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UniProtKB/Swiss-Prot entry O84561

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

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Entry information
Entry name DLDH_CHLTR
Primary accession number O84561
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 66)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex
Gene name
Name: lpdA
OrderedLocusNames: CT_557
From
Chlamydia trachomatis [TaxID: 813] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=D/UW-3/Cx;
DOI=10.1126/science.282.5389.754; PubMed=9784136 [NCBI, ExPASy, EBI, Israel, Japan]
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis.";
Science 282:754-759(1998).
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
AE001273; AAC68159.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E71500; E71500.
RefSeq NP_220072.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
ModBase O84561.
Enzyme and pathway databases
BioCyc CTRA315277:CT557-MON; -.
2D gel databases
PHCI-2DPAGE O84561; -.
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: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 884341; -.
GenomeReviews AE001273_GR; CT_557.
KEGG ctr:CT557; -.
Phylogenomic databases
HOGENOM O84561; -.
Genome annotation databases
CMR O84561; CT_557.
Other
ProtoNet O84561.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   465  465     Dihydrolipoyl dehydrogenase. PRO_0000068026
NP_BIND   34    42  9     FAD (By similarity). 
NP_BIND   180   184  5     NAD (By similarity). 
NP_BIND   264   267  4     NAD (By similarity). 
ACT_SITE   439   439        Proton acceptor (By similarity). 
BINDING   51    51        FAD (By similarity). 
BINDING   114   114        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   203   203        NAD (By similarity). 
BINDING   237   237        NAD; via amide nitrogen (By similarity). 
BINDING   307   307        FAD (By similarity). 
BINDING   315   315        FAD; via amide nitrogen (By similarity). 
DISULFID   42    47        Redox-active (By similarity). 
Sequence information
Length: 465 AA [This is the length of the unprocessed precursor] Molecular weight: 49491 Da [This is the MW of the unprocessed precursor] CRC64: 56449CCD2AB61477 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEKREAGG TCLNRGCIPS KALLAGAEVV 

        70         80         90        100        110        120 
TQIRHADQFG IHVEGFSINY PAMVQRKDSV VRSIRDGLNG LIRSNKITVF SGRGSLISST 

       130        140        150        160        170        180 
EVKILGENPS VIKAHSIILA TGSEPRAFPG IPFSAESPRI LCSTGVLNLK EIPQKMAIIG 

       190        200        210        220        230        240 
GGVIGCEFAS LFHTLGSEVS VIEASSQILA LNNPDISKTM FDKFTRQGLR FVLEASVSNI 

       250        260        270        280        290        300 
EDIGDRVRLT INGNVEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDATMRTNVP 

       310        320        330        340        350        360 
NIYAIGDITG KWQLAHVASH QGIIAARNIA GHKEEIDYSA VPSVIFTFPE VASVGLSPTA 

       370        380        390        400        410        420 
AQQQKIPVKV TKFPFRAIGK AVAMGEADGF AAIISHETTQ QILGAYVIGP HASSLISEIT 

       430        440        450        460 
LAVRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPAKK
O84561 in FASTA format

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