PURU1_ARATH
ID PURU1_ARATH Reviewed; 323 AA.
AC Q93YQ3;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Formyltetrahydrofolate deformylase 1, mitochondrial;
DE EC=3.5.1.10;
DE Flags: Precursor;
GN Name=PURU1; OrderedLocusNames=At5g47435; ORFNames=MNJ7.1;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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}.
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DR EMBL; AB018117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED95511.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95512.1; -; Genomic_DNA.
DR EMBL; AK117593; BAC42250.1; -; mRNA.
DR EMBL; AY059833; AAL24315.1; -; mRNA.
DR EMBL; AY081459; AAM10021.1; -; mRNA.
DR RefSeq; NP_568682.1; NM_124115.4.
DR RefSeq; NP_851145.1; NM_180814.3.
DR AlphaFoldDB; Q93YQ3; -.
DR SMR; Q93YQ3; -.
DR BioGRID; 20039; 2.
DR IntAct; Q93YQ3; 1.
DR STRING; 3702.AT5G47435.2; -.
DR iPTMnet; Q93YQ3; -.
DR PaxDb; Q93YQ3; -.
DR PRIDE; Q93YQ3; -.
DR ProteomicsDB; 224803; -.
DR EnsemblPlants; AT5G47435.1; AT5G47435.1; AT5G47435.
DR EnsemblPlants; AT5G47435.2; AT5G47435.2; AT5G47435.
DR GeneID; 834791; -.
DR Gramene; AT5G47435.1; AT5G47435.1; AT5G47435.
DR Gramene; AT5G47435.2; AT5G47435.2; AT5G47435.
DR KEGG; ath:AT5G47435; -.
DR Araport; AT5G47435; -.
DR TAIR; locus:505006677; AT5G47435.
DR eggNOG; KOG3076; Eukaryota.
DR HOGENOM; CLU_038395_3_0_1; -.
DR InParanoid; Q93YQ3; -.
DR OMA; HADHHTD; -.
DR OrthoDB; 943824at2759; -.
DR PhylomeDB; Q93YQ3; -.
DR PRO; PR:Q93YQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93YQ3; baseline and differential.
DR Genevisible; Q93YQ3; 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; 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 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.
PE 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; One-carbon metabolism; Photorespiration;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..323
FT /note="Formyltetrahydrofolate deformylase 1, mitochondrial"
FT /id="PRO_0000424342"
FT DOMAIN 41..124
FT /note="ACT"
FT ACT_SITE 267
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 36452 MW; A45061CBE8B7C5DB CRC64;
MIRRITERAS GFAKNIPILK SSRFHGESLD SSVSPVLIPG VHVFHCQDAV GIVAKLSDCI
AAKGGNILGY DVFVPENNNV FYSRSEFIFD PVKWPRSQVD EDFQTIAQRY GALNSVVRVP
SIDPKYKIAL LLSKQDHCLV EMLHKWQDGK LPVDITCVIS NHERASNTHV MRFLERHGIP
YHYVSTTKEN KREDDILELV KDTDFLVLAR YMQILSGNFL KGYGKDVINI HHGLLPSFKG
GYPAKQAFDA GVKLIGATSH FVTEELDSGP IIEQMVESVS HRDNLRSFVQ KSEDLEKKCL
TRAIKSYCEL RVLPYGTNKT VVF
