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Database: UniProt
Entry: A0A0D2DWJ4_9EURO
LinkDB: A0A0D2DWJ4_9EURO
Original site: A0A0D2DWJ4_9EURO 
ID   A0A0D2DWJ4_9EURO        Unreviewed;       540 AA.
AC   A0A0D2DWJ4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=PV06_00143 {ECO:0000313|EMBL:KIW47448.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47448.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW47448.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47448.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR   EMBL; KN847332; KIW47448.1; -; Genomic_DNA.
DR   RefSeq; XP_016267664.1; XM_016400611.1.
DR   AlphaFoldDB; A0A0D2DWJ4; -.
DR   STRING; 215243.A0A0D2DWJ4; -.
DR   GeneID; 27352217; -.
DR   VEuPathDB; FungiDB:PV06_00143; -.
DR   HOGENOM; CLU_021594_4_1_1; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000053342; 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:UP000053342}.
FT   DOMAIN          85..416
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          482..534
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  58305 MW;  52845FF382A0D077 CRC64;
     MMLGRLSSSV KTPTSAKSSL SHASKAVRSS QSLRIPAQRL SCSYPSQASR RPSPATFSTS
     PSSYRTFSTT RNMAASTRTE TDAFGPIEVP SDKYWGAQTQ RSLGNFKINQ PQDRMPEGVV
     RAFGILKGAA ATVNMRYGLD PKVGEAIQQA AAEVAALKLI DHFPLVVWQT GSGTQSNMNA
     NEVISNRAIE ILGGQMGSKK PVHPNDHVNM SASSNDSFPT VMHIAAVLDF EQRLIPALTN
     LRDALQKKVE AFDKIIKIGR THLQDATPLT LGQEFSGYVA QLDRNLERIQ ASLPHLRQLA
     QGGTAVGTGL NTFKGFAEGI AEEVTKMTGT EFITAPNKFE VLAAHDSIVE ASGTLNTLAV
     SLFKIANDIR YLGSGPRCGL GELVLPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHTA
     ATVGGLSGQF ELNVFKPLMI RNLLHSSRIL SDAMNGFVEH LVEGLQADEK RIGTLLHESL
     MLVTCLNPVI GYDMASKVAK NAHKKGLTLK ESAMELKALS SEDFDKYVRP ELMLAPKEKK
//
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