Reviewed, UniProtKB/Swiss-Prot P05314 (NIR_SPIOL)

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

3562 [NCBI]

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 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

1 – 32

32

Chloroplast

Chain

33 – 594

562

Ferredoxin--nitrite reductase, chloroplastic

PRO_0000019706

Sites

Metal binding

473

1

Iron-sulfur (4Fe-4S)

Metal binding

479

1

Iron-sulfur (4Fe-4S)

Metal binding

514

1

Iron-sulfur (4Fe-4S)

Metal binding

518

1

Iron (siroheme axial ligand)

Metal binding

518

1

Iron-sulfur (4Fe-4S)

Natural variations

Natural variant

221

1

I → V Probable allelic variation.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

594

Helix Strand Turn

Details...

Beta strand

58 – 62

5

Beta strand

65 – 68

4

Helix

70 – 72

3

Helix

78 – 85

8

Helix

90 – 93

4

Helix

96 – 100

5

Helix

105 – 108

4

Helix

112 – 119

8

Helix

121 – 125

5

Beta strand

127 – 129

3

Helix

131 – 134

4

Beta strand

138 – 141

4

Helix

145 – 147

3

Beta strand

148 – 150

3

Helix

151 – 162

12

Helix

163 – 167

5

Beta strand

170 – 172

3

Beta strand

178 – 183

6

Helix

185 – 187

3

Helix

188 – 196

9

Turn

197 – 199

3

Beta strand

206 – 210

5

Turn

217 – 221

5

Helix

230 – 240

11

Turn

241 – 245

5

Helix

248 – 250

3

Beta strand

259 – 261

3

Helix

271 – 273

3

Beta strand

274 – 293

20

Beta strand

306 – 313

8

Helix

314 – 316

3

Helix

317 – 331

15

Helix

337 – 339

3

Helix

342 – 349

8

Helix

351 – 359

9

Beta strand

386 – 390

5

Beta strand

396 – 401

6

Helix

404 – 406

3

Helix

410 – 423

14

Beta strand

424 – 431

8

Turn

432 – 434

3

Beta strand

435 – 442

8

Turn

443 – 445

3

Helix

446 – 449

4

Helix

453 – 456

4

Turn

465 – 468

4

Beta strand

469 – 472

4

Helix

475 – 477

3

Helix

487 – 500

14

Beta strand

508 – 514

7

Helix

521 – 523

3

Beta strand

524 – 534

11

Beta strand

540 – 548

9

Beta strand

560 – 567

8

Turn

568 – 570

3

Helix

571 – 582

12

Sequences

	Sequence		Length	Mass (Da)
	P05314-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 2B3DCAAC16DE06A3	FASTA	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

EMBL
GenBank
DDBJ

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

PIR

S16603.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.7.7.1. 286.

Family and domain databases

InterPro

IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[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

Search...

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:	January 19, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)