Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6D9J6 (DSBD_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbD

EC=1.8.1.8
Alternative name(s):
Protein-disulfide reductase
Short name=Disulfide reductase
Gene names
Name:dsbD
Ordered Locus Names:ECA0618
OrganismErwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]
Taxonomic identifier29471 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length577 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 MF_00399

Catalytic activity

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

Subcellular location

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

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 577554Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000304385

Regions

Transmembrane182 – 20221Helical; Potential
Transmembrane225 – 24521Helical; Potential
Transmembrane255 – 27521Helical; Potential
Transmembrane308 – 32821Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane369 – 38921Helical; Potential
Transmembrane396 – 41621Helical; Potential
Domain437 – 577141Thioredoxin

Amino acid modifications

Disulfide bond131 ↔ 137Redox-active By similarity
Disulfide bond194 ↔ 316Redox-active By similarity
Disulfide bond492 ↔ 495Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D9J6 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 28B54B667E4016C0

FASTA57762,917
        10         20         30         40         50         60 
MAQRIFTLIF LLWTAVGTPQ VAASSFGQKL FGNSTTSRFL PVDGAFAFEF QQQGNQLNLR 

        70         80         90        100        110        120 
WDIHPDYYLY RAQIKIEGNG ATLGKVELPQ GESHNDEFFG QVFILRDRLA LAVPIEQAES 

       130        140        150        160        170        180 
GATVKVTYQG CADAGFCYPP ETRTVPLSQV LATANTDSPI NTLSGQTAPP QTTPMPFSPW 

       190        200        210        220        230        240 
WALLIGIGVA FTPCVLPMYP LIASLVLGRK EQLTPRRTLL LSMTYVQGMA LTYTLLGLIV 

       250        260        270        280        290        300 
AAAGLRFQAA LQHPYILIGL SVMFIALALS MFGLYTLQLP SSVQTRLTEW SNRQQGGSVT 

       310        320        330        340        350        360 
GVFCMGALAG LICSPCTTAP LSAILLYIAQ SGNMLAGGGT LYLYALGMGL PLILVTLFGN 

       370        380        390        400        410        420 
KLLPRSGPWM QYVKEAFGFI ILALPVFLLE RILGEAWGIR LWSALGIAFF GWALMLTLSS 

       430        440        450        460        470        480 
KKGWMRGVQL LLLAGVVISA KPLQDWVFPP TGTAQTHTSA LNFAPVANIA DLNSALAKSP 

       490        500        510        520        530        540 
QPVMLDLYAD WCVACKEFEK YTFSDPAVQN HLSRITLLQA DVTANREEQN ALLKKLQVLG 

       550        560        570 
LPTIVFFDTQ GKEIPGSRVT GFMNAEQFQA HLQKFSP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG73534.1.
RefSeqYP_048735.1. NC_004547.2.

3D structure databases

HSSPHSSP built from PDB template 1VRS based on UniProtKB P36655.
ProteinModelPortalQ6D9J6.
SMRQ6D9J6. Positions 37-152, 461-577.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2882295.
GenomeReviewsGene locus ECA0618 in contig BX950851_GR.
KEGGeca:ECA0618.
NMPDRfig|218491.3.peg.2966.
PATRIC20476406. VBIPecAtr54885_0614.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG640883.
OMATHILWAG.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycECAR218491:ECA0618-MONOMER.

Family and domain databases

HAMAPMF_00399. DbsD.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR022910. Thiol_diS_interchange_DbsD.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK04084.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBD_ERWCT
AccessionPrimary (citable) accession number: Q6D9J6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families