ID C5ZX67_9HELI Unreviewed; 277 AA.
AC C5ZX67;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EES89735.1};
GN ORFNames=HCAN_1022 {ECO:0000313|EMBL:EES89735.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89735.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES89735.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
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; CM000776; EES89735.1; -; Genomic_DNA.
DR RefSeq; WP_006655724.1; NZ_DS990368.1.
DR AlphaFoldDB; C5ZX67; -.
DR STRING; 537970.HCAN_1022; -.
DR eggNOG; COG0788; Bacteria.
DR HOGENOM; CLU_038395_3_0_7; -.
DR OrthoDB; 9806170at2; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000007032; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007032}.
FT DOMAIN 4..79
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ SEQUENCE 277 AA; 32197 MW; 7122C82FF2F766C3 CRC64;
MRFVLKIQTP DKKGLITQIT QIIFQFNLNI LKNDEFVDKE NNLFFMRSEI EGECEIAILK
QKIKAIINDE SSQVEILPCQ KKKIVILCTK ESHCLGDLLI RYDSNELNAD ILAVISNYEV
LKPLCQKFRL PFICISHEGK SREDHEKQII EVLKQYPSDY IILAKYMRIL SPNFVQEFEG
QLINIHHSFL PAFVGANPYK QAYERGVKII GATAHFVNNE LDEGPIIYQD ITKVNHTMDW
KEMQKHGRDV EKIVLSKALN LALEEKIFVY HNKTIVF
//