ID A0A0A2WAF8_BEABA Unreviewed; 532 AA.
AC A0A0A2WAF8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=BBAD15_g4693 {ECO:0000313|EMBL:KGQ09969.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ09969.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ09969.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ09969.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ09969.1}.
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DR EMBL; ANFO01000381; KGQ09969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2WAF8; -.
DR STRING; 1245745.A0A0A2WAF8; -.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:EnsemblFungi.
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:UP000030106}.
FT DOMAIN 74..407
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 473..525
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 532 AA; 57165 MW; 08B7ED39C1B1A661 CRC64;
MLRATSRRLA ATGLASSRSY SRLAAAATAP TCRPAAIVPP QLASNHSLSS LQQRGFRTTT
LRMASTRSES DAFGEIQVPS DKYWGAQTER SLENFRINQP HDRMPPPIIK AFGILKGAAA
TVNMRYGLDP KIGQAIQQAA KEVADGKLMD HFPLVVWQTG SGTQSNMNAN EVISNRAIEI
LGGKMGSKSP VHPNDHVNRS ASSNDTFPTV MHIAAVLDLE GELLPALRSL RAALQAKVDA
FDTRGIIKIG RTHLQDATPL TLAQEFSGYV AQLDFGIKRV EASLTDLRLL AQGGTAVGTG
INTFKGFAEA IAEEVSNMTG TEFKTAPNKF EALAAHDAIV QAHGSLNTLA TSLTKIAQDI
RYLGSGPRCG LGELILPENE PGSSIMPGKV NPTQCEALTM VCAQVMGNNV ATTIGGMNGQ
FELNVYKPLI IRNLLHSSRI LADGMRSFEK NLVAGLQANE AKIASIMKES LMLVTCLNPK
IGYDMASKVA KNAHKKGLTL KESAMELQAL TSEEFDTLVK PELMVVPSEY KQ
//