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C3LUH4 (C3LUH4_VIBCM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 19. 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 2 HAMAP MF_00163

Short name=PDF 2 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 2 HAMAP MF_00163
Gene names
Name:def-2 EMBL ACP07129.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:VCM66_A0148
OrganismVibrio cholerae serotype O1 (strain M66-2) [Complete proteome] [HAMAP]
Taxonomic identifier579112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length168 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 site1341 By similarity HAMAP MF_00163
Metal binding911Iron By similarity HAMAP MF_00163
Metal binding1331Iron By similarity HAMAP MF_00163
Metal binding1371Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
C3LUH4 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: F51EDDE3B6C14C59

FASTA16818,671
        10         20         30         40         50         60 
MAVLEILTAP DPRLRVQSKQ VTDVASVQTL IDDLLDTLYA TDNGIGLAAP QVGREEAIVV 

        70         80         90        100        110        120 
IDLSDNRDQP LVLINPKVVS GSNKEMGQEG CLSVPDYYAD VERYTSVVVE ALDREGKPLR 

       130        140        150        160 
IETSDFLAIV MQHEIDHLSG NLFIDYLSPL KQQMAMKKVK KHVKNRAR 

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References

[1]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed: 19115014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001234 Genomic DNA. Translation: ACP07129.1.
RefSeqYP_002811786.1. NC_012580.1.

3D structure databases

ProteinModelPortalC3LUH4.
SMRC3LUH4. Positions 2-168.
ModBaseSearch...

Protein-protein interaction databases

STRINGC3LUH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7781441.
GenomeReviewsGene locus VCM66_A0148 in contig CP001234_GR.
KEGGvcm:VCM66_A0148.
PATRIC20069390. VBIVibCho108967_2705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMINAHIE.
ProtClustDBPRK12846.

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 nameC3LUH4_VIBCM
AccessionPrimary (citable) accession number: C3LUH4
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)