ID A0A1F8RY81_9CHLR Unreviewed; 287 AA.
AC A0A1F8RY81;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=A2148_05685 {ECO:0000313|EMBL:OGO52391.1};
OS Chloroflexi bacterium RBG_16_68_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797660 {ECO:0000313|EMBL:OGO52391.1, ECO:0000313|Proteomes:UP000176790};
RN [1] {ECO:0000313|EMBL:OGO52391.1, ECO:0000313|Proteomes:UP000176790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGO52391.1}.
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DR EMBL; MGOB01000027; OGO52391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RY81; -.
DR STRING; 1797660.A2148_05685; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000176790; Unassembled WGS sequence.
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; 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; TIGR00655; PurU; 1.
DR PANTHER; PTHR42706; FORMYLTETRAHYDROFOLATE DEFORMYLASE; 1.
DR PANTHER; PTHR42706:SF1; FORMYLTETRAHYDROFOLATE DEFORMYLASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01842; ACT; 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}.
FT DOMAIN 9..89
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ SEQUENCE 287 AA; 32538 MW; CA43102DCB80D642 CRC64;
MSDEGVTAVL LLSCPDQKGL VAAVSDFLYR NDGNIIHADQ HTDQEESIFL QRVEWELAGS
AIAREEIGGA FQPIAERFGM TWSLDFSDYV PRIALFASRL PHCLYDLLAR WRMGEFRAEV
PLVVSNHADL RPIAEDFGVA FHSFSITPET KVAQEERLLA MLEEERIDLI VLARYMQVLG
ERFVAQYRNR IINIHHSFLP AFAGGRPYHL AHERGVKIIG ATAHYVTPEL DEGPIIEQDV
ARVSHRDSVA DLIRKGRDLE KVVLARAVDL HLRRRILVYG NKTVVFD
//
