ID   FUMC_RHIME              Reviewed;         463 AA.
AC   Q92PB6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000255|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743}; OrderedLocusNames=R01859;
GN   ORFNames=SMc00149;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS), AND SUBUNIT.
RG   New York structural genomics research consortium (NYSGRC);
RA   Eswaramoorthy S., Evans B., Foti R., Gizzi A., Hillerich B., Kar A.,
RA   Seidel J.L.R., Villigas G., Zencheck W., Almo S.C., Swaminathan S.;
RT   "Crystal structure of a fumarate hydratase.";
RL   Submitted (JUL-2010) to the PDB data bank.
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       ECO:0000269|Ref.3}.
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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC46438.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL591688; CAC46438.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_385965.3; NC_003047.1.
DR   PDB; 4HGV; X-ray; 2.09 A; A/B/C/D=1-463.
DR   PDBsum; 4HGV; -.
DR   AlphaFoldDB; Q92PB6; -.
DR   SMR; Q92PB6; -.
DR   EnsemblBacteria; CAC46438; CAC46438; SMc00149.
DR   KEGG; sme:SMc00149; -.
DR   PATRIC; fig|266834.11.peg.3302; -.
DR   eggNOG; COG0114; Bacteria.
DR   OrthoDB; 9802809at2; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000001976; 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   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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lyase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..463
FT                   /note="Fumarate hydratase class II"
FT                   /id="PRO_0000161305"
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"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          12..17
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           24..32
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           42..61
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           67..81
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           100..117
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   TURN            122..125
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           140..158
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           160..178
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          190..196
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           197..217
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           264..269
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           272..298
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           328..352
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           362..386
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           388..390
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           395..404
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           407..411
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           413..416
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           418..431
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           435..440
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   TURN            441..443
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           447..453
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   HELIX           456..458
FT                   /evidence="ECO:0007829|PDB:4HGV"
FT   STRAND          459..461
FT                   /evidence="ECO:0007829|PDB:4HGV"
SQ   SEQUENCE   463 AA;  49133 MW;  A500EDE8A6789C5F CRC64;
     MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI VKQAAARANM
     ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT QSNMNANEVV SNRAIELLGG
     VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI ACAERVIHDL LPALKHLHKA LEEKVKAFDH
     IIKIGRTHTQ DATPLTLGQE FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV
     GFAEKVAEEI AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS
     GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA GSQGHFELNV
     YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA ALDRSLMLVT ALAPKIGYDN
     AAKIAKTAHK NGTTLREEAV GGGYVTDEEF DAVVRPETMI GPA
//