ID   A9BSB2_DELAS            Unreviewed;       307 AA.
AC   A9BSB2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   04-NOV-2026, entry version 92.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000256|HAMAP-Rule:MF_01927, ECO:0000256|NCBIfam:TIGR00655};
DE            EC=3.5.1.10 {ECO:0000256|HAMAP-Rule:MF_01927, ECO:0000256|NCBIfam:TIGR00655};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000256|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000256|HAMAP-Rule:MF_01927};
GN   OrderedLocusNames=Daci_1081 {ECO:0000313|EMBL:ABX33726.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33726.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX33726.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000884; ABX33726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9BSB2; -.
DR   STRING; 398578.Daci_1081; -.
DR   KEGG; dac:Daci_1081; -.
DR   eggNOG; COG0788; Bacteria.
DR   HOGENOM; CLU_038395_3_0_4; -.
DR   OMA; AAHEMDW; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000000784; Chromosome.
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   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; NF004684; PRK06027.1; 1.
DR   NCBIfam; TIGR00655; PurU; 1.
DR   PANTHER; PTHR42706; FORMYLTETRAHYDROFOLATE DEFORMYLASE; 1.
DR   PANTHER; PTHR42706:SF1; FORMYLTETRAHYDROFOLATE DEFORMYLASE 2, 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT   DOMAIN          31..105
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   307 AA;  34098 MW;  E824277E881B1ED6 CRC64;
     MWFLRTFPER VTCAGSCPCC DNCAAMTQAY ILTLSCPDRL GLVHAVSGFL LEQGGNIEEA
     AQYNDPATGL FFMRVQFACN GCDPAALRAA LADLGGQYQM KWRLHTKAEA MKTVLMVSKE
     GHCLNDLLFR WKSGLLPVDI RAIISNHREF YQLAASYNIP FHHIPVTAAT KAQAEAKQFE
     IIEAEGAELV VLARYMQVLS NDLCTKLAGR AINIHHSFLP SFKGAKPYYQ AHDRGVKLIG
     ATAHYVTADL DEGPIIEQDV ARADHTDTVE DLTARGRDTE SQVLARAVKW HSEHRVILNG
     HKTVVFR
//