ID   FUMC_CHLTR              Reviewed;         463 AA.
AC   O84863;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-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=CT_855;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68452.1; -; Genomic_DNA.
DR   PIR; H71462; H71462.
DR   RefSeq; NP_220377.1; NC_000117.1.
DR   RefSeq; WP_009872244.1; NC_000117.1.
DR   AlphaFoldDB; O84863; -.
DR   SMR; O84863; -.
DR   STRING; 272561.CT_855; -.
DR   EnsemblBacteria; AAC68452; AAC68452; CT_855.
DR   GeneID; 884656; -.
DR   KEGG; ctr:CT_855; -.
DR   PATRIC; fig|272561.5.peg.944; -.
DR   HOGENOM; CLU_021594_4_1_0; -.
DR   InParanoid; O84863; -.
DR   OrthoDB; 9802809at2; -.
DR   BioCyc; MetaCyc:CT_855-MONOMER; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000000431; 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; 1.10.40.30; 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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..463
FT                   /note="Fumarate hydratase class II"
FT                   /id="PRO_0000161269"
FT   ACT_SITE        185
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         95..97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         126..129
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         136..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   BINDING         321..323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT   SITE            328
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   463 AA;  50339 MW;  428E3DA10A839853 CRC64;
     MRQENDSLGI VLVPEDKLFG AQTGRSQEFF SYGKESMPLE IIHALVKIKK CAAKANGDLG
     CLDAKRRDMI VAATDEILSG EFDEHFPLKV WQTGSGTQSN MNVNEVIANL AIQRHGGELG
     SKHPVHPNDH VNKSQSSNDV FPTAMHIAAV QSIKGSLIPA LEHLKKVIDA KALEFARDIK
     IGRTHLMDAV PMTLGQEFSG YSCQLHNCLE RIGFSLTHLY ELAIGGTAIG TGLNVPEGFV
     EKVIQYLRRE TGEPFVPASN YFAALSNHDA LVQAHGSLTV LACALVKIAT DLSFLGSGPR
     CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSIIFSGTK GNFELNVMKP
     VIIYDFLQSV NLLAGAMRSF ADYFVCGLKV NKGQLQQNVE RSLMLVTALA PVLGYDKCSK
     IALKAFHENL SLKEACVSLG FLSEKEFDEH VIPGLMVGNR GHE
//