Reviewed, UniProtKB/Swiss-Prot P57303 (DLDH_BUCAI)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes

Gene names

Name:	lpdA
Ordered Locus Names:	BU207

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity.
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
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 – 473	473	Dihydrolipoyl dehydrogenase		PRO_0000068019
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	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)
	P57303-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: E851CEE0105E1C5D	FASTA	473	51,955
	10 20 30 40 50 60 MNKKIYTQVV VIGSGPAGYS AAFRCADLGL DTVLIERYDK LGGVCLNVGC IPSKTLLHIA 70 80 90 100 110 120 KVIKEAKELH KTGVSFNKPD IDIKKIKNWK QHIVNKLTDG LSSMRKKRKI RIFQGHAIFE 130 140 150 160 170 180 TDKSLCVTNT EDKFTIFFDN AIIATGSKPI KIPSIPHDDI RIWDSTDALS LKKIPNNFLI 190 200 210 220 230 240 IGSGIIGLEM ATIYSALGSK VDIIDRFNHF LPVIDEDISS IYKKSINQQF NLMLNTHIDK 250 260 270 280 290 300 VEVKKDALIV DMIHENIPKK NILYDAVLVA IGRTPNIDSL GLDRIGLKIN NFGFIQVNNQ 310 320 330 340 350 360 LKTNIPHIYA IGDVAGTPML AHKGVHEGHI AAEVISGKNH YFEPKVIPSI AYTDPEIAWV 370 380 390 400 410 420 GLSEKEAKQE NINYEVAIFP WNASGRAIAS NCSIGKTKLI FNKQNNKIIG GSIVGSNAGE 430 440 450 460 470 LIGEVGLAIE MGCDAEDIAL TIHAHPTLSE SIGLSAEVFQ GTVTDVLNFK LNK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12924.1.
RefSeq	NP_240038.1.
3D structure databases
HSSP	HSSP built from PDB template 1OJT based on UniProtKB Q51225.
ModBase	Search...
Genome annotation databases
GeneID	1109650.
GenomeReviews	Gene locus BU207 in contig BA000003_GR.
KEGG	buc:BU207.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57303.
OMA	MMDGLMA.
Enzyme and pathway databases
BioCyc	BSP107806:BU207-MON.
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_BUCAI

Accession

Primary (citable) accession number: P57303

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 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)