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
//