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}.
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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
//