P31973 (FENR_SYNP2) 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
Ordered Locus Names:	SYNPCC7002_A0853

Organism

Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]

Taxonomic identifier

32049 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length	402 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 Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	phycobilisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide 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

Chain

1 – 402

402

Ferredoxin--NADP reductase

PRO_0000167637

Regions

Domain

18 – 74

57

CpcD-like

Domain

120 – 245

126

FAD-binding FR-type

Nucleotide binding

179 – 182

4

FAD

Nucleotide binding

200 – 202

3

FAD

Nucleotide binding

218 – 220

3

FAD

Nucleotide binding

292 – 293

2

NADP By similarity

Nucleotide binding

322 – 323

2

NADP By similarity

Nucleotide binding

332 – 336

5

NADP By similarity

Nucleotide binding

361 – 362

2

NADP By similarity

Sites

Binding site

182

1

NADP By similarity

Binding site

202

1

NADP By similarity

Binding site

206

1

FAD By similarity

Binding site

260

1

FAD By similarity

Binding site

260

1

NADP; via amide nitrogen By similarity

Binding site

332

1

NADP By similarity

Binding site

400

1

NADP By similarity

Secondary structure

1

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402

Helix Strand Turn

Details...

Beta strand

119 – 121

3

Beta strand

123 – 132

10

Beta strand

142 – 148

7

Beta strand

161 – 165

5

Beta strand

167 – 170

4

Turn

171 – 173

3

Beta strand

179 – 183

5

Turn

187 – 192

6

Beta strand

196 – 202

7

Beta strand

205 – 207

3

Turn

209 – 211

3

Beta strand

214 – 216

3

Helix

218 – 224

7

Beta strand

233 – 239

7

Beta strand

252 – 258

7

Helix

259 – 262

4

Helix

263 – 273

11

Beta strand

284 – 294

11

Helix

295 – 297

3

Helix

301 – 310

10

Turn

312 – 314

3

Beta strand

315 – 321

7

Turn

322 – 324

3

Helix

335 – 341

7

Helix

343 – 350

8

Beta strand

355 – 361

7

Helix

363 – 365

3

Helix

366 – 379

14

Helix

384 – 393

10

Beta strand

397 – 401

5

Sequences

	Sequence		Length	Mass (Da)
	P31973 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 5203060291BAFAE7	FASTA	402	45,015
	10 20 30 40 50 60 MYGITSTANS TGNQSYANRL FIYEVVGLGG DGRNENSLVR KSGTTFITVP YARMNQEMQR 70 80 90 100 110 120 ITKLGGKIVS IRPAEDAAQI VSEGQSSAQA SAQSPMASST KIVHPKTTDT SVPVNIYRPK 130 140 150 160 170 180 TPFLGKCIEN YELVDEGGSG TVRHVTFDIS EGDLRYLEGQ SIGIIPPGED KNGKPHKLRL 190 200 210 220 230 240 YSIASTRHGD MEDNKTVSLC VRQLEYQDPE SGETVYGVCS TYLCNLPVGT DDVKITGPVG 250 260 270 280 290 300 KEMLLPDDED ATVVMLATGT GIAPFRAFLW RMFKEQHEDY KFKGKAWLIF GVPYTANILY 310 320 330 340 350 360 KDDFEKMAAE NPDNFRLTYA ISREQKTADG GKVYVQSRVS EYADELFEMI QKPNTHVYMC 370 380 390 400 GLKGMQPPID ETFTAEAEKR GLNWEEMRRS MKKEHRWHVE VY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product." Schluchter W.M., Bryant D.A. Biochemistry 31:3092-3102(1992) [PubMed: 1554697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[2]	"Complete sequence of Synechococcus sp. PCC 7002." Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27264 / PCC 7002 / PR-6.
[3]	"Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant." Schluchter W.M., Zhao J., Bryant D.A. J. Bacteriol. 175:3343-3352(1993) [PubMed: 8501038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M86234 Genomic DNA. Translation: AAA27323.1.
CP000951 Genomic DNA. Translation: ACA98857.1.
M99378 Genomic DNA. Translation: AAA27310.1.

RefSeq

YP_001734113.1. NC_010475.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B5O	X-ray	2.50	A/B	1-402	[»]

ProteinModelPortal

P31973.

SMR

P31973. Positions 111-402.

ModBase

Search...

Protein-protein interaction databases

STRING

P31973.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

6056783.

GenomeReviews

Gene locus SYNPCC7002_A0853 in contig CP000951_GR.

KEGG

syp:SYNPCC7002_A0853.

PATRIC

23816218. VBISynSp37135_1066.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG353752.

OMA

GRMYIQD.

PhylomeDB

P31973.

ProtClustDB

CLSK893276.

Family and domain databases

InterPro

IPR008213. CpcD-like_dom.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

KO

K02641.

PANTHER

PTHR19384:SF1. FRD_Red. 1 hit.

Pfam

PF01383. CpcD. 1 hit.
PF00667. FAD_binding_1. 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...

Entry information

Entry name

FENR_SYNP2

Accession

Primary (citable) accession number: P31973
Secondary accession number(s): B1XII6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program