ID E3I0W2_RHOVT Unreviewed; 470 AA.
AC E3I0W2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=Rvan_1966 {ECO:0000313|EMBL:ADP71202.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP71202.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002292; ADP71202.1; -; Genomic_DNA.
DR RefSeq; WP_013419588.1; NC_014664.1.
DR AlphaFoldDB; E3I0W2; -.
DR STRING; 648757.Rvan_1966; -.
DR KEGG; rva:Rvan_1966; -.
DR eggNOG; COG0114; Bacteria.
DR HOGENOM; CLU_021594_4_1_5; -.
DR OrthoDB; 9802809at2; -.
DR UniPathway; UPA00223; UER01007.
DR Proteomes; UP000001399; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00743}.
FT DOMAIN 18..348
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 414..467
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT REGION 128..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT ACT_SITE 324
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 135..138
FT /ligand="substrate"
FT /note="in site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT BINDING 330..332
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
FT SITE 337
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00743"
SQ SEQUENCE 470 AA; 50143 MW; D2B272BD19A26DA2 CRC64;
MTEDVSPSAT RTETDTFGPI DVPANHYWGA QTQRSLGNFK IGGERMPIPL VHALGIVKKA
AAKTNLALGN LEQPLHDAIV AAAEEVIAGK LDAEFPLVVW QTGSGTQSNM NANEVISNRA
IEMLGGEKGS KKPVHPNDHV NRSQSSNDTF PTAMRIAAAV EVNKALLPAL DHLASAIEAK
AEEFKDIIKI GRTHLQDATP VTLGQEFSGY AAQLRFGIER VKATLPRLYL LAQGGTAVGT
GLNTPIGFAE KFADEVEKET GLPFVTAPNK FEALASNDAE VELSGALNVL ATSLFKIAND
IRLMGSGPRS GIAEISLPEN EPGSSIMPGK VNPTQCEALT MVCAQVMGNN VAITVAGSQG
HFELNVYKPV IIYNLLQSIR LISDAAVSFT DHCVVGIVAN RARIEDLLER SLMLVTALAP
KIGYDKAAKI AKTAHKHGTT LREEALALGY VSEEDFNALM KPELMIKPGV
//
