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Q5N5L5 (Q5N5L5_SYNP6) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 62. 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-Rule MF_00163

Short name=PDF HAMAP-Rule MF_00163
EC=3.5.1.88 HAMAP-Rule MF_00163
Alternative name(s):
Polypeptide deformylase HAMAP-Rule MF_00163
Gene names
Name:def HAMAP-Rule MF_00163
Ordered Locus Names:syc0213_d EMBL BAD78403.1
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP] EMBL BAD78403.1
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_00163

Catalytic activity

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

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP-Rule MF_00163 RuleBase RU003335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1521 By similarity HAMAP-Rule MF_00163
Metal binding1091Iron By similarity HAMAP-Rule MF_00163
Metal binding1091Zinc PDB 4DR8 PDB 4DR9
Metal binding1511Iron By similarity HAMAP-Rule MF_00163
Metal binding1511Zinc; via tele nitrogen PDB 4DR8 PDB 4DR9
Metal binding1551Iron By similarity HAMAP-Rule MF_00163
Metal binding1551Zinc; via tele nitrogen PDB 4DR8 PDB 4DR9

Sequences

Sequence LengthMass (Da)Tools
Q5N5L5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 7F8107DD9B120FB7

FASTA19221,350
        10         20         30         40         50         60 
MTAAVAIRVA KKKLAKPPLD LHYLGDRVLR QPAKRVSRID DELRQTIRQM LQTMYSADGI 

        70         80         90        100        110        120 
GLAAPQVGIN KQLIVIDLEL EDEQAPPLVL INPKIERTAG DLEQCQEGCL SIPGVYLDVE 

       130        140        150        160        170        180 
RPEIVEVSYK DENGRPQRLV ADGLLARCIQ HEMDHLNGVL FVDRVENRLE LNEALDKKGF 

       190 
AVQAVRPVAA AS 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[2]"Structure and function of a cyanophage-encoded peptide deformylase."
Frank J.A., Lorimer D., Youle M., Witte P., Craig T., Abendroth J., Rohwer F., Edwards R.A., Segall A.M., Burgin A.B.
ISME J. 7:1150-1160(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-192 IN COMPLEX WITH ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008231 Genomic DNA. Translation: BAD78403.1.
RefSeqYP_170923.1. NC_006576.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DR8X-ray1.55A/B/C/D2-192[»]
4DR9X-ray1.90A/B/C/D2-192[»]
ProteinModelPortalQ5N5L5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc0213_d.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD78403; BAD78403; syc0213_d.
GeneID3199121.
KEGGsyc:syc0213_d.
PATRIC32485956. VBISynElo117686_0255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAPNQYAEV.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-219-MONOMER.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ5N5L5_SYNP6
AccessionPrimary (citable) accession number: Q5N5L5
Entry history
Integrated into UniProtKB/TrEMBL: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)