FUMC_RHIME
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 03-AUG-2022, entry version 117.
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; Proteobacteria; 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};
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; 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 STRING; 266834.SMc00149; -.
DR EnsemblBacteria; CAC46438; CAC46438; SMc00149.
DR KEGG; sme:SMc00149; -.
DR PATRIC; fig|266834.11.peg.3302; -.
DR eggNOG; COG0114; Bacteria.
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; 1.10.275.10; -; 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 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
