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Q5LRA7

- Q5LRA7_RUEPO

UniProt

Q5LRA7 - Q5LRA7_RUEPO

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Protein

Dihydrolipoyl dehydrogenase

Gene

SPO2222

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.UniRule annotation

Cofactori

Note: Binds 1 FAD per subunit.

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: TIGR
  2. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADUniRule annotation, PyruvateImported

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Ordered Locus Names:SPO2222Imported
OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)Imported
Taxonomic identifieri246200 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
ProteomesiUP000001023: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytosolic pyruvate dehydrogenase complex Source: TIGR
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi246200.SPO2222.

Structurei

3D structure databases

ProteinModelPortaliQ5LRA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.UniRule annotation

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

HOGENOMiHOG000276708.
KOiK00382.
OMAiKLKIPGC.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5LRA7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAQSYDVIV IGAGPGGYVA AIRAAQLGLK ACVVEREHLG GICLNWGCIP
60 70 80 90 100
TKALLRSSEV FHLMERAKEF GLKADNIGYD LDAVVKRSRG VAKQLSGGIG
110 120 130 140 150
HLMKKNKIDV VMGEATIPAK GKVSVKTDKG TQELTAKNII LATGARAREL
160 170 180 190 200
PGLEADGDLV WTYKHALQPV RMPKKLLVIG SGAIGIEFAS FYNTLGADTT
210 220 230 240 250
VVEVMDRVLP VEDAEISAFA KKSFVKQGMK IMEKSMVKQL DRAKGKVTAH
260 270 280 290 300
IETGGKVEKL EFDTVISAVG IVGNVENLGL EALGVKIDRT HVVTDAYCRT
310 320 330 340 350
GVEGLYAIGD IAGAPWLAHK ASHEGVMVAE LIAGKHAHPV KPESIAGCTY
360 370 380 390 400
CHPQVASVGY TEAKAKELGY DIKVGRFPFI GNGKAIALGE VEGMIKTIFD
410 420 430 440 450
AKTGELLGAH MVGAEVTEMI QGYVVGRQLE TTEEDLMHTV FPHPTLSEMM
460
HESVLDAYGR VIHM
Length:464
Mass (Da):49,696
Last modified:February 1, 2005 - v1
Checksum:i590944C589FBCDA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV95488.1.
RefSeqiYP_167448.1. NC_003911.12.

Genome annotation databases

EnsemblBacteriaiAAV95488; AAV95488; SPO2222.
GeneIDi3194814.
KEGGisil:SPO2222.
PATRICi23377797. VBIRuePom114501_2250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV95488.1 .
RefSeqi YP_167448.1. NC_003911.12.

3D structure databases

ProteinModelPortali Q5LRA7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246200.SPO2222.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV95488 ; AAV95488 ; SPO2222 .
GeneIDi 3194814.
KEGGi sil:SPO2222.
PATRICi 23377797. VBIRuePom114501_2250.

Phylogenomic databases

HOGENOMi HOG000276708.
KOi K00382.
OMAi KLKIPGC.
OrthoDBi EOG6QCD6D.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700808 / DSM 15171 / DSS-3Imported.

Entry informationi

Entry nameiQ5LRA7_RUEPO
AccessioniPrimary (citable) accession number: Q5LRA7
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 2005
Last sequence update: February 1, 2005
Last modified: November 26, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3