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P29899 (CYCL_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 30, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c-L
Alternative name(s):
Cytochrome c551I
Cytochrome c552
Gene names
Name:moxG
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron acceptor for MDH. Acts in methanol oxidation.

Subcellular location

Periplasm Potential.

Induction

During growth on methanol.

Post-translational modification

Binds 1 heme group per subunit.

Biophysicochemical properties

Redox potential:

E0 is about +190 mV.

Ontologies

Keywords
   Biological processElectron transport
Methanol utilization
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Technical term3D-structure
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

methanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 177155Cytochrome c-L
PRO_0000006553

Sites

Metal binding831Iron (heme axial ligand)
Binding site791Heme (covalent)
Binding site821Heme (covalent)

Secondary structure

............................... 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29899 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 6949FBDC8B2C056E

FASTA17719,396
        10         20         30         40         50         60 
MTKPRILAAF AMTLIIPVAA MAAPQFFNII DGSPLNFDDA MEEGRDTEAV KHFLETGENV 

        70         80         90        100        110        120 
YNEDPEILPE AEELYAGMCS GCHGHYAEGK IGPGLNDAYW TYPGNETDVG LFSTLYGGAT 

       130        140        150        160        170 
GQMGPMWGSL TLDEMLRTMA WVRHLYTGDP KDASWLTDEQ KAGFTPFQPK SSGEDQS 

« Hide

References

[1]"Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth."
van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H., Harms N., Oltmann L.F., Stouthamer A.H.
J. Bacteriol. 173:6948-6961(1991) [PubMed: 1657871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Pd 1222.
[2]"Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i."
Chen L., Durley R., Mathews F.S., Davidson V.L.
Science 264:86-90(1994) [PubMed: 8140419] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57684 Genomic DNA. Translation: AAA25583.1.
PIRB41377.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG2X-ray2.25D/H/L/P23-177[»]
1MG3X-ray2.40D/H/L/P23-177[»]
2GC4X-ray1.90D/H/L/P23-169[»]
2GC7X-ray1.90D/H/L/P23-169[»]
2MTAX-ray2.40C23-169[»]
ProteinModelPortalP29899.
SMRP29899. Positions 23-169.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009056. Cyt_c_dom.
IPR003088. Cyt_c_I.
IPR009153. Cyt_cL.
[Graphical view]
Gene3DG3DSA:1.10.760.10. Cytochrome_c_R. 1 hit.
PfamPF00034. Cytochrom_C. 1 hit.
[Graphical view]
PIRSFPIRSF000008. Cytochrome_c551i. 1 hit.
SUPFAMSSF46626. Cytochrome_c. 1 hit.
TIGRFAMsTIGR03872. Cytochrome_MoxG. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYCL_PARDE
AccessionPrimary (citable) accession number: P29899
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 30, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references