(data stored in ACNUC1104 zone)

SWISSPROT: FUMC_STRCO

ID   FUMC_STRCO              Reviewed;         461 AA.
AC   Q9FBN6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 104.
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=SCO5042; ORFNames=SCK7.15c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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;
CC         EC=4.2.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
CC       malate 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
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:0000255|HAMAP-Rule:MF_00743}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}.
DR   EMBL; AL939122; CAC05887.1; -; Genomic_DNA.
DR   RefSeq; NP_629194.1; NC_003888.3.
DR   RefSeq; WP_011030018.1; NC_003888.3.
DR   SMR; Q9FBN6; -.
DR   STRING; 100226.SCO5042; -.
DR   EnsemblBacteria; CAC05887; CAC05887; CAC05887.
DR   GeneID; 1100483; -.
DR   KEGG; sco:SCO5042; -.
DR   PATRIC; fig|100226.15.peg.5121; -.
DR   eggNOG; ENOG4105C9Q; Bacteria.
DR   eggNOG; COG0114; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   InParanoid; Q9FBN6; -.
DR   KO; K01679; -.
DR   OMA; FELNVYN; -.
DR   PhylomeDB; Q9FBN6; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000001973; 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;
DR   PRODOM; Q9FBN6.
DR   SWISS-2DPAGE; Q9FBN6.
KW   Complete proteome; Cytoplasm; Lyase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    461       Fumarate hydratase class II.
FT                                /FTId=PRO_0000161322.
FT   REGION       98    100       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      123    126       Substrate binding (B site).
FT                                {ECO:0000255|HAMAP-Rule:MF_00743}.
FT   REGION      133    135       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      318    320       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   ACT_SITE    182    182       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00743}.
FT   ACT_SITE    312    312       {ECO:0000255|HAMAP-Rule:MF_00743}.
FT   BINDING     120    120       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   BINDING     181    181       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   BINDING     313    313       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00743}.
FT   SITE        325    325       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00743}.
SQ   SEQUENCE   461 AA;  49068 MW;  0853F809C265A62D CRC64;
     MSEYRIEHDS MGEVRVPADA KWRAQTQRAV ENFPVSGQRI ERAHIEALAR IKSAAAKVNA
     ELGVLDEDVA GAIQEAAGEV AEGKWDEHFP VDVFQTGSGT SSNMNTNEVV ATLATERLGR
     DVHPNDHVNA SQSSNDVFPS SIHIAATAAV TRDLIPALDH LAGALERKAG EFADVVKSGR
     THLMDATPVT LGQEFGGYAA QVRYGIERLQ ASLPRLAELP LGGTAVGTGI NTPPGFSAAV
     IEEVARATGL PLTEARDHFE AQGARDGIVE TSGQLRTIGV GLTKIANDLR WMASGPRTGL
     AEISLPDLQP GSSIMPGKVN PVIPEAVLMV AAQVTGNDAT VAAAGAAGNF ELNVMLPVIA
     KNVLESVRLL ANVSRLLADR TVDGIVAHPE RAREYAESSP SVVTPLNKYL GYEEAAKVAK
     RALAERKTIR QTVLEGGYVE RGDLTREQLD QALDVLRMTR P
//

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