ID H0ZD26_TAEGU Unreviewed; 509 AA.
AC H0ZD26;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00013409};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=FH {ECO:0000313|Ensembl:ENSTGUP00000008487.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008487.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000008487.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000008487.2}
RP IDENTIFICATION.
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; H0ZD26; -.
DR STRING; 59729.ENSTGUP00000008487; -.
DR Ensembl; ENSTGUT00000008578.2; ENSTGUP00000008487.2; ENSTGUG00000008229.2.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; H0ZD26; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
DR TreeFam; TF300441; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000007754; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
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:UP000007754}.
FT DOMAIN 57..388
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 454..506
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 509 AA; 54641 MW; E4D9B2424916D502 CRC64;
MHRSLRACRR LGRSAGLLLS SPPPPLPPAT PGRWIPAPPR AAMSSQEAFR IEYDTFGELK
VPSDKYYGAQ TVRSTMNFKI GGVSERMPVQ VIRAFGILKR AAAEVNQDYG LDPKIAKAIV
QAANEVAEGK LNDHFPLVVW QTGSGTQTNM NVNEVISNRA IEIMGGTLGS KKPVHPNDHV
NKSQSSNDTF PTAMHIAAAQ EVNEVLLPGL KKLQNALEGK SKEFSQIIKI GRTHTQDAVP
LTLGQEFSGY VQQIKYGVAR IESTMPRVYQ LAAGGTAVGT GLNTRIGFAE KVAAKVAELT
GLPFVTAPNK FEALAAHDAL VELSGAMNTV ACSLMKIAND IRFLGSGPRS GLGELILPEN
EPGSSIMPGK VNPTQCEAVT MVAAQVMGNH VAVTVGGSNG HFELNVFKPM MIKNVLNSAR
LLGDVCVSFT DNCVVGIQAN TDRINKLMNE SLMLVTALNP HIGYDKAAKI AKTAHKEGTT
LKEAAIKLGF LTSDQFDQWV KPKDMLGPQ
//
