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Q9KPF6 (DLDH_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex
Gene names
Name:lpd
Ordered Locus Names:VC_2412
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Dihydrolipoyl dehydrogenase
PRO_0000068052

Regions

Nucleotide binding36 – 4510FAD By similarity
Nucleotide binding182 – 1865NAD By similarity
Nucleotide binding270 – 2734NAD By similarity

Sites

Active site4451Proton acceptor By similarity
Binding site541FAD By similarity
Binding site1171FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2051NAD By similarity
Binding site2381NAD; via amide nitrogen By similarity
Binding site3131FAD By similarity
Binding site3211FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond45 ↔ 50Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KPF6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 85F814A35F8E90F3

FASTA47550,995
        10         20         30         40         50         60 
MSKEIKAQVV VLGAGPAGYS AAFRCADLGL DTVIIERYNT LGGVCLNVGC IPSKALLHVA 

        70         80         90        100        110        120 
KVIEEAKALT EHGIVFGEPK TDIDKVRLWK EKVINQLTGG LAGMAKMRKV NVVNGYGKFT 

       130        140        150        160        170        180 
GPNTIEVDGE EGKTVVTFDN AIVAAGSRPI KLPFIPHEDP RIWDSTDALE LKEVPGKLLI 

       190        200        210        220        230        240 
MGGGIIGLEM ATVYHSLGSK IDVVEMFDQL IPAADKDMVK VYTKRIKDKF NLMLETKVTA 

       250        260        270        280        290        300 
VEAKEDGIYV SMEGKSAPAQ AERYDAVLVA IGRVPNGKLL DAEKAGLEVD ERGFIRVDKQ 

       310        320        330        340        350        360 
MRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVISGKKH YFDPKVIPSI AYTEPEVAWV 

       370        380        390        400        410        420 
GKTEKEAKAE GINYEVATFP WAASGRAIAS DCADGMTKLI FDKETHRVIG GAIVGTNGGE 

       430        440        450        460        470 
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GTITDLPNAK AKKKK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE003852 Genomic DNA. Translation: AAF95555.1.
PIRB82079.
RefSeqNP_232042.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KPF6.
SMRQ9KPF6. Positions 19-470.
ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC2412.

Proteomic databases

PRIDEQ9KPF6.

Protocols and materials databases

DNASU2613081.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95555; AAF95555; VC_2412.
GeneID2613081.
KEGGvch:VC2412.
PATRIC20083841. VBIVibCho83274_2295.

Phylogenomic databases

eggNOGCOG1249.
KOK00382.
OMAGMAAEIY.
ProtClustDBPRK06467.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PANTHERPTHR22912:SF20. PTHR22912:SF20. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_VIBCH
AccessionPrimary (citable) accession number: Q9KPF6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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