FUM2_ARATH
ID FUM2_ARATH Reviewed; 499 AA.
AC Q9FI53; Q8VY72;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Fumarate hydratase 2 {ECO:0000303|PubMed:20202172};
DE Short=AtFUM2 {ECO:0000303|PubMed:29688630};
DE Short=Fumarase 2 {ECO:0000303|PubMed:20202172};
DE EC=4.2.1.2 {ECO:0000269|PubMed:29688630};
GN Name=FUM2 {ECO:0000303|PubMed:20202172}; OrderedLocusNames=At5g50950;
GN ORFNames=K3K7.11;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] (ISOFORMS 1 AND 3).
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 FUNCTION, 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 [5]
RP FUNCTION.
RX PubMed=27440755; DOI=10.1104/pp.16.00852;
RA Dyson B.C., Miller M.A., Feil R., Rattray N., Bowsher C.G., Goodacre R.,
RA Lunn J.E., Johnson G.N.;
RT "FUM2, a cytosolic fumarase, is essential for acclimation to low
RT temperature in Arabidopsis thaliana.";
RL Plant Physiol. 172:118-127(2016).
RN [6]
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: Cytosolic fumarate hydratase that catalyzes the reversible
CC stereospecific interconversion of fumarate to L-malate
CC (PubMed:29688630). Catalyzes the dehydration of L-malate to fumarate in
CC the cytosol: required for the massive fumarate accumulation during the
CC day in plants grown under high nitrogen (PubMed:20202172). Also
CC required for acclimation of photosynthesis to cold: acts by mediating
CC accumulation of fumarate at low temperature, leading to reduce
CC accumulation of phosphorylated sugars (PubMed:27440755).
CC {ECO:0000269|PubMed:20202172, ECO:0000269|PubMed:27440755,
CC 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, Asn and Gln (PubMed:29688630).
CC Malate dehydratase activity (malate to fumarate) is inhibited by
CC citrate, succinate, ADP and ATP (PubMed:29688630).
CC {ECO:0000269|PubMed:29688630}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for fumarate (at pH 7.7) {ECO:0000269|PubMed:29688630};
CC KM=0.6 mM for (S)-malate (at pH 7.7) {ECO:0000269|PubMed:29688630};
CC KM=0.5 mM for fumarate (at pH 8.0) {ECO:0000269|PubMed:29688630};
CC KM=1.7 mM for (S)-malate (at pH 8.0) {ECO:0000269|PubMed:29688630};
CC KM=0.5 mM for fumarate (at pH 8.2) {ECO:0000269|PubMed:29688630};
CC KM=1.9 mM for (S)-malate (at pH 8.2) {ECO:0000269|PubMed:29688630};
CC Note=kcat is 23.04 sec(-1) for fumarate (at pH 7.7)
CC (PubMed:29688630). kcat is 22.15 sec(-1) for fumarate (at pH 8.0)
CC (PubMed:29688630). kcat is 18.3 sec(-1) for fumarate (at pH 8.2)
CC (PubMed:29688630). kcat is 5.22 sec(-1) for (S)-malate (at pH 7.7)
CC (PubMed:29688630). kcat is 14.79 sec(-1) for (S)-malate (at pH 8.0)
CC (PubMed:29688630). kcat is 17.1 sec(-1) for (S)-malate (at pH 8.2)
CC (PubMed:29688630). {ECO:0000269|PubMed:29688630};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29688630}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20202172}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FI53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FI53-2; Sequence=VSP_011355;
CC Name=3;
CC IsoId=Q9FI53-3; Sequence=VSP_011356, VSP_011357;
CC -!- DISRUPTION PHENOTYPE: Decreased fumarate levels, while malate levels
CC increase (PubMed:20202172). Leaves display lower levels of many amino
CC acids during the day, but higher levels at night, consistent with a
CC link between fumarate and amino acid metabolism (PubMed:20202172).
CC Plants are unable to acclimate photosynthesis in response to cold
CC (PubMed:27440755). {ECO:0000269|PubMed:20202172,
CC ECO:0000269|PubMed:27440755}.
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; AB017063; BAB08741.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96014.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96015.1; -; Genomic_DNA.
