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UniProtKB/Swiss-Prot entry O34324


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

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Entry information
Entry name DLDH3_BACSU
Primary accession number O34324
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 76)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of acetoin cleaving system
Gene name
Name: acoL
Synonyms: yfjH
OrderedLocusNames: BSU08090
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=10368162 [NCBI, ExPASy, EBI, Israel, Japan]
Huang M., Oppermann-Sanio F.B., Steinbuchel A.;
"Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway.";
J. Bacteriol. 181:3837-3841(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AC327;
PubMed=8969503 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto H., Uchiyama S., Sekiguchi J.;
"Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization.";
Microbiology 142:3057-3065(1996).
[3]
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).
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
AF006075; AAC05585.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D78509; BAA24293.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99108; CAB12638.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69581; G69581.
RefSeq NP_388690.1; -.
3D structure databases
HSSP P14218; 1LPF. [HSSP ENTRY / PDB]
ModBase O34324.
Enzyme and pathway databases
BioCyc BSUB224308:BSU0809-MON; -.
Organism-specific databases
SubtiList BG12561; ACOL. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045150; Biological process: acetoin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01350; lipoamide_DH; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
Genome annotation databases
GeneID 939702; -.
GenomeReviews AL009126_GR; BSU08090.
KEGG bsu:BSU08090; -.
NMPDR fig|224308.1.peg.809; -.
Phylogenomic databases
HOGENOM O34324; -.
Genome annotation databases
CMR O34324; BSU08090.
Other
ProtoNet O34324.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetoin catabolism; Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   458  458     Dihydrolipoyl dehydrogenase. PRO_0000068018
NP_BIND   30    38  9     FAD (By similarity). 
NP_BIND   177   181  5     NAD (By similarity). 
NP_BIND   263   266  4     NAD (By similarity). 
ACT_SITE   437   437        Proton acceptor (By similarity). 
BINDING   47    47        FAD (By similarity). 
BINDING   112   112        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   200   200        NAD (By similarity). 
BINDING   305   305        FAD (By similarity). 
BINDING   313   313        FAD; via amide nitrogen (By similarity). 
DISULFID   38    43        Redox-active (By similarity). 
Sequence information
Length: 458 AA [This is the length of the unprocessed precursor] Molecular weight: 48853 Da [This is the MW of the unprocessed precursor] CRC64: 2496832534945183 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTLAIIGGGP AGYAAAVSAA QQGRNVLLID KGKLGGTCLN EGCIPTKSLL ESANVLDKIK 

        70         80         90        100        110        120 
HADSFGIELP AGAISVDWSK MQSRKQQVVS QLVQGVQYLM KKNQIQVVKG TASFLSERKL 

       130        140        150        160        170        180 
LIEGENGKEI READQVLIAS GSEPIELPFA PFDGEWILDS KDALSLSEIP SSLVIVGGGV 

       190        200        210        220        230        240 
IGCEYAGLFA RLGSQVTIIE TADRLIPAED EDIARLFQEK LEEDGVEVHT SSRLGRVDQT 

       250        260        270        280        290        300 
AKTAIWKSGQ REFKTKADYV LVAIGRKPRL DGLQLEQAGV DFSPKGIPVN GHMQTNVPHI 

       310        320        330        340        350        360 
YACGDAIGGI QLAHAAFHEG IIAASHASGR DVKINEKHVP RCIYTSPEIA CIGMTERQAR 

       370        380        390        400        410        420 
SIYGDVKIGE FSFSANGKAL IKQQAEGKVK IMAEPEFGEI VGVSMIGPDV TELIGQAAAI 

       430        440        450 
MNGEMTADMA EHFIAAHPTL SETLHEALLS TIGLAVHA 

O34324 in FASTA format

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