P21890 (FENR_ANASO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferredoxin--NADP reductase
Short name=FNR
EC=1.18.1.2

Gene names

Name:

petH

Organism

Anabaena sp. (strain PCC 7119)

Taxonomic identifier

1168 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Subcellular location	Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note: May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 cpcD-like domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Cellular component	Membrane Phycobilisome Thylakoid
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	phycobilisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	NADP binding Traceable author statement PubMed 15110249. Source: UniProtKB ferredoxin-NADP+ reductase activity Traceable author statement PubMed 15110249. Source: UniProtKB flavin adenine dinucleotide binding Traceable author statement PubMed 15110249. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
isiB	P0A3E0	5	EBI-593915,EBI-593907
petF	P0A3C8	5	EBI-593915,EBI-637080

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 440

440

Ferredoxin--NADP reductase

PRO_0000167632

Regions

Domain

17 – 75

59

CpcD-like

Domain

155 – 279

125

FAD-binding FR-type

Nucleotide binding

214 – 217

4

FAD

Nucleotide binding

235 – 237

3

FAD

Nucleotide binding

253 – 255

3

FAD

Nucleotide binding

330 – 331

2

NADP By similarity

Nucleotide binding

360 – 361

2

NADP

Nucleotide binding

370 – 374

5

NADP

Nucleotide binding

399 – 400

2

NADP By similarity

Sites

Binding site

217

1

NADP By similarity

Binding site

237

1

NADP

Binding site

241

1

FAD

Binding site

294

1

FAD

Binding site

294

1

NADP; via amide nitrogen

Binding site

438

1

NADP By similarity

Experimental info

Sequence conflict

180

1

I → L AA sequence Ref.3

Secondary structure

1

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440

Helix Strand Turn

Details...

Beta strand

144 – 147

4

Beta strand

151 – 153

3

Beta strand

158 – 167

10

Beta strand

173 – 175

3

Beta strand

177 – 183

7

Turn

185 – 187

3

Beta strand

196 – 200

5

Beta strand

202 – 204

3

Beta strand

208 – 210

3

Beta strand

214 – 218

5

Turn

222 – 227

6

Beta strand

228 – 237

10

Beta strand

240 – 242

3

Beta strand

243 – 248

6

Beta strand

249 – 251

3

Helix

253 – 259

7

Beta strand

266 – 273

8

Beta strand

275 – 277

3

Beta strand

286 – 292

7

Helix

293 – 295

3

Helix

296 – 307

12

Helix

309 – 314

6

Beta strand

324 – 332

9

Helix

333 – 335

3

Helix

339 – 348

10

Turn

350 – 352

3

Beta strand

353 – 359

7

Turn

360 – 362

3

Beta strand

368 – 370

3

Helix

373 – 379

7

Helix

381 – 388

8

Beta strand

393 – 399

7

Helix

403 – 416

14

Turn

417 – 419

3

Helix

422 – 431

10

Beta strand

435 – 439

5

Sequences

	Sequence		Length	Mass (Da)
	P21890 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 8E1F61D0F09338B6	FASTA	440	48,865
	10 20 30 40 50 60 MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV PYNRMNQEMQ 70 80 90 100 110 120 RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS EGNGKATPVK TDSGAKAFAK 130 140 150 160 170 180 PPAEEQLKKK DNKGNTMTQA KAKHADVPVN LYRPNAPFIG KVISNEPLVK EGGIGIVQHI 190 200 210 220 230 240 KFDLTGGNLK YIEGQSIGII PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE 250 260 270 280 290 300 YKHPESGETV YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR 310 320 330 340 350 360 TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP DNFRLTYAIS 370 380 390 400 410 420 REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL RGMEEGIDAA LSAAAAKEGV 430 440 TWSDYQKDLK KAGRWHVETY

References

[1]	"Homology of the N-terminal domain of the petH gene product from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker polypeptide." Fillat M.F., Flores E., Gomez-Moreno C. Plant Mol. Biol. 22:725-729(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of the ferredoxin-NADP(+)-reductase gene from Anabaena PCC 7119." Fillat M.F., Bakker H.A.C., Weisbeek P.J. Nucleic Acids Res. 18:7161-7161(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-440.
[3]	"Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis." Sancho J., Peleato M.L., Gomez-Moreno C., Edmondson D.E. Arch. Biochem. Biophys. 260:200-207(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 152-183. Strain: 1403.46.
[4]	"X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8-A resolution, and crystallographic studies of NADP+ binding at 2.25-A resolution." Serre L., Vellieux F.M.D., Medina M., Gomez-Moreno C., Fontecilla-Camps J.-C., Frey M. J. Mol. Biol. 263:20-39(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
[5]	"Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer." Martinez-Julvez M., Hermoso J., Hurley J.K., Mayoral T., Sanz-Aparicio J., Tollin G., Gomez-Moreno C., Medina M. Biochemistry 37:17680-17691(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-440.
[6]	"Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by X-ray crystallography." Mayoral T., Medina M., Sanz-Aparicio J., Gomez-Moreno C., Hermoso J.A. Proteins 38:60-69(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
[7]	"Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule." Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M. Acta Crystallogr. D 56:1408-1412(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X72394 Genomic DNA. Translation: CAA51088.1.
X54039 Genomic DNA. Translation: CAA37973.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B2R	X-ray	1.80	A	137-440	[»]
1BJK	X-ray	2.30	A	146-440	[»]
1BQE	X-ray	2.45	A	146-440	[»]
1E62	X-ray	2.30	A	137-440	[»]
1E63	X-ray	2.30	A	137-440	[»]
1E64	X-ray	2.30	A	137-440	[»]
1EWY	X-ray	2.38	A/B	138-440	[»]
1GJR	X-ray	2.10	A	137-440	[»]
1GO2	X-ray	1.70	A	137-440	[»]
1GR1	X-ray	2.50	A	138-440	[»]
1H42	X-ray	2.15	A	137-440	[»]
1H85	X-ray	2.30	A	146-440	[»]
1OGI	X-ray	1.64	A	138-440	[»]
1OGJ	X-ray	1.64	A	138-440	[»]
1QGY	X-ray	1.70	A	146-440	[»]
1QGZ	X-ray	2.30	A	146-440	[»]
1QH0	X-ray	1.93	A	146-440	[»]
1QUE	X-ray	1.80	A	138-440	[»]
1QUF	X-ray	2.25	A	137-440	[»]
1W34	X-ray	1.73	A	137-439	[»]
1W35	X-ray	1.90	A	137-439	[»]
1W87	X-ray	3.00	A/B	137-439	[»]
2BMW	X-ray	1.50	A	137-440	[»]
2BSA	X-ray	1.92	A	138-439	[»]
2VYQ	X-ray	1.90	A	137-439	[»]
2VZL	X-ray	1.93	A	137-439	[»]
2X3U	X-ray	1.93	A	138-439	[»]

ProteinModelPortal

P21890.

SMR

P21890. Positions 138-440.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21890. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

PANTHER

PTHR19384:SF1. PTHR19384:SF1. 1 hit.

Pfam

PF01383. CpcD. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000361. Frd-NADP+_RD. 1 hit.

PRINTS

PR00371. FPNCR.

SMART

SM01094. CpcD. 1 hit.
[Graphical view]

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51441. CPCD_LIKE. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P21890.

Entry information

Entry name

FENR_ANASO

Accession

Primary (citable) accession number: P21890

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program