ID A0A3M6VVI1_9STRA Unreviewed; 489 AA.
AC A0A3M6VVI1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=DD237_002783 {ECO:0000313|EMBL:RQM09943.1}, DD238_001200
GN {ECO:0000313|EMBL:RMX69866.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX69866.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|Proteomes:UP000282087, ECO:0000313|Proteomes:UP000286097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R13 {ECO:0000313|EMBL:RQM09943.1,
RC ECO:0000313|Proteomes:UP000286097}, and R14
RC {ECO:0000313|EMBL:RMX69866.1, ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
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:RMX69866.1}.
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DR EMBL; QLLG01000011; RMX69866.1; -; Genomic_DNA.
DR EMBL; QKXF01000662; RQM09943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6VVI1; -.
DR STRING; 542832.A0A3M6VVI1; -.
DR VEuPathDB; FungiDB:DD237_002783; -.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR Proteomes; UP000286097; 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; PR00145; ARGSUCLYASE.
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:UP000282087}.
FT DOMAIN 36..368
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 434..486
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 489 AA; 52273 MW; 5A3C48904674B4B3 CRC64;
MLSAAVGKAA ATSSRLTVVK VVRAASTFRV ETDSIGEVKV DDSKYWGAQT QRSLENFPIG
GARERMPIPV IKAFGVVKKC AAKYNLEKGK LEATVAEKII AAADDVIAGK LDDHFPLVVF
QTGSGTQSNM NTNEVISNRA IELAGGVLGS KTPVHPNDHV NMGQSSNDSF PTAMHIAAVQ
EVHRVLLPGL YKLHDALDVK VKEFDDIIKI GRTHTQDATP LTLGQEFSGY REQIAVSIER
VERVLPNLCK LALGGTAVGT GLNTSKGYDA EIAKIIAEET KLPFITAPNK FEALAAHDAV
VEASGVMNTI ACSLMKIAND IRFLGSGPRS GLGELTLPAN EPGSSIMPGK VNPTQCEAIT
MVCAQVMGNH VAVTVGGSNG HFELNVFKPV MISNLLSSIR LIGDSCNAFT DNCVVGIEAN
REKIDQLMKN SLMLVTALNP HIGYDKASKV AKKAHQDGAT LRETVIALGY LTGEEFDRFV
RPEEMVGPK
//
