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}.
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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
//