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Fumarate hydratase class II (Fumarase C) (EC 4.2.1.2) (Aerobic fumarase) (Iron-independent fumarase)

 D2S9P8_GEOOG            Unreviewed;       472 AA.
D2S9P8;
02-MAR-2010, integrated into UniProtKB/TrEMBL.
02-MAR-2010, sequence version 1.
23-MAY-2018, entry version 54.
RecName: Full=Fumarate hydratase class II {ECO:0000256|HAMAP-Rule:MF_00743};
Short=Fumarase C {ECO:0000256|HAMAP-Rule:MF_00743};
EC=4.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00743};
AltName: Full=Aerobic fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
AltName: Full=Iron-independent fumarase {ECO:0000256|HAMAP-Rule:MF_00743};
Name=fumC {ECO:0000256|HAMAP-Rule:MF_00743};
OrderedLocusNames=Gobs_1000 {ECO:0000313|EMBL:ADB73761.1};
Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 /
G-20).
Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
Geodermatophilus.
NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB73761.1, ECO:0000313|Proteomes:UP000001382};
[1] {ECO:0000313|Proteomes:UP000001382}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20
{ECO:0000313|Proteomes:UP000001382};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F.,
Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
"The complete genome of Geodermatophilus obscurus DSM 43160.";
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific
interconversion of fumarate to L-malate. {ECO:0000256|HAMAP-
Rule:MF_00743}.
-!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_00743}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
malate from fumarate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00743}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00743}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}.
-!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic
A site, and the non-catalytic B site that may play a role in the
transfer of substrate or product between the active site and the
solvent. Alternatively, the B site may bind allosteric effectors.
{ECO:0000256|HAMAP-Rule:MF_00743}.
-!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
Fumarase subfamily. {ECO:0000256|HAMAP-Rule:MF_00743}.
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EMBL; CP001867; ADB73761.1; -; Genomic_DNA.
RefSeq; WP_012947202.1; NC_013757.1.
ProteinModelPortal; D2S9P8; -.
STRING; 526225.Gobs_1000; -.
EnsemblBacteria; ADB73761; ADB73761; Gobs_1000.
KEGG; gob:Gobs_1000; -.
eggNOG; ENOG4105C9Q; Bacteria.
eggNOG; COG0114; LUCA.
HOGENOM; HOG000061737; -.
KO; K01679; -.
OMA; VSFTDNC; -.
OrthoDB; POG091H01XG; -.
BioCyc; GOBS526225:G1GH8-1010-MONOMER; -.
UniPathway; UPA00223; UER01007.
Proteomes; UP000001382; Chromosome.
GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
CDD; cd01362; Fumarase_classII; 1.
Gene3D; 1.10.275.10; -; 1.
HAMAP; MF_00743; FumaraseC; 1.
InterPro; IPR005677; Fum_hydII.
InterPro; IPR024083; Fumarase/histidase_N.
InterPro; IPR018951; Fumarase_C_C.
InterPro; IPR020557; Fumarate_lyase_CS.
InterPro; IPR000362; Fumarate_lyase_fam.
InterPro; IPR022761; Fumarate_lyase_N.
InterPro; IPR008948; L-Aspartase-like.
PANTHER; PTHR11444; PTHR11444; 1.
Pfam; PF10415; FumaraseC_C; 1.
Pfam; PF00206; Lyase_1; 1.
PRINTS; PR00149; FUMRATELYASE.
SUPFAM; SSF48557; SSF48557; 1.
PROSITE; PS00163; FUMARATE_LYASES; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000001382};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
Lyase {ECO:0000256|HAMAP-Rule:MF_00743, ECO:0000256|SAAS:SAAS00674282,
ECO:0000313|EMBL:ADB73761.1};
Reference proteome {ECO:0000313|Proteomes:UP000001382};
Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
DOMAIN 23 347 Lyase_1. {ECO:0000259|Pfam:PF00206}.
DOMAIN 413 471 FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
REGION 109 111 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
REGION 134 137 Substrate binding (B site).
{ECO:0000256|HAMAP-Rule:MF_00743}.
REGION 144 146 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
REGION 329 331 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
ACT_SITE 193 193 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00743}.
ACT_SITE 323 323 {ECO:0000256|HAMAP-Rule:MF_00743}.
BINDING 192 192 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00743}.
BINDING 324 324 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00743}.
SITE 336 336 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00743}.
SEQUENCE 472 AA; 50006 MW; C3433023C53E373E CRC64;
MPAETQAAQQ DGTDYRIEHD SMGEVRVPAW AKWRAQTQRA VENFPISGTP IERELIGALA
AIKGAAAAVN ASLGVLPQET ADAIGTAAAS VARGEWDEHF PIDVFQTGSG TSSNMNTNEV
IASLATEALG SPVHPNDHVN ASQSSNDVFP SAIHVAATRA IVRDLIPALQ HLEASLSRKA
EEFAEVVKSG RTHLMDATPV TLGQEFGGYA AAVRYGVERL QASLPRIGEL PLGGTAVGTG
INTPPGFAAA IIERLAAELD LPLSEARDHF EAQSSRDALV EGSGQLKTIA VGLVKIANDL
RWMGSGPRTG LGEIQLPDLQ PGSSIMPGKV NPVIPEAVIQ VSAQVIGNDA AVTFAGTTGV
FELNVTLPLM ARNVLESIRL LANASRILAD RCVDGIVANV DRCREYAESS PSIVTPLNKY
IGYEEAAKVA KQSLAEQKTI RQVVVERGYV EQGKLTEQQL DEALDVLSMT HP


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