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A3PMS0 (A3PMS0_RHOS1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase RuleBase RU003335
Gene names
Ordered Locus Names:Rsph17029_2534
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. SAAS SAAS000181

Sequence similarities

Belongs to the polypeptide deformylase family. RuleBase RU003335

Ontologies

Keywords
   Biological processProtein biosynthesis SAAS SAAS000181
   LigandMetal-binding SAAS SAAS000181
   Molecular functionHydrolase SAAS SAAS000181
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A3PMS0 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 9926029F20D05787

FASTA16718,713
        10         20         30         40         50         60 
MIRPFVMYPD KRLKTVAAPV EAVTDEIRAI WTDMIETMDA MPGYGLAAPQ IGVMLRLAVV 

        70         80         90        100        110        120 
DCSESRGKAI RLANPEILHA SGQFREHEEG SPNLPGASAV VSRPRAVTVR FLNEAGETEE 

       130        140        150        160 
RDFVDIWATS VQHQIDHLDG RLYIDRLSPL KRKMVVAKSE KYLRRVG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000577 Genomic DNA. Translation: ABN77636.1.
RefSeqYP_001044408.1. NC_009049.1.

3D structure databases

ProteinModelPortalA3PMS0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3PMS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4895431.
GenomeReviewsGene locus Rsph17029_2534 in contig CP000577_GR.
KEGGrsh:Rsph17029_2534.
PATRIC23172953. VBIRhoSph114483_2767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAQHQIDHL.
ProtClustDBCLSK934097.

Enzyme and pathway databases

BioCycRSPH349101:RSPH17029_2534-MONOMER.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. Pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA3PMS0_RHOS1
AccessionPrimary (citable) accession number: A3PMS0
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)