Ferredoxin--NADP reductase 2 - Bacillus thuringiensis (strain Al Hakam)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Ferredoxin--NADP reductase 2
Short name=FNR 2
Short name=Fd-NADP(+) reductase 2
EC=1.18.1.2

Gene names

Ordered Locus Names:

BALH_4465

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2 reduced ferredoxin + NADP⁺ + H⁺ = 2 oxidized ferredoxin + NADPH. HAMAP-Rule MF_01685
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 2 family.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	NADP binding Inferred from electronic annotation. Source: HAMAP ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: HAMAP flavin adenine dinucleotide binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

Ferredoxin--NADP reductase 2 HAMAP-Rule MF_01685

PRO_0000364803

Sites

Binding site

20

1

FAD By similarity

Binding site

39

1

FAD By similarity

Binding site

47

1

FAD By similarity

Binding site

52

1

FAD By similarity

Binding site

92

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

126

1

FAD; via amide nitrogen By similarity

Binding site

287

1

FAD By similarity

Binding site

328

1

FAD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A0RKB9 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 9539B7A18B6378B7
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FASTA

331

36,721

        10         20         30         40         50         60 
MKVAENQKVY DITIIGGGPT GLFTAFYGGM RQASVKIIES LPQLGGQLSA LYPEKYIYDV 

        70         80         90        100        110        120 
AGFPKVRAQE LVDNLKEQMK KFDPTVCLEE AVDTLEKQAD GIFKLVTNKQ THYSKSVIIT 

       130        140        150        160        170        180 
AGNGAFQPRR LELEGTAKYE KKNLHYFVDD MNKFAGKRVV VFGGGDSAVD WTMMLEPIAD 

       190        200        210        220        230        240 
KVTIVHRRDK FRAHEHSVES LMNSRAEVST PYVPVELIGD DKIEQVVLQH VKTEEKIIID 

       250        260        270        280        290        300 
VDDVIVNYGF VSSLGPIKNW GLDIQKNSIL VNSKMETNIP GIYAAGDICT YEGKVKLIAC 

       310        320        330 
GFGEAPTAVN NAKAYFDPNA KLQPMHSSSM F

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References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam."
Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S.

Brettin T.S.
J. Bacteriol. 189:3680-3681(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Al Hakam.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK87662.1.
RefSeq	YP_897169.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0RKB9.
ModBase	Search...
Protein-protein interaction databases
STRING	412694.BALH_4465.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK87662; ABK87662; BALH_4465.
GeneID	4542353.
KEGG	btl:BALH_4465.
PATRIC	19001976. VBIBacThu63319_4959.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0492.
HOGENOM	HOG000072909.
KO	K00384.
OMA	WALMLEP.
ProtClustDB	CLSK873605.
Enzyme and pathway databases
BioCyc	BTHU412694:GH1W-4344-MONOMER.
Family and domain databases
HAMAP	MF_01685. FENR2.
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR022890. Fd--NADP_Rdtase_type_2. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR000103. Pyridine_nuc-diS_OxRdtase_2. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
ProtoNet	Search...

Entry information

Entry name

FENR2_BACAH

Accession

Primary (citable) accession number: A0RKB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents