(data stored in ACNUC7421 zone)

HOGENOM: STAAS_1_PE1013

ID   STAAS_1_PE1013                       STANDARD;      PRT;   183 AA.
AC   STAAS_1_PE1013; Q6GAC3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Peptide deformylase; Short=PDF; EC=3.5.1 88;AltName:
DE   Full=Polypeptide deformylase; (STAAS_1.PE1013).
GN   Name=def; Synonyms=def1, pdf1; OrderedLocusNames=SAS1026;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MSSA476.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAS_1.PE1013.
CC       Staphylococcus aureus subsp. aureus MSSA476 chromosome, complete genome
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DEF_STAAS
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of
CC       newly synthesized proteins. Requires at least a dipeptide for an
CC       efficient rate of reaction. N-terminal L-methionine is a
CC       prerequisite for activity but the enzyme has broad specificity at
CC       other positions (By similarity).
CC   -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate +
CC       methionyl peptide.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion (By similarity).
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC   -!- GENE_FAMILY: HOG000243507 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6GAC3; -.
DR   EMBL; BX571857; CAG42800.1; -; Genomic_DNA.
DR   RefSeq; YP_043150.1; NC_002953.3.
DR   ProteinModelPortal; Q6GAC3; -.
DR   SMR; Q6GAC3; 1-183.
DR   STRING; Q6GAC3; -.
DR   EnsemblBacteria; EBSTAT00000023590; EBSTAP00000022757; EBSTAG00000023589.
DR   GeneID; 2864091; -.
DR   GenomeReviews; BX571857_GR; SAS1026.
DR   KEGG; sas:SAS1026; -.
DR   eggNOG; COG0242; -.
DR   GeneTree; EBGT00050000024244; -.
DR   OMA; ADGEGCL; -.
DR   ProtClustDB; PRK00150; -.
DR   BioCyc; SAUR282459:SAS1026-MON; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:EC.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00163; Pep_deformylase; 1; -.
DR   InterPro; IPR000181; Fmet_deformylase.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   Gene3D; G3DSA:3.90.45.10; Fmet_deformylase; 1.
DR   PANTHER; PTHR10458; Fmet_deformylase; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; Fmet_deformylase; 1.
DR   TIGRFAMs; TIGR00079; Pept_deformyl; 1.
DR   HOGENOMDNA; STAAS_1.PE1013; -.
KW   Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   183 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLTMKDIIRD GHPTLRQKAA ELELPLTKEE KETLIAMREF LVNSQDEEIA KRYGLRSGVG
     LAAPQINISK RMIAVLIPDD GSGKSYDYML VNPKIVSHSV QEAYLPTGEG CLSVDDNVAG
     LVHRHNRITI KAKDIEGNDI QLRLKGYPAI VFQHEIDHLN GVMFYDHIDK DHPLQPHTDA
     VEV
//

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