FUMC_BACSU
ID FUMC_BACSU Reviewed; 462 AA.
AC P07343; O32194;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
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}; Synonyms=citG;
GN OrderedLocusNames=BSU33040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=3923430; DOI=10.1093/nar/13.1.131;
RA Miles J.S., Guest J.R.;
RT "Complete nucleotide sequence of the fumarase gene (citG) of Bacillus
RT subtilis 168.";
RL Nucleic Acids Res. 13:131-140(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=168;
RX PubMed=2998952; DOI=10.1016/0378-1119(85)90207-0;
RA Feavers I.M., Miles J.S., Moir A.;
RT "The nucleotide sequence of a spore germination gene (gerA) of Bacillus
RT subtilis 168.";
RL Gene 38:95-102(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=168;
RX PubMed=2509423; DOI=10.1128/jb.171.11.5933-5939.1989;
RA Price V.A., Feavers I.M., Moir A.;
RT "Role of sigma H in expression of the fumarase gene (citG) in vegetative
RT cells of Bacillus subtilis 168.";
RL J. Bacteriol. 171:5933-5939(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-462.
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
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}.
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DR EMBL; X01701; CAA25849.1; -; Genomic_DNA.
DR EMBL; AJ223978; CAA11749.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15294.1; -; Genomic_DNA.
DR EMBL; M11918; AAA22464.1; -; Genomic_DNA.
DR EMBL; Z93941; CAB07973.1; -; Genomic_DNA.
DR PIR; A23033; UFBSC8.
DR RefSeq; NP_391184.1; NC_000964.3.
DR RefSeq; WP_003228523.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P07343; -.
DR SMR; P07343; -.
DR IntAct; P07343; 2.
DR MINT; P07343; -.
DR STRING; 224308.BSU33040; -.
DR jPOST; P07343; -.
DR PaxDb; P07343; -.
DR PRIDE; P07343; -.
DR EnsemblBacteria; CAB15294; CAB15294; BSU_33040.
DR GeneID; 938591; -.
DR KEGG; bsu:BSU33040; -.
DR PATRIC; fig|224308.179.peg.3581; -.
DR eggNOG; COG0114; Bacteria.
DR InParanoid; P07343; -.
DR OMA; HDSMGEV; -.
DR PhylomeDB; P07343; -.
DR BioCyc; BSUB:BSU33040-MON; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000001570; 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..462
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161255"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 97..99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 127..130
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 329
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT CONFLICT 66
FT /note="A -> V (in Ref. 1; CAA25849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50532 MW; 8D797D18FEA82C06 CRC64;
MEYRIERDTM GEVKVPADKF WGAQTQRSKE NFKIGSEKMP MRVVKAFAIL KRSTALANKR
LGNLDAEKAE AIAAVCDDVL KGKYDDNFPL VVWQTGSGTQ SNMNMNEVVA NRATALLKEK
NSDQTIHPND DVNRSQSSND TFPTAMHVAA VLAVYEQLVP ALDQLRNTLD EKAKAYNDIV
KIGRTHLQDA TPLTLGQEIS GWVHMLDRSK EMILEATDKM RALAIGGTAV GTGINAHPEF
GELVSEEITK LTGQTFSSSP NKFHALTSHD EITYAHGALK ALAADLMKIA NDVRWLASGP
RCGIGEIVIP ENEPGSSIMP GKVNPTQSEA LTMIAAQIMG NDATIGFAAS QGNFELNVFK
PVIIYNFLQS VQLLSDGMNS FHDKCAVGIE PNKETIQENL SNSLMLVTAL NPHIGYENAA
KIAKLAHKEG LTLKEAALKL ELLTEEQFNE MVKPEDMVKP KA
