ID A0A1G2TFL1_9BACT Unreviewed; 425 AA.
AC A0A1G2TFL1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=A3C70_01410 {ECO:0000313|EMBL:OHA96067.1};
OS Candidatus Zambryskibacteria bacterium RIFCSPHIGHO2_02_FULL_43_14.
OC Bacteria; Candidatus Zambryskibacteria.
OX NCBI_TaxID=1802748 {ECO:0000313|EMBL:OHA96067.1, ECO:0000313|Proteomes:UP000178175};
RN [1] {ECO:0000313|EMBL:OHA96067.1, ECO:0000313|Proteomes:UP000178175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 Fmt family. {ECO:0000256|ARBA:ARBA00010699}.
CC -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC {ECO:0000256|ARBA:ARBA00010759, ECO:0000256|HAMAP-Rule:MF_00163}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHA96067.1}.
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DR EMBL; MHVR01000012; OHA96067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2TFL1; -.
DR Proteomes; UP000178175; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR CDD; cd00487; Pep_deformylase; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR Gene3D; 3.90.45.10; Peptide deformylase; 1.
DR HAMAP; MF_00163; Pep_deformylase; 1.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR InterPro; IPR023635; Peptide_deformylase.
DR InterPro; IPR036821; Peptide_deformylase_sf.
DR NCBIfam; TIGR00079; pept_deformyl; 1.
DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF01327; Pep_deformylase; 1.
DR PRINTS; PR01576; PDEFORMYLASE.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF56420; Peptide deformylase; 1.
PE 3: Inferred from homology;
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|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00163}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 215..318
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 348..400
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT ACT_SITE 152
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00163"
SQ SEQUENCE 425 AA; 47836 MW; 1CFC319C289C6357 CRC64;
MTKTKILQRD APVLREATKS VPIKNIGSKK IRDILKKMKE ALHSEKDGVA IAAPQIGESL
RIFIVNSQAL ALISHFGKIK TDKELNDLVF INPEIIKTSK KKRQMEEGCL SVRWLYGQVK
RSEKVTLRAY DETGKLLERG ASGLLAQIFQ HETDHLNGIL FIDKAENIQE ILPSRDTKFV
FFGSSRFSDY VLEELENMGF SPVLKITSTK EPLPMEKLKN LGAEVFVVAS FGKILPKELI
DLPKHKTLNI HPSLLPQLRG AAPIQGAILK QNESGITIIR IDEKMDHGPI LAQAKVSLFP
WPDHYHVIEE KLGRAGGRML GELLPKWILG KIQEKPQNDA VATYTKLVKK EDGLLNLDDS
AEENLRKVLA YSTWPGAYMF FKNKKGGEVR VIVKDAKVED GKFLPTCVIP AGKREMNWQD
FLRGN
//
