ID M4B132_XIPMA Unreviewed; 494 AA.
AC M4B132;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00013409};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000020429.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000020429.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000020429.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; M4B132; -.
DR STRING; 8083.ENSXMAP00000020429; -.
DR Ensembl; ENSXMAT00000020457.2; ENSXMAP00000020429.2; ENSXMAG00000020382.2.
DR eggNOG; KOG1317; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; M4B132; -.
DR OMA; AKWRAQT; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000002852; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 42..373
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 439..491
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 494 AA; 52696 MW; 2FB0D45F2FCAAF1F CRC64;
MQNSPPPPPP ARRPGLRPGS CVALSHLSMA GSEFRIERDT FGELKVPADK YYGAQTVRST
LNFKIGGPSE RMPIQVIKAF GILKRAAAEV NKDYGLDPKL ADAIVKAADE VSAGKLDDHF
PLVVWQTGSG TQTNMNVNEV ISNRAIEILG GKLGSKDPVH PNDHVNKSQS SNDTFPTAMH
IAVATEVHHV LLPGLQTLHD ALAAKAEEFK DIIKIGRTHT QDAVPLSLGQ EFSAYVQQVK
YSIERVKAAM PRVYELAAGG TAVGTGLNTR IGFAEKVAAT VASLTGLPFI TAPNKFEALA
AHDALVELSG ALNTVAVSMM KVANDIRFLG SGPRSGLGEL ILPENEPGSS IMPGKVNPTQ
CEAMTMVAAQ VMGNHVAVTV GGSNGHFELN VFKPMMVKNV LNSARLLGDA SVSFTNNCVV
GIQANTERIN KLMNESLMLV TALNPHIGYD KAATIAKTAH KKGSTLKAVA VELGYLTEEQ
FDQWVKPSEM LGPK
//
