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Database: UniProt
Entry: R9PDV5_PSEHS
LinkDB: R9PDV5_PSEHS
Original site: R9PDV5_PSEHS 
ID   R9PDV5_PSEHS            Unreviewed;       472 AA.
AC   R9PDV5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=PHSY_007165 {ECO:0000313|EMBL:GAC99563.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC99563.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR   EMBL; DF238831; GAC99563.1; -; Genomic_DNA.
DR   RefSeq; XP_012193150.1; XM_012337760.1.
DR   AlphaFoldDB; R9PDV5; -.
DR   STRING; 1305764.R9PDV5; -.
DR   GeneID; 24112429; -.
DR   eggNOG; KOG1317; Eukaryota.
DR   HOGENOM; CLU_021594_4_1_1; -.
DR   OrthoDB; 1341425at2759; -.
DR   Proteomes; UP000014071; 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:UP000014071}.
FT   DOMAIN          14..345
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          411..463
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   472 AA;  50690 MW;  E1445B99F30E14ED CRC64;
     MSQGKFRSEK DTFGPLQVPA DRYWGAQTQR SLQNFDIGGP QERMPEPLIE AFGVLKKAAA
     TVNKSFGLDP KVADAICQAA DEVIGGKLHG HFPLVVFQTG SGTQTNMNVN EVISNRAIEI
     LGGELGSKKP VHPNDHVNMS QSSNDTFPTA MHVASVTQIT KSLIPALEEL RAALDAKRAE
     FDDIIKIGRT HLQDATPLTL GQEFSGYVKQ VDNGIERVKG VIPRLSQLAQ GGTAVGTGLN
     TYIGFDKKVA AEISNITGLH FETAENKFEA LAAHDAIVEA SGALNTVAVS MMKIANDIRY
     LGSGPRCGLG ELSLPENEPG SSIMPGKVNP TQCEALTMVA AQVMGNNTTI SVAGSYGQFE
     LNVFKPVLIK NLLQSIRLLA DGARSFTKNC VVGIEANRDT INKILNESLM LATILNSHLG
     YDNVAAAAKK AHKEGTKLVE ATVALGFMTE EEFKKIVRPE FMLGPTEYKG KN
//
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