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Protein

Dihydrolipoyl dehydrogenase

Gene

Ppha_2012

Organism
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein predictedi

Functioni

Catalytic activityi

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

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GlycolysisSAAS annotation

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADUniRule annotation

Enzyme and pathway databases

BioCyciPPHA324925:GHBF-2051-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Ordered Locus Names:Ppha_2012Imported
OrganismiPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)Imported
Taxonomic identifieri324925 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon
Proteomesi
  • UP000002724 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi324925.Ppha_2012.

Structurei

3D structure databases

ProteinModelPortaliB4SCL9.
SMRiB4SCL9. Positions 2-478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 340336FAD/NAD-binding_domInterPro annotationAdd
BLAST
Domaini359 – 467109Pyr_redox_dimInterPro annotationAdd
BLAST

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiVFISIGR.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4SCL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKQFDVLVI GAGPGGYIAA IRAAQLGFSV ACCEFSAYDD PAGEPRLGGT
60 70 80 90 100
CLNAGCIPLK ALVASSELFE KASHHLAEHG ITFGGVNIDV ATMQQRKEAI
110 120 130 140 150
VTKMTAGVQF LFRKNRITLL KGRGSFAGRT DAGYRIMING KDGEEELLAQ
160 170 180 190 200
KVIIATGSKA RQIPNIAVDN VCICDNEGAL KFTEAPKKLG VIGAGVIGLE
210 220 230 240 250
VGSVWRRLGA EVTILEVMTS FLGAADESVS REASKLFLKQ GLHIKLGVRI
260 270 280 290 300
GQAKQTANGV SIAYTDDQGS EHILECDKLI VSVGRTPYTE GLNLEAIGLQ
310 320 330 340 350
TDERGFIPVN DHCATAAPGV YAIGDVVRGP MLAHKAEDEG VMAAELIAGQ
360 370 380 390 400
KPHLDYNSMP WVIYTTPEIA WVGKTEQQLR KEGHDYKTGQ FPFAANGRAL
410 420 430 440 450
GLGDAEGFIK MLADATTDEI LGVHIIGASA SDLIAEAALA MEFRASSEDV
460 470
ARTCHPHPSL SEVMREAALA IEKRALNM
Length:478
Mass (Da):50,916
Last modified:September 23, 2008 - v1
Checksum:i11DBC9BA16A4DE51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001110 Genomic DNA. Translation: ACF44224.1.
RefSeqiWP_012508704.1. NC_011060.1.

Genome annotation databases

EnsemblBacteriaiACF44224; ACF44224; Ppha_2012.
KEGGipph:Ppha_2012.
PATRICi22904776. VBIPelPha134556_2160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001110 Genomic DNA. Translation: ACF44224.1.
RefSeqiWP_012508704.1. NC_011060.1.

3D structure databases

ProteinModelPortaliB4SCL9.
SMRiB4SCL9. Positions 2-478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi324925.Ppha_2012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF44224; ACF44224; Ppha_2012.
KEGGipph:Ppha_2012.
PATRICi22904776. VBIPelPha134556_2160.

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.
HOGENOMiHOG000276708.
KOiK00382.
OMAiVFISIGR.
OrthoDBiEOG6QCD6D.

Enzyme and pathway databases

BioCyciPPHA324925:GHBF-2051-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5477 / BU-1Imported.

Entry informationi

Entry nameiB4SCL9_PELPB
AccessioniPrimary (citable) accession number: B4SCL9
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: April 13, 2016
This is version 59 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.