Ferredoxin--NADP reductase 2 - Bacillus thuringiensis subsp. konkukian (strain 97-27)

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:

BT9727_4639

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [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_0000364805

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

Q6HBX6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 9539B7A18B6378B7
Show »

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

« Hide

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis."
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., 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., Hill K.K., Hitchcock P.

Gilna P.
J. Bacteriol. 188:3382-3390(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63212.1.
RefSeq	YP_038950.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HBX6.
ModBase	Search...
Protein-protein interaction databases
STRING	281309.BT9727_4639.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT63212; AAT63212; BT9727_4639.
GeneID	2858766.
KEGG	btk:BT9727_4639.
PATRIC	18990478. VBIBacThu119411_4937.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0492.
HOGENOM	HOG000072909.
KO	K00384.
OMA	WALMLEP.
ProtClustDB	CLSK873605.
Enzyme and pathway databases
BioCyc	BTHU281309:GJID-4731-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_BACHK

Accession

Primary (citable) accession number: Q6HBX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 65 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