FOLD1_ARATH
ID FOLD1_ARATH Reviewed; 352 AA.
AC A2RVV7; C0Z3J6; F4ITV6; Q84W19; Q9ZVI8;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Bifunctional protein FolD 1, mitochondrial;
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase;
DE EC=1.5.1.5;
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE EC=3.5.4.9;
DE Flags: Precursor;
GN Name=FOLD1; Synonyms=DHC1; OrderedLocusNames=At2g38660; ORFNames=T6A23.14;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
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: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC methenyltetrahydrofolate to 10-formyltetrahydrofolate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9;
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2RVV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RVV7-2; Sequence=VSP_053392;
CC Name=3;
CC IsoId=A2RVV7-3; Sequence=VSP_053393, VSP_053394;
CC Name=4;
CC IsoId=A2RVV7-4; Sequence=VSP_053390, VSP_053391;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Fold1, puru1 and puru2
CC triple mutant shows no photorespiratory phenotype.
CC {ECO:0000269|PubMed:18628352}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005499; AAC67352.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC09564.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09565.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09566.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09567.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62489.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62490.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62491.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62492.1; -; Genomic_DNA.
DR EMBL; BT004325; AAO42321.1; -; mRNA.
DR EMBL; BT030098; ABN04836.1; -; mRNA.
DR EMBL; AK319160; BAH57275.1; -; mRNA.
DR PIR; G84807; G84807.
DR RefSeq; NP_001031508.1; NM_001036431.3. [A2RVV7-2]
DR RefSeq; NP_001118472.1; NM_001125000.3. [A2RVV7-1]
DR RefSeq; NP_001189703.1; NM_001202774.1. [A2RVV7-3]
DR RefSeq; NP_001324644.1; NM_001336716.1. [A2RVV7-4]
DR RefSeq; NP_001324645.1; NM_001336717.1. [A2RVV7-4]
DR RefSeq; NP_001324646.1; NM_001336718.1. [A2RVV7-4]
DR RefSeq; NP_001324647.1; NM_001336715.1. [A2RVV7-4]
DR RefSeq; NP_181400.2; NM_129423.6. [A2RVV7-1]
DR AlphaFoldDB; A2RVV7; -.
DR SMR; A2RVV7; -.
DR BioGRID; 3790; 1.
DR IntAct; A2RVV7; 1.
DR STRING; 3702.AT2G38660.3; -.
DR PaxDb; A2RVV7; -.
DR PRIDE; A2RVV7; -.
DR ProteomicsDB; 230109; -. [A2RVV7-1]
DR EnsemblPlants; AT2G38660.1; AT2G38660.1; AT2G38660. [A2RVV7-1]
DR EnsemblPlants; AT2G38660.2; AT2G38660.2; AT2G38660. [A2RVV7-2]
DR EnsemblPlants; AT2G38660.3; AT2G38660.3; AT2G38660. [A2RVV7-1]
DR EnsemblPlants; AT2G38660.4; AT2G38660.4; AT2G38660. [A2RVV7-3]
DR EnsemblPlants; AT2G38660.5; AT2G38660.5; AT2G38660. [A2RVV7-4]
DR EnsemblPlants; AT2G38660.6; AT2G38660.6; AT2G38660. [A2RVV7-4]
DR EnsemblPlants; AT2G38660.7; AT2G38660.7; AT2G38660. [A2RVV7-4]
DR EnsemblPlants; AT2G38660.8; AT2G38660.8; AT2G38660. [A2RVV7-4]
DR GeneID; 818448; -.
DR Gramene; AT2G38660.1; AT2G38660.1; AT2G38660. [A2RVV7-1]
DR Gramene; AT2G38660.2; AT2G38660.2; AT2G38660. [A2RVV7-2]
DR Gramene; AT2G38660.3; AT2G38660.3; AT2G38660. [A2RVV7-1]
DR Gramene; AT2G38660.4; AT2G38660.4; AT2G38660. [A2RVV7-3]
DR Gramene; AT2G38660.5; AT2G38660.5; AT2G38660. [A2RVV7-4]
DR Gramene; AT2G38660.6; AT2G38660.6; AT2G38660. [A2RVV7-4]
DR Gramene; AT2G38660.7; AT2G38660.7; AT2G38660. [A2RVV7-4]
DR Gramene; AT2G38660.8; AT2G38660.8; AT2G38660. [A2RVV7-4]
DR KEGG; ath:AT2G38660; -.
DR Araport; AT2G38660; -.
DR TAIR; locus:2064143; AT2G38660.
DR eggNOG; KOG0089; Eukaryota.
DR HOGENOM; CLU_034045_1_2_1; -.
DR InParanoid; A2RVV7; -.
DR OMA; ATPQSCI; -.
DR OrthoDB; 1004679at2759; -.
DR PhylomeDB; A2RVV7; -.
DR BioCyc; ARA:AT2G38660-MON; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:A2RVV7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A2RVV7; baseline and differential.
DR Genevisible; A2RVV7; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Mitochondrion; Multifunctional enzyme;
KW NADP; One-carbon metabolism; Oxidoreductase; Photorespiration;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..352
FT /note="Bifunctional protein FolD 1, mitochondrial"
FT /id="PRO_0000424344"
FT VAR_SEQ 164..185
FT /note="HLNESKILNMVRLEKDVDGFHP -> VCFSFFSLDVVMGDVSVVDVKD (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053390"
FT VAR_SEQ 186..352
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053391"
FT VAR_SEQ 243..352
FT /note="RHDATVSTVHAFTKDPEHITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGT
FT TPVEDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLEAAKRIFL
FT -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053392"
FT VAR_SEQ 319..332
FT /note="GVASAITPVPGGVG -> DRRLHAVRVINDLF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053393"
FT VAR_SEQ 333..352
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_053394"
SQ SEQUENCE 352 AA; 38048 MW; 25D08FF2E8EBCC3A CRC64;
MLMIARKALA SAHTKAFRLA TRDVHCFSSI LVSPPLVSLD LPENWIPYSD PPPPVSFETE
QKTVVIDGNV IAEEIRTKII SEVGKMKKAV GKVPGLAVVL VGEQRDSQTY VRNKIKACEE
TGIKSVLAEL PEDCTEGQII SVLRKFNEDT SIHGILVQLP LPQHLNESKI LNMVRLEKDV
DGFHPLNVGN LAMRGREPLF VSCTPKGCVE LLIRTGVEIA GKNAVVIGRS NIVGLPMSLL
LQRHDATVST VHAFTKDPEH ITRKADIVIA AAGIPNLVRG SWLKPGAVVI DVGTTPVEDS
SCEFGYRLVG DVCYEEALGV ASAITPVPGG VGPMTITMLL CNTLEAAKRI FL
