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Reviewed, UniProtKB/Swiss-Prot A5UI29 (DSBD_HAEIG)

Last modified June 16, 2009. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CGSHiGG_07975
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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.

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.

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_1000049610

Regions

Transmembrane178 – 19821 Potential
Transmembrane230 – 25021 Potential
Transmembrane254 – 27421 Potential
Transmembrane296 – 31621 Potential
Transmembrane337 – 35721 Potential
Transmembrane376 – 39621 Potential
Transmembrane397 – 41721 Potential
Transmembrane420 – 44021 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
A5UI29-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: A156D89A9059E681

FASTA57964,454
        10         20         30         40         50         60 
MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDIADGYYL 

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

       130        140        150        160        170        180 
YQGCTEGFCY PPETKVLRIG DLAVSQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWAIFG 

       190        200        210        220        230        240 
FFVLGLGLAF 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 GDLFTGAVTL YLLALGMGVP LMLITLFGNK 

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

       430        440        450        460        470        480 
FGYAIKIISF ALAMVTVQPL QNWIWQTQTT TQSAVENMPV SQVKFKQIKN TEELDRTLAE 

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

       550        560        570 
VMGLPTILFF DQQNNEIKGS RVTGFMDADA FSNWIEKLL 

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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:RESEARCH103.1-RESEARCH103.18(2007) [PubMed: 17550610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000672 Genomic DNA. Translation: ABR00435.1.
RefSeqYP_001292818.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5227482.
GenomeReviewsGene locus CGSHiGG_07975 in contig CP000672_GR.
KEGGhiq:CGSHiGG_07975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA5UI29. PVFLLSR.

Family and domain databases

HAMAPMF_00399.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBD_HAEIG
AccessionPrimary (citable) accession number: A5UI29
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 16, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents