ID A0A0L1IM95_ASPNO Unreviewed; 549 AA.
AC A0A0L1IM95;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=ANOM_010430 {ECO:0000313|EMBL:KNG80736.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG80736.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG80736.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG80736.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-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:KNG80736.1}.
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DR EMBL; JNOM01000549; KNG80736.1; -; Genomic_DNA.
DR RefSeq; XP_015401659.1; XM_015555686.1.
DR AlphaFoldDB; A0A0L1IM95; -.
DR STRING; 1509407.A0A0L1IM95; -.
DR GeneID; 26812234; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000037505; 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:UP000037505}.
FT DOMAIN 94..425
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 491..543
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 549 AA; 59045 MW; 4D6B4991C67B5237 CRC64;
MLTPSNSRSA VRSMASLAHA ASRASASSPA VARSALACAA RSPASLGCRR ALSTNSRQLQ
FPRLQSLNTI SSKRAFGTTA RMASETRVET DAFGEIEVPA DKYWGAQTQR SLGNFDINQP
QDRMPEGVVK AFGILKGAAA TVNMKFGLDP KVGEAIQKAA AEVAEGKLLD HFPLVVWQTG
SGTQSNMNSN EVISNRAIEI LGGKMGSKKP VHPNDHVNMS ASSNDSFPTA MHIAAVLELE
GTLLPSLKSL RDALQVKVEN FEKIIKIGRT HLQDATPLTL GQEFSGYVAQ LDRNIERVQN
SLPHLRYLAQ GGTAVGTGLN TFKGFDEAIA AEVTKMTGTE FKTAPNKFEV LAAHDAIVEA
SGSLNTLACS LFKIAQDIRY LGSGPRCGLG ELILPENEPG SSIMPGKVNP TQCESLTMIC
SQVMGNHVAA TVGGMNGQFE LNVFKPVMIR NLLHSSRILS DGMKSFEKNL VHGLEANEPR
INSLLHESLM LVTCLNPVIG YDMASKVAKN AHKKGLTLKQ SAMELQALSE EDFDTHVRPE
LMLAPKEKK
//
