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UniProtKB/Swiss-Prot entry P54550


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NAMA_BACSU
Primary accession number P54550
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name NADPH dehydrogenase
Synonyms EC 1.6.99.1
Xenobiotic reductase
Gene name
Name: namA
OrderedLocusNames: BSU23820
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes.";
Microbiology 142:3103-3111(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION.
STRAIN=168;
DOI=10.1074/jbc.M211778200; PubMed=12660247 [NCBI, ExPASy, EBI, Israel, Japan]
Fitzpatrick T.B., Amrhein N., Macheroux P.;
"Characterization of yqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response.";
J. Biol. Chem. 278:19891-19897(2003).
[4]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATES, AND SUBUNIT.
DOI=10.1074/jbc.M502587200; PubMed=15890652 [NCBI, ExPASy, EBI, Israel, Japan]
Kitzing K., Fitzpatrick T.B., Wilken C., Sawa J., Bourenkov G.P., Macheroux P., Clausen T.;
"The 1.3 A crystal structure of the flavoprotein YqjM reveals a novel class of old yellow enzymes.";
J. Biol. Chem. 280:27904-27913(2005).
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.
  • CATALYTIC ACTIVITY: NADPH + acceptor = NADP+ + reduced acceptor.
  • COFACTOR: FMN.
  • ENZYME REGULATION: Inhibited by p-hydroxybenzaldehyde (pHBA) and p-nitrophenol (pNP).
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=19 µM for duroquinone;
    KM=109 µM for nitroglycerin;
    KM=293 µM for cyclohex-2-enone;
    KM=705 µM for 2,4,6-trinitrotoluene;
    KM=841 µM for menadione;
    KM=2602 µM for trans-hex-2-enal;
    Note=The highest catalytic efficiency was observed with N- ethylmaleimide for which the KM is inferior to 1.0 µM;
  • SUBUNIT: Homotetramer. Composed of a dimer of active dimers.
  • INDUCTION: By toxic xenobiotic compounds (2,4,6-trinitrotoluene and nitroglycerin), and in response to oxidative stress (hydrogen peroxide and paraquat).
  • MISCELLANEOUS: Forms a charge transfer complex with a variety of phenolic compounds.
  • SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D84432; BAA12619.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99116; CAB14314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E69964; E69964.
RefSeq NP_390263.1; -.
3D structure databases
PDB
1Z41; X-ray; 1.30 A; A/B=1-338.[ExPASy / RCSB / EBI]
1Z42; X-ray; 1.85 A; A/B=1-338.[ExPASy / RCSB / EBI]
1Z44; X-ray; 1.40 A; A/B=1-338.[ExPASy / RCSB / EBI]
1Z48; X-ray; 1.80 A; A/B=1-338.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1Z41; -.
1Z42; -.
1Z44; -.
1Z48; -.
ModBase P54550.
Enzyme and pathway databases
BioCyc BSUB224308:BSU2381-MON; -.
Organism-specific databases
SubtiList BG11742; namA. [Micado]
Ontologies
GO
GO:0003959; Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01614; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.
BLOCKS P54550.
Genome annotation databases
GeneID 938698; -.
GenomeReviews AL009126_GR; BSU23820.
KEGG bsu:BSU23820; -.
NMPDR fig|224308.1.peg.2387; -.
Phylogenomic databases
HOGENOM P54550; -.
Genome annotation databases
CMR P54550; BSU23820.
Other
ProtoNet P54550.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   338  337     NADPH dehydrogenase. PRO_0000216119
NP_BIND   23    27  5     FMN. 
BINDING   28    28        Substrate. 
BINDING   164   164        Substrate. 
BINDING   167   167        Substrate. 
BINDING   215   215        FMN. 
BINDING   308   308        FMN. 
HELIX   4     6  3      
STRAND   9    11  3      
STRAND   14    22  9      
STRAND   33    35  3      
HELIX   39    50  12      
STRAND   54    64  11      
HELIX   65    67  3      
HELIX   79    81  3      
HELIX   82    94  13      
STRAND   98   104  7      
HELIX   107   109  3      
STRAND   117   121  5      
HELIX   136   155  20      
STRAND   159   165  7      
HELIX   170   175  6      
TURN   177   179  3      
STRAND   187   189  3      
HELIX   190   207  18      
STRAND   212   217  6      
HELIX   228   240  13      
STRAND   245   249  5      
TURN   262   265  4      
HELIX   266   276  11      
STRAND   279   282  4      
HELIX   289   297  9      
STRAND   302   306  5      
HELIX   308   312  5      
HELIX   316   323  8      
HELIX   332   334  3      
TURN   335   337  3      
Sequence information
Length: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37584 Da [This is the MW of the unprocessed precursor] CRC64: BDC52D34236326FE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARKLFTPIT IKDMTLKNRI VMSPMCMYSS HEKDGKLTPF HMAHYISRAI GQVGLIIVEA 

        70         80         90        100        110        120 
SAVNPQGRIT DQDLGIWSDE HIEGFAKLTE QVKEQGSKIG IQLAHAGRKA ELEGDIFAPS 

       130        140        150        160        170        180 
AIAFDEQSAT PVEMSAEKVK ETVQEFKQAA ARAKEAGFDV IEIHAAHGYL IHEFLSPLSN 

       190        200        210        220        230        240 
HRTDEYGGSP ENRYRFLREI IDEVKQVWDG PLFVRVSASD YTDKGLDIAD HIGFAKWMKE 

       250        260        270        280        290        300 
QGVDLIDCSS GALVHADINV FPGYQVSFAE KIREQADMAT GAVGMITDGS MAEEILQNGR 

       310        320        330 
ADLIFIGREL LRDPFFARTA AKQLNTEIPA PVQYERGW 

P54550 in FASTA format

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