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Database: UniProt
Entry: A0A1J5LHM3_9PROT
LinkDB: A0A1J5LHM3_9PROT
Original site: A0A1J5LHM3_9PROT 
ID   A0A1J5LHM3_9PROT        Unreviewed;       294 AA.
AC   A0A1J5LHM3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000256|HAMAP-Rule:MF_01927};
DE            EC=3.5.1.10 {ECO:0000256|HAMAP-Rule:MF_01927};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000256|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000256|HAMAP-Rule:MF_01927};
GN   ORFNames=BM562_00100 {ECO:0000313|EMBL:OIQ33482.1};
OS   Alphaproteobacteria bacterium MedPE-SWcel.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ33482.1, ECO:0000313|Proteomes:UP000183546};
RN   [1] {ECO:0000313|EMBL:OIQ33482.1, ECO:0000313|Proteomes:UP000183546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ33482.1};
RX   PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA   Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT   "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT   Associated Bacteria from the Mediterranean Sea.";
RL   Front. Microbiol. 7:996-996(2016).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000256|HAMAP-
CC       Rule:MF_01927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + H2O = (6S)-5,6,7,8-
CC         tetrahydrofolate + formate + H(+); Xref=Rhea:RHEA:19833,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:195366; EC=3.5.1.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01927};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01927}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000256|HAMAP-
CC       Rule:MF_01927}.
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:OIQ33482.1}.
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DR   EMBL; MPDC01000001; OIQ33482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5LHM3; -.
DR   STRING; 1860092.BM562_00100; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000183546; Unassembled WGS sequence.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04875; ACT_F4HF-DF; 1.
DR   CDD; cd08648; FMT_core_Formyl-FH4-Hydrolase_C; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   HAMAP; MF_01927; PurU; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041729; Formyl-FH4-Hydrolase_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR004810; PurU.
DR   InterPro; IPR044074; PurU_ACT.
DR   NCBIfam; TIGR00655; PurU; 1.
DR   PANTHER; PTHR42706; FORMYLTETRAHYDROFOLATE DEFORMYLASE; 1.
DR   PANTHER; PTHR42706:SF1; FORMYLTETRAHYDROFOLATE DEFORMYLASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PIRSF; PIRSF036480; FormyFH4_hydr; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01927};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01927}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01927}.
FT   DOMAIN          5..82
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   294 AA;  32929 MW;  E615D3894133397B CRC64;
     MSNYALTVTC RSTRGIVAAI ATFLAENECN ITDSAQFDDK ETGNFFMRVS FESARAVDLA
     KLTEGFAEAA DPFDMDYEFH DETEKMKVVI MVSRFGHCLN DLLYRWRIGA LPIDIVAVIS
     NHMEYQKVVV NHDIPFHCIK VTPQNKPEAE ARIMSVVEET GAELIVLARY MQILSDEMCQ
     KMSGKIINIH HSFLPSFKGA NPYKQAFQRG VKLIGATSHY VTADLDEGPI IEQDIVRVTH
     AQSPNDYVSL GRDVESQVLA RAIHAHIHRR VFLNGNKTVV FPASPGSYAS ERMG
//
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