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Entry: A0A0Q7CUH5_9CAUL
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ID   A0A0Q7CUH5_9CAUL        Unreviewed;       463 AA.
AC   A0A0Q7CUH5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ECO:0000313|EMBL:KQW68236.1};
GN   ORFNames=ASC73_17110 {ECO:0000313|EMBL:KQW68236.1};
OS   Phenylobacterium sp. Root1277.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW68236.1, ECO:0000313|Proteomes:UP000051150};
RN   [1] {ECO:0000313|EMBL:KQW68236.1, ECO:0000313|Proteomes:UP000051150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1277 {ECO:0000313|EMBL:KQW68236.1,
RC   ECO:0000313|Proteomes:UP000051150};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW68236.1, ECO:0000313|Proteomes:UP000051150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1277 {ECO:0000313|EMBL:KQW68236.1,
RC   ECO:0000313|Proteomes:UP000051150};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQW68236.1}.
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DR   EMBL; LMDZ01000007; KQW68236.1; -; Genomic_DNA.
DR   RefSeq; WP_056025668.1; NZ_LMDZ01000007.1.
DR   AlphaFoldDB; A0A0Q7CUH5; -.
DR   UniPathway; UPA00223; UER01007.
DR   Proteomes; UP000051150; 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; PR00145; ARGSUCLYASE.
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, ECO:0000313|EMBL:KQW68236.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051150};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT   DOMAIN          12..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   463 AA;  49343 MW;  18710F69D2E8105B CRC64;
     MTATRTETDT FGPIEVATNV YWGAQSQRSI GNFKIGWEKQ PKPVIRALGI VKRAAAEANM
     ELGKLDPKIG AAIVAAAQEV IDGKLDDHFP LVVWQTGSGT QSNMNANEVI SNRAIEMLGG
     VMGSKSPVHP NDHVNMSQSS NDTYPTAMHI ACAEQVAKEL MPALEHLHAA LKVKVKAFDH
     IIKIGRTHTQ DATPLTLGQE FSGYSQQVAN GVRRIKDTLA GLYELAQGGT AVGTGLNAPV
     GFAELVAQKI ADITRLPFVT APNKFEALAA HDAMVFSHGA INTMAGSLFK IANDIRFLGS
     GPRSGLGELA LPENEPGSSI MPGKVNPTQC EALTMVCTQV FGNNATLTFA GASGHFELNV
     FNPVMAYNFL QSCRLLADAS ISFTDNCVVG IEAREDNIRA ALERSLMLVT ALNGKIGYDN
     AAKIAKTAHK NGTTLREEAV GGGYVTNEEF DALVRPEKMI SPG
//
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