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A5UDI9 (DSBD_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:CGSHiEE_07605
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length579 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 – 1616 Potential
Chain17 – 579563Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_1000049609

Regions

Transmembrane178 – 19821Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane296 – 31621Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane397 – 41721Helical; Potential
Transmembrane420 – 44021Helical; Potential
Domain449 – 579131Thioredoxin

Amino acid modifications

Disulfide bond124 ↔ 129Redox-active By similarity
Disulfide bond193 ↔ 315Redox-active By similarity
Disulfide bond495 ↔ 498Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UDI9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 12B4D67BC4FAA107

FASTA57964,505
        10         20         30         40         50         60 
MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDITDGYYL 

        70         80         90        100        110        120 
YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGTF NNADDKVEIT 

       130        140        150        160        170        180 
YQGCTEGFCY PPETKVLRIG DLAISQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWTIFG 

       190        200        210        220        230        240 
FFLLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA 

       250        260        270        280        290        300 
AIGLPFQIAL QHPYVMIGLS ILFVVLALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG 

       310        320        330        340        350        360 
AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAATL YLLALGMGVP LMLITLFGNK 

       370        380        390        400        410        420 
ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWEPRL WAGLATVFFI WFALQMSKNG 

       430        440        450        460        470        480 
FGYAIKIISF VLAMVTVQPL QNWIWQTQTT TQSAVENKSV SQVKFKQIKN TEELDRTLAE 

       490        500        510        520        530        540 
NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVNMTKNSP ENKALMERFN 

       550        560        570 
VMGLPTILFF DQQNNEIKGS RVTGFMDADA FSNWLKALH

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed: 17550610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000671 Genomic DNA. Translation: ABQ98840.1.
RefSeqYP_001291223.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UDI9.
SMRA5UDI9. Positions 459-578.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5UDI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5226086.
GenomeReviewsGene locus CGSHiEE_07605 in contig CP000671_GR.
KEGGhip:CGSHiEE_07605.
PATRIC20279198. VBIHaeInf81350_1532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHBG640883.
OMARILPEVW.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycHINF374930:CGSHIEE_07605-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_HAEIE
AccessionPrimary (citable) accession number: A5UDI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 40 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

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