(data stored in ACNUC7421 zone)

SWISSPROT: D1CEI7_THET1

ID   D1CEI7_THET1            Unreviewed;       472 AA.
AC   D1CEI7;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=Tter_0422 {ECO:0000313|EMBL:ACZ41343.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41343.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41343.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41343.1; -; Genomic_DNA.
DR   RefSeq; WP_012874378.1; NC_013525.1.
DR   STRING; 525904.Tter_0422; -.
DR   EnsemblBacteria; ACZ41343; ACZ41343; Tter_0422.
DR   KEGG; ttr:Tter_0422; -.
DR   eggNOG; ENOG4105C9Q; Bacteria.
DR   eggNOG; COG0114; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   KO; K01679; -.
DR   OMA; FELNVYN; -.
DR   OrthoDB; 734949at2; -.
DR   BioCyc; TTER525904:G1GGS-426-MONOMER; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CEI7.
DR   SWISS-2DPAGE; D1CEI7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00674282,
KW   ECO:0000313|EMBL:ACZ41343.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN       14    344       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      409    461       FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
FT   REGION      100    102       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      131    134       Substrate binding (B site).
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   REGION      141    143       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   REGION      326    328       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00743}.
FT   ACT_SITE    190    190       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   ACT_SITE    320    320       {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   BINDING     189    189       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   BINDING     321    321       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00743}.
FT   SITE        333    333       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00743}.
SQ   SEQUENCE   472 AA;  50806 MW;  8483109C535D9AEA CRC64;
     MTDGRFRIER DSMGEVRVPA DAYYGAQTQR AVENFPISDL RFPRRFIKAL GQIKMAAAEV
     NADLGLLDPE IARAIVQAAQ EVIEGKMDSQ FVVDIFQTGS GTSTNMNANE VIANRAIELL
     GGEIGTKSPV HPNDHVNLGQ SSNDVIPTAI HVSTLSAIQE DLEPALSELL AALREKSVEF
     MPIIKTGRTH LQDATPIRLG QEFEGYAGQV ERALQRLSYA KAELSEVALG GTAVGTGINT
     HPEFARRVCE KLSQLNGFEI RETTNHFQAQ SSLDACVLTS GVLKTIAVSL MKIANDIRWL
     GSGPRAGIGE LELPEVQPGS SIMPGKVNPV IAESLLMVCA QVIGSDAVVA TGGQWGNFEL
     NTMMPVVAYN LLQSVEIMAS ASSNFARKCV RGLRATERGP QLVEQGLAIC TALAPEIGYD
     AAAKIAQEAH RTGRTIREVA RERTQLSDEE LDRILNPEVM TEPGRNIGPA GG
//

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