ID D3F2X3_CONWI Unreviewed; 440 AA.
AC D3F2X3;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Cwoe_5854 {ECO:0000313|EMBL:ADB54254.1};
OS Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS 100937 / ID131577).
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Conexibacteraceae; Conexibacter.
OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB54254.1, ECO:0000313|Proteomes:UP000008229};
RN [1] {ECO:0000313|EMBL:ADB54254.1, ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RX PubMed=21304704;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA Hugenholtz P.;
RT "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL Stand. Genomic Sci. 2:212-219(2010).
RN [2] {ECO:0000313|Proteomes:UP000008229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC {ECO:0000313|Proteomes:UP000008229};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Conexibacter woesei DSM 14684.";
RL Submitted (JAN-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00743}.
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DR EMBL; CP001854; ADB54254.1; -; Genomic_DNA.
DR RefSeq; WP_012937305.1; NC_013739.1.
DR AlphaFoldDB; D3F2X3; -.
DR STRING; 469383.Cwoe_5854; -.
DR KEGG; cwo:Cwoe_5854; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_11; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000008229; Chromosome.
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 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 PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR11444:SF22; FUMARATE HYDRATASE CLASS II; 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:ADB54254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 5..318
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 385..433
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 164
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 294
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 115..117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 307
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 440 AA; 46001 MW; 705571E6E86935F2 CRC64;
MGVQEQEQLW GGETTKAVAN FPVSGERVPV PVVRWLGRIK GAAARVNGEL GLLDGEIAER
IAAAGDEIAA GKHDGQFPVD VFQTGSGTSS NMNANEVIAT LSGAHQNDHV NMGQSSNDVF
PSAVHLAALD EATNDLLPAL ERLEAAFAAK AAAFEDIVKS GRTHLMDAVP VTLGQEFSGY
AAQIRLGAKR VRNALPQVAQ IPLGGTATGT GLNTHPEFAA RVRGKLAESS GLEILPPEDP
FEAQGNRDAL VELSGALKVI AVSLTKIAND LALMGSGPRA GIGELFLPEL QKGSSIMPGK
VNPVIPEVVL QVSAQVIGND TAITVGGLQG QFELNVRIPL IARNLLQSIS LLANTSRLFA
EKCVEGITAN EAGCERSAES TLAVATALNP FIGYDKASEI VKEAASSGRT LREVALEKGV
SEETYNEAID LRRIARGSAA
//
