ID   FUMC_LEPIC              Reviewed;         464 AA.
AC   Q72VY3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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};
GN   OrderedLocusNames=LIC_10162;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS68791.1; -; Genomic_DNA.
DR   RefSeq; WP_000857390.1; NC_005823.1.
DR   AlphaFoldDB; Q72VY3; -.
DR   SMR; Q72VY3; -.
DR   GeneID; 61143516; -.
DR   KEGG; lic:LIC_10162; -.
DR   HOGENOM; CLU_021594_4_1_12; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000007037; Chromosome I.
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; PR00145; ARGSUCLYASE.
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; Tricarboxylic acid cycle.
FT   CHAIN           1..464
FT                   /note="Fumarate hydratase class II"
FT                   /id="PRO_0000161282"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   ACT_SITE        317
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         128..131
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         138..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         323..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   SITE            330
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   464 AA;  50397 MW;  AE316E36BAB02FA8 CRC64;
     MKTRIETDSM GEIAVDDSKY WGAQTERSLH HFHIGNDRFP REMIRALGIL KKSAAVVNAE
     LGLLSEDKKK LIVQAADEVI SGKLDEHFPL SVWQTGSGTQ TNMNSNEVIS NRAIEIAGGV
     KGSKKPIHPN DDVNKAQSSN DTFPTAMHIA AAEQLNQKLI PALIQLKETF KKKTDEFQNI
     IKIGRTHLQD ATPLTLGQEF SGYVQQLEYN IARVKAVLPS VYRLALGGTA VGTGLNTHPQ
     FAVKAAAQIA KETGLPFVSA ENKFEALAAH DSLVETSGVL KTIAASLMKI ANDIRWLSSG
     PRCGIGEISI PENEPGSSIM PGKVNPTQSE QMTMVAAQVI ANDVAVNIGG ASGNFELNVF
     KPLIIHNVLN SIRLLSDSCV SFEEHCARGI IPNKEKLNEH LNNSLMLVTA LNPHIGYDNA
     AKIAKNAHKK GTTLKESGIE LGLLTSEQFD QWVLPEKMIH PSVD
//