ID A0A066XUP9_COLSU Unreviewed; 470 AA.
AC A0A066XUP9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN ORFNames=CSUB01_03356 {ECO:0000313|EMBL:KDN71424.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71424.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN71424.1}.
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DR EMBL; JMSE01000185; KDN71424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XUP9; -.
DR STRING; 1173701.A0A066XUP9; -.
DR eggNOG; KOG1317; Eukaryota.
DR HOGENOM; CLU_021594_4_1_1; -.
DR OMA; AKWRAQT; -.
DR OrthoDB; 1341425at2759; -.
DR Proteomes; UP000027238; 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:UP000027238}.
FT DOMAIN 12..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..463
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 50773 MW; AC3095638F31D8C9 CRC64;
MAETRTESDA FGEIQVPADK YWGAQTERSL ENFKINQPQD RMPPPIIKAF GILKGAAATV
NMRYGLDEKI GKAIQQAAAE VAEGKLLDHF PLVVWQTGSG TQSNMNANEV ISNRAIEILG
GVKGSKKPVH PNDHVNRSAS SNDTFPTVMH IAAVLEIENE LIPALKSLRD ALQKKVDEFE
AKKIIKIGRT HLQDATPLTL GQEFSGYVAQ LDAGIKRVET SLPDLRLLAQ GGTAVGTGIN
TFQGFAEAIA EEVTKMTGTE FKTAPNKFEA LAAHDAIVQA HGSLNTIAGS LSKIAQDIRY
LGSGPRCGLG ELILPENEPG SSIMPGKVNP TQCEALTMVC AQVMGNHVAT TIGGMNGQFE
LNVYKPLVIR NLLHSVRILS DGMRSFEKNL VVGLQANEEK IASIMKESLM LVTTLNPKIG
YDMASKVAKN AHKKGLTLKE SALELNALSE EDFDKLVRPE LMIGPSAYKP
//
