ID W6PTW9_PENRF Unreviewed; 535 AA.
AC W6PTW9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=FUM1 {ECO:0000313|EMBL:CDM27295.1};
GN ORFNames=PROQFM164_S01g001104 {ECO:0000313|EMBL:CDM27295.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM27295.1};
RN [1] {ECO:0000313|EMBL:CDM27295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM27295.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084}.
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DR EMBL; HG792015; CDM27295.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PTW9; -.
DR STRING; 1365484.W6PTW9; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
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;
FT DOMAIN 81..412
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 478..530
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 535 AA; 57985 MW; 1E7575536723F19F CRC64;
MNSTSSRAAV RSMATLTHAA RATPAARSVL SPFATRSLSS NTRQFVQFPR LQSLNTFSNK
RSFGTTVRMS VDPRTESDAF GEIQVPGDKY WGAQTQRSLK NFDINQPQDR MPAPLIKAFG
ILKGAAAEVN MKYGLDPKIG EAIKQAAAEV AEGKLLDHFP LVVWQTGSGT QSNMNSNEVI
SNRAIEILGG TMGSKKPVHP NDHVNMSASS NDSFPTVMHI AAVVELEQSL LPALKELRDA
LQVKVDKFQH IIKIGRTHLQ DATPLTLGQE FSGYVAQLDR NIERVQSSLP HLRLLAQGGT
AVGTGLNTFK GFDEAVAAEI TKLTGTEFKT APNKFEVLAA HDSIIEASGS LNTLAASLFK
IAQDVRYLGS GPRCGLGELS LPENEPGSSI MPGKVNPTQC ESLTMICAQV MGNHVAATIG
GMNGQFELNV FKPLMIANLL HSVRILSDGM HSFRIHLVEG LEANEGRINS LLHESLMLVT
CLNPVIGYDM ASKVAKNAHK KNLTLKESAM ELKALSSEEF DKHVRPELML APKEL
//
