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UniProtKB/Swiss-Prot entry P66004

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

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Entry information
Entry name DLDH_MYCTU
Primary accession number P66004
Secondary accession number O53747
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of alpha keto acid dehydrogenase complexes
Gene name
Name: lpd
OrderedLocusNames: Rv0462, MT0478
ORFNames: MTV038.06
From
Mycobacterium tuberculosis [TaxID: 1773] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
[3]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD, DISULFIDE BOND, SUBUNIT, FUNCTION, AND MUTAGENESIS OF ASP-5; ASN-43; ARG-93; LYS-103; HIS-386 AND PHE-464.
DOI=10.1074/jbc.M507466200; PubMed=16093239 [NCBI, ExPASy, EBI, Israel, Japan]
Rajashankar K.R., Bryk R., Kniewel R., Buglino J.A., Nathan C.F., Lima C.D.;
"Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis.";
J. Biol. Chem. 280:33977-33983(2005).
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
BX842573; CAA17417.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK44702.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B70828; B70828.
RefSeq NP_214976.1; -.
NP_334888.1; -.
3D structure databases
PDB
2A8X; X-ray; 2.40 A; A/B=1-464.[ExPASy / RCSB / EBI]
PDBsum 2A8X; -.
ModBase P66004.
Organism-specific databases
TubercuList Rv0462; -.
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).
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 P66004.
Genome annotation databases
GeneID 886300; -.
923824; -.
GenomeReviews AE000516_GR; MT0478.
AL123456_GR; Rv0462.
KEGG mtc:MT0478; -.
mtu:Rv0462; -.
TIGR MT0478; -.
Phylogenomic databases
HOGENOM P66004; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   464  464     Dihydrolipoyl dehydrogenase. PRO_0000068034
NP_BIND   33    41  9     FAD. 
NP_BIND   178   182  5     NAD (By similarity). 
NP_BIND   266   269  4     NAD (By similarity). 
ACT_SITE   443   443        Proton acceptor (By similarity). 
BINDING   50    50        FAD. 
BINDING   113   113        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   201   201        NAD (By similarity). 
BINDING   309   309        FAD. 
BINDING   317   317        FAD; via amide nitrogen. 
DISULFID   41    46        Redox-active. 
MUTAGEN   5     5        D->A: Reduces lipoamide dehydrogenase activity by 95%. 
MUTAGEN   43    43        N->A: Reduces lipoamide dehydrogenase activity by 89%. 
MUTAGEN   93    93        R->A: Reduces lipoamide dehydrogenase activity by 94%. 
MUTAGEN   93    93        R->E: Reduces lipoamide dehydrogenase activity by 96%. 
MUTAGEN   103   103        K->E: Reduces lipoamide dehydrogenase activity by 82%. 
MUTAGEN   386   386        H->K: Reduces lipoamide dehydrogenase activity by 91%. 
MUTAGEN   464   464        F->A: Reduces lipoamide dehydrogenase activity by 95%. 
STRAND   2     9  8      
HELIX   13    24  12      
STRAND   29    32  4      
HELIX   39    44  6      
HELIX   46    65  20      
TURN   66    70  5      
STRAND   71    73  3      
HELIX   79   103  25      
STRAND   107   109  3      
STRAND   111   125  15      
STRAND   131   140  10      
STRAND   144   146  3      
HELIX   161   165  5      
STRAND   172   177  6      
HELIX   181   192  12      
STRAND   196   200  5      
STRAND   202   207  6      
HELIX   212   225  14      
STRAND   228   230  3      
STRAND   234   240  7      
STRAND   245   253  9      
STRAND   255   265  11      
STRAND   269   271  3      
STRAND   274   276  3      
HELIX   278   281  4      
STRAND   289   291  3      
STRAND   304   306  3      
HELIX   308   311  4      
HELIX   317   332  16      
HELIX   342   344  3      
STRAND   347   349  3      
STRAND   351   359  9      
HELIX   362   367  6      
STRAND   372   378  7      
HELIX   379   381  3      
HELIX   383   388  6      
STRAND   394   400  7      
TURN   401   404  4      
STRAND   405   413  9      
HELIX   416   419  4      
HELIX   420   428  9      
HELIX   433   436  4      
HELIX   448   458  11      
Sequence information
Length: 464 AA [This is the length of the unprocessed precursor] Molecular weight: 49239 Da [This is the MW of the unprocessed precursor] CRC64: DD93D95DC6F76B22 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA IVEPKYWGGV CLNVGCIPSK ALLRNAELVH 

        70         80         90        100        110        120 
IFTKDAKAFG ISGEVTFDYG IAYDRSRKVA EGRVAGVHFL MKKNKITEIH GYGTFADANT 

       130        140        150        160        170        180 
LLVDLNDGGT ESVTFDNAII ATGSSTRLVP GTSLSANVVT YEEQILSREL PKSIIIAGAG 

       190        200        210        220        230        240 
AIGMEFGYVL KNYGVDVTIV EFLPRALPNE DADVSKEIEK QFKKLGVTIL TATKVESIAD 

       250        260        270        280        290        300 
GGSQVTVTVT KDGVAQELKA EKVLQAIGFA PNVEGYGLDK AGVALTDRKA IGVDDYMRTN 

       310        320        330        340        350        360 
VGHIYAIGDV NGLLQLAHVA EAQGVVAAET IAGAETLTLG DHRMLPRATF CQPNVASFGL 

       370        380        390        400        410        420 
TEQQARNEGY DVVVAKFPFT ANAKAHGVGD PSGFVKLVAD AKHGELLGGH LVGHDVAELL 

       430        440        450        460 
PELTLAQRWD LTASELARNV HTHPTMSEAL QECFHGLVGH MINF
P66004 in FASTA format

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