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UniProtKB/Swiss-Prot entry P42974


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

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Entry information
Entry name DHNA_BACSU
Primary accession number P42974
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name NADH dehydrogenase
Synonyms EC 1.6.99.3
Alkyl hydroperoxide reductase
Gene name
Name: ahpF
Synonyms: ndh
OrderedLocusNames: BSU40100
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;
Kasahara Y., Nakai S., Yoshikawa H., Ogasawara N.;
"36kb sequence between gntZ and trnY of B. subtilis genome.";
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-509.
STRAIN=168 / JH642;
DOI=10.1016/0378-1119(94)90735-8; PubMed=8125345 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Aronson A.I.;
"A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene.";
Gene 140:85-90(1994).
[4]
PROTEIN SEQUENCE OF 1-29.
STRAIN=168 / YB886;
PubMed=8180695 [NCBI, ExPASy, EBI, Israel, Japan]
Hartford O.M., Dowds B.C.A.;
"Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis.";
Microbiology 140:297-304(1994).
Comments
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
D78193; BAA11269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99124; CAB16047.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19710; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR G69583; G69583.
RefSeq NP_391890.1; -.
3D structure databases
HSSP P35340; 1FL2. [HSSP ENTRY / PDB]
ModBase P42974.
Enzyme and pathway databases
BioCyc BSUB224308:BSU4007-MON; -.
Organism-specific databases
SubtiList BG11204; ahpF. [Micado]
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0003954; Molecular function: NADH dehydrogenase activity (inferred from electronic annotation from EC).
GO:0015035; Molecular function: protein disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 2.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000238; AhpF; 1.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03140; AhpF; 1.
PROSITE PS51354; GLUTAREDOXIN_2; 1.
PS00573; PYRIDINE_REDOX_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P42974.
Genome annotation databases
GeneID 937717; -.
GenomeReviews AL009126_GR; BSU40100.
KEGG bsu:BSU40100; -.
NMPDR fig|224308.1.peg.4016; -.
Phylogenomic databases
HOGENOM P42974; -.
Genome annotation databases
CMR P42974; BSU40100.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase; Redox-active center; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1    509  509     NADH dehydrogenase. PRO_0000166789
NP_BIND   210    241  32     FAD (By similarity). 
NP_BIND   349    379  31     NAD (By similarity). 
NP_BIND   469    479  11     FAD (By similarity). 
REGION   1   ?183        Membrane-binding. 
REGION   ?184    509        Catalytic. 
DISULFID   337    340        Redox-active (By similarity). 
CONFLICT   29     29        G -> E (in Ref. 4; AA sequence). 
CONFLICT   227    227        T -> D (in Ref. 3). 
CONFLICT   393    393        Y -> I (in Ref. 3). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 54874 Da [This is the MW of the unprocessed precursor] CRC64: 487FFF089CA3A079 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVLDANIKAQ LNQYMQLIEN DIVLKVSAGE DDTSKDMLAL VDELASMSSK ISVEKAELNR 

        70         80         90        100        110        120 
TPSFSVNRVG EDTGVTFAGI PLGHEFTSLV LALLQVSGRP PKVDQKVIDQ VKKISGEYHF 

       130        140        150        160        170        180 
ESYISLTCHN CPDVVQALNM MSVLNPNITH TMIDGAAYKA EVESKNIMAV PTVYLNGESF 

       190        200        210        220        230        240 
GSGRMTLEEI LAKMGSGTDA SEFADKEPFD VLVVGGGPAG ASAAIYTARK GIRTGVVAER 

       250        260        270        280        290        300 
FGGQVLDTMS IENFISVKAT EGPKLAASLE EHVKEYDIDV MNLQRAKRLE KKDLFELELE 

       310        320        330        340        350        360 
NGAVLKSKTV ILSTGARWRN VNVPGEQEFK NKGVAYCPHC DGPLFEGKDV AVIGGGNSGI 

       370        380        390        400        410        420 
EAAIDLAGIV NHVTVLEFAP ELKADEVLQK RLYSLPNVTV VKNAQTKEIT GDQSVNGITY 

       430        440        450        460        470        480 
VDRETGEEKH VELQGVFVQI GLVPNTEWLE GTVERNRMGE IIVDKHGATS VPGLFAAGDC 

       490        500 
TDSAYNQIII SMGSGATAAL GAFDYLIRN 

P42974 in FASTA format

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