ID A0A158HT32_9BURK Unreviewed; 468 AA.
AC A0A158HT32;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=AWB66_02613 {ECO:0000313|EMBL:SAL47081.1};
OS Caballeronia telluris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL47081.1, ECO:0000313|Proteomes:UP000054717};
RN [1] {ECO:0000313|EMBL:SAL47081.1, ECO:0000313|Proteomes:UP000054717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL47081.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; FCNZ02000008; SAL47081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158HT32; -.
DR STRING; 326475.AWB66_02613; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000054717; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054717};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 17..347
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..465
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 193
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 323
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 103..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 134..137
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 329..331
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 336
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 468 AA; 50379 MW; CEAEA926C970F1AD CRC64;
MTEQAKGDVR LEKDTFGEIA VPNHKLWGAQ TQRSLQNFKI SSEKQSPELI TALAIVKRAA
AEVNLELKVL DEKKARAIIQ AADEIIDGKH PDEFPLAVWQ TGSGTQTNMN LNEVIANRAS
ELMGGQRGEE RLVHPNDDVN RGQSSNDVFP TAMHVAAAYA IVKHLVPSLK VLRETLDEKA
KAFDHIVKIG RTHLQDATPL TLGQEFSGYV AQLDQGVRHV EATLPHLYQL AQGGTAVGTG
LNAHPAFAAK VAQAIGKLTG LPFETAPNKF EVMAAADALV AAHGALKTVA ASLMKIANDI
RWLASGPRCG LGELSIPENE PGSSIMPGKV NPTQSEAVTM LCCQVFGNDV AVNFGGASGN
FELNVFRPMI AHNMLQSVRL LADGAQSFND NCAVGIEPNE KRIESLLNES LMLVTALNPH
IGYDKAAQIA KKAHKEGTTL KASALALGYV TEAQFDEWVK PEEMVGKR
//
