FUMC_XYLFT
ID FUMC_XYLFT Reviewed; 473 AA.
AC Q87DC2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=PD_0763;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO28632.1; -; Genomic_DNA.
DR AlphaFoldDB; Q87DC2; -.
DR SMR; Q87DC2; -.
DR PRIDE; Q87DC2; -.
DR EnsemblBacteria; AAO28632; AAO28632; PD_0763.
DR KEGG; xft:PD_0763; -.
DR HOGENOM; CLU_021594_4_1_6; -.
DR OMA; RIATIWN; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000002516; 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 PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Tricarboxylic acid cycle.
FT CHAIN 1..473
FT /note="Fumarate hydratase class II"
FT /id="PRO_0000161330"
FT ACT_SITE 189
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT ACT_SITE 319
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 105..107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 130..133
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT BINDING 325..327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
FT SITE 332
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743"
SQ SEQUENCE 473 AA; 50411 MW; 2524DE56009C298D CRC64;
MEMQMSNSDR YRIEHDSMGD LRVPIDALWG AQTQRAIENF PISGRSMPQG FIHALGFIKA
AAAKVNAELG LLPKSMAKEI EAAALDVAAG RYDAEFPVDI YQTGSGTSSN MNANEVIATL
AMRATKGPIH PNDHVNLGQS SNDVVPTAIR ISATLAVQGR LLPALKHLRK MINKRARGLG
SVVKTGRTHL MDAMPLTFAQ EFGAWSAQIV SAEARLNDTL KRLHRLPLGG TAIGTGINTD
PHFGRNAVKV LSALTGIHFE SANNKFEGLA AQDDLVELSG QFNTLAVALM KIANDLRWMN
AGPLAGLGEI ELPALQPGSS IMPGKVNPVI PEAVVMVASQ VIGHHTAVTV AGQSGNFQLN
VTLPLIAYNL LESATLLGNV VMLLADKVIV GLKVRQDRVQ EVLERNPILV TALNPIIGYE
KAAVIAKRAY KEHRPVLEVA CEESNLNPVE LARLLDPAAL TEGGIHVVGG GGG
