NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
"Clustering of genes with function in the biosynthesis of bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium vibrioforme.";
Hereditas 125:93-96(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J., Bryant D.A., Richardson P.;
"Complete sequence of Chlorobaculum parvum NCIB 8327.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes (By similarity).
CATALYTIC ACTIVITY: Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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

Z83933; CAB06298.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP001099; ACF11143.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T17191; T17191.

RefSeq

YP_001998343.1; -.

3D structure databases

HSSP

P11959; 1EBD. [HSSP ENTRY / PDB]

ModBase

O50311.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148;	Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from EC).
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

6419649; -.

GenomeReviews

CP001099_GR; Cpar_0724.

CMR

O50311; Cpar_0724.

Other

ProtoNet

O50311.

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

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 469`	`469`	`Dihydrolipoyl dehydrogenase.`	`PRO_0000068023`
`NP_BIND`	`40 48`	`9`	`FAD (By similarity).`
`NP_BIND`	`186 190`	`5`	`NAD (By similarity).`
`NP_BIND`	`275 278`	`4`	`NAD (By similarity).`
`ACT_SITE`	`450 450`		`Proton acceptor (By similarity).`
`BINDING`	`57 57`		`FAD (By similarity).`
`BINDING`	`120 120`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`209 209`		`NAD (By similarity).`
`BINDING`	`317 317`		`FAD (By similarity).`
`BINDING`	`325 325`		`FAD; via amide nitrogen (By similarity).`
`DISULFID`	`48 53`		`Redox-active (By similarity).`
`CONFLICT`	`42 42`		`A -> R (in Ref. 1; CAB06298).`
`CONFLICT`	`463 463`		`A -> S (in Ref. 1; CAB06298).`
`CONFLICT`	`466 467`		`QS -> PN (in Ref. 1; CAB06298).`

Sequence information

Length: 469 AA [This is the length of the unprocessed precursor]

Molecular weight: 48755 Da [This is the MW of the unprocessed precursor]

CRC64: 97FDD6D88E8249F8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQQSESSSAQ FDVAVIGSGP GGYEAALHAA RHGMKVCLVE KASLGGVCVN WGCIPTKALL 

        70         80         90        100        110        120 
RSAEVYDLAK NPSEFGVNVS ELSFDLAQAV KRSRKVSLKS SKGVEFMLKK AKVEVWRGEA 

       130        140        150        160        170        180 
VLTGSKGVKV TAEDGSERSL EAANIIVATG AQPRVIPGLE PDGKKIITSR EALILKDVPE 

       190        200        210        220        230        240 
SMIVVGGGAI GVEMAWFYAK AGAKVTIVEL MPRLLPAEEA EVSEALKRSF EKVDITVQCG 

       250        260        270        280        290        300 
AKLGNVAISE FGVNADLLAE GKEPQKIEAS CMLVAVGVTG VIDGLGLDAA GIETERGFIR 

       310        320        330        340        350        360 
TDELCRTSAS GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKLPEPLSEP LIPRCVYAQP 

       370        380        390        400        410        420 
SVASVGLTEE AAIAAGYKVL VGRSQFAASG KANAYGQLEG FVKLVFNAET GKMLGGHLIG 

       430        440        450        460 
HDAVELIGEL GLACRYGVTA EGLVGTVHAH PTLSETVREA AFAALQSKG

O50311 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools