FUM1_ARATH
ID FUM1_ARATH Reviewed; 492 AA.
AC P93033; O24649;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fumarate hydratase 1, mitochondrial {ECO:0000303|PubMed:20202172};
DE Short=AtFUM1 {ECO:0000303|PubMed:29688630};
DE Short=Fumarase 1 {ECO:0000303|PubMed:20202172};
DE EC=4.2.1.2 {ECO:0000269|PubMed:29688630};
DE Flags: Precursor;
GN Name=FUM1 {ECO:0000303|PubMed:20202172}; OrderedLocusNames=At2g47510;
GN ORFNames=T30B22.19;
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].
RA Behal R.H., Oliver D.J.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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].
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20202172; DOI=10.1111/j.1365-313x.2010.04189.x;
RA Pracharoenwattana I., Zhou W., Keech O., Francisco P.B., Udomchalothorn T.,
RA Tschoep H., Stitt M., Gibon Y., Smith S.M.;
RT "Arabidopsis has a cytosolic fumarase required for the massive allocation
RT of photosynthate into fumaric acid and for rapid plant growth on high
RT nitrogen.";
RL Plant J. 62:785-795(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-28.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=29688630; DOI=10.1111/febs.14483;
RA Zubimendi J.P., Martinatto A., Valacco M.P., Moreno S., Andreo C.S.,
RA Drincovich M.F., Tronconi M.A.;
RT "The complex allosteric and redox regulation of the fumarate hydratase and
RT malate dehydratase reactions of Arabidopsis thaliana Fumarase 1 and 2 gives
RT clues for understanding the massive accumulation of fumarate.";
RL FEBS J. 285:2205-2224(2018).
CC -!- FUNCTION: Catalyzes the reversible stereospecific interconversion of
CC fumarate to L-malate (PubMed:29688630). Catalyzes the hydration of
CC fumarate to L-malate in the tricarboxylic acid (TCA) cycle to
CC facilitate a transition step in the production of energy in the form of
CC NADH (By similarity). {ECO:0000250|UniProtKB:P08417,
CC ECO:0000250|UniProtKB:P10173, ECO:0000269|PubMed:29688630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000269|PubMed:29688630};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461;
CC Evidence={ECO:0000269|PubMed:29688630};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462;
CC Evidence={ECO:0000269|PubMed:29688630};
CC -!- ACTIVITY REGULATION: Fumarate hydratase activity (fumarate to L-malate)
CC is strongly inhibited by phosphoenolpyruvate, citrate, oxaloacetate,
CC ATP and ADP (PubMed:29688630). Malate dehydratase activity (malate to
CC fumarate) is activated by oxaloacetate, pyruvate, Asn and Gln
CC (PubMed:29688630). Malate dehydratase activity (malate to fumarate) is
CC inhibited by citrate, succinate, ADP, ATP, glucose-6P and
CC phosphoenolpyruvate (PubMed:29688630). {ECO:0000269|PubMed:29688630}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for fumarate (at pH 8.0) {ECO:0000269|PubMed:29688630};
CC KM=1.8 mM for (S)-malate (at pH 8.0) {ECO:0000269|PubMed:29688630};
CC Note=kcat is 21 sec(-1) for fumarate (at pH 8.0) (PubMed:29688630).
CC kcat is 15.3 sec(-1) for (S)-malate (at pH 8.0) (PubMed:29688630).
CC {ECO:0000269|PubMed:29688630};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000250|UniProtKB:P08417,
CC ECO:0000250|UniProtKB:P10173}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29688630}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:20202172, ECO:0000305|PubMed:25732537}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:20202172}.
CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC site, and the non-catalytic B site that may play a role in the transfer
CC of substrate or product between the active site and the solvent.
CC Alternatively, the B site may bind allosteric effectors.
CC {ECO:0000250|UniProtKB:P05042, ECO:0000250|UniProtKB:P9WN93}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000305}.
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DR EMBL; U82202; AAB39989.1; -; mRNA.
DR EMBL; AC002535; AAC62859.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10852.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10853.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62150.1; -; Genomic_DNA.
DR EMBL; AF020303; AAB71399.1; -; Genomic_DNA.
