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Database: UniProt
Entry: A0A1H6BQM3_9RHOB
LinkDB: A0A1H6BQM3_9RHOB
Original site: A0A1H6BQM3_9RHOB 
ID   A0A1H6BQM3_9RHOB        Unreviewed;       294 AA.
AC   A0A1H6BQM3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04488045_3695 {ECO:0000313|EMBL:SEG62755.1};
OS   Thalassococcus halodurans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassococcus.
OX   NCBI_TaxID=373675 {ECO:0000313|EMBL:SEG62755.1, ECO:0000313|Proteomes:UP000236752};
RN   [1] {ECO:0000313|EMBL:SEG62755.1, ECO:0000313|Proteomes:UP000236752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26915 {ECO:0000313|EMBL:SEG62755.1,
RC   ECO:0000313|Proteomes:UP000236752};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNUZ01000008; SEG62755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6BQM3; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000236752; 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 2, 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236752}.
FT   DOMAIN          5..77
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01927"
SQ   SEQUENCE   294 AA;  32589 MW;  16C0FDBEC76832DF CRC64;
     MTKYVLTVTC NSTRGIVAAI SGFLTDHGCN ITDSAQFDDP ETGKFFMRVS FVSEEGATLD
     ALQADFTPVA SPFGMDYAFH DEAVKMKVVI MVSRFGHCLN DLLYRWRIGA LPIDIVAVIS
     NHTEYQKVVE NHDLPFHHIP VTKENKPVAE GEIMDVVRDT GAELIVLARY MQILSDEMCQ
     KMSGRIINIH HSFLPSFKGA NPYKQAFQRG VKLIGATAHY VTADLDEGPI IEQDIVRITH
     AQSAADYVSL GRDVEAQVFA RAIHAHIHHR VFQNGNKTIV FPASPGGFAS ERMG
//
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