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Protein

Thiol:disulfide interchange protein CycY

Gene

cycY

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cytochrome c-type biogenesis

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-474-MONOMER.
RETL1328306-WGS:GSTH-4038-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein CycY
Alternative name(s):
Cytochrome c biogenesis protein CycY
Gene namesi
Name:cycY
Synonyms:ccmG
Ordered Locus Names:blr0471
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
Proteomesi
  • UP000002526 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence analysisAdd
BLAST
Chaini38 – 194157Thiol:disulfide interchange protein CycYPRO_0000034287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 ↔ 95Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi224911.blr0471.

Structurei

Secondary structure

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 784Combined sources
Beta strandi83 – 886Combined sources
Helixi93 – 10513Combined sources
Beta strandi111 – 1199Combined sources
Helixi122 – 13211Combined sources
Beta strandi137 – 1426Combined sources
Helixi146 – 1505Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi166 – 1749Combined sources
Helixi178 – 1836Combined sources
Helixi185 – 1928Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNGX-ray1.14A39-194[»]
ProteinModelPortaliP30960.
SMRiP30960. Positions 50-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30960.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 190145ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbE subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4107QX9. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000097218.
InParanoidiP30960.
KOiK02199.
OrthoDBiEOG6WX4Q5.
PhylomeDBiP30960.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR004799. Periplasmic_diS_OxRdtase_DsbE.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00385. dsbE. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQSTSANP QRRTFLMVLP LIAFIGLALL FWFRLGSGDP SRIPSALIGR
60 70 80 90 100
PAPQTALPPL EGLQADNVQV PGLDPAAFKG KVSLVNVWAS WCVPCHDEAP
110 120 130 140 150
LLTELGKDKR FQLVGINYKD AADNARRFLG RYGNPFGRVG VDANGRASIE
160 170 180 190
WGVYGVPETF VVGREGTIVY KLVGPITPDN LRSVLLPQME KALK
Length:194
Mass (Da):21,126
Last modified:November 1, 1995 - v2
Checksum:i826A75D22AA0C593
GO

Sequence cautioni

The sequence AAA26196.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60874 Genomic DNA. Translation: AAA26196.1. Different initiation.
BA000040 Genomic DNA. Translation: BAC45736.1.
PIRiD39741.
RefSeqiNP_767111.1. NC_004463.1.
WP_011083302.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC45736; BAC45736; BAC45736.
GeneIDi1048774.
KEGGibja:blr0471.
PATRICi21184407. VBIBraJap65052_0481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60874 Genomic DNA. Translation: AAA26196.1. Different initiation.
BA000040 Genomic DNA. Translation: BAC45736.1.
PIRiD39741.
RefSeqiNP_767111.1. NC_004463.1.
WP_011083302.1. NC_004463.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNGX-ray1.14A39-194[»]
ProteinModelPortaliP30960.
SMRiP30960. Positions 50-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.blr0471.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC45736; BAC45736; BAC45736.
GeneIDi1048774.
KEGGibja:blr0471.
PATRICi21184407. VBIBraJap65052_0481.

Phylogenomic databases

eggNOGiENOG4107QX9. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000097218.
InParanoidiP30960.
KOiK02199.
OrthoDBiEOG6WX4Q5.
PhylomeDBiP30960.

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-474-MONOMER.
RETL1328306-WGS:GSTH-4038-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP30960.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR004799. Periplasmic_diS_OxRdtase_DsbE.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00385. dsbE. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: USDA 110RIF15.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 39-194, DISULFIDE BOND.

Entry informationi

Entry nameiCYCY_BRADU
AccessioniPrimary (citable) accession number: P30960
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.