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Database: UniProt
Entry: A0A0A8L308_9SACH
LinkDB: A0A0A8L308_9SACH
Original site: A0A0A8L308_9SACH 
ID   A0A0A8L308_9SACH        Unreviewed;       490 AA.
AC   A0A0A8L308;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=KLDO_g1735 {ECO:0000313|EMBL:CDO93438.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93438.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO93438.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) 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:CDO93438.1}.
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DR   EMBL; CCBQ010000025; CDO93438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L308; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000031516; 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;
FT   DOMAIN          37..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   490 AA;  52908 MW;  2E388579BAE2CE59 CRC64;
     MLRSSFVSRG LRTNKGLAAG YQSLRMVSHR VETDAFGEIE VPSDKYWGAQ TQRSLQNFKI
     GGPREKMPEP IVRAFGVLKK SAAVVNEGLG TLDPEVAKPI KQAADEVAQG KLLDHFPLVV
     FQTGSGTQSN MNANEVISNR AIELIGGELG SKKIHPNNHC NQAQSSNDTF PSVMHIAAVT
     EITRHLLPEL VALKDALKSK SDEFQDIVKI GRTHLQDATP LTLGQEFSGY VQQVENGIVR
     VEQSMHHLKF LAQGGTAVGT GLNTKVGFAE KIAEQVSKET GIEFKTAPNK FEALAAHDAV
     VEASGALNTL AVSLFKIAND IRYLGSGPRC GYGELSLPEN EPGSSIMPGK VNPTQNEALT
     QVCVQVMGNH AAITFAGASG QFELNVFKPV MISNLLSSIR LLGDASNSFR IHCVEGIQAN
     KDRIAKLLHE SLMLVTALNP KIGYDAASKV AKNAHKKGIT LKESALQLNV LSSEEFDEWV
     IPENMIGPKD
//
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