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Database: UniProt
Entry: A0A366QM53_9HYPO
LinkDB: A0A366QM53_9HYPO
Original site: A0A366QM53_9HYPO 
ID   A0A366QM53_9HYPO        Unreviewed;       529 AA.
AC   A0A366QM53;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=FIESC28_11223 {ECO:0000313|EMBL:RBR06001.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR06001.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR06001.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR06001.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RBR06001.1}.
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DR   EMBL; QKXC01000366; RBR06001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366QM53; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000253153; 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:InterPro.
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;
FT   DOMAIN          71..404
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          470..522
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   529 AA;  56884 MW;  A996AA26722E014B CRC64;
     MLRTVTGRAA ASGLIKSALP RVSQAAAPTC SLAPQLRLQS KSSVAGLRLS RAIHSTSVRM
     SQTRTESDAF GEIQVPADRY WGAQTERSLE NFRINQPQDR MPPPIVKAFG ILKGAAATVN
     MRYGLDPKIG AAIQQAAQEV ADGKLLDHFP LVVWQTGSGT QSNMNANEVI SNRAIEILGG
     TMGSKKPVHP NDHVNRSASS NDTFPTVMHI AAVLDIESEL LPALRSLRDA IQKKVDEFEA
     KKIIKIGRTH LQDATPLTLA QEFSGYVAQL DFGIKRVESS LPDLRLLAQG GTAVGTGINT
     FQGFAEAIAE EVTKMTGTEF KTAPNKFEAL AAHDAIVQAH GSLNTLAASL TKIAQDIRYL
     GSGPRCGLGE LNLPENEPGS SIMPGKVNPT QCEALTMVCA QVMGNHVATT IGGMNGQFEL
     NVYKPLVIRN LLHSSRLLTD GMRSFEKNLV AGLNANEEKI ASIMKESLML VTCLNPKIGY
     DMASKVAKNA HKKGLTLKES ALELKALTEE EFDTLVKPEL MVGPSPYKG
//
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