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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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