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

 A0A0L6JEL6_9RHIZ        Unreviewed;       471 AA.
A0A0L6JEL6;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
27-SEP-2017, entry version 13.
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};
ORFNames=AKJ13_02460 {ECO:0000313|EMBL:KNY24139.1};
Methylobacterium sp. ARG-1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Methylobacteriaceae; Methylobacterium.
NCBI_TaxID=1692501 {ECO:0000313|EMBL:KNY24139.1, ECO:0000313|Proteomes:UP000036734};
[1] {ECO:0000313|Proteomes:UP000036734}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ARG-1 {ECO:0000313|Proteomes:UP000036734};
Hirst R., James-Pederson M., Tai A.;
"Draft Genome Sequence of Methylobacterium sp. Strain ARG-1 Isolated
from the White-Rot Fungus, Armillaria gallica.";
Submitted (JUL-2015) 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNY24139.1}.
-----------------------------------------------------------------------
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EMBL; LHCD01000002; KNY24139.1; -; Genomic_DNA.
RefSeq; WP_050731918.1; NZ_LHCD01000002.1.
EnsemblBacteria; KNY24139; KNY24139; AKJ13_02460.
PATRIC; fig|1692501.3.peg.1949; -.
UniPathway; UPA00223; UER01007.
Proteomes; UP000036734; Unassembled WGS sequence.
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.
TIGRFAMs; TIGR00979; fumC_II; 1.
PROSITE; PS00163; FUMARATE_LYASES; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000036734};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
Lyase {ECO:0000256|HAMAP-Rule:MF_00743,
ECO:0000256|SAAS:SAAS00674282};
Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
DOMAIN 18 348 Lyase_1. {ECO:0000259|Pfam:PF00206}.
DOMAIN 414 466 FumaraseC_C. {ECO:0000259|Pfam:PF10415}.
REGION 104 106 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
REGION 135 138 Substrate binding (B site).
{ECO:0000256|HAMAP-Rule:MF_00743}.
REGION 145 147 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
REGION 330 332 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00743}.
ACT_SITE 194 194 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00743}.
ACT_SITE 324 324 {ECO:0000256|HAMAP-Rule:MF_00743}.
BINDING 193 193 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00743}.
BINDING 325 325 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00743}.
SITE 337 337 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00743}.
SEQUENCE 471 AA; 49188 MW; 393A4ED9AAD5CDB5 CRC64;
MSPTETGTAT RTESDTFGPI EVPAHRYWGA QTQRSIQNFK IGTERMPAPL VHALGLVKQA
AALVNKDLGA LEPKLADAIA AAAAEVVAGK HDEEFPLVVW QTGSGTQSNM NANEVIASLA
NEALGGKRGG KSPIHPNDHV NRGQSSNDTF PTAMHIAVAR EISGRLMPAL THLHTALDAK
AKAFESIVKI GRTHLQDATP VSLGQEFSGY AAQVALGGSR VAATLPGVLA LAQGGTAVGT
GLNAHPDFAN QFAAKVAELT GLEFTSAANK FEALATHDAL VFTQGALSAL AAGLFKIAQD
IRLLGSGPRS GLGELSLPEN EPGSSIMPGK VNPTQCEALT MVCCQVVGNA TTVSFAGSQG
NFELNVFKPV IANAVLQSIR LLADAAVSFT DNCVVGIKAN EDKIADLMSR SLMLVTALAP
SIGYDKAAEI AKTAHKNGTT LKEEALRLGY VTEEEFERVV RPETMLAPSA E


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