ID   PURU2_ARATH             Reviewed;         328 AA.
AC   F4JP46; O23579;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Formyltetrahydrofolate deformylase 2, mitochondrial;
DE            EC=3.5.1.10;
DE   Flags: Precursor;
GN   Name=PURU2; OrderedLocusNames=At4g17360; ORFNames=dl4715c, FCAALL.417;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=18628352; DOI=10.1105/tpc.108.058701;
RA   Collakova E., Goyer A., Naponelli V., Krassovskaya I., Gregory J.F. III,
RA   Hanson A.D., Shachar-Hill Y.;
RT   "Arabidopsis 10-formyl tetrahydrofolate deformylases are essential for
RT   photorespiration.";
RL   Plant Cell 20:1818-1832(2008).
CC   -!- FUNCTION: Deformylase involved in photorespiration. Prevents excessive
CC       accumulation of 5-formyl tetrahydrofolate (THF), a potent inhibitor of
CC       the Gly decarboxylase/Ser hydroxymethyltransferase complex.
CC       {ECO:0000269|PubMed:18628352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-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:57454; EC=3.5.1.10;
CC         Evidence={ECO:0000269|PubMed:18628352};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18628352}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, cotyledons, roots, seeds and
CC       flowers. {ECO:0000269|PubMed:18628352}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Puru1 and puru2 double
CC       mutant shows a 70-fold increase in Gly levels and accumulates elevated
CC       levels of 5- and 10-formyl THF. Embryo development arrests between
CC       heart and early bent cotyledon stages, and mature seeds are shriveled,
CC       accumulate low amounts of lipids, and fail to germinate. Puru1 and
CC       puru2 double mutant is only conditionally lethal and is rescued by
CC       growth under nonphotorespiratory conditions. Puru1, puru2 and fold1
CC       triple mutant shows no photorespiratory phenotype.
CC       {ECO:0000269|PubMed:18628352}.
CC   -!- SIMILARITY: Belongs to the PurU family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB10517.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78739.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z97343; CAB10517.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161546; CAB78739.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83880.1; -; Genomic_DNA.
DR   PIR; H71442; H71442.
DR   RefSeq; NP_193467.2; NM_117840.5.
DR   AlphaFoldDB; F4JP46; -.
DR   SMR; F4JP46; -.
DR   STRING; 3702.AT4G17360.1; -.
DR   PaxDb; F4JP46; -.
DR   PRIDE; F4JP46; -.
DR   ProteomicsDB; 226462; -.
DR   EnsemblPlants; AT4G17360.1; AT4G17360.1; AT4G17360.
DR   GeneID; 827448; -.
DR   Gramene; AT4G17360.1; AT4G17360.1; AT4G17360.
DR   KEGG; ath:AT4G17360; -.
DR   Araport; AT4G17360; -.
DR   TAIR; locus:2130893; AT4G17360.
DR   eggNOG; KOG3076; Eukaryota.
DR   HOGENOM; CLU_038395_3_0_1; -.
DR   InParanoid; F4JP46; -.
DR   OrthoDB; 943824at2759; -.
DR   PRO; PR:F4JP46; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JP46; baseline and differential.
DR   Genevisible; F4JP46; AT.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009853; P:photorespiration; IMP:TAIR.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IMP:TAIR.
DR   CDD; cd04875; ACT_F4HF-DF; 1.
DR   CDD; cd08648; FMT_core_Formyl-FH4-Hydrolase_C; 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; IPR001555; GART_AS.
DR   InterPro; IPR004810; PurU.
DR   InterPro; IPR044074; PurU_ACT.
DR   PANTHER; PTHR42706; PTHR42706; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   PRINTS; PR01575; FFH4HYDRLASE.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00373; GART; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Mitochondrion; One-carbon metabolism; Photorespiration;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..328
FT                   /note="Formyltetrahydrofolate deformylase 2, mitochondrial"
FT                   /id="PRO_0000424343"
FT   DOMAIN          46..129
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250"
FT   CONFLICT        78
FT                   /note="F -> L (in Ref. 1; CAB10517 and 2; CAB78739)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  37296 MW;  E05FB4F3800F1599 CRC64;
     MIRRVSTTSC LSATAFRSFT KWSFKSSQFH GESLDSSVSP LLIPGFHVFH CPDVVGIVAK
     LSDCIAAKGG NILGYDVFVP ENKNVFYSRS EFIFDPVKWP RRQMDEDFQT IAQKFSALSS
     VVRVPSLDPK YKIALLLSKQ DHCLVEMLHK WQDGKLPVDI TCVISNHERA PNTHVMRFLQ
     RHGISYHYLP TTDQNKIEEE ILELVKGTDF LVLARYMQLL SGNFLKGYGK DVINIHHGLL
     PSFKGRNPVK QAFDAGVKLI GATTHFVTEE LDSGPIIEQM VERVSHRDNL RSFVQKSEDL
     EKKCLMKAIK SYCELRVLPY GTQRTVVF