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C1D9E3 (C1D9E3_LARHH) 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 1 HAMAP MF_00163
Short name=PDF 1 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 1 HAMAP MF_00163
Gene names
Name:def1 HAMAP MF_00163
Ordered Locus Names:LHK_02061
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Laribacter

Protein attributes

Sequence length183 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 site1441 By similarity HAMAP MF_00163
Metal binding1011Iron By similarity HAMAP MF_00163
Metal binding1431Iron By similarity HAMAP MF_00163
Metal binding1471Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
C1D9E3 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: BD8F277CF5384F02

FASTA18319,992
        10         20         30         40         50         60 
MSIRTVIKMG DPRLLLSAEP VTAFGTPQLT RLVEDLWETM KVHSGAGLAA PQIGENLQVV 

        70         80         90        100        110        120 
VFGTGEPNPR YPDAGIVPPT VLINPIVTPL GASMEDGWEG CLSLPGLRGA VPRYASVRYQ 

       130        140        150        160        170        180 
GFDLYGQPID RTVEGFHARV VQHECDHLWG FLYPMRMKDM SRFGFTDTLF PAIAEVEALP 


VAG

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References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed: 19283063] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001154 Genomic DNA. Translation: ACO75045.1.
RefSeqYP_002796054.1. NC_012559.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1D9E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7757674.
GenomeReviewsGene locus LHK_02061 in contig CP001154_GR.
KEGGlhk:LHK_02061.
PATRIC22300975. VBILarHon49832_1876.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANWEDCEM.

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.
ProtoNetSearch...

Entry information

Entry nameC1D9E3_LARHH
AccessionPrimary (citable) accession number: C1D9E3
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 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)
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