(data stored in SCRATCH zone)

SWISSPROT: A8FP75_SHESH

ID   A8FP75_SHESH            Unreviewed;       170 AA.
AC   A8FP75;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Peptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00726330};
DE            Short=PDF {ECO:0000256|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000256|HAMAP-Rule:MF_00163, ECO:0000256|SAAS:SAAS00726330};
DE   AltName: Full=Polypeptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163};
GN   Name=def {ECO:0000256|HAMAP-Rule:MF_00163};
GN   OrderedLocusNames=Ssed_0035 {ECO:0000313|EMBL:ABV34648.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34648.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34648.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34648.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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: Formyl-L-methionyl peptide + H(2)O = formate +
CC       methionyl peptide. {ECO:0000256|HAMAP-Rule:MF_00163,
CC       ECO:0000256|SAAS:SAAS00726210}.
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:SAAS00726107}.
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DR   EMBL; CP000821; ABV34648.1; -; Genomic_DNA.
DR   RefSeq; WP_012004174.1; NC_009831.1.
DR   ProteinModelPortal; A8FP75; -.
DR   STRING; 425104.Ssed_0035; -.
DR   EnsemblBacteria; ABV34648; ABV34648; Ssed_0035.
DR   KEGG; sse:Ssed_0035; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243509; -.
DR   KO; K01462; -.
DR   OMA; DIVIWPH; -.
DR   OrthoDB; POG091H02B0; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
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   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; A8FP75.
DR   SWISS-2DPAGE; A8FP75.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS00726151, ECO:0000313|EMBL:ABV34648.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS00726179};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS00726273}.
FT   ACT_SITE    134    134       {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL        91     91       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       133    133       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       137    137       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   170 AA;  19257 MW;  49ACC46E902997F7 CRC64;
     MSLLKVLRFP DERLRTIAKP VAEFNADLQA QIDNMFDTMY EEKGIGLAAT QVDFHQHLII
     MDLQDDVERP TVFINMEITA RDGSCTNEEG CLSVPGIYAN VDRAESVTIK AFDREGVEFT
     LDADGLFAIC LQHELDHLNG KLFVDYLSPL KRQRIKQKLE KAARLEAKQG
//

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