ID A0A2V1E602_9PLEO Unreviewed; 545 AA.
AC A0A2V1E602;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, entry version 11.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=DM02DRAFT_515600 {ECO:0000313|EMBL:PVI05993.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI05993.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI05993.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI05993.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR EMBL; KZ805311; PVI05993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1E602; -.
DR STRING; 97972.A0A2V1E602; -.
DR Proteomes; UP000244855; 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:UP000244855}.
FT DOMAIN 89..421
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 487..539
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 545 AA; 59047 MW; A28F4AB3A7E319B4 CRC64;
MFRPSIVKVR PAEARALRSW AHARINPSSP SKLAWAASSG GAIRSRSLST LPRPAITGTH
SQIQATYQHR HFSSTSTMAS TRTESDAFGE IQVPGDKYWG AQTERSLENF KINQPQDRMP
PPIVKAFGIL KGAAATVNMK FGLADPKIGK AIQQAAEEVA SLKLIDHFPL VVWQTGSGTQ
SNMNANEVIS NRAIEILGGT MGSKKPVHPN DHVNMSASSN DTFPTVMHIA AVIDFEESLL
PALKGLRDAL KKKADMFEKI IKIGRTHLQD ATPLTLGQEF SGYVQQLDFG IERIQSSLPR
LKMLAQGGTA VGTGINTFKG FAEDIASEVS KMTGHDFITA PNKFEALAAH DAVVEAHGQL
NTLAASLFKI AQDIRFLGSG PRCGLGELKL PENEPGSSIM PGKVNPTQCE SLTMVCTQVF
GNNAATTFAG SQGNFELNVF KPVMIRNLLH SSRILADAMK SFEKNLVEGL EADEKRIASL
LNESLMLVTC LNPVIGYDAA SKTAKNAHKK GITLKESALE LKTISEEDFD KYVRPELMIA
PADKK
//
