FUMC2_BRADU
ID FUMC2_BRADU Reviewed; 473 AA.
AC P28894;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Fumarate hydratase class II 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE Short=Fumarase C 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE AltName: Full=Aerobic fumarase 2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE AltName: Full=Iron-independent fumarase 2 {ECO:0000255|HAMAP-Rule:MF_00743};
GN Name=fumC2 {ECO:0000255|HAMAP-Rule:MF_00743}; Synonyms=fumC;
GN OrderedLocusNames=blr6519;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=1856685; DOI=10.1099/00221287-137-4-991;
RA Acuna G., Ebeling S., Hennecke H.;
RT "Cloning, sequencing, and mutational analysis of the Bradyrhizobium
RT japonicum fumC-like gene: evidence for the existence of two different
RT fumarases.";
RL J. Gen. Microbiol. 137:991-1000(1991).
RN [2]
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=AAA26211.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC51784.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M79457; AAA26211.1; ALT_INIT; Genomic_DNA.
DR EMBL; M79457; AAA26212.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC51784.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_773159.2; NC_004463.1.
DR AlphaFoldDB; P28894; -.
DR SMR; P28894; -.
DR STRING; 224911.27354798; -.
DR EnsemblBacteria; BAC51784; BAC51784; BAC51784.
DR KEGG; bja:blr6519; -.
DR PATRIC; fig|224911.5.peg.6668; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_5; -.
DR InParanoid; P28894; -.
DR OMA; HDSMGEV; -.
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; 1.10.275.10; -; 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; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00979; fumC_II; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..473
FT /note="Fumarate hydratase class II 2"
FT /id="PRO_0000161259"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 328
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 108..110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 139..142
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 334..336
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 341
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT CONFLICT 91..94
FT /note="IDGS -> STAD (in Ref. 1; AAA26211/AAA26212)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> R (in Ref. 1; AAA26211/AAA26212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 50924 MW; CDB35CFA32062957 CRC64;
MAKSARTKTA RPATRTETDS FGPIEVPSDR YWGAQTERSR QNFRIGTDRM PISLVHALGI
VKLAAAQSNR ELGLLDQRRA SAIIRAAREV IDGSLDDHFP LVVWQTGSGT QTNMNLNEVI
ANRANELLGG ELGAKKPVHP NDHVNMSQSS NDSFPTAMHI AAASRITADL VPALGELLRA
LRKKEKEFAK IVKIGRTHTQ DATPLTLGQE FSGYAAQVES GIARLKVAVK ELYPLAQGGT
AVGTGLNAKP RFARLFAKHV AGITKLPFTS AANKFEALAS NDAYVLAHGA ISSVATGLFK
IANDIRLLGS GPRSGLGELI LPENEPGSSI MPGKVNPTQC EAMTMVCCQV FGNHTAITVA
GSQGHFELNV YKPVLAYNML HSIRLMADAA RSFTEHCVSG IRADEKRISE LMQRSLMLVT
ALAPKIGYDN AAKVAKTAHA NGTTLKEEAL RLGFVTADEF DRLVQPEKMT KPG
