GenomeNet

Database: UniProt
Entry: D9T2U7_MICAI
LinkDB: D9T2U7_MICAI
Original site: D9T2U7_MICAI 
ID   D9T2U7_MICAI            Unreviewed;       510 AA.
AC   D9T2U7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Peptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163};
DE            Short=PDF {ECO:0000256|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000256|HAMAP-Rule:MF_00163};
DE   AltName: Full=Polypeptide deformylase {ECO:0000256|HAMAP-Rule:MF_00163};
GN   Name=def {ECO:0000256|HAMAP-Rule:MF_00163};
GN   OrderedLocusNames=Micau_6151 {ECO:0000313|EMBL:ADL49645.1};
OS   Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS   129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL49645.1, ECO:0000313|Proteomes:UP000001908};
RN   [1] {ECO:0000313|EMBL:ADL49645.1, ECO:0000313|Proteomes:UP000001908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC   {ECO:0000313|Proteomes:UP000001908};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Hirsch A.M., Woyke T.;
RT   "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly
CC       synthesized proteins. Requires at least a dipeptide for an efficient
CC       rate of reaction. N-terminal L-methionine is a prerequisite for
CC       activity but the enzyme has broad specificity at other positions.
CC       {ECO:0000256|HAMAP-Rule:MF_00163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-
CC         terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA-
CC         COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00163};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-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|ARBA:ARBA00010759, ECO:0000256|HAMAP-Rule:MF_00163}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002162; ADL49645.1; -; Genomic_DNA.
DR   RefSeq; WP_013289242.1; NC_014391.1.
DR   AlphaFoldDB; D9T2U7; -.
DR   STRING; 644283.Micau_6151; -.
DR   KEGG; mau:Micau_6151; -.
DR   eggNOG; COG0242; Bacteria.
DR   HOGENOM; CLU_545028_0_0_11; -.
DR   OMA; PPLHARY; -.
DR   OrthoDB; 3203858at2; -.
DR   Proteomes; UP000001908; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.90.45.10; Peptide deformylase; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PEPTIDE DEFORMYLASE; 1.
DR   PANTHER; PTHR10458:SF22; PEPTIDE DEFORMYLASE; 1.
DR   Pfam; PF13560; HTH_31; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF56420; Peptide deformylase; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT   DOMAIN          17..71
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   ACT_SITE        476
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT   BINDING         433
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT   BINDING         475
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT   BINDING         479
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
SQ   SEQUENCE   510 AA;  58062 MW;  1AE4D75E2B3406BC CRC64;
     MTTSPIERAA DSFAAELARH RTGRGLSKKQ LATMMGFDPS YVSHVEGRRH RPTEDFARRA
     EAVLEASGAI WQRFREYDEL RHGRTGTAHR DPPVPGQWLP PGTGLVVERE MATLTHTGDG
     YHCAIRRELY NAGTEPVTRY LVRVAVDRYP NDPGRSNRHH REHPLTFAEL QLTAYRDDGN
     GREPMHWRAK HDRDAFKEIW LLFENDEGRF PLYPGDRVTI EYAYRVGRDK WGPWFQRAVR
     LPTRHLAVRL DLPADLDPKV WGAETSLSAE EGPLRTPIQR SADGGRVVFD WGTDDPPLNA
     RYRMQWRFRS PEPDAEPDSA PTGGARVRAS DRMRAVGIVQ RGDDLLRQRA RQFDLPADEQ
     HARQVIDRLA AMLVRLDELH PFSKGVGLAA PQLGIGWSAA LVRPADRAAD PVVLLNPRVV
     DAATETDEQY EGCLSFFDHR GLVPRPLRID VEHALWDGSR VITSYEYAMA RLVAHEIDHL
     EGRLYVDRMA PGVPLVPVEE YRETGTPWRY
//
DBGET integrated database retrieval system