ID A0A318AGG4_9MICC Unreviewed; 292 AA.
AC A0A318AGG4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:PXA79566.1};
GN ORFNames=DCC25_08710 {ECO:0000313|EMBL:PXA79566.1};
OS Auritidibacter sp. NML120636.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Auritidibacter.
OX NCBI_TaxID=2170743 {ECO:0000313|EMBL:PXA79566.1, ECO:0000313|Proteomes:UP000247286};
RN [1] {ECO:0000313|EMBL:PXA79566.1, ECO:0000313|Proteomes:UP000247286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML120636 {ECO:0000313|EMBL:PXA79566.1,
RC ECO:0000313|Proteomes:UP000247286};
RA Bernard K., Pacheco A.L., Burdz T., Wiebe D., Beniac D., Booth T.,
RA Goldenberger D., Seth-Smith H., Egli A., Bernier A.-M.;
RT "Auritidibacter winnipegensis sp. nov. recovered from Human Clinical
RT Materials and Emendation of the Genus Auritidibacter (Yassin et al 2011).";
RL Submitted (MAY-2018) 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}.
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:PXA79566.1}.
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DR EMBL; QHLO01000009; PXA79566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318AGG4; -.
DR UniPathway; UPA00074; UER00170.
DR Proteomes; UP000247286; 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 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 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:UP000247286}.
FT DOMAIN 12..92
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 236
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ SEQUENCE 292 AA; 32541 MW; BA396C3BB01CD86B CRC64;
MPADTAAEHR LVVTLSCANQ PGIVHAITGC LLKLEGDITE SQQFGSPDTG TFFMRVTFTS
PYSRDEADPI FDQVREDFAM DLNVWDANGR TKTIIMCSKD GRTLNELLFQ QRAGTLPIDV
PVIVSNHLDL QPMAYFYDIP FVHIPLVKNA DGTDNKADAE ARLMQLVNEY NVELVVLARY
MQILSDELVQ KLEGKAINIH HSFLPSFKGA KPYHQAHARG VKLIGATAHY VTADLDEGPI
IEQRVHRVNH GLTAGDFVDR GRSVEGATLA QAVQWHAEHR VLLDGRRTVI FE
//
