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Database: UniProt
Entry: A0A0F4ZJM4_9PEZI
LinkDB: A0A0F4ZJM4_9PEZI
Original site: A0A0F4ZJM4_9PEZI 
ID   A0A0F4ZJM4_9PEZI        Unreviewed;       531 AA.
AC   A0A0F4ZJM4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=TD95_003490 {ECO:0000313|EMBL:KKA30722.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30722.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA30722.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30722.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) 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:KKA30722.1}.
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DR   EMBL; LAEV01000286; KKA30722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4ZJM4; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000033483; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033483}.
FT   DOMAIN          73..406
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          472..524
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   531 AA;  57038 MW;  19377E6A2B160018 CRC64;
     MFRSVSARAV ASTVSRSSII NATSTTIRNA AAATSTSRFA AVRTVSIPAL RSLHTTSANM
     SAASTRTESD AFGEIQVPSD KYWGAQTERS LENFKINQPQ DRMPPAIVKA FGILKGAAAT
     VNMRYGLDPT IGKAIQQAAA EVAEGKLLDH FPLVVWQTGS GTQSNMNANE VISNRAIEIL
     GGVMGSKKPV HPNDHVNRSA SSNDTFPTVM HIAAVLELEN ELLPSLKSLR DALQAKVDDF
     EAKNIIKIGR THLQDATPLT LAQEFSGYVA QLSYGIERVE RSLPELRLLA QGGTAVGTGI
     NTFEGFAEAI AEEVTKMTGT EFKTAPNKFE ALAAHDAVVH AHGALNTLAT SLTKIAQDIR
     YLGSGPRCGL GELSLPENEP GSSIMPGKVN PTQCEALTMV CAQVMGNHVA TTIGGMNGQF
     ELNVYKPLVI RNLLHSSRIL SDAMRSFEKN LVLGLKANED KISNIMKESL MLVTCLNPKI
     GYDMASKVAK NAHKKGLTLK QSALELNALT EEEFDTLVRP ELMVGPKPYK G
//
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