(data stored in ACNUC1104 zone)

SWISSPROT: A4F736_SACEN

ID   A4F736_SACEN            Unreviewed;       191 AA.
AC   A4F736;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
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   ECO:0000313|EMBL:CAL99860.1};
GN   OrderedLocusNames=SACE_0514 {ECO:0000313|EMBL:CAL99860.1};
GN   ORFNames=A8924_0912 {ECO:0000313|EMBL:PFG93662.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99860.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99860.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99860.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93662.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93662.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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:
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; AM420293; CAL99860.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93662.1; -; Genomic_DNA.
DR   RefSeq; WP_009950930.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0514; -.
DR   EnsemblBacteria; CAL99860; CAL99860; SACE_0514.
DR   KEGG; sen:SACE_0514; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243508; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   OrthoDB; 1649129at2; -.
DR   BioCyc; SERY405948:SACE_RS02525-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F736.
DR   SWISS-2DPAGE; A4F736.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS01077916, ECO:0000313|EMBL:CAL99860.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   ACT_SITE    142    142       {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL        99     99       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       141    141       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       145    145       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   191 AA;  20924 MW;  B868A93E9E4B6501 CRC64;
     MAVHPIRIVG DPVLHNPTRL VENFDDELRT LVDDMFETMA AASGVGLAAN QIGVDLRLFV
     YDCPDDEGVQ HRGVVVNPVL ETTEVPESMP DPEEDWEGCL SVPGESFPTG RADWAKVTGS
     DVDGNPVEVE GTGFFARCLQ HETDHLDGFL YLSRLVGRHA RAAKKTVKRN GWGVPGMSWD
     PSEHGDPFAD E
//

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