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Database: UniProt
Entry: C3K8H1_PSEFS
LinkDB: C3K8H1_PSEFS
Original site: C3K8H1_PSEFS 
ID   C3K8H1_PSEFS            Unreviewed;       288 AA.
AC   C3K8H1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 99.
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};
DE   Flags: Precursor;
GN   Name=purU2 {ECO:0000313|EMBL:CAY48565.1};
GN   Synonyms=purU {ECO:0000256|HAMAP-Rule:MF_01927};
GN   OrderedLocusNames=PFLU_2332 {ECO:0000313|EMBL:CAY48565.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY48565.1};
RN   [1] {ECO:0000313|EMBL:CAY48565.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY48565.1};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2] {ECO:0000313|EMBL:CAI2796581.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAI2796581.1};
RA   Fortmann-Grote C.;
RL   Submitted (OCT-2023) 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; OV986001; CAI2796581.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY48565.1; -; Genomic_DNA.
DR   RefSeq; WP_012723558.1; NC_012660.1.
DR   AlphaFoldDB; C3K8H1; -.
DR   PATRIC; fig|216595.4.peg.2547; -.
DR   eggNOG; COG0788; Bacteria.
DR   HOGENOM; CLU_038395_3_0_6; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP001152918; 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   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; 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; PS51257; PROKAR_LIPOPROTEIN; 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          93..269
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   288 AA;  32536 MW;  1355D4866D4000E3 CRC64;
     MDASREHYIL KITCPAASGI VAAISACLAQ QQCYISELAQ FDDEFTGQFF MRAVFRFNTG
     VSGDIGALRN GLGDLAGGFD MHWQLFSSRQ PTRVLLMVSK FDHCLTDLLY RHRKGEMDMH
     ITAVVSNHLD LRAMAEREGI RFIYLPITQD TKARQEAELM RIVEDTQTDL VVLARYMQIL
     SDGLCQQLSG RAINIHHSFL PGFKGAKPYH QAYDRGVKLI GATAHYVTSD LDEGPIIEQE
     IQRVDHTHLP DSLVAIGRDT ETVALSKALK YHLEHRVFIN QDKTVIFR
//
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