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Database: UniProt
Entry: O34990
LinkDB: O34990
Original site: O34990 
ID   PURU_BACSU              Reviewed;         300 AA.
AC   O34990; Q796M2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000255|HAMAP-Rule:MF_01927};
DE            EC=3.5.1.10 {ECO:0000255|HAMAP-Rule:MF_01927};
DE   AltName: Full=Formyl-FH(4) hydrolase {ECO:0000255|HAMAP-Rule:MF_01927};
GN   Name=purU {ECO:0000255|HAMAP-Rule:MF_01927}; Synonyms=ykkE;
GN   OrderedLocusNames=BSU13110;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Devine K.M.;
RT   "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 113; 254 AND 264.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate
CC       (formyl-FH4) to formate and tetrahydrofolate (FH4). {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01927}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01927}.
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DR   EMBL; AJ002571; CAA05590.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13168.2; -; Genomic_DNA.
DR   PIR; C69857; C69857.
DR   RefSeq; NP_389194.2; NC_000964.3.
DR   RefSeq; WP_003245802.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34990; -.
DR   SMR; O34990; -.
DR   STRING; 224308.BSU13110; -.
DR   jPOST; O34990; -.
DR   PaxDb; 224308-BSU13110; -.
DR   EnsemblBacteria; CAB13168; CAB13168; BSU_13110.
DR   GeneID; 939854; -.
DR   KEGG; bsu:BSU13110; -.
DR   PATRIC; fig|224308.179.peg.1423; -.
DR   eggNOG; COG0788; Bacteria.
DR   InParanoid; O34990; -.
DR   OrthoDB; 9806170at2; -.
DR   PhylomeDB; O34990; -.
DR   BioCyc; BSUB:BSU13110-MONOMER; -.
DR   UniPathway; UPA00074; UER00170.
DR   Proteomes; UP000001570; 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   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; One-carbon metabolism; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Formyltetrahydrofolate deformylase"
FT                   /id="PRO_0000360820"
FT   DOMAIN          21..102
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01927"
FT   CONFLICT        113
FT                   /note="E -> N (in Ref. 1; CAA05590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="E -> K (in Ref. 1; CAA05590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="A -> T (in Ref. 1; CAA05590)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  34477 MW;  3D8545C6802990E3 CRC64;
     MKSYMTQRLD EYRDGNEDKG RLLVSCPDQP GIVSAVSAFL FEHGANIIES NQYTTDPEGG
     RFFLRIEFDC AGIREKKSSL QAAFASVAEK FDMTWSLTLA SELKRVAIFV SKELHCLHEL
     IWEWQTGNLM AEIAVVISNH EEARELVERL NIPFHYMKAN KDIRAEVEKK QLELLEQYDV
     DVIVLARYMQ ILTPDFVSAH PNRIINIHHS FLPAFIGANP YKRAYERGVK LIGATSHYVT
     NDLDEGPIIE QDIERVDHRD NAEALKNIGR TIERSVLARA VKWHLEDRVI VHENKTIVFN
//
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