Reviewed, UniProtKB/Swiss-Prot P72740 (DLDH_SYNY3)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
      Short name=LPD
    E3 component of pyruvate complex

Gene names

Name:	lpdA
Synonyms:	pdhD
Ordered Locus Names:	slr1096

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.
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	Cell inner membrane; Peripheral membrane protein; Periplasmic side 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	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
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: InterPro plasma membrane 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 474	473	Dihydrolipoyl dehydrogenase		PRO_0000068051
Regions
	Nucleotide binding	36 – 44	9	FAD By similarity
	Nucleotide binding	184 – 188	5	NAD By similarity
	Nucleotide binding	275 – 278	4	NAD By similarity
Sites
	Active site	459	1	Proton acceptor By similarity
	Binding site	53	1	FAD By similarity
	Binding site	119	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	207	1	NAD By similarity
	Binding site	323	1	FAD By similarity
	Binding site	331	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	44 ↔ 49		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P72740-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A2EFD28D8D9C69E1	FASTA	474	50,832
	10 20 30 40 50 60 MSQDFDYDLV IIGAGVGGHG AALHAVKCGL KTAIIEAKDM GGTCVNRGCI PSKALLAASG 70 80 90 100 110 120 RVREMSDQDH LQQLGIQING VTFTREAIAA HANDLVSKIQ SDLTNSLTRL KVDTIRGWGK 130 140 150 160 170 180 VSGPQEVTVI GDNETRILKA KEIMLCPGSV PFVPPGIEID HKTVFTSDEA VKLETLPQWI 190 200 210 220 230 240 AIIGSGYIGL EFSDVYTALG CEVTMIEALP DLMPGFDPEI AKIAERVLIK SRDIETYTGV 250 260 270 280 290 300 FATKIKAGSP VEIELTDAKT KEVIDTLEVD ACLVATGRIP ATKNLGLETV GVETDRRGFI 310 320 330 340 350 360 EVNDQMQVIK DGKPVPHLWA VGDATGKMML AHAASGQGVV AVENICGRKT EVDYRAIPAA 370 380 390 400 410 420 AFTHPEISYV GLTEAQAKEL GEKEGFVVST AKTYFKGNSK ALAEKETDGI AKVVYRQDTG 430 440 450 460 470 ELLGAHIIGI HASDLIQEAA QAIADRKSVR ELAFHVHAHP TLSEVLDEAY KRAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803." Engels A., Pistorius E.K. Microbiology 143:3543-3553(1997) [PubMed: 9387233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000022 Genomic DNA. Translation: BAA16755.1. Different initiation. Z48564 Genomic DNA. Translation: CAA88451.1.
PIR	S74603.
RefSeq	NP_440075.1.
3D structure databases
HSSP	HSSP built from PDB template 1JEH based on UniProtKB P09624.
ModBase	Search...
Protein-protein interaction databases
IntAct	P72740. 2 interactions.
Genome annotation databases
GeneID	953374.
GenomeReviews	Gene locus slr1096 in contig BA000022_GR.
KEGG	syn:slr1096.
NMPDR	fig|1148.1.peg.176.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P72740.
Enzyme and pathway databases
BioCyc	SSP1148:SLR1096-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_SYNY3

Accession

Primary (citable) accession number: P72740
Secondary accession number(s): Q53395

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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