(data stored in ACNUC7421 zone)

SWISSPROT: Q500S9_PSEU2

ID   Q500S9_PSEU2            Unreviewed;       168 AA.
AC   Q500S9;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Peptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077920};
DE            Short=PDF {ECO:0000256|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077920};
DE   AltName: Full=Polypeptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163};
GN   Name=def {ECO:0000256|HAMAP-Rule:MF_00163};
GN   OrderedLocusNames=Psyr_0019 {ECO:0000313|EMBL:AAY35093.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35093.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35093.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35093.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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. {ECO:0000256|HAMAP-Rule:MF_00163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate
CC         + N-terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420,
CC         Rhea:RHEA-COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731;
CC         EC=3.5.1.88; Evidence={ECO:0000256|HAMAP-Rule:MF_00163,
CC         ECO:0000256|SAAS:SAAS01115621};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00163};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000256|HAMAP-Rule:MF_00163};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS01077936}.
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DR   EMBL; CP000075; AAY35093.1; -; Genomic_DNA.
DR   RefSeq; WP_003401459.1; NC_007005.1.
DR   RefSeq; YP_233131.1; NC_007005.1.
DR   STRING; 205918.Psyr_0019; -.
DR   EnsemblBacteria; AAY35093; AAY35093; Psyr_0019.
DR   GeneID; 3365494; -.
DR   KEGG; psb:Psyr_0019; -.
DR   PATRIC; fig|205918.7.peg.19; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243509; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   BioCyc; PSYR205918:G1G4J-19-MONOMER; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00487; Pep_deformylase; 1.
DR   Gene3D; 3.90.45.10; -; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PTHR10458; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500S9.
DR   SWISS-2DPAGE; Q500S9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077916, ECO:0000313|EMBL:AAY35093.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077917};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077930}.
FT   ACT_SITE    135    135       {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL        92     92       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       134    134       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       138    138       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   168 AA;  19243 MW;  32DA65D9807CF755 CRC64;
     MAILNILEFP DSRLRTIAKP VAMVDDGIRQ LVDDMFETMY EAPGIGLAAT QVNVHKRVVV
     MDLSEDRSEP MVFINPEIEK LTDEMDQYQE GCLSVPGFYE NVDRPQKVRV KALDRDGKPY
     ELVAEGLLAI CIQHECDHLN GKLFVDYLSN LKRDRIKKKL EKQHKLNA
//

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