ID Q0PAA0_CAMJE Unreviewed; 274 AA.
AC Q0PAA0;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 ECO:0000313|EMBL:CAL34918.1};
GN OrderedLocusNames=Cj0790 {ECO:0000313|EMBL:CAL34918.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34918.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL34918.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL34918.1; -; Genomic_DNA.
DR PIR; F81350; F81350.
DR RefSeq; WP_002852510.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344197.1; NC_002163.1.
DR AlphaFoldDB; Q0PAA0; -.
DR IntAct; Q0PAA0; 4.
DR STRING; 192222.Cj0790; -.
DR PaxDb; 192222-Cj0790; -.
DR DNASU; 905095; -.
DR EnsemblBacteria; CAL34918; CAL34918; Cj0790.
DR GeneID; 905095; -.
DR KEGG; cje:Cj0790; -.
DR PATRIC; fig|192222.6.peg.778; -.
DR eggNOG; COG0788; Bacteria.
DR HOGENOM; CLU_038395_3_0_7; -.
DR OrthoDB; 9806170at2; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000000799; 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 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; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004810; PurU.
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.
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:UP000000799}.
FT DOMAIN 80..256
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ SEQUENCE 274 AA; 31686 MW; 84D98F82E5B2EE11 CRC64;
MISVLKICTK DQKGLIYRIS DVIFKYHINI VKNDEFVGEG MFFFRALLEG EFDKEAFIGT
LEAMLGQEAL IELCEKRKKD IVVFATKESH CLGDLLIKHY SNELEANIKA VISNHNSLKD
LVEKFEIPYH FISAENLDRK EQENQILKCL EQYKFDYLVL AKYMRILSPD FVRHFEGKII
NIHHSFLPAF IGANPYKQAF ERGVKIIGAT AHFVNNNLDE GPIITQAVSP VNHEFTWQDM
QQAGRNIEKD VLSKALDLAF EDRIFIHNNK TIIF
//
