ID I2GWK1_TETBL Unreviewed; 500 AA.
AC I2GWK1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=TBLA0A07130 {ECO:0000313|EMBL:CCH58503.1};
GN ORFNames=TBLA_0A07130 {ECO:0000313|EMBL:CCH58503.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58503.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH58503.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR EMBL; HE806316; CCH58503.1; -; Genomic_DNA.
DR RefSeq; XP_004178022.1; XM_004177974.1.
DR AlphaFoldDB; I2GWK1; -.
DR STRING; 1071380.I2GWK1; -.
DR GeneID; 14493618; -.
DR KEGG; tbl:TBLA_0A07130; -.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR InParanoid; I2GWK1; -.
DR OMA; PADRYFG; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
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:UP000002866}.
FT DOMAIN 48..379
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 445..497
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 500 AA; 54570 MW; F0167D4F5158642A CRC64;
MLKSAATLRQ PVVSLNIFRN CQRSFSITPV SHSIADLQGT RTETDSFGEI QVPANKYWGA
QTQRSFMNFK IGGERERMPE PIIRAFGQQK KAAAIVNNSL GTLDDTLKDA IVQAAEEVSQ
GLLNEHFPLV VFQTGSGTQS NMNANEVISN RAIELLGGTL GSKQVHPNNH VNQSQSSNDT
FPTVMHIAAL TEITNTLLPN LIVLRETLDS KAKEFEKIIK IGRTHLQDAT PLTLGQEFSG
YTQQLTNAIK RIEKNLPELQ YIAQGGTAVG TGLNTKIGFA EQFARQLSNQ TNLSFLTSPN
KFESLAAHDA IVNVHASLNT LACSLFKISQ DIRYLASGPR CGYGELSIPE NEPGSSIMPG
KVNPTQNEAM CQACVQVMGN NSTISFAGAS GQFELNTYKP LMIANLLSST RLLSDAIFSF
NLHCATGIQA NKDKIDRLLH ESLMLVTSLN PKIGYDAASK VAKNAHHKGI TLKQSALELD
ILSSKQFDEW VRPENMLGPN
//
