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Reviewed, UniProtKB/Swiss-Prot Q928C2 (NAMA_LISIN)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADPH dehydrogenase
    EC=1.6.99.1
Alternative name(s):
    Xenobiotic reductase
Gene names
Name: namA
Ordered Locus Names: lin2614
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Catalytic activity

NADPH + acceptor = NADP+ + reduced acceptor. HAMAP MF_01614

Cofactor

FMN By similarity.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.

Ontologies

Keywords
   LigandFMN
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFMN binding

Inferred from electronic annotation. Source: InterPro

NADPH dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338NADPH dehydrogenase HAMAP MF_01614
PRO_0000216122

Regions

Nucleotide binding22 – 265FMN By similarity

Sites

Binding site271Substrate By similarity
Binding site1631Substrate By similarity
Binding site1661Substrate By similarity
Binding site2141FMN By similarity
Binding site3071FMN By similarity

Sequences

Sequence LengthMass (Da)Tools
Q928C2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 491FECA770CA6C48

FASTA33837,120
        10         20         30         40         50         60 
MSKLFSEYKL KDVTLKNRIV MSPMCMYSVE NKDGIATDFH FAHYVSRAAG GTGLVILEAT 

        70         80         90        100        110        120 
AVQEVGRISE FDLGLWNDEQ VPALKRLVDG LHYHGAKAGI QLAHAGRKAV LPGEIVAPSA 

       130        140        150        160        170        180 
IPFDEKSAKP VELTKEAIKE VVADFKRAAY RAKEAGFDVI EIHAAHGYLI HQFLSPISNR 

       190        200        210        220        230        240 
REDNYGGPAG NRYKILSDII KAVKEVWDGP IIVRVSATDY AHGGLQLEDH IPFAKWMKAD 

       250        260        270        280        290        300 
GVELIDVSTG GLVNVEPPVF PGYQVPFADE IRRGAGIATG ALGLITRGEQ AEEILCNERA 

       310        320        330 
DLIIIGRELL RNPYFAKEAA ETLGETIEAP KQYSRAWK 

« Hide

Cross-references

Sequence databases

AL596173 Genomic DNA. Translation: CAC97841.1.
PIRAI1758.
RefSeqNP_471944.1.

3D structure databases

HSSPHSSP built from PDB template 1ICQ based on UniProtKB Q9XG54.
ModBaseSearch...

Genome annotation databases

GeneID1131443.
GenomeReviewsGene locus lin2614 in contig AL592022_GR.
KEGGlin:lin2614.
NMPDRfig|272626.1.peg.2597.

Organism-specific databases

ListiListLIN2614.
CMRSearch...

Phylogenomic databases

HOGENOMQ928C2.
OMAQ928C2. WVEDGWN.

Enzyme and pathway databases

BioCycLINN272626:LIN2614-MON.
BRENDA1.6.99.1. 270396.

Family and domain databases

HAMAPMF_01614.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00724. Oxidored_FMN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNAMA_LISIN
AccessionPrimary (citable) accession number: Q928C2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents