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Q2SSS0 (Q2SSS0_MYCCT) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 45. 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 HAMAP MF_00163
Short name=PDF HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase HAMAP MF_00163
Gene names
Name:def HAMAP MF_00163 EMBL ABC01689.1
Ordered Locus Names:MCAP_0206
OrganismMycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154) [Complete proteome] [HAMAP]
Taxonomic identifier340047 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions By similarity. HAMAP MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 SAAS SAAS000181

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1711 By similarity HAMAP MF_00163
Metal binding1261Iron By similarity HAMAP MF_00163
Metal binding1701Iron By similarity HAMAP MF_00163
Metal binding1741Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q2SSS0 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5A946D2E3A3383FA

FASTA20023,344
        10         20         30         40         50         60 
MDKSYLLQDQ IPSNSWLVKD HKKEIIRTKS TKIIDPTNLS NDEELVLKKL IDFVTFSQDE 

        70         80         90        100        110        120 
NNNNINNKDY LRPAVGLAAP QIGVNKDMFY VRFQLDNNKI EQYAMINTKL ISTSTQIACL 

       130        140        150        160        170        180 
KNGEGCLSVD NDHLGFVPRH YKIVVQGYDW LTKQYLTLTL RNYQAIVFQH EMDHNIGILY 

       190        200 
YDHINKTDPL YKDNSWIIIE

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References

[1]Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O., Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000123 Genomic DNA. Translation: ABC01689.1.
RefSeqYP_424193.1. NC_007633.1.

3D structure databases

ProteinModelPortalQ2SSS0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SSS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3829109.
GenomeReviewsGene locus MCAP_0206 in contig CP000123_GR.
KEGGmcp:MCAP_0206.
PATRIC20004877. VBIMycCap130493_0209.
TIGRMCAP_0206.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMALKNGEGC.
PhylomeDBQ2SSS0.
ProtClustDBCLSK745701.

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 nameQ2SSS0_MYCCT
AccessionPrimary (citable) accession number: Q2SSS0
Entry history
Integrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: December 14, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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