ID A0A0G9GVS2_LACPN Unreviewed; 460 AA.
AC A0A0G9GVS2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ODO61097.1};
GN ORFNames=ASV54_04355 {ECO:0000313|EMBL:APD00612.1}, AVR83_00440
GN {ECO:0000313|EMBL:AOB21498.1}, C7M40_01168
GN {ECO:0000313|EMBL:QHM49222.1}, Lp19_2477
GN {ECO:0000313|EMBL:KZU94503.1}, LPJSA22_01053
GN {ECO:0000313|EMBL:ODO61097.1}, LpLQ80_04905
GN {ECO:0000313|EMBL:AWI39882.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO61097.1, ECO:0000313|Proteomes:UP000094892};
RN [1] {ECO:0000313|Proteomes:UP000183026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF1298 {ECO:0000313|Proteomes:UP000183026};
RA McLeod A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOB21498.1, ECO:0000313|Proteomes:UP000093296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF {ECO:0000313|EMBL:AOB21498.1,
RC ECO:0000313|Proteomes:UP000093296};
RA Petkau K., Fast D., Duggal A., Foley E.;
RT "Comparative evaluation of the genomes of common bacterial members of the
RT Drosophila intestinal community.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KZU94503.1, ECO:0000313|Proteomes:UP000076882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19.1 {ECO:0000313|EMBL:KZU94503.1,
RC ECO:0000313|Proteomes:UP000076882};
RA Martino M.E.;
RT "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT uncoupling from niche constraints.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ODO61097.1, ECO:0000313|Proteomes:UP000094892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSA22 {ECO:0000313|EMBL:ODO61097.1,
RC ECO:0000313|Proteomes:UP000094892};
RA Choi H.S.;
RT "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT fermented soybean paste.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QHM49222.1, ECO:0000313|Proteomes:UP000465032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM49222.1,
RC ECO:0000313|Proteomes:UP000465032};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AWI39882.1, ECO:0000313|Proteomes:UP000244922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ80 {ECO:0000313|EMBL:AWI39882.1,
RC ECO:0000313|Proteomes:UP000244922};
RA Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA Cai Y., Suzuki C.;
RT "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT for Preparation of Fermented Liquid Feed for Pig.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:APD00612.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF1298 {ECO:0000313|EMBL:APD00612.1};
RA McLeod A., Fagerlund A., Rud I., Axelsson L.;
RT "Genome sequence of Lactobacillus plantarum MF1298, a candidate probiotic
RT associated with unfavorable effect.";
RL Submitted (AUG-2018) 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; CP013753; AOB21498.1; -; Genomic_DNA.
DR EMBL; CP013149; APD00612.1; -; Genomic_DNA.
DR EMBL; CP028977; AWI39882.1; -; Genomic_DNA.
DR EMBL; LUXM01000033; KZU94503.1; -; Genomic_DNA.
DR EMBL; MCOL01000001; ODO61097.1; -; Genomic_DNA.
DR EMBL; CP028241; QHM49222.1; -; Genomic_DNA.
DR RefSeq; WP_003641313.1; NZ_WYDR01000013.1.
DR GeneID; 77217587; -.
DR KEGG; lpb:SH83_04615; -.
DR PATRIC; fig|1590.142.peg.1024; -.
DR OMA; AKWRAQT; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000076882; Unassembled WGS sequence.
DR Proteomes; UP000093296; Chromosome.
DR Proteomes; UP000094892; Unassembled WGS sequence.
DR Proteomes; UP000183026; Chromosome.
DR Proteomes; UP000244922; Chromosome.
DR Proteomes; UP000465032; 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 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 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00743};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 12..338
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 405..457
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 314
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 320..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 327
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 460 AA; 49497 MW; A18DF35948A7D3ED CRC64;
MTEYRVESDT LGEVKIPANA LWGAQTERSR HNFPTGTKMP LEMIRALLQI KRAAAIANKE
VEAMTAEKAD LIVAAIDKLL ALDDEDLRKD FPLVVYQTGS GTQTNMNVNE VVAHMAGKIN
PDIEILPNDD VNHGQSSNDI FPTAMNITAA VAVDKLIAAA EHLLAELKIK QKKYWRVVKI
GRTHLQDATP LTFGQEVSGW ASAIEHDIAY LKQLNPTLGE LAMGGTAVGT GLNAAPHFAE
NIAAAMSKLY GIEFTADSNK FYGLAHHSGL NVVHGAIKTL AADLMKIAND VRFLASGPRA
GYDELNIPAN EPGSSIMPGK VNPTQAEAIT MAAVRVMGND VVVDLASSQG NFEMNVYKTV
LIDAFLESAE LLAGTITGFT DRMIAGLTVN QDRMAELVDS SLMTVTALSP HIGYHDSAMI
AQAAEKAGTT LREAAIKSGK VTAEQFDEWM VPLDMTNIDD
//
