Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiol:disulfide interchange protein DsbD

Gene

dsbD

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.UniRule annotation

Catalytic activityi

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

Cytochrome c-type biogenesisUniRule annotation, Electron transportUniRule annotation, Transport

Keywords - Ligandi

NADUniRule annotation

Enzyme and pathway databases

BioCyciCPIN264198:GIW3-3205-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbDUniRule annotation (EC:1.8.1.8UniRule annotation)
Alternative name(s):
Protein-disulfide reductaseUniRule annotation
Gene namesi
Name:dsbDUniRule annotation
Ordered Locus Names:Reut_A3151Imported
OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))Imported
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002697 Componenti: Chromosome 1

Subcellular locationi

  • Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei212 – 23221HelicalUniRule annotationAdd
BLAST
Transmembranei258 – 27821HelicalUniRule annotationAdd
BLAST
Transmembranei290 – 31021HelicalUniRule annotationAdd
BLAST
Transmembranei334 – 35421HelicalUniRule annotationAdd
BLAST
Transmembranei375 – 39521HelicalUniRule annotationAdd
BLAST
Transmembranei410 – 43021HelicalUniRule annotationAdd
BLAST
Transmembranei431 – 45121HelicalUniRule annotationAdd
BLAST
Transmembranei467 – 48721HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membraneUniRule annotation, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939UniRule annotationAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi143 ↔ 149Redox-activeUniRule annotation
Disulfide bondi231 ↔ 351Redox-activeUniRule annotation
Disulfide bondi550 ↔ 553Redox-activeUniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_A3151.

Structurei

3D structure databases

ProteinModelPortaliQ46WH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini488 – 634147ThioredoxinUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbD subfamily.UniRule annotation
Contains 1 thioredoxin domain.UniRule annotation

Keywords - Domaini

Redox-active centerUniRule annotation, SignalUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG4232.
HOGENOMiHOG000254982.
KOiK04084.
OMAiYISQTRD.
OrthoDBiEOG69D3B9.

Family and domain databases

Gene3Di2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_00399. DbsD.
InterProiIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERiPTHR32234:SF0. PTHR32234:SF0. 1 hit.
PfamiPF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q46WH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMGFALLAR SYGAGWARHI AAVLAVMVAW LCLVTGAHAA TEDDFLPPEQ
60 70 80 90 100
AFRFAARQID PQTIEVRFDV ASGYYLYRER FAFAARPDTV RLGQPEFPHG
110 120 130 140 150
KVKFDETFGK EMETYRDAVV IRLPVQSAPA DGKWSLVVTS QGCADKGLCY
160 170 180 190 200
PPMESVYKVG GSPLGNLFAD RPRSEATVPP AASARPGTEA VAPPARLDEN
210 220 230 240 250
DRIAGVLASR NLGVVLALFF GLGLLLTFTP CVLPMVPILS SIVVGEHATR
260 270 280 290 300
SRALVVSLAY VLGMAVVYTA IGVAAGLLGE GLAAALQTPA VLAAFAALMV
310 320 330 340 350
ALSLSMFGLY ELQLPQHWQT RLTATSNRRQ GGQVIGAAAM GAISALIVGP
360 370 380 390 400
CVTAPLAGAL AYIAQTRDAV TGGTALLAMA LGMGVPLVLV GVGAGNLLPR
410 420 430 440 450
AGHWMEATKR FFGFLLLGVA IWMVTPVLPA WLTMALWAAL LLVAAVFLGA
460 470 480 490 500
FDALGAEARG LARLGKGLGV LAALAGAILL LGLASGGRDP LQPLAHLSLA
510 520 530 540 550
RVAGGGAETA AGPQSVRFER VRSVAELDAR VAQAAAAGKP VLLDFYADWC
560 570 580 590 600
VSCKEMEHLT FTDAKVRARM SEIVLLQADV TANNADDKAL LKRFGLFGPP
610 620 630
GIILFGADGR ERPVRVIGYQ SAGRFLDSLE RAFGTRPST
Length:639
Mass (Da):67,140
Last modified:September 13, 2005 - v1
Checksum:i6F99003AB556A031
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62511.1.
RefSeqiWP_011299294.1. NC_007347.1.

Genome annotation databases

EnsemblBacteriaiAAZ62511; AAZ62511; Reut_A3151.
KEGGireu:Reut_A3151.
PATRICi20232016. VBIRalEut24049_3834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA. Translation: AAZ62511.1.
RefSeqiWP_011299294.1. NC_007347.1.

3D structure databases

ProteinModelPortaliQ46WH2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264198.Reut_A3151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ62511; AAZ62511; Reut_A3151.
KEGGireu:Reut_A3151.
PATRICi20232016. VBIRalEut24049_3834.

Phylogenomic databases

eggNOGiCOG4232.
HOGENOMiHOG000254982.
KOiK04084.
OMAiYISQTRD.
OrthoDBiEOG69D3B9.

Enzyme and pathway databases

BioCyciCPIN264198:GIW3-3205-MONOMER.

Family and domain databases

Gene3Di2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_00399. DbsD.
InterProiIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERiPTHR32234:SF0. PTHR32234:SF0. 1 hit.
PfamiPF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JMP134 / LMG 1197Imported.

Entry informationi

Entry nameiQ46WH2_CUPPJ
AccessioniPrimary (citable) accession number: Q46WH2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 22, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.