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UniProtKB/Swiss-Prot entry P09623

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

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Entry information
Entry name DLDH_PIG
Primary accession number P09623
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 84)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
Gene name
Name: DLD
Synonyms: LAD
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3693355 [NCBI, ExPASy, EBI, Israel, Japan]
Otulakowski G., Robinson B.H.;
"Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases.";
J. Biol. Chem. 262:17313-17318(1987).
[2]
 PROTEIN SEQUENCE OF 36-89; 91-104; 317-331; 346-360; 388-417 AND 450-482.
TISSUE=Heart;
PubMed=6954534 [NCBI, ExPASy, EBI, Israel, Japan]
Williams C.H. Jr., Arscott L.D., Schulz G.E.;
"Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase.";
Proc. Natl. Acad. Sci. U.S.A. 79:2199-2201(1982).
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
J03489; AAA31069.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28448; DEPGLP.
RefSeq NP_999227.1; -.
UniGene Ssc.224
3D structure databases
HSSP P09624; 1JEH. [HSSP ENTRY / PDB]
SMR P09623; 37-509.
ModBase P09623.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
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:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
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.
ProtoNet P09623.
Genome annotation databases
GeneID 397129; -.
KEGG ssc:397129; -.
Phylogenomic databases
HOVERGEN P09623; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    35  35     Mitochondrion. 
CHAIN   36   509  474     Dihydrolipoyl dehydrogenase, mitochondrial. PRO_0000030298
NP_BIND   71    80  10     FAD (By similarity). 
NP_BIND   183   185  3     FAD (By similarity). 
NP_BIND   220   227  8     NAD (By similarity). 
NP_BIND   361   364  4     FAD (By similarity). 
ACT_SITE   487   487        Proton acceptor (By similarity). 
BINDING   89    89        FAD (By similarity). 
BINDING   154   154        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   243   243        NAD (By similarity). 
BINDING   278   278        NAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   314   314        NAD; via amide nitrogen (By similarity). 
BINDING   355   355        FAD (By similarity). 
MOD_RES   127   127        N6-acetyllysine (By similarity). 
DISULFID   80    85        Redox-active (By similarity). 
CONFLICT   95    97        SHY -> GHA (in Ref. 2; AA sequence). 
CONFLICT   346   346        K -> R (in Ref. 2; AA sequence). 
CONFLICT   351   351        Y -> A (in Ref. 2; AA sequence). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 54185 Da [This is the MW of the unprocessed precursor] CRC64: 38A0469FED071300 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQSWSRVYCT LAKRGHFNRI AHGLQGVSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 

       130        140        150        160        170        180 
EKMMEQKSNA VKALTGGIAH LFKQNKVVRV NGYGKITGKN QVTATKADGS TEVINTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTV VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVELLGHVGG IGIDMEVSKN FQRILQKQGF KFKLNTKVIG ATKKSDGNID VSIEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 

       370        380        390        400        410        420 
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 

       430        440        450        460        470        480 
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHIIGPGA GEMINEAALA LEYGASCEDI 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKAINF
P09623 in FASTA format

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