ID 5FCL_ARATH Reviewed; 277 AA.
AC Q8L539; F4K2F3; Q84WD9; Q9FYA5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase, mitochondrial;
DE Short=5-FCL;
DE EC=6.3.3.2;
DE Flags: Precursor;
GN Name=5FCL; OrderedLocusNames=At5g13050; ORFNames=T19L5.10;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12207015; DOI=10.1074/jbc.m205632200;
RA Roje S., Janave M.T., Ziemak M.J., Hanson A.D.;
RT "Cloning and characterization of mitochondrial 5-formyltetrahydrofolate
RT cycloligase from higher plants.";
RL J. Biol. Chem. 277:42748-42754(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-277 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-277 (ISOFORM 1).
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15888445; DOI=10.1074/jbc.m503106200;
RA Goyer A., Collakova E., Diaz de la Garza R., Quinlivan E.P., Williamson J.,
RA Gregory J.F., Shachar-Hill Y., Hanson A.D.;
RT "5-Formyltetrahydrofolate is an inhibitory but well tolerated metabolite in
RT Arabidopsis leaves.";
RL J. Biol. Chem. 280:26137-26142(2005).
CC -!- FUNCTION: Contributes to tetrahydrofolate metabolism and
CC photorespiration through the regulation of serine
CC hydroxymethyltransferase. Prefers the pentalutamyl to the monoglutamyl
CC form of 5-formyltetrahydrofolate. {ECO:0000269|PubMed:12207015,
CC ECO:0000269|PubMed:15888445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC Evidence={ECO:0000269|PubMed:12207015};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for 5-formyltetrahydrofolate {ECO:0000269|PubMed:12207015};
CC KM=35.2 uM for ATP {ECO:0000269|PubMed:12207015};
CC Vmax=11.5 umol/min/mg enzyme toward 5-formyltetrahydrofolate
CC {ECO:0000269|PubMed:12207015};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:12207015};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:12207015}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:12207015}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L539-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L539-2; Sequence=VSP_054249, VSP_054250;
CC -!- DISRUPTION PHENOTYPE: Reduced growth rate and delayed flowering.
CC {ECO:0000269|PubMed:15888445}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF516365; AAM90960.1; -; mRNA.
DR EMBL; AL391711; CAC05433.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91844.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91845.1; -; Genomic_DNA.
DR EMBL; BX830290; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT024502; ABD19683.1; -; mRNA.
DR EMBL; AY084396; AAM60972.1; -; mRNA.
DR EMBL; BT003924; AAO41971.1; -; mRNA.
DR RefSeq; NP_001031873.1; NM_001036796.2. [Q8L539-2]
DR RefSeq; NP_568284.1; NM_121308.2. [Q8L539-1]
DR AlphaFoldDB; Q8L539; -.
DR SMR; Q8L539; -.
DR STRING; 3702.Q8L539; -.
DR iPTMnet; Q8L539; -.
DR PaxDb; 3702-AT5G13050-1; -.
DR ProteomicsDB; 243267; -. [Q8L539-1]
DR EnsemblPlants; AT5G13050.1; AT5G13050.1; AT5G13050. [Q8L539-1]
DR EnsemblPlants; AT5G13050.2; AT5G13050.2; AT5G13050. [Q8L539-2]
DR GeneID; 831144; -.
DR Gramene; AT5G13050.1; AT5G13050.1; AT5G13050. [Q8L539-1]
DR Gramene; AT5G13050.2; AT5G13050.2; AT5G13050. [Q8L539-2]
DR KEGG; ath:AT5G13050; -.
DR Araport; AT5G13050; -.
DR TAIR; AT5G13050; 5-FCL.
DR eggNOG; KOG3093; Eukaryota.
DR HOGENOM; CLU_066245_2_0_1; -.
DR InParanoid; Q8L539; -.
DR OMA; DKWGIPT; -.
DR OrthoDB; 298720at2759; -.
DR PhylomeDB; Q8L539; -.
DR BioCyc; ARA:AT5G13050-MONOMER; -.
DR BRENDA; 6.3.3.2; 399.
DR SABIO-RK; Q8L539; -.
DR PRO; PR:Q8L539; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L539; baseline and differential.
DR Genevisible; Q8L539; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IMP:TAIR.
DR Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR InterPro; IPR002698; FTHF_cligase.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR02727; MTHFS_bact; 1.
DR PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..277
FT /note="5-formyltetrahydrofolate cyclo-ligase,
FT mitochondrial"
FT /id="PRO_0000428719"
FT BINDING 60..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 207..211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 209..214
FT /note="GGYYDT -> ATTTLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_054249"
FT VAR_SEQ 215..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_054250"
SQ SEQUENCE 277 AA; 31233 MW; 221250EBE1D074FE CRC64;
MIGARVFCIT TTALRRSPIF FFPKIPTRPV FRLSPATRPI VAMSTTSKNQ EELDSIFKQK
RVVRSTVRKS LKAMDPSLRT QQDEAIQKTV LEAPWFKSCK GLCAYISCKS LNEVDTSKIL
SEILQHPDSN TQKKLYVPWV EDKNSNMRML HISHMEDLVA NSMNILEPAP VDAQGNDRED
VLQADEPIDL FILPGLAFDR CGRRLGRGGG YYDTFLKRYQ DRAKEKGWRY PLMVALSYSP
QILEDGSIPV TPNDVLIDAL VTPSGVVPIT PRATESM
//
