ID S3D4W5_OPHP1 Unreviewed; 533 AA.
AC S3D4W5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=F503_01233 {ECO:0000313|EMBL:EPE08450.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08450.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE08450.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08450.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR EMBL; KE148149; EPE08450.1; -; Genomic_DNA.
DR AlphaFoldDB; S3D4W5; -.
DR STRING; 1262450.S3D4W5; -.
DR VEuPathDB; FungiDB:F503_01233; -.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000016923; 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:UP000016923}.
FT DOMAIN 75..408
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 474..526
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 533 AA; 57060 MW; 6EC1C573199E1CEB CRC64;
MLRSVRIAAP GVARTLLRSV PRTTSACSAT TATTAKSSIV STPSFLSSST RAFHASTIRM
SSDSSNTRTE SDAFGEIQVP ADKYWGAQTE RSLENFRINQ PQDRMPPPIV KAFGILKGAA
ATVNMNFGLD PTVGKAIQQA AKEVADLKLL DHFPLVVWQT GSGTQSNMNA NEVISNRAIE
ILGGKMGSKK PVHPNDHVNR SASSNDTFPT VMHIAAVLEI EGELLPAIRS LRAALQAKVD
DFEAKGIIKI GRTHLQDATP LTLAQEFSGY VAQLDYGIQR VESSLPHLRQ LAQGGTAVGT
GINTFVGFAE AIAAEVSQMT GTHFETAPNK FEALAAHDAL VQASGTLNTL AASLSKIGQD
IRYLGSGPRC GLGELSLPEN EPGSSIMPGK VNPTQCEALT MVCAQVMGNH VAATIGGMNG
QFELNVYKPL IIRNVLHSVR LLTDGMRSFE KNLVVGLQAN EEKISNIMKE SLMLVTCLNP
KIGYDMASKV AKNAHKKGLT LKQSALELDA LTEEEFDTLV RPELMVGPSP YKA
//
