ID   FUMC1_BRADU             Reviewed;         478 AA.
AC   Q89XM2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Fumarate hydratase class II 1 {ECO:0000255|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C 1 {ECO:0000255|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase 1 {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase 1 {ECO:0000255|HAMAP-Rule:MF_00743};
GN   Name=fumC1 {ECO:0000255|HAMAP-Rule:MF_00743};
GN   OrderedLocusNames=bll0286;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC45551.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000040; BAC45551.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_766926.2; NC_004463.1.
DR   RefSeq; WP_011083118.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89XM2; -.
DR   SMR; Q89XM2; -.
DR   STRING; 224911.AAV28_40670; -.
DR   EnsemblBacteria; BAC45551; BAC45551; BAC45551.
DR   GeneID; 64020146; -.
DR   KEGG; bja:bll0286; -.
DR   PATRIC; fig|224911.44.peg.8806; -.
DR   eggNOG; COG0114; Bacteria.
DR   HOGENOM; CLU_021594_4_1_5; -.
DR   InParanoid; Q89XM2; -.
DR   OrthoDB; 9802809at2; -.
DR   PhylomeDB; Q89XM2; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..478
FT                   /note="Fumarate hydratase class II 1"
FT                   /id="PRO_0000161260"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         98..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         129..132
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         324..326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   478 AA;  51299 MW;  A33EC007B6A88B44 CRC64;
     MNDLRKETDS LGEVNVPADK LWGAQTQRSL EHFSIGRDLM PREMIQSYAI LKKAAANANY
     AGGRLDGKIH KLIVHTCDEI LAGQHHDMFP LHVWMTGSGT QFNMNVNEVI SNRCCQLAGT
     ALGSKLPVHP NDHVNMSQSS NDSFPSAMYI AAAMNVTQRL VPAVEALHDA IAAKSNQWDD
     IVKIGRTHMQ DATPLTLGQE WSGYAAMLAD GLARIDDALK GVFRLALGGT AVGTGINAAP
     GFAEAVAAEI ARLTGLPFVS APNKFAVQGA HDALVQLSGT LRTLAGSLYK IANDIRLLSC
     GPRAGFAELR IPENEPGSSI MPGKVNPTQA EALTMIAVQV MANDVAVGFG GAGGYLEMNV
     YKPLIIHNIA QSVTILTDGC TNFRTFLVEG TEPNRKKIKE YVERSLMLVT ALAPVIGYDK
     ASRIAHYAMD NDLTLKSAAL KLGFVTEPEF DRIVDPAKMV KPYVAEIKVP LAIGAKTG
//