(data stored in SCRATCH zone)

SWISSPROT: Q47SS0_THEFY

ID   Q47SS0_THEFY            Unreviewed;       463 AA.
AC   Q47SS0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
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=Tfu_0459 {ECO:0000313|EMBL:AAZ54497.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54497.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54497.1; -; Genomic_DNA.
DR   RefSeq; WP_011290906.1; NC_007333.1.
DR   STRING; 269800.Tfu_0459; -.
DR   EnsemblBacteria; AAZ54497; AAZ54497; Tfu_0459.
DR   KEGG; tfu:Tfu_0459; -.
DR   eggNOG; ENOG4105C9Q; Bacteria.
DR   eggNOG; COG0114; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   KO; K01679; -.
DR   OMA; FELNVYN; -.
DR   OrthoDB; 734949at2; -.
DR   BioCyc; TFUS269800:G1G4Q-466-MONOMER; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000000434; 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; Q47SS0.
DR   SWISS-2DPAGE; Q47SS0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00674282,
KW   ECO:0000313|EMBL:AAZ54497.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN       12    336       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      402    460       FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
FT   REGION       98    100       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      123    126       Substrate binding (B site).
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   REGION      133    135       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      318    320       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   ACT_SITE    182    182       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   ACT_SITE    312    312       {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   BINDING     181    181       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   BINDING     313    313       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   SITE        325    325       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
SQ   SEQUENCE   463 AA;  49546 MW;  D91BFAA723B88D7F CRC64;
     MTEYRIERDS MGEVKVPVEA KWRAQTQRAV ENFPISGQGL EAAHIAALGH IKAAAAKVNA
     ELGVIKEDMA EAIREAALEV AAGKWNDQFP VDVFQTGSGT SSNMNANEVI ATLATERLGQ
     PVHPNDHVNA SQSSNDVFPS SIHIAATSAL INELIPALKH LEETLSAKAS EFATVVKSGR
     THLMDATPVT LGQEFDGYAA QVRYGIERIE ASLPRVAELP LGGTAVGTGI NTPEGFSAKV
     IAEIARATGL PLTKARNHFE AQGARDALVE LSGQLRTIAV SFCKIANDIR WMGSGPRTGL
     SEIFLPDLQP GSSIMPGKVN PVLCESMLQV ASQVVGNDAA VAFGGSTGNF ELNVQLPLIA
     RNVLESIRLL ANISRVFADR CVAGITANEE RCREYAESSP SIVTPLNRYI GYEEAAKVAK
     QALAERKTIR QVVIERGYIA QGKLTEAQLD EALDVLAMTN SQK
//

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