(data stored in SCRATCH zone)

SWISSPROT: B2UI27_RALPJ

ID   B2UI27_RALPJ            Unreviewed;       461 AA.
AC   B2UI27;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
DE            Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
DE            EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
DE   AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
GN   Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
GN   OrderedLocusNames=Rpic_4127 {ECO:0000313|EMBL:ACD29228.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29228.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
CC       interconversion of fumarate to L-malate. {ECO:0000256|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;
CC         EC=4.2.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
CC       malate from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic
CC       A site, and the non-catalytic B site that may play a role in the
CC       transfer of substrate or product between the active site and the
CC       solvent. Alternatively, the B site may bind allosteric effectors.
CC       {ECO:0000256|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily. {ECO:0000256|HAMAP-Rule:MF_00743}.
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DR   EMBL; CP001069; ACD29228.1; -; Genomic_DNA.
DR   RefSeq; WP_012430207.1; NC_010678.1.
DR   STRING; 402626.Rpic_4127; -.
DR   EnsemblBacteria; ACD29228; ACD29228; Rpic_4127.
DR   GeneID; 6285530; -.
DR   KEGG; rpi:Rpic_4127; -.
DR   PATRIC; fig|402626.5.peg.374; -.
DR   eggNOG; ENOG4105C9Q; Bacteria.
DR   eggNOG; COG0114; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   KO; K01679; -.
DR   OMA; FELNVYN; -.
DR   OrthoDB; 734949at2; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000002566; Chromosome 2.
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;
DR   PRODOM; B2UI27.
DR   SWISS-2DPAGE; B2UI27.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743,
KW   ECO:0000256|SAAS:SAAS00674282};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN       11    341       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      407    460       FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
FT   REGION       97     99       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      128    131       Substrate binding (B site).
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   REGION      138    140       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      323    325       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   ACT_SITE    187    187       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   ACT_SITE    317    317       {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   BINDING     318    318       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   SITE        330    330       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
SQ   SEQUENCE   461 AA;  49587 MW;  6D8E9A5C28E69557 CRC64;
     MTTRTERDTF GPIEVPADHL WGAQTQRSLQ NFDIAGDRMP RELIDALARI KRASATVNQR
     LGLLSADKAN AIVGAADEVI AGKHPNEFPL VVWQTGSGTQ TNMNMNEVLA NRASELLGGE
     RGEARLVHPN DDVNRSQSSN DVFPTAMHVA AVTAITHHLI PSLRTLRETL AKKAADFNDI
     IKIGRTHLQD ATPLTLGQEF SGYVAQLQHN ETHLNAALPH LCELALGGTA VGTGLNAPAG
     YAEQVAEELA QLTGLPFITS PNKFETMASA DGLVHAHGAL KTLAASLTKI ANDIRWLASG
     PRSGLGEISI PENEPGSSIM PGKVNPTQSE AVTMLCAQVY GNDVAVNVGG ASGNFELNVF
     RPMIAYNFLH SVRLLADGMR SFNDHCAAGI EPNRDRIDEL VQRSLMLVTA LNPHIGYDKS
     AQIAKKAHKE GTSLREAALA LGYVTSEQFD AWVRPENMVG R
//

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