(data stored in ACNUC1104 zone)

SWISSPROT: DEF4_STRCO

ID   DEF4_STRCO              Reviewed;         216 AA.
AC   Q9K4A0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Peptide deformylase 4 {ECO:0000255|HAMAP-Rule:MF_00163};
DE            Short=PDF 4 {ECO:0000255|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000255|HAMAP-Rule:MF_00163};
DE   AltName: Full=Polypeptide deformylase 4 {ECO:0000255|HAMAP-Rule:MF_00163};
GN   Name=def4 {ECO:0000255|HAMAP-Rule:MF_00163};
GN   OrderedLocusNames=SCO5221; ORFNames=SC7E4.18;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00163};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00163};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000255|HAMAP-Rule:MF_00163};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00163}.
DR   EMBL; AL939122; CAB94606.1; -; Genomic_DNA.
DR   RefSeq; NP_629368.1; NC_003888.3.
DR   RefSeq; WP_003973751.1; NC_003888.3.
DR   SMR; Q9K4A0; -.
DR   STRING; 100226.SCO5221; -.
DR   PRIDE; Q9K4A0; -.
DR   EnsemblBacteria; CAB94606; CAB94606; CAB94606.
DR   GeneID; 1100662; -.
DR   KEGG; sco:SCO5221; -.
DR   PATRIC; fig|100226.15.peg.5305; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243508; -.
DR   InParanoid; Q9K4A0; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   PhylomeDB; Q9K4A0; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IBA:GO_Central.
DR   GO; GO:0043686; P:co-translational protein modification; IBA:GO_Central.
DR   GO; GO:0031365; P:N-terminal protein amino acid modification; IBA:GO_Central.
DR   GO; GO:0018206; P:peptidyl-methionine modification; IBA:GO_Central.
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; Q9K4A0.
DR   SWISS-2DPAGE; Q9K4A0.
KW   Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    216       Peptide deformylase 4.
FT                                /FTId=PRO_0000082855.
FT   ACT_SITE    178    178       {ECO:0000255|HAMAP-Rule:MF_00163}.
FT   METAL       135    135       Iron. {ECO:0000255|HAMAP-Rule:MF_00163}.
FT   METAL       177    177       Iron. {ECO:0000255|HAMAP-Rule:MF_00163}.
FT   METAL       181    181       Iron. {ECO:0000255|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   216 AA;  24184 MW;  562FDF5C60732AAF CRC64;
     MAQQDTDQQH PGVLPVDDEG FVVDSQDCEE READWRGRGT SRPITVVGNP VLHKECEDVT
     DFGEEFQQLV ADMFASQRTA EGVGLAANQI GVSKKVFVYD CPDDEGVRHV GVVCNPRLVE
     LPADRRRLDD SNEGCLSVPT AYAPLARPDY AEVTGQDEKG NPVKVRGTGY FARCLQHETD
     HLYGYLYIDR LSKRERKDAL RQMAENEPRY PVVAND
//

If you have problems or comments...

PBIL Back to PBIL home page