informationi

Entry nameiQ9SLP6_MAIZE
AccessioniPrimary (citable) accession number: Q9SLP6
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 102 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.