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
//