ID   PURU_ECOL6              Reviewed;         280 AA.
AC   P0A440; P38480;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000255|HAMAP-Rule:MF_01927};
DE            EC=3.5.1.10 {ECO:0000255|HAMAP-Rule:MF_01927};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000255|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000255|HAMAP-Rule:MF_01927}; OrderedLocusNames=c1696;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000255|HAMAP-
CC       Rule:MF_01927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-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:57454; EC=3.5.1.10;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01927}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01927}.
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DR   EMBL; AE014075; AAN80163.1; -; Genomic_DNA.
DR   RefSeq; WP_000555849.1; NC_004431.1.
DR   AlphaFoldDB; P0A440; -.
DR   SMR; P0A440; -.
DR   STRING; 199310.c1696; -.
DR   EnsemblBacteria; AAN80163; AAN80163; c1696.
DR   GeneID; 66674946; -.
DR   KEGG; ecc:c1696; -.
DR   eggNOG; COG0788; Bacteria.
DR   HOGENOM; CLU_038395_3_2_6; -.
DR   OMA; HADHHTD; -.
DR   BioCyc; ECOL199310:C1696-MON; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
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   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   PANTHER; PTHR42706; PTHR42706; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   TIGRFAMs; TIGR00655; PurU; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Hydrolase; One-carbon metabolism; Purine biosynthesis.
FT   CHAIN           1..280
FT                   /note="Formyltetrahydrofolate deformylase"
FT                   /id="PRO_0000074962"
FT   DOMAIN          8..86
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   280 AA;  31921 MW;  55BC16B62727A419 CRC64;
     MHSLQRKVLR TICPDQKGLI ARITNICYKH ELNIVQNNEF VDHRTGRFFM RTELEGIFND
     STLLADLDSA LPEGSVRELN PAGRRRIVIL VTKEAHCLGD LLMKANYGGL DVEIAAVIGN
     HDTLRSLVER FDIPFELVSH EGLSRNEHDQ KMADAIDAYQ PDYVVLAKYM RVLTPEFVAR
     FPNKIINIHH SFLPAFIGAR PYHQAYERGV KIIGATAHYV NDNLDEGPII MQDVIHVDHT
     YTAEDMMRAG RDVEKNVLSR ALYKVLAQRV FVYGNRTIIL