FUMC_CHLPN
ID FUMC_CHLPN Reviewed; 460 AA.
AC Q9Z6P6;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=CPn_1013, CP_0840, CpB1051;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD19150.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38632.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99220.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98980.1; -; Genomic_DNA.
DR PIR; A72009; A72009.
DR PIR; B86617; B86617.
DR RefSeq; NP_225207.1; NC_000922.1.
DR RefSeq; WP_010883646.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6P6; -.
DR SMR; Q9Z6P6; -.
DR STRING; 115711.CP_0840; -.
DR EnsemblBacteria; AAD19150; AAD19150; CPn_1013.
DR EnsemblBacteria; AAF38632; AAF38632; CP_0840.
DR GeneID; 45051070; -.
DR KEGG; cpa:CP_0840; -.
DR KEGG; cpj:fumC; -.
DR KEGG; cpn:CPn_1013; -.
DR KEGG; cpt:CpB1051; -.
DR PATRIC; fig|115713.3.peg.1110; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_0; -.
DR OrthoDB; 734949at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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 3: Inferred from homology;
KW Cytoplasm; Lyase; Tricarboxylic acid cycle.
FT CHAIN 1..460
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161268"
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 460 AA; 50441 MW; A59DA2D41F2100F1 CRC64;
MRQEKDSLGI VEVPEDKLYG AQTMRSRNFF SWGPELMPYE VIRALVWIKK CAAQANQDLG
FLDSKHCDMI VAAADEILEG GFEEHFPLKV WQTGSGTQSN MNVNEVIANL AIRHHGGVLG
SKDPIHPNDH VNKSQSSNDV FPTAMHIAAV ISLKNKLIPA LDHMIRVLDA KVEEFRHDVK
IGRTHLMDAV PMTLGQEFSG YSSQLRHCLE SIAFSLAHLY ELAIGATAVG TGLNVPEGFV
EKIIHYLRKE TDEPFIPASN YFSALSCHDA LVDAHGSLAT LACALTKIAT DLSFLGSGPR
CGLGELFFPE NEPGSSIMPG KVNPTQCEAL QMVCAQVLGN NQTVIIGGSR GNFELNVMKP
VIIYNFLQSV DLLSEGMRAF SEFFVKGLKV NKARLQDNIN NSLMLVTALA PVLGYDKCSK
AALKAFHESI SLKEACLALG YLSEKEFDRL VVPENMVGNH