DR EMBL; AY054252; AAL06911.1; -; mRNA.
DR EMBL; AY062460; AAL32538.1; -; mRNA.
DR EMBL; BT003361; AAO29979.1; -; mRNA.
DR PIR; T00433; T00433.
DR RefSeq; NP_001078075.1; NM_001084606.2.
DR RefSeq; NP_001324328.1; NM_001337266.1.
DR RefSeq; NP_182273.1; NM_130319.4.
DR AlphaFoldDB; P93033; -.
DR SMR; P93033; -.
DR BioGRID; 4699; 5.
DR IntAct; P93033; 2.
DR STRING; 3702.AT2G47510.1; -.
DR iPTMnet; P93033; -.
DR MetOSite; P93033; -.
DR SwissPalm; P93033; -.
DR PaxDb; P93033; -.
DR PRIDE; P93033; -.
DR ProteomicsDB; 230004; -.
DR EnsemblPlants; AT2G47510.1; AT2G47510.1; AT2G47510.
DR EnsemblPlants; AT2G47510.2; AT2G47510.2; AT2G47510.
DR EnsemblPlants; AT2G47510.3; AT2G47510.3; AT2G47510.
DR GeneID; 819364; -.
DR Gramene; AT2G47510.1; AT2G47510.1; AT2G47510.
DR Gramene; AT2G47510.2; AT2G47510.2; AT2G47510.
DR Gramene; AT2G47510.3; AT2G47510.3; AT2G47510.
DR KEGG; ath:AT2G47510; -.
DR Araport; AT2G47510; -.
DR TAIR; locus:2061966; AT2G47510.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; P93033; -.
DR OMA; HDSMGEV; -.
DR OrthoDB; 1022919at2759; -.
DR PhylomeDB; P93033; -.
DR BRENDA; 4.2.1.2; 399.
DR UniPathway; UPA00223; UER01007.
DR PRO; PR:P93033; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93033; baseline and differential.
DR Genevisible; P93033; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IDA:UniProtKB.
DR GO; GO:0006106; P:fumarate metabolic process; IDA:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01362; Fumarase_classII; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00743; FumaraseC; 1.
DR InterPro; IPR005677; Fum_hydII.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00979; fumC_II; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Lyase; Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 29..492
FT /note="Fumarate hydratase 1, mitochondrial"
FT /id="PRO_0000010329"
FT ACT_SITE 216
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT ACT_SITE 346
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 127..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 157..160
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 167..169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 352..354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT SITE 359
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT CONFLICT 8..9
FT /note="RR -> A (in Ref. 1; AAB39989)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> R (in Ref. 1; AAB39989)"
FT /evidence="ECO:0000305"
FT CONFLICT 393..394
FT /note="IA -> TS (in Ref. 1; AAB39989)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="P -> R (in Ref. 1; AAB39989)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="Y -> C (in Ref. 1; AAB39989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 53000 MW; DF07D2D393966B3E CRC64;
MSIYVASRRL SGGTTVTALR YATSLRSYST SFREERDTFG PIQVPSDKLW GAQTQRSLQN
FEIGGERERM PEPIVRAFGV LKKCAAKVNM EYGLDPTIGK AIMQAAQEVA EGKLNDHFPL
VVWQTGSGTQ SNMNANEVIA NRAAEILGRK RGEKCVHPND HVNRSQSSND TFPTVMHIAA
ATEINSRLIP SLKTLHSTLE SKSFEFKDIV KIGRTHTQDA TPLTLGQEFG GYATQVKYGL
NRVTCTLPRL YQLAQGGTAV GTGLNTKKGF DVKIAAAVAE ETNLPFVTAE NKFEALAAHD
ACVETSGSLN TIATSLMKIA NDIRFLGSGP RCGLGELVLP ENEPGSSIMP GKVNPTQCEA
LTMVCAQVMG NHVAVTVGGS NGHFELNVFK PVIASALLHS VRLIADASAS FEKNCVRGIE
ANRERISKLL HESLMLVTSL NPKIGYDNAA AVAKKAHKEG CTLKEAALNL GVLTAEEFDT
LVVPEKMIGP SD
