GenomeNet

Database: UniProt
Entry: M1EPP1_MUSPF
LinkDB: M1EPP1_MUSPF
Original site: M1EPP1_MUSPF 
ID   M1EPP1_MUSPF            Unreviewed;       465 AA.
AC   M1EPP1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00013409};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
DE   Flags: Fragment;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AER98589.1};
RN   [1] {ECO:0000313|EMBL:AER98589.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AER98589.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JP009992; AER98589.1; -; mRNA.
DR   AlphaFoldDB; M1EPP1; -.
DR   UniPathway; UPA00223; UER01007.
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   2: Evidence at transcript level;
FT   DOMAIN          14..345
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          411..463
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AER98589.1"
FT   NON_TER         465
FT                   /evidence="ECO:0000313|EMBL:AER98589.1"
SQ   SEQUENCE   465 AA;  49782 MW;  029E7C53905C1138 CRC64;
     ASQNSFRIEF DTFGELKVPN DKYYGAQTVR STMNFKIGGA TERMPIPVIK AFGILKRAAA
     EVNQDYGLDS KIAEAIMKAA DEVAEGKLND HFPLVVWQTG SGTQTNMNVN EVISNRAIEM
     LGGELGSKKP VHPNDHVNKS QSSNDTFPTA MHIAAAIEVH NVLLPGLQKL HDALHAKSKE
     FAQIIKIGRT HTQDAVPLTL GQEFSGYVQQ VKYAMARIKA AMPRVYELAA GGTAVGTGLN
     TRIGFAEKVA AKVAALTGLP FVTAPNKFEA LAAHDALVEL SGAMNTSACS LMKIANDIRF
     LGSGPRSGLG ELILPENEPG SSIMPGKVNP TQCEALTMVA AQVMGNHVAV TVGGSNGHFE
     LNVFKPMMIK NVLHSARLLG DAAVSFTENC VVGIQANTER INKLMNESLM LVTALNPHIG
     YDKAAKIAKT AHKNGSTLKA TAIELGFLTA EQFDEWVKPK DMLGP
//
DBGET integrated database retrieval system