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UniProtKB/Swiss-Prot entry Q9PJI3

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

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Entry information
Entry name DLDH_CHLMU
Primary accession number Q9PJI3
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
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: TC_0846
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
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
AE002160; AAF39644.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B81658; B81658.
RefSeq NP_297219.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
ModBase Q9PJI3.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0846-MON; -.
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: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:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008033; Biological process: tRNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR002218; GIDA.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF01134; GIDA; 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 Q9PJI3.
Genome annotation databases
GeneID 1246214; -.
GenomeReviews AE002160_GR; TC_0846.
KEGG cmu:TC0846; -.
TIGR TC_0846; -.
Phylogenomic databases
HOGENOM Q9PJI3; -.
Other
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_0000068024
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: 49562 Da [This is the MW of the unprocessed precursor] CRC64: 1F395C7550DD5818 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEEREAGG TCLNRGCIPS KALLASAEIV 

        70         80         90        100        110        120 
AQIRHADQFG IHINGFSIDY PAMVQRKDTV VRSIRDGLNG LIRSNKITVF SGRGSLISST 

       130        140        150        160        170        180 
EVKILGETPS VIKAQSIILA TGSEPRAFPG VPFSQQSPRI LCSTGVLNLK EIPQKMAIIG 

       190        200        210        220        230        240 
GGVIGCEFAS LFHTLGSEVS VIEASQQILA LNNPDISKTM FDKFTRHGIR FMLGASVSSI 

       250        260        270        280        290        300 
EDMGDRVRLT INGNIEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDSTMRTNVP 

       310        320        330        340        350        360 
NIYAIGDITG KWQLAHVASH QGIVAARNIA GHKDEIDYSA VPSVIFTFPE VASVGLSPTS 

       370        380        390        400        410        420 
AQQQGIPVKV TKFPFRAIGK AVAMGESDGF AAIISHETSQ QILGAYVIGP HASSLISEIT 

       430        440        450        460 
LAIRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPTRK
Q9PJI3 in FASTA format

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