FUMH_CAEEL
ID FUMH_CAEEL Reviewed; 501 AA.
AC O17214;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable fumarate hydratase, mitochondrial {ECO:0000250|UniProtKB:P07954};
DE Short=Fumarase {ECO:0000250|UniProtKB:P07954};
DE EC=4.2.1.2 {ECO:0000250|UniProtKB:P07954};
DE Flags: Precursor;
GN Name=fum-1 {ECO:0000312|WormBase:H14A12.2a}; ORFNames=H14A12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the reversible stereospecific interconversion of
CC fumarate to L-malate. In mitochondrion, 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. {ECO:0000250|UniProtKB:P07954}.
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:0000250|UniProtKB:P07954};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000250|UniProtKB:P07954}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07954}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P08417}. Cytoplasm
CC {ECO:0000250|UniProtKB:P08417}.
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; FO081548; CCD72341.1; -; Genomic_DNA.
DR PIR; C88508; C88508.
DR RefSeq; NP_498642.1; NM_066241.7.
DR AlphaFoldDB; O17214; -.
DR SMR; O17214; -.
DR BioGRID; 41267; 44.
DR DIP; DIP-25418N; -.
DR IntAct; O17214; 3.
DR STRING; 6239.H14A12.2a; -.
DR World-2DPAGE; 0020:O17214; -.
DR EPD; O17214; -.
DR PaxDb; O17214; -.
DR PeptideAtlas; O17214; -.
DR EnsemblMetazoa; H14A12.2.1; H14A12.2.1; WBGene00001503.
DR GeneID; 176059; -.
DR KEGG; cel:CELE_H14A12.2; -.
DR UCSC; H14A12.2a; c. elegans.
DR CTD; 176059; -.
DR WormBase; H14A12.2a; CE11580; WBGene00001503; fum-1.
DR eggNOG; KOG1317; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; O17214; -.
DR OMA; HDSMGEV; -.
DR OrthoDB; 1022919at2759; -.
DR PhylomeDB; O17214; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01007.
DR PRO; PR:O17214; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001503; Expressed in larva and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Lyase; Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..501
FT /note="Probable fumarate hydratase, mitochondrial"
FT /id="PRO_0000010328"
FT ACT_SITE 226
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT ACT_SITE 356
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 167..170
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05042"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT BINDING 362..364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WN93"
FT SITE 369
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P05042"
SQ SEQUENCE 501 AA; 53647 MW; DA578BE105509C1D CRC64;
MSAVSMLQGE MLARGGAVIA RGASLATARN FSRTTVPMAK IRKERDTFGE LEVPADKYYG
AQTARSQMNF KIGGPEERMP IPVIHAFGIL KKAAALVNTE FGLDKKLADA ISQAADEVVD
GKLDEHFPLV TWQTGSGTQS NMNVNEVISN RAIEILGGEL GSKKPVHPND HVNMSQSSND
TFPTAMHIAV GREVNSRLLP ALKKLRTALH NKAEEFKDII KIGRTHTQDA VPLTLGQEFS
AYVTQLDNSI ARVESTLPRL YQLAAGGTAV GTGLNTRKGF AEKVAATVSE LTGLPFVTAP
NKFEALAAHD ALVEVHGALN TVAVSFMKIG NDIRFLGSGP RCGLGELSLP ENEPGSSIMP
GKVNPTQCEA ITMVAAQVMG NQVAVSVGGS NGHFELNVFK PLIVRNVLQS TRLLADSAVS
FTDHCVDGIV ANKDNIAKIM RESLMLVTAL NPHIGYDNAA KIAKTAHKNG TTLVQEAVKL
GILTEEQFAQ WVKPENMLGP K
