GenomeNet

Database: UniProt
Entry: A0A285RGQ6_9RHOB
LinkDB: A0A285RGQ6_9RHOB
Original site: A0A285RGQ6_9RHOB 
ID   A0A285RGQ6_9RHOB        Unreviewed;       464 AA.
AC   A0A285RGQ6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=SAMN05877831_101108 {ECO:0000313|EMBL:SOB93084.1};
OS   Rhodobacter maris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=446682 {ECO:0000313|EMBL:SOB93084.1, ECO:0000313|Proteomes:UP000219111};
RN   [1] {ECO:0000313|Proteomes:UP000219111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA276 {ECO:0000313|Proteomes:UP000219111};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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; EC=4.2.1.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00743};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate
CC       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 A
CC       site, and the non-catalytic B site that may play a role in the transfer
CC       of substrate or product between the active site and the solvent.
CC       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. Fumarase
CC       subfamily. {ECO:0000256|ARBA:ARBA00009084, ECO:0000256|HAMAP-
CC       Rule:MF_00743}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; OBMT01000001; SOB93084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285RGQ6; -.
DR   OrthoDB; 9802809at2; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000219111; Unassembled WGS sequence.
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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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   NCBIfam; TIGR00979; fumC_II; 1.
DR   PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00743};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN          13..342
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          408..460
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         98..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         129..132
FT                   /ligand="substrate"
FT                   /note="in site B"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   BINDING         324..326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT   SITE            331
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ   SEQUENCE   464 AA;  49500 MW;  7D4860CF3BBAC9BF CRC64;
     MTATRTETDS FGPLEVPADK YWGAQTQRSI MNFPIGWERQ PVPIIRALGV IKKAAALVNK
     AQGDMAPEIA DAIVAAATEV IEGKFDDNFP LVVWQTGSGT QSNMNANEVI SNRAIEMLGG
     QMGSKKPVHP NDHCNMGQSS NDTFPTAMHV AIACHARDVL IPGLEKLSKA LWAKSDEFKD
     IIKIGRTHTQ DATPLTLGQE FSGYATQVDR GIARVKLALT HIYELAQGGT AVGTGLNTKV
     GWDTRIAAQI AEITGLPFVT APNKFEALAA HDAMVFFSGA LKTVAASLFK IANDMRLLGS
     GPRSGLGELI LPENEPGSSI MPGKVNPTQA EALTMVCAHV MGNDAAVGFA GSQGHFELNV
     YNPMMSYNVL QSMQLLGDSA SAFTDNMVVG TQANTARIDK LMKESLMLVT ALAPTIGYDA
     ATKVAKTAHK NGTTLREEAI ALGYVDGETF DRIVRPEDMI GPKG
//
DBGET integrated database retrieval system