NADPH dehydrogenase - Bacillus pumilus (strain SAFR-032)

Preferred order of sections

Names and origin

Protein names

Recommended name:
NADPH dehydrogenase
EC=1.6.99.1

Alternative name(s):
Xenobiotic reductase

Gene names

Name:	namA
Ordered Locus Names:	BPUM_2112

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reduction of the double bond of an array of alpha, beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes By similarity. HAMAP MF_01614
Catalytic activity	NADPH + acceptor = NADP⁺ + reduced acceptor. HAMAP MF_01614
Cofactor	FMN By similarity. HAMAP MF_01614
Subunit structure	Homotetramer By similarity. HAMAP MF_01614
Sequence similarities	Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.

Ontologies

Keywords
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH dehydrogenase activity Inferred from electronic annotation. Source: EC pentaerythritol trinitrate reductase activity Inferred from electronic annotation. Source: EC trichloro-p-hydroquinone reductive dehalogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 338

338

NADPH dehydrogenase HAMAP MF_01614

PRO_1000069456

Regions

Nucleotide binding

23 – 27

5

FMN By similarity

Sites

Binding site

28

1

Substrate By similarity

Binding site

164

1

Substrate By similarity

Binding site

167

1

Substrate By similarity

Binding site

215

1

FMN By similarity

Binding site

308

1

FMN By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A8FEW4 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 55640EE0A00E7407
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FASTA

338

37,484

        10         20         30         40         50         60 
METKLFSPWT LKGVTLKNRI VMSPMCMYSS YDRDGKLQPF HFTHYISRAQ GQAGLIMVEA 

        70         80         90        100        110        120 
SAVSPEGRIS DQDLGIWSDE HIEGFASLNE QIKAYGTKTA IQLAHAGRKA ELDGDILAPS 

       130        140        150        160        170        180 
SIPFDEQSKT PVQMSVDQIK DTVQAFQDAA VRAKKAGFDI IEIHGAHGYL INEFLSPLAN 

       190        200        210        220        230        240 
HRTDDYGGSP ENRYRFLREV VNAVNEVWDG PLFVRVSASD YTTKGLDIAD YIGIATWLKE 

       250        260        270        280        290        300 
QGVDLIDVSS GAVVQARIST FPGYQVTFAE KIKEGAGIQT GAVGLITSGV QAEEILRNQR 

       310        320        330 
ADLIFIGREF LRDPYFPKTA AEELRTSIEG PRQYDRAW

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References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032."
Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C.

Weinstock G.M.
PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV62781.1.
RefSeq	YP_001487341.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FEW4.
SMR	A8FEW4. Positions 4-338.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FEW4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000065120; EBBACP00000063453; EBBACG00000065111.
GeneID	5621381.
GenomeReviews	Gene locus BPUM_2112 in contig CP000813_GR.
KEGG	bpu:BPUM_2112.
PATRIC	18968128. VBIBacPum16546_2160.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1902.
GeneTree	EBGT00050000002219.
HOGENOM	HBG583461.
OMA	WVEDGWN.
ProtClustDB	PRK13523.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_2112-MONOMER.
Family and domain databases
HAMAP	MF_01614. NamA. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR023663. NADPH_DH. IPR001155. OxRdtase_FMN_N. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00724. Oxidored_FMN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAMA_BACP2

Accession

Primary (citable) accession number: A8FEW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 27 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

Regions

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