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Protein

Ferredoxin--nitrite reductase, chloroplastic

Gene

NIR

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

NH3 + 2 H2O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H+.

Cofactori

Protein has several cofactor binding sites:
  • sirohemeNote: Binds 1 siroheme per subunit.
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi: nitrate reduction (assimilation)

This protein is involved in the pathway nitrate reduction (assimilation), which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrate reduction (assimilation) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi473Iron-sulfur (4Fe-4S)1
Metal bindingi479Iron-sulfur (4Fe-4S)1
Metal bindingi514Iron-sulfur (4Fe-4S)1
Metal bindingi518Iron (siroheme axial ligand)1
Metal bindingi518Iron-sulfur (4Fe-4S)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi1.7.7.1. 5812.
UniPathwayiUPA00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin--nitrite reductase, chloroplastic (EC:1.7.7.1)
Gene namesi
Name:NIR
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32ChloroplastAdd BLAST32
ChainiPRO_000001970633 – 594Ferredoxin--nitrite reductase, chloroplasticAdd BLAST562

Expressioni

Inductioni

By nitrate.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1594
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi58 – 62Combined sources5
Beta strandi65 – 68Combined sources4
Helixi70 – 72Combined sources3
Helixi78 – 85Combined sources8
Helixi90 – 93Combined sources4
Helixi96 – 100Combined sources5
Helixi105 – 108Combined sources4
Helixi112 – 119Combined sources8
Helixi121 – 125Combined sources5
Beta strandi127 – 129Combined sources3
Helixi131 – 134Combined sources4
Beta strandi138 – 141Combined sources4
Helixi145 – 147Combined sources3
Beta strandi148 – 150Combined sources3
Helixi151 – 162Combined sources12
Helixi163 – 167Combined sources5
Beta strandi170 – 172Combined sources3
Beta strandi178 – 183Combined sources6
Helixi185 – 187Combined sources3
Helixi188 – 196Combined sources9
Turni197 – 199Combined sources3
Beta strandi206 – 210Combined sources5
Turni217 – 221Combined sources5
Helixi230 – 240Combined sources11
Turni241 – 245Combined sources5
Helixi248 – 250Combined sources3
Beta strandi259 – 261Combined sources3
Helixi271 – 273Combined sources3
Beta strandi274 – 293Combined sources20
Beta strandi306 – 313Combined sources8
Helixi314 – 316Combined sources3
Helixi317 – 331Combined sources15
Helixi337 – 339Combined sources3
Helixi342 – 349Combined sources8
Helixi351 – 359Combined sources9
Beta strandi386 – 390Combined sources5
Beta strandi396 – 401Combined sources6
Helixi404 – 406Combined sources3
Helixi410 – 423Combined sources14
Beta strandi424 – 431Combined sources8
Turni432 – 434Combined sources3
Beta strandi435 – 442Combined sources8
Turni443 – 445Combined sources3
Helixi446 – 449Combined sources4
Helixi453 – 456Combined sources4
Turni465 – 468Combined sources4
Beta strandi469 – 472Combined sources4
Helixi475 – 477Combined sources3
Helixi487 – 500Combined sources14
Beta strandi508 – 514Combined sources7
Helixi521 – 523Combined sources3
Beta strandi524 – 534Combined sources11
Beta strandi540 – 548Combined sources9
Beta strandi560 – 567Combined sources8
Turni568 – 570Combined sources3
Helixi571 – 582Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AKJX-ray2.80A33-594[»]
ProteinModelPortaliP05314.
SMRiP05314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05314.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLPVNKII PSSTTLLSSS NNNRRRNNSS IRCQKAVSPA AETAAVSPSV
60 70 80 90 100
DAARLEPRVE ERDGFWVLKE EFRSGINPAE KVKIEKDPMK LFIEDGISDL
110 120 130 140 150
ATLSMEEVDK SKHNKDDIDV RLKWLGLFHR RKHHYGRFMM RLKLPNGVTT
160 170 180 190 200
SEQTRYLASV IKKYGKDGCA DVTTRQNWQI RGVVLPDVPE IIKGLESVGL
210 220 230 240 250
TSLQSGMDNV RNPVGNPLAG IDPHEIVDTR PFTNLISQFV TANSRGNLSI
260 270 280 290 300
TNLPRKWNPC VIGSHDLYEH PHINDLAYMP ATKNGKFGFN LLVGGFFSIK
310 320 330 340 350
RCEEAIPLDA WVSAEDVVPV CKAMLEAFRD LGFRGNRQKC RMMWLIDELG
360 370 380 390 400
MEAFRGEVEK RMPEQVLERA SSEELVQKDW ERREYLGVHP QKQQGLSFVG
410 420 430 440 450
LHIPVGRLQA DEMEELARIA DVYGSGELRL TVEQNIIIPN VENSKIDSLL
460 470 480 490 500
NEPLLKERYS PEPPILMKGL VACTGSQFCG QAIIETKARA LKVTEEVQRL
510 520 530 540 550
VSVTRPVRMH WTGCPNSCGQ VQVADIGFMG CMTRDENGKP CEGADVFVGG
560 570 580 590
RIGSDSHLGD IYKKAVPCKD LVPVVAEILI NQFGAVPRER EEAE
Length:594
Mass (Da):66,394
Last modified:November 1, 1988 - v1
Checksum:i2B3DCAAC16DE06A3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti221I → V Probable allelic variation. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07568 mRNA. Translation: CAA30453.1.
X17031 Genomic DNA. Translation: CAA34893.1.
PIRiS16603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07568 mRNA. Translation: CAA30453.1.
X17031 Genomic DNA. Translation: CAA34893.1.
PIRiS16603.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AKJX-ray2.80A33-594[»]
ProteinModelPortaliP05314.
SMRiP05314.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00653.
BRENDAi1.7.7.1. 5812.

Miscellaneous databases

EvolutionaryTraceiP05314.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNIR_SPIOL
AccessioniPrimary (citable) accession number: P05314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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 one 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.