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Database: UniProt
Entry: G0VE52_NAUCC
LinkDB: G0VE52_NAUCC
Original site: G0VE52_NAUCC 
ID   G0VE52_NAUCC            Unreviewed;       493 AA.
AC   G0VE52;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   Name=NCAS0D02620 {ECO:0000313|EMBL:CCC69843.1};
GN   OrderedLocusNames=NCAS_0D02620 {ECO:0000313|EMBL:CCC69843.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69843.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC69843.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) 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; HE576755; CCC69843.1; -; Genomic_DNA.
DR   RefSeq; XP_003676204.1; XM_003676156.1.
DR   AlphaFoldDB; G0VE52; -.
DR   STRING; 1064592.G0VE52; -.
DR   GeneID; 11530109; -.
DR   KEGG; ncs:NCAS_0D02620; -.
DR   eggNOG; KOG1317; Eukaryota.
DR   HOGENOM; CLU_021594_4_1_1; -.
DR   InParanoid; G0VE52; -.
DR   OMA; AKWRAQT; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000001640; Chromosome 4.
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:UP000001640}.
FT   DOMAIN          40..371
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          437..489
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   493 AA;  53814 MW;  C2EB7D27A53784A3 CRC64;
     MLKLKLANPT ILRLQASRMS LSTTTAASQQ QYRIETDSFG EIKVPADKYW GAQTQRSFQN
     FKIGGSRERI PDPIITAFGI LKKSAAIVNE SLGTLDPKVA DPIKKAADEV VQGKLKDHFP
     LVVFQTGSGT QTNMNVNEVI SNRAIELVGG KLGSKQIHPN NHCNQSQSSN DTFPSVMHIA
     AVLEITNSLI PELTKLKDAL DVKAKEFADI VKIGRTHLQD ATPLTLGQEF SGYVQQLENG
     IYRIESSLYH LKFLAQGGTA VGTGLNTKIG FDKLIAEEVS KETGIEFKTA PNKFEALAAH
     DAIVFASGAL NTVAGSLFKI AQDIRYLGSG PRCGYGELQL PENEPGSSIM PGKVNPTQNE
     AMTQVCVQIM GNNQTISIAG SQGQFELNVY KPLMIANLLN SIRLMTDACK SFRIHCIDDL
     KANKDKINEN LNKSLMLVTA LNPKIGYDAA SKIAKNAHLK NITLKESALE LKYLTAEEFD
     EWVVPENMIG PKP
//
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