Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C1DHE4 (C1DHE4_AZOVD) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 37. Feed History...

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

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493

EC=5.2.1.8 RuleBase RU000493
Gene names
Ordered Locus Names:Avin_23510 EMBL ACO78539.1
OrganismAzotobacter vinelandii (strain DJ / ATCC BAA-1303) [Complete proteome] [HAMAP] EMBL ACO78539.1
Taxonomic identifier322710 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins By similarity.

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Sequence similarities

Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase RuleBase RU003420
   Technical term3D-structure PDB 3T1U
Complete proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site511Succinate PDB 3T1U
Binding site971Succinate PDB 3T1U

Sequences

Sequence LengthMass (Da)Tools
C1DHE4 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: A7C2E78E0943ABC8

FASTA16417,831
        10         20         30         40         50         60 
MIKLQTNHGT ITLKLFADKA PETAANFEQY VKDGHYDGTI FHRVIDGFMI QGGGFEPGMK 

        70         80         90        100        110        120 
QKSTRAPIKN EANNGLSNKK YTIAMARTPD PHSASAQFFI NVKDNAFLDH TAPTAHGWGY 

       130        140        150        160 
AVFGEVVEGT DVVDRIKSVA TGSRAGHGDV PVDDVIIEKA EIVE 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized to support diverse anaerobic metabolic processes."
Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G., Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., Houmiel K., Imperial J. expand/collapse author list , Kennedy C., Larson T.J., Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R., Dixon R., Wood D.
J. Bacteriol. 191:4534-4545(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJ / ATCC BAA-1303.
[2]"Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide."
Christoforides E., Dimou M., Katinakis P., Bethanis K., Karpusas M.
Acta Crystallogr. F 68:259-264(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-163 IN COMPLEX WITH SUCCINATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001157 Genomic DNA. Translation: ACO78539.1.
RefSeqYP_002799514.1. NC_012560.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T1UX-ray2.00A2-163[»]
ProteinModelPortalC1DHE4.
SMRC1DHE4. Positions 1-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING322710.Avin_23510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO78539; ACO78539; Avin_23510.
GeneID7761267.
KEGGavn:Avin_23510.
PATRIC21030925. VBIAzoVin72790_2232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065978.
KOK03768.
OMAKKYSIAM.
OrthoDBEOG6S26C3.
ProtClustDBCLSK866787.

Enzyme and pathway databases

BioCycAVIN322710:GJ0M-2350-MONOMER.

Family and domain databases

InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1DHE4_AZOVD
AccessionPrimary (citable) accession number: C1DHE4
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)