ID A0A0V0QER3_PSEPJ Unreviewed; 490 AA.
AC A0A0V0QER3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=PPERSA_00862 {ECO:0000313|EMBL:KRX00635.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX00635.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX00635.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX00635.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX00635.1}.
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DR EMBL; LDAU01000183; KRX00635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QER3; -.
DR EnsemblProtists; KRX00635; KRX00635; PPERSA_00862.
DR InParanoid; A0A0V0QER3; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000054937; 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:UP000054937}.
FT DOMAIN 34..365
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 431..483
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 490 AA; 53720 MW; 0D7B7FFDD3611550 CRC64;
MLSKIAKTVV RQTKNRQVFC FSSQQYRSEY DSFGEIKVPA DKYWGAQTQR SFQNFDICRD
IDKMPKSIVK AFGILKKSIA KINMDNYGLD KKIGDAIIQA ADEVAQGFHN DQFPLVIWQT
GSGTQSNMNA NEVISNRATE ILGGEKGSKL VHPNDHVNRS QSSNDTFPTV TNIAVVVQTN
EVLIPALDHL IEALEQKQNE FKDIIKIGRT HTQDATPLTL GQEFSGYVQI VKNAKERILK
SLPGVQQLAQ GGTAVGTGLN AYIGYAEKVA EQVSLETGYK FETAPNKFEA LQTCDALIEL
SGSLNTLAVG LHKIANDLRF LGSGPRSGLG ELSLPENEPG SSIMPGKVNP TQCESLTMIS
AQVIGHHVAA TIGGMNGHFE LNVYRPLIAK DVLHSIRLLG DGMRSFTNNC VVGIEANTDK
IEQLMNQSLM LVTALNPHIG YDNAAKIAKH AHKNGQTLLE AGEELGLVTK EQYKEWVKPE
EMIGPKPHKK
//
