ID A4JCL8_BURVG Unreviewed; 464 AA.
AC A4JCL8;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=Bcep1808_1010 {ECO:0000313|EMBL:ABO54021.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO54021.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000614; ABO54021.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JCL8; -.
DR KEGG; bvi:Bcep1808_1010; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_4; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000002287; Chromosome 1.
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:ABO54021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 13..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 189
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 319
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 130..133
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 325..327
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 332
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 464 AA; 49798 MW; 715A8CE605DF47EF CRC64;
MNEAVRMERD TFGEIAVPAD RLWGAQTERS LQNFRISTEK QSPELIHALA IVKRAAAAVN
QALGVLADDK ARAIIDAADE IIAGKHPREF PLAVWQTGSG TQTNMNLNEV IANRASELLG
GERGEARKVH PNDDVNRGQS SNDVFPTAMH VAAAYAIVNH LLPALRTLRT TLDAKSKAFA
DIVKIGRTHL QDATPLTLGQ EFSGYVAQLD QGIRHVESAL PHLYELALGG TAVGTGLNAH
PEFAVRVADE IGRLTKLPFV TAPSKFEVMA AADALVFAHG ALKTVAAGLM KIANDVRWLA
SGPRCGLGEL SIPENEPGSS IMPGKVNPTQ SEAVTMLCCQ VFGNDVAVNV GGASGNFELN
VFRPMIAHNV LQSVRLLADG AQSFNDHCAV GIEPNRVRID LLLNESLMLV TALNPHIGYD
KSAQIAKKAH KEGTTLKAAA LALGYLTEAE FDEWVRPEQM IGSR
//
