Reviewed, UniProtKB/Swiss-Prot Q9KPF6 (DLDH_VIBCH)

Names and origin

Protein names

Recommended 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

Organism

Vibrio cholerae [Complete proteome] [HAMAP]

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 475	475	Dihydrolipoyl dehydrogenase		PRO_0000068052
Regions
	Nucleotide binding	36 – 45	10	FAD By similarity
	Nucleotide binding	182 – 186	5	NAD By similarity
	Nucleotide binding	270 – 273	4	NAD By similarity
Sites
	Active site	445	1	Proton acceptor By similarity
	Binding site	54	1	FAD By similarity
	Binding site	117	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	205	1	NAD By similarity
	Binding site	238	1	NAD; via amide nitrogen By similarity
	Binding site	313	1	FAD By similarity
	Binding site	321	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	45 ↔ 50		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KPF6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 85F814A35F8E90F3	FASTA	475	50,995
	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

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE003852 Genomic DNA. Translation: AAF95555.1.
PIR	B82079.
RefSeq	NP_232042.1.
3D structure databases
HSSP	HSSP built from PDB template 1OJT based on UniProtKB Q51225.
ModBase	Search...
Genome annotation databases
GeneID	2613081.
GenomeReviews	Gene locus VC_2412 in contig AE003852_GR.
KEGG	vch:VC2412.
TIGR	VC_2412.
Phylogenomic databases
HOGENOM	Q9KPF6.
OMA	PFIPEDP.
Enzyme and pathway databases
BRENDA	1.8.1.4. 19019.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_VIBCH

Accession

Primary (citable) accession number: Q9KPF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)