ID A0A2N3NI23_9PEZI Unreviewed; 524 AA.
AC A0A2N3NI23;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=jhhlp_001407 {ECO:0000313|EMBL:PKS12109.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS12109.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS12109.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS12109.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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:PKS12109.1}.
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DR EMBL; NLAX01000004; PKS12109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3NI23; -.
DR STRING; 41688.A0A2N3NI23; -.
DR VEuPathDB; FungiDB:jhhlp_001407; -.
DR InParanoid; A0A2N3NI23; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000233524; 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:UP000233524}.
FT DOMAIN 66..399
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 465..517
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 524 AA; 56682 MW; 4E24336B37B7BA15 CRC64;
MRPSVRLPQV LAAAARGNAL ALRCNSLTAP ARLSARLPTT YKLTRRSLHQ TTLKMAATRT
ESDAFGEIQV PSDKYWGAQT ERSLENFRIN QPQDRMPFPI VKAFGILKGA AATVNMRYGL
DPKIGKAIQQ AAAEVAEGKL TDHFPLVVWQ TGSGTQSNMN ANEVISNRAI EILGGEMGSK
KPVHPNDHVN RSASSNDTFP TVMHIAGVLE IEGDLLPALR SLRDALQKKV DTFEAKNIIK
IGRTHLQDAT PLTLAQEFSG YVAQLDSSIK RVESSLPDLR LLAQGGTAVG TGINTFEGFA
EAIAEEVTKM TGTEFKTAPN KFEALAAHDA VVQAHGSLNT LAAVLTKIAQ DIRYLGSGPR
CGLGELILPE NEPGSSIMPG KVNPTQCEAL TMVCAQVMGN HVATTIGGMN GQFELNVYKP
LIIRNLLHSI RILADGMRSF EKNLVDGLQA NEEKIASIMK ESLMLVTCLN PKIGYDMASK
VAKNAHKKGL TLKQSALELN ALTEEEFDTL VKPELMVGPK PYKA
//