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Database: UniProt
Entry: A0A091D067_FUKDA
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ID   A0A091D067_FUKDA        Unreviewed;       508 AA.
AC   A0A091D067;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00013409};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=H920_13240 {ECO:0000313|EMBL:KFO25479.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25479.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO25479.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO25479.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydration of fumarate to L-malate in the
CC       tricarboxylic acid (TCA) cycle to facilitate a transition step in the
CC       production of energy in the form of NADH.
CC       {ECO:0000256|ARBA:ARBA00003146}.
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:0000256|ARBA:ARBA00024594};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461;
CC         Evidence={ECO:0000256|ARBA:ARBA00024594};
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:0000256|ARBA:ARBA00024453};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462;
CC         Evidence={ECO:0000256|ARBA:ARBA00024453};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000256|ARBA:ARBA00004859}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR   EMBL; KN123358; KFO25479.1; -; Genomic_DNA.
DR   RefSeq; XP_010640964.1; XM_010642662.2.
DR   AlphaFoldDB; A0A091D067; -.
DR   STRING; 885580.ENSFDAP00000009217; -.
DR   Ensembl; ENSFDAT00000022227; ENSFDAP00000009217; ENSFDAG00000017263.
DR   GeneID; 104875211; -.
DR   CTD; 2271; -.
DR   eggNOG; KOG1317; Eukaryota.
DR   OMA; AKWRAQT; -.
DR   OrthoDB; 1341425at2759; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          56..387
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          453..505
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   508 AA;  54494 MW;  8504DD28DA24B099 CRC64;
     MYRALRLLAW SRRLLRAPAL ASSPGVGGAA VLPLWSQNAA RMASQNSFRI EYDTFGELKV
     PNDKYYGAQT VRSTMNFKIG GVTERMPIPV IKAFGILKRA AAEVNQDYGL DPKIATAIMK
     AADEVAEGKL NDHFPLVVWQ TGSGTQTNMN VNEVISNRAI EMLGGELGSK KPVHPNDHVN
     KSQSSNDTFP TAMHIAAAVE VHEVLLPGLQ KLHDGLSAKS KEFAQIIKIG RTHTQDAVPL
     SLGQEFSGYV QQVQYAMARI KAALPRIYEL AAGGTAVGTG LNTRVGFAEK VAAKVAALTG
     LPFVTAPNKF EALAAHDALV ELSGAMNTTA CSLMKIANDI RFLGSGPRSG LGELILPENE
     PGSSIMPGKV NPTQCEAMTM VAAQVMGNHV AVTVGGSNGH FELNVFKPMM IKNVLHSARL
     LGDASVSFTE NCVVGIQANT ERINKLMNES LMLVTALNPH IGYDKAAKIA KTAHKNGSTL
     KETAIELGYL TAQQFDEWVK PKDMLGPK
//
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