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Reviewed, UniProtKB/Swiss-Prot P30960 (CYCY_BRAJA)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 cycY
Alternative name(s):
    Cytochrome c biogenesis protein cycY
Gene names
Name: cycY
Synonyms: ccmG
Ordered Locus Names: blr0471
OrganismBradyrhizobium japonicum [Complete proteome] [HAMAP]
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for disulfide bond formation in some periplasmic proteins. Also act as a disulfide oxidoreductase in cytochromes c biogenesis. The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur By similarity.

Subcellular location

Periplasm Probable.

Sequence similarities

Belongs to the thioredoxin family. DsbE subfamily.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Biological processCytochrome c-type biogenesis
   Cellular componentPeriplasm
   DomainRedox-active center
Signal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cytochrome complex assembly

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular functiondisulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 194157Thiol:disulfide interchange protein cycY
PRO_0000034287

Regions

Domain46 – 190145Thioredoxin

Amino acid modifications

Disulfide bond92 ↔ 95Redox-active Ref.3

Secondary structure

....................... 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30960-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 826A75D22AA0C593

FASTA19421,126
        10         20         30         40         50         60 
MSEQSTSANP QRRTFLMVLP LIAFIGLALL FWFRLGSGDP SRIPSALIGR PAPQTALPPL 

        70         80         90        100        110        120 
EGLQADNVQV PGLDPAAFKG KVSLVNVWAS WCVPCHDEAP LLTELGKDKR FQLVGINYKD 

       130        140        150        160        170        180 
AADNARRFLG RYGNPFGRVG VDANGRASIE WGVYGVPETF VVGREGTIVY KLVGPITPDN 

       190 
LRSVLLPQME KALK 

« Hide

References

« Hide 'large scale' references
[1]"Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes."
Ramseier T.M., Winteler H.V., Hennecke H.
J. Biol. Chem. 266:7793-7803(1991) [PubMed: 1850420] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110RIF15.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.
[3]"Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment."
Edeling M.A., Guddat L.W., Fabianek R.A., Thoeny-Meyer L., Martin J.L.
Structure 10:973-979(2002) [PubMed: 12121652] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 39-194, DISULFIDE BOND.

Cross-references

Sequence databases

M60874 Genomic DNA. Translation: AAA26196.1. Different initiation.
BA000040 Genomic DNA. Translation: BAC45736.1.
PIRD39741.
RefSeqNP_767111.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KNGX-ray1.14A39-194[»]
ModBaseSearch...

Genome annotation databases

GeneID1048774.
GenomeReviewsGene locus blr0471 in contig BA000040_GR.
KEGGbja:blr0471.
NMPDRfig|224911.1.peg.471.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP30960.
OMAP30960. KWLAEFH.

Enzyme and pathway databases

BioCycBJAP224911:BLR0471-MON.

Family and domain databases

InterProIPR004799. periplasmic_diS_OxRdtase_DsbE.
IPR013740. Redoxin.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
ProDomPD003679. Thioredoxin_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00385. dsbE. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYCY_BRAJA
AccessionPrimary (citable) accession number: P30960
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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