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Database: UniProt
Entry: E6QVJ1_9ZZZZ
LinkDB: E6QVJ1_9ZZZZ
Original site: E6QVJ1_9ZZZZ 
ID   E6QVJ1_9ZZZZ            Unreviewed;       221 AA.
AC   E6QVJ1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE            EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN   ORFNames=CARN7_2079 {ECO:0000313|EMBL:CBI11264.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI11264.1};
RN   [1] {ECO:0000313|EMBL:CBI11264.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) 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:CBI11264.1}.
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DR   EMBL; CABR01000130; CBI11264.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6QVJ1; -.
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   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR005677; Fum_hydII.
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   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   Lyase {ECO:0000313|EMBL:CBI11264.1}.
FT   DOMAIN          33..106
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          172..202
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   221 AA;  24076 MW;  F3EF53CCC4CDF522 CRC64;
     MFLHQDPTLL VRLREHSKGY KQSGNAAVTA RAAANGRYGT TFMATRPLAV ALMKIANDVR
     WLSSGPRSGL GEISIPENEP GSSIMPGKVN PTQCEALTML CCQVFGNDVA ITVGGASGNF
     ELNVFKPLIA HNFSHSLRLL ADGMASFEEH CVRGIKANRG RVAELMERSL MLVTALTPHI
     GYDRAAEIAK HAHHDGSTLE DIQKMAVKRV REDERTNINT P
//
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