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Q2GID0 (Q2GID0_ANAPZ) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 44. 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 EMBL ABD43563.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:APH_1372
OrganismAnaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]
Taxonomic identifier212042 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length187 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 site1531 By similarity HAMAP MF_00163
Metal binding1101Iron By similarity HAMAP MF_00163
Metal binding1521Iron By similarity HAMAP MF_00163
Metal binding1561Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q2GID0 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 4596C6A1C0688D71

FASTA18721,196
        10         20         30         40         50         60 
MSVRPLVVLP DSRLFLCSEE VRETDFCEKF NSLVEDMFDT MYAEQGIGLA AVQVGVHKRI 

        70         80         90        100        110        120 
FVIDLGPKTE ESSEIADDPD GYHSTCGPMV VINPEIVEKS VDLVSMEEGC LSVPDQRELV 

       130        140        150        160        170        180 
VRPERIVMQY TDLHGKRKIL KAQGLLSRCL QHEIDHLNGT VFLKHISKLK RDLVMQKMRK 


AASLRKN

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000235 Genomic DNA. Translation: ABD43563.1.
RefSeqYP_505871.1. NC_007797.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2GID0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3930818.
GenomeReviewsGene locus APH_1372 in contig CP000235_GR.
KEGGaph:APH_1372.
NMPDRfig|212042.5.peg.1320.
PATRIC20951546. VBIAnaPha602_1466.
TIGRAPH_1372.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAKANGWLA.
PhylomeDBQ2GID0.
ProtClustDBCLSK747409.

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 nameQ2GID0_ANAPZ
AccessionPrimary (citable) accession number: Q2GID0
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2006
Last sequence update: March 21, 2006
Last modified: December 14, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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