Q5LRA7 (Q5LRA7_RUEPO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase RuleBase RU003692
EC=1.8.1.4 RuleBase RU003692

Gene names

Ordered Locus Names:

SPO2222 EMBL AAV95488.1

Organism

Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP] EMBL AAV95488.1

Taxonomic identifier

246200 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria › Ruegeria pomeroyi

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. RuleBase RU003692
Cofactor	Binds 1 FAD per subunit By similarity. RuleBase RU003692
Miscellaneous	The active site is a redox-active disulfide bond By similarity. RuleBase RU003692
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691

Ontologies

Keywords
Domain	Redox-active center RuleBase RU003691
Ligand	FAD RuleBase RU003691 Flavoprotein RuleBase RU003691 NAD RuleBase RU003692 Pyruvate EMBL AAV95488.1
Molecular function	Oxidoreductase RuleBase RU003691
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Traceable author statement Ref.1. Source: TIGR cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosolic pyruvate dehydrogenase complex Traceable author statement Ref.1. Source: TIGR
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5LRA7 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 590944C589FBCDA7	FASTA	464	49,696
	10 20 30 40 50 60 MAAQSYDVIV IGAGPGGYVA AIRAAQLGLK ACVVEREHLG GICLNWGCIP TKALLRSSEV 70 80 90 100 110 120 FHLMERAKEF GLKADNIGYD LDAVVKRSRG VAKQLSGGIG HLMKKNKIDV VMGEATIPAK 130 140 150 160 170 180 GKVSVKTDKG TQELTAKNII LATGARAREL PGLEADGDLV WTYKHALQPV RMPKKLLVIG 190 200 210 220 230 240 SGAIGIEFAS FYNTLGADTT VVEVMDRVLP VEDAEISAFA KKSFVKQGMK IMEKSMVKQL 250 260 270 280 290 300 DRAKGKVTAH IETGGKVEKL EFDTVISAVG IVGNVENLGL EALGVKIDRT HVVTDAYCRT 310 320 330 340 350 360 GVEGLYAIGD IAGAPWLAHK ASHEGVMVAE LIAGKHAHPV KPESIAGCTY CHPQVASVGY 370 380 390 400 410 420 TEAKAKELGY DIKVGRFPFI GNGKAIALGE VEGMIKTIFD AKTGELLGAH MVGAEVTEMI 430 440 450 460 QGYVVGRQLE TTEEDLMHTV FPHPTLSEMM HESVLDAYGR VIHM

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000031 Genomic DNA. Translation: AAV95488.1.
RefSeq	YP_167448.1. NC_003911.11.
3D structure databases
ProteinModelPortal	Q5LRA7.
ModBase	Search...
Protein-protein interaction databases
STRING	246200.SPO2222.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV95488; AAV95488; SPO2222.
GeneID	3194814.
KEGG	sil:SPO2222.
PATRIC	23377797. VBIRuePom114501_2250.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000276708.
KO	K00382.
OMA	EHEGVVC.
ProtClustDB	PRK06416.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. 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]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q5LRA7_RUEPO

Accession

Primary (citable) accession number: Q5LRA7

Entry history

Integrated into UniProtKB/TrEMBL:	February 1, 2005
Last sequence update:	February 1, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)