Ferredoxin--nitrite reductase, chloroplastic precursor - Spinacia oleracea (Spinach)

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Reviewed, UniProtKB/Swiss-Prot P05314 (NIR_SPIOL)

Last modified June 16, 2009. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Ferredoxin--nitrite reductase, chloroplastic
EC=1.7.7.1

Gene names

Name:

NIR

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	NH₃ + 2 H₂O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H⁺.
Cofactor	Binds 1 siroheme per subunit. Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Nitrogen metabolism; nitrate reduction (assimilation).
Subunit structure	Monomer.
Subcellular location	Plastid › chloroplast.
Induction	By nitrate.
Sequence similarities	Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	4Fe-4S Heme Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-nitrite reductase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

32

Chloroplast

Chain

562

Ferredoxin--nitrite reductase, chloroplastic

PRO_0000019706

Sites

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron (siroheme axial ligand)

Metal binding

1

Iron-sulfur (4Fe-4S)

Natural variations

Natural variant

1

I → V Probable allelic variation.

Secondary structure

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594

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P05314-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 2B3DCAAC16DE06A3
Show »

594

66,394

        10         20         30         40         50         60 
MASLPVNKII PSSTTLLSSS NNNRRRNNSS IRCQKAVSPA AETAAVSPSV DAARLEPRVE 

        70         80         90        100        110        120 
ERDGFWVLKE EFRSGINPAE KVKIEKDPMK LFIEDGISDL ATLSMEEVDK SKHNKDDIDV 

       130        140        150        160        170        180 
RLKWLGLFHR RKHHYGRFMM RLKLPNGVTT SEQTRYLASV IKKYGKDGCA DVTTRQNWQI 

       190        200        210        220        230        240 
RGVVLPDVPE IIKGLESVGL TSLQSGMDNV RNPVGNPLAG IDPHEIVDTR PFTNLISQFV 

       250        260        270        280        290        300 
TANSRGNLSI TNLPRKWNPC VIGSHDLYEH PHINDLAYMP ATKNGKFGFN LLVGGFFSIK 

       310        320        330        340        350        360 
RCEEAIPLDA WVSAEDVVPV CKAMLEAFRD LGFRGNRQKC RMMWLIDELG MEAFRGEVEK 

       370        380        390        400        410        420 
RMPEQVLERA SSEELVQKDW ERREYLGVHP QKQQGLSFVG LHIPVGRLQA DEMEELARIA 

       430        440        450        460        470        480 
DVYGSGELRL TVEQNIIIPN VENSKIDSLL NEPLLKERYS PEPPILMKGL VACTGSQFCG 

       490        500        510        520        530        540 
QAIIETKARA LKVTEEVQRL VSVTRPVRMH WTGCPNSCGQ VQVADIGFMG CMTRDENGKP 

       550        560        570        580        590 
CEGADVFVGG RIGSDSHLGD IYKKAVPCKD LVPVVAEILI NQFGAVPRER EEAE

References

[1]	"Isolation of cDNA clones coding for spinach nitrite reductase: complete sequence and nitrate induction." Back E., Burkhart W., Moyer M., Privalle L., Rothstein S. Mol. Gen. Genet. 212:20-26(1988) [PubMed: 3163766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Isolation of the spinach nitrite reductase gene promoter which confers nitrate inducibility on GUS gene expression in transgenic tobacco." Back E., Dunne W., Schneiderbauer A., de Framond A., Rastogi R., Rothstein S.J. Plant Mol. Biol. 17:9-18(1991) [PubMed: 1868226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Dark green Bloomsdale. Tissue: Leaf.
[3]	"Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron-sulfur:siroheme cofactor." Swamy U., Wang M., Tripathy J.N., Kim S.K., Hirasawa M., Knaff D.B., Allen J.P. Biochemistry 44:16054-16063(2005) [PubMed: 16331965] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), IRON-CLUSTER BINDING AT CYS-473; CYS-479; CYS-514 AND CYS-518, HEME BINDING AT CYS-518.

Cross-references

Sequence databases

X07568 mRNA. Translation: CAA30453.1.
X17031 Genomic DNA. Translation: CAA34893.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AKJ	X-ray	2.80	A	33-594	[»]

ModBase

Enzyme and pathway databases

BRENDA

1.7.7.1. 286.

Family and domain databases

InterPro

IPR006066. Nir_Si_BS.
IPR006067. Nir_Sir_4Fe4S.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
[Graphical view]

Pfam

PF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]

PRINTS

PR00397. SIROHAEM.

PROSITE

PS00365. NIR_SIR. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

NIR_SPIOL

Accession

Primary (citable) accession number: P05314

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents