(data stored in SCRATCH zone)

SWISSPROT: C3MF24_SINFN

ID   C3MF24_SINFN            Unreviewed;       174 AA.
AC   C3MF24;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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=NGR_c00570 {ECO:0000313|EMBL:ACP23861.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23861.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23861.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP23861.1; -; Genomic_DNA.
DR   RefSeq; WP_012706646.1; NC_012587.1.
DR   RefSeq; YP_002824614.1; NC_012587.1.
DR   STRING; 394.NGR_c00570; -.
DR   EnsemblBacteria; ACP23861; ACP23861; NGR_c00570.
DR   GeneID; 7790636; -.
DR   KEGG; rhi:NGR_c00570; -.
DR   PATRIC; fig|394.7.peg.2850; -.
DR   eggNOG; ENOG4108Z02; Bacteria.
DR   eggNOG; COG0242; LUCA.
DR   HOGENOM; HOG000243509; -.
DR   KO; K01462; -.
DR   OMA; VCIQHEI; -.
DR   OrthoDB; POG091H02B0; -.
DR   Proteomes; UP000001054; 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; C3MF24.
DR   SWISS-2DPAGE; C3MF24.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163,
KW   ECO:0000256|SAAS:SAAS00726151, ECO:0000313|EMBL:ACP23861.1};
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:UP000001054}.
FT   ACT_SITE    137    137       {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL        94     94       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       136    136       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
FT   METAL       140    140       Iron. {ECO:0000256|HAMAP-Rule:MF_00163}.
SQ   SEQUENCE   174 AA;  19407 MW;  EE4FAE40957113B9 CRC64;
     MTIKPLIILP DPILRQVSTP VETIDADIRR LADDMLETMY DAPGIGLAAI QIGVPRRLLV
     LDVSKEGEEK TPLVFINPKI VKSSEERSVY EEGCLSIPDY YAEVERPAAI AVEYLDRDGK
     QQSVEADGLL ATCLQHEIDH LNGVLFIDYI SKLKRDMVIR KFTKAAKTRG AKAI
//

If you have problems or comments...

PBIL Back to PBIL home page