ID A0A0A2XAX1_THEFI Unreviewed; 464 AA.
AC A0A0A2XAX1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
DE Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
DE EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
DE AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
DE AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
GN Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743,
GN ECO:0000313|EMBL:KGQ22334.1};
GN ORFNames=THFILI_09635 {ECO:0000313|EMBL:KGQ22334.1};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ22334.1, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ22334.1, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ22334.1,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC interconversion of fumarate to L-malate. {ECO:0000256|HAMAP-
CC Rule:MF_00743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00743};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A
CC site, and the non-catalytic B site that may play a role in the transfer
CC of substrate or product between the active site and the solvent.
CC Alternatively, the B site may bind allosteric effectors.
CC {ECO:0000256|HAMAP-Rule:MF_00743}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC subfamily. {ECO:0000256|ARBA:ARBA00009084, ECO:0000256|HAMAP-
CC Rule:MF_00743}.
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:KGQ22334.1}.
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DR EMBL; JPSL02000040; KGQ22334.1; -; Genomic_DNA.
DR RefSeq; WP_038062970.1; NZ_JPSL02000040.1.
DR AlphaFoldDB; A0A0A2XAX1; -.
DR STRING; 276.THFILI_09635; -.
DR PATRIC; fig|276.5.peg.836; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000030364; 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-UniRule.
DR GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000313|EMBL:KGQ22334.1};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 11..342
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 408..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 318
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 129..132
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 324..326
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 331
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 464 AA; 50716 MW; AF0E45E2BFB37C86 CRC64;
MEYRIERDTM GEVKVPADKY WGAQTQRSLE NFKIGGERFR MPIQIIRAYG MLKKAAARAN
LELGELPEEI ARAIIQAAEE VVQGKLDDHF PLVVFQTGSG TQTNMNVNEV IANRASELLG
KPLGSKHVHP NDHVNRGQSS NDTFPTAMYV AVALELNRVL YPAVEGLIAT FQEKARAFDS
IVKVGRTHLM DAVPITLGQE IGSWAAQLEY ALSALREMEK GLYRLAIGGT AVGTGLNAHP
RFGELVARYL AEETGLPFRV AENRFAALAA HDELTNVMGA VRTLAAALMK IGNDVRWLAS
GPYAGIGEIF IPANEPGSSI MPGKVNPTQV EALTMVAVRV YGNDLAVSFA DSQGNFQLNV
YKPVMAHAAL EAIDLLADAV NSFNEHLAVG IEPNLERIQE HLEKNPMLAT ALNKAIGYDK
AAEIVKKAIK EKKTLKQAAL ELGYLTEEEF DRIVVPMRLA KPHA
//
