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5FCL_ARATH
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   03-AUG-2022, entry version 122.
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 = 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.AT5G13050.1; -.
DR   iPTMnet; Q8L539; -.
DR   PaxDb; Q8L539; -.
DR   PRIDE; Q8L539; -.
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; locus:2179827; AT5G13050.
DR   eggNOG; KOG3093; Eukaryota.
DR   HOGENOM; CLU_066245_2_0_1; -.
DR   InParanoid; Q8L539; -.
DR   OMA; DKWGIPT; -.
DR   PhylomeDB; Q8L539; -.
DR   BioCyc; ARA:AT5G13050-MON; -.
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; IBA:GO_Central.
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:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IMP:TAIR.
DR   Gene3D; 3.40.50.10420; -; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR02727; MTHFS_bact; 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
 
 
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