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UniProtKB/Swiss-Prot entry P72740

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

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Entry information
Entry name DLDH_SYNY3
Primary accession number P72740
Secondary accession number Q53395
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 73)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
LPD
E3 component of pyruvate complex
Gene name
Name: lpdA
Synonyms: pdhD
OrderedLocusNames: slr1096
From
Synechocystis sp. (strain PCC 6803) [TaxID: 1148] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/3.3.109; PubMed=8905231 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, AND CHARACTERIZATION.
PubMed=9387233 [NCBI, ExPASy, EBI, Israel, Japan]
Engels A., Pistorius E.K.;
"Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803.";
Microbiology 143:3543-3553(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
BA000022; BAA16755.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48564; CAA88451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S74603; S74603.
RefSeq NP_440075.1; -.
3D structure databases
HSSP P09624; 1JEH. [HSSP ENTRY / PDB]
ModBase P72740.
Protein-protein interaction databases
IntAct P72740; 2.
Enzyme and pathway databases
BioCyc SSP1148:SLR1096-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
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: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 953374; -.
GenomeReviews BA000022_GR; slr1096.
KEGG syn:slr1096; -.
NMPDR fig|1148.1.peg.176; -.
Phylogenomic databases
HOGENOM P72740; -.
Genome annotation databases
CMR P72740; slr1096.
Other
ProtoNet P72740.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   474  473     Dihydrolipoyl dehydrogenase. PRO_0000068051
NP_BIND   36    44  9     FAD (By similarity). 
NP_BIND   184   188  5     NAD (By similarity). 
NP_BIND   275   278  4     NAD (By similarity). 
ACT_SITE   459   459        Proton acceptor (By similarity). 
BINDING   53    53        FAD (By similarity). 
BINDING   119   119        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   207   207        NAD (By similarity). 
BINDING   323   323        FAD (By similarity). 
BINDING   331   331        FAD; via amide nitrogen (By similarity). 
DISULFID   44    49        Redox-active (By similarity). 
Sequence information
Length: 474 AA [This is the length of the unprocessed precursor] Molecular weight: 50832 Da [This is the MW of the unprocessed precursor] CRC64: A2EFD28D8D9C69E1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSQDFDYDLV IIGAGVGGHG AALHAVKCGL KTAIIEAKDM GGTCVNRGCI PSKALLAASG 

        70         80         90        100        110        120 
RVREMSDQDH LQQLGIQING VTFTREAIAA HANDLVSKIQ SDLTNSLTRL KVDTIRGWGK 

       130        140        150        160        170        180 
VSGPQEVTVI GDNETRILKA KEIMLCPGSV PFVPPGIEID HKTVFTSDEA VKLETLPQWI 

       190        200        210        220        230        240 
AIIGSGYIGL EFSDVYTALG CEVTMIEALP DLMPGFDPEI AKIAERVLIK SRDIETYTGV 

       250        260        270        280        290        300 
FATKIKAGSP VEIELTDAKT KEVIDTLEVD ACLVATGRIP ATKNLGLETV GVETDRRGFI 

       310        320        330        340        350        360 
EVNDQMQVIK DGKPVPHLWA VGDATGKMML AHAASGQGVV AVENICGRKT EVDYRAIPAA 

       370        380        390        400        410        420 
AFTHPEISYV GLTEAQAKEL GEKEGFVVST AKTYFKGNSK ALAEKETDGI AKVVYRQDTG 

       430        440        450        460        470 
ELLGAHIIGI HASDLIQEAA QAIADRKSVR ELAFHVHAHP TLSEVLDEAY KRAV
P72740 in FASTA format

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