(data stored in ACNUC7421 zone)

SWISSPROT: C6WHU3_ACTMD

ID   C6WHU3_ACTMD            Unreviewed;       195 AA.
AC   C6WHU3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Amir_0427 {ECO:0000313|EMBL:ACU34394.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34394.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34394.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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; CP001630; ACU34394.1; -; Genomic_DNA.
DR   RefSeq; WP_012783057.1; NC_013093.1.
DR   STRING; 446462.Amir_0427; -.
DR   EnsemblBacteria; ACU34394; ACU34394; Amir_0427.
DR   KEGG; ami:Amir_0427; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243508; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   OrthoDB; POG091H02B0; -.
DR   Proteomes; UP000002213; 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; C6WHU3.
DR   SWISS-2DPAGE; C6WHU3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS00726151, ECO:0000313|EMBL:ACU34394.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
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   195 AA;  21247 MW;  75EAC7F7F522BAA9 CRC64;
     MAVHPIRIAG DPVLHNPTRP VDEHDDELRA LIADMYETMA AANGVGLAAN QIGVDLRLFV
     YDCPDDEGVR RRGEVVNPVL QTSDVPLGMP DPDDDYEGCL SAPGESYPTG RASWAKVTGT
     DGNGDPVEVE GTGFFARCLQ HETDHLDGYL YLDRLVGRHK RASKKMIKAN GWGVPGLSWD
     PATSEDPFAD DEDED
//

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