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Q46WH2 (Q46WH2_CUPPJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbD HAMAP-Rule MF_00399

EC=1.8.1.8 HAMAP-Rule MF_00399
Alternative name(s):
Protein-disulfide reductase HAMAP-Rule MF_00399
Gene names
Name:dsbD HAMAP-Rule MF_00399
Ordered Locus Names:Reut_A3151 EMBL AAZ62511.1
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP] EMBL AAZ62511.1
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00399

Catalytic activity

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP-Rule MF_00399

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00399.

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily. HAMAP-Rule MF_00399

Contains 1 thioredoxin domain. HAMAP-Rule MF_00399

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 By similarity HAMAP-Rule MF_00399

Regions

Transmembrane212 – 23221Helical; By similarity HAMAP-Rule MF_00399
Transmembrane258 – 27821Helical; By similarity HAMAP-Rule MF_00399
Transmembrane290 – 31021Helical; By similarity HAMAP-Rule MF_00399
Transmembrane334 – 35421Helical; By similarity HAMAP-Rule MF_00399
Transmembrane375 – 39521Helical; By similarity HAMAP-Rule MF_00399
Transmembrane410 – 43021Helical; By similarity HAMAP-Rule MF_00399
Transmembrane431 – 45121Helical; By similarity HAMAP-Rule MF_00399
Transmembrane467 – 48721Helical; By similarity HAMAP-Rule MF_00399
Domain488 – 634147Thioredoxin By similarity HAMAP-Rule MF_00399

Amino acid modifications

Disulfide bond143 ↔ 149Redox-active By similarity HAMAP-Rule MF_00399
Disulfide bond231 ↔ 351Redox-active By similarity HAMAP-Rule MF_00399
Disulfide bond550 ↔ 553Redox-active By similarity HAMAP-Rule MF_00399

Sequences

Sequence LengthMass (Da)Tools
Q46WH2 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 6F99003AB556A031

FASTA63967,140
        10         20         30         40         50         60 
MSMGFALLAR SYGAGWARHI AAVLAVMVAW LCLVTGAHAA TEDDFLPPEQ AFRFAARQID 

        70         80         90        100        110        120 
PQTIEVRFDV ASGYYLYRER FAFAARPDTV RLGQPEFPHG KVKFDETFGK EMETYRDAVV 

       130        140        150        160        170        180 
IRLPVQSAPA DGKWSLVVTS QGCADKGLCY PPMESVYKVG GSPLGNLFAD RPRSEATVPP 

       190        200        210        220        230        240 
AASARPGTEA VAPPARLDEN DRIAGVLASR NLGVVLALFF GLGLLLTFTP CVLPMVPILS 

       250        260        270        280        290        300 
SIVVGEHATR SRALVVSLAY VLGMAVVYTA IGVAAGLLGE GLAAALQTPA VLAAFAALMV 

       310        320        330        340        350        360 
ALSLSMFGLY ELQLPQHWQT RLTATSNRRQ GGQVIGAAAM GAISALIVGP CVTAPLAGAL 

       370        380        390        400        410        420 
AYIAQTRDAV TGGTALLAMA LGMGVPLVLV GVGAGNLLPR AGHWMEATKR FFGFLLLGVA 

       430        440        450        460        470        480 
IWMVTPVLPA WLTMALWAAL LLVAAVFLGA FDALGAEARG LARLGKGLGV LAALAGAILL 

       490        500        510        520        530        540 
LGLASGGRDP LQPLAHLSLA RVAGGGAETA AGPQSVRFER VRSVAELDAR VAQAAAAGKP 

       550        560        570        580        590        600 
VLLDFYADWC VSCKEMEHLT FTDAKVRARM SEIVLLQADV TANNADDKAL LKRFGLFGPP 

       610        620        630 
GIILFGADGR ERPVRVIGYQ SAGRFLDSLE RAFGTRPST 

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References

[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 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ62511.1.
RefSeqYP_297355.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ46WH2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A3151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ62511; AAZ62511; Reut_A3151.
GeneID3610991.
KEGGreu:Reut_A3151.
PATRIC20232016. VBIRalEut24049_3834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHOG000254982.
KOK04084.
OMASCIEMEK.
OrthoDBEOG69D3B9.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-3205-MONOMER.

Family and domain databases

Gene3D2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPMF_00399. DbsD.
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERPTHR32234. PTHR32234. 1 hit.
PfamPF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ46WH2_CUPPJ
AccessionPrimary (citable) accession number: Q46WH2
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)