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Database: UniProt
Entry: O17214
LinkDB: O17214
Original site: O17214 
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   27-MAR-2024, entry version 168.
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; 45.
DR   DIP; DIP-25418N; -.
DR   IntAct; O17214; 3.
DR   STRING; 6239.H14A12.2a.1; -.
DR   World-2DPAGE; 0020:O17214; -.
DR   EPD; O17214; -.
DR   PaxDb; 6239-H14A12-2a; -.
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   AGR; WB:WBGene00001503; -.
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; AKWRAQT; -.
DR   OrthoDB; 1341425at2759; -.
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 cell types or 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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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   NCBIfam; TIGR00979; fumC_II; 1.
DR   PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 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
//
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