ID E6PFF5_9ZZZZ Unreviewed; 477 AA.
AC E6PFF5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=fumarate hydratase {ECO:0000256|ARBA:ARBA00012921};
DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921};
GN Name=fumC {ECO:0000313|EMBL:CBH75191.1};
GN ORFNames=CARN1_1516 {ECO:0000313|EMBL:CBH75191.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH75191.1};
RN [1] {ECO:0000313|EMBL:CBH75191.1}
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:CBH75191.1}.
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DR EMBL; CABL01000006; CBH75191.1; -; Genomic_DNA.
DR AlphaFoldDB; E6PFF5; -.
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; PR00145; ARGSUCLYASE.
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:CBH75191.1}.
FT DOMAIN 22..356
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 423..474
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 477 AA; 51347 MW; D61115D4C27388ED CRC64;
MTITNTASNG ALQSRKETDS MGAIDVPADK YYGAQSARSL IHFEIGEGTW PRDVMPKQVI
VAMAQLKKAA ALVNHDLGKL DAEKTKLIVA AADEVIAGKL DAHFPLRIWQ TGSGTQTNMN
VNEVISNRAI EIAGGEMGSK KPIHPNDHVN MSQSSNDTFP TAMHMAAAEA MVAMLPPVQK
LRDALDAKAK AWKDIVKVGR THLQDATPLT LGQEFSGYVT QLDRAMVACR EALDHLYDLA
IGGTAVGTGL NAHPEFANRA AAKLAELTKL PFRSHPNKFT ALASHDDFVF ASGALKMLGA
ALMKIANDVR WLGSGPRAGI GELVLPENEP GSSIMPGKVN PTQSEAMTMV CVQVFGNDVA
ITMGASQGNF ELNVFNPVMI SNFLHSTTLL RDACTMFREH CIEGLQANEP VIAKYLAESL
MTVTALSPKI GYDKAAEIAK KAHHDGATLK ETALKLGYVT AEEFDTIVVP REMTYPK
//