DR EMBL; AY052197; AAK97668.1; -; mRNA.
DR EMBL; AY072393; AAL62385.1; -; mRNA.
DR EMBL; AY113070; AAM47378.1; -; mRNA.
DR RefSeq; NP_199908.1; NM_124474.4. [Q9FI53-1]
DR RefSeq; NP_851166.1; NM_180835.3. [Q9FI53-2]
DR AlphaFoldDB; Q9FI53; -.
DR SMR; Q9FI53; -.
DR BioGRID; 20414; 1.
DR IntAct; Q9FI53; 1.
DR STRING; 3702.AT5G50950.1; -.
DR PaxDb; Q9FI53; -.
DR PRIDE; Q9FI53; -.
DR ProteomicsDB; 228890; -. [Q9FI53-1]
DR EnsemblPlants; AT5G50950.1; AT5G50950.1; AT5G50950. [Q9FI53-2]
DR EnsemblPlants; AT5G50950.2; AT5G50950.2; AT5G50950. [Q9FI53-1]
DR GeneID; 835168; -.
DR Gramene; AT5G50950.1; AT5G50950.1; AT5G50950. [Q9FI53-2]
DR Gramene; AT5G50950.2; AT5G50950.2; AT5G50950. [Q9FI53-1]
DR KEGG; ath:AT5G50950; -.
DR Araport; AT5G50950; -.
DR TAIR; locus:2157413; AT5G50950.
DR eggNOG; KOG1317; Eukaryota.
DR InParanoid; Q9FI53; -.
DR OMA; MPRQIIQ; -.
DR PhylomeDB; Q9FI53; -.
DR BioCyc; ARA:AT5G50950-MON; -.
DR BioCyc; MetaCyc:AT5G50950-MON; -.
DR BRENDA; 4.2.1.2; 399.
DR PRO; PR:Q9FI53; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI53; baseline and differential.
DR Genevisible; Q9FI53; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0006106; P:fumarate metabolic process; IDA:UniProtKB.
DR GO; GO:0006108; P:malate metabolic process; IDA:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; IMP:TAIR.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:TAIR.
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 Alternative splicing; Cytoplasm; Lyase; Reference proteome;
KW Transit peptide.
FT CHAIN 1..499
FT /note="Fumarate hydratase 2"
FT /id="PRO_0000010330"
FT REGION 19..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT ACT_SITE 353
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 134..136
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 164..167
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 174..176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 359..361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT SITE 366
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT VAR_SEQ 210..214
FT /note="SFEFK -> VTHLM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_011356"
FT VAR_SEQ 215..499
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_011357"
FT VAR_SEQ 472..499
FT /note="HAAMKLGVLTSEEFDTLVVPEKMIGPSD -> VNNKLLTFSSLNKSEFKPIF
FT SKRKHVHVCYNIFVVLFWI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011355"
SQ SEQUENCE 499 AA; 54084 MW; A84422EB032FCB4E CRC64;
MAALTMQFEG EKKNVSEVAD VTLKQEDEQQ ERRSYSTPFR EERDTFGPIQ VPSDKLWGAQ
TQRSLQNFEI GGDRERMPEP IVRAFGVLKK CAAKVNMEYG LDPMIGEAIM EAAQEVAEGK
LNDHFPLVVW QTGSGTQSNM NANEVIANRA AEILGHKRGE KIVHPNDHVN RSQSSNDTFP
TVMHIAAATE ITSRLIPSLK NLHSSLESKS FEFKDIVKIG RTHTQDATPL TLGQEFGGYA
TQVEYGLNRV ACTLPRIYQL AQGGTAVGTG LNTKKGFDVK IAAAVAEETN LPFVTAENKF
EALAAHDACV ETSGSLNTIA TSLMKIANDI RFLGSGPRCG LGELSLPENE PGSSIMPGKV
NPTQCEALTM VCAQVMGNHV AVTIGGSNGH FELNVFKPVI ASALLHSIRL IADASASFEK
NCVRGIEANR ERISKLLHES LMLVTSLNPK IGYDNAAAVA KRAHKEGCTL KHAAMKLGVL
TSEEFDTLVV PEKMIGPSD
