Y2582_METMA
ID Y2582_METMA Reviewed; 170 AA.
AC Q8PTX6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Nudix hydrolase MM_2582 {ECO:0000303|PubMed:34864834};
DE EC=3.6.1.- {ECO:0000269|PubMed:34864834};
DE AltName: Full=Prenyl-phosphatase {ECO:0000305};
GN OrderedLocusNames=MM_2582 {ECO:0000312|EMBL:AAM32278.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000312|EMBL:AAM32278.1, ECO:0000312|Proteomes:UP000000595};
RN [1] {ECO:0000312|EMBL:AAM32278.1, ECO:0000312|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000312|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=34864834; DOI=10.1093/bbb/zbab205;
RA Ishibashi Y., Matsushima N., Ito T., Hemmi H.;
RT "Isopentenyl diphosphate/dimethylallyl diphosphate-specific Nudix hydrolase
RT from the methanogenic archaeon Methanosarcina mazei.";
RL Biosci. Biotechnol. Biochem. 86:246-253(2022).
CC -!- FUNCTION: Hydrolyzes homoallylic isopentenyl diphosphate (IPP), its
CC allylic isomer dimethylallyl diphosphate (DMAPP) and short-chain prenyl
CC diphosphates geranyl diphosphate (GPP) and farnesyl diphosphate (FPP)
CC to their corresponding monophosphate forms with high activity. The
CC preferred substrate is IPP. ADP, NADPH, Ap5A and thiamine diphosphate
CC (TPP) are weakly hydrolyzed. No hydrolysis with ATP, dNTPs, 8-OH-dGTP,
CC NAD+, FAD or acetyl-CoA. The likely physiological role of this enzyme
CC is to provide a substrate dimethylallyl phosphate (DMAP) for prenylated
CC flavin mononucleotide (prenyl-FMN) synthase MM_1871 involved in the
CC biosynthesis of prenyl-FMN, a coenzyme required in the archaea-specific
CC mevalonate pathway. {ECO:0000269|PubMed:34864834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + H2O = dimethylallyl phosphate +
CC H(+) + phosphate; Xref=Rhea:RHEA:70507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:88052; Evidence={ECO:0000269|PubMed:34864834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isopentenyl diphosphate = H(+) + isopentenyl phosphate +
CC phosphate; Xref=Rhea:RHEA:70503, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:65078,
CC ChEBI:CHEBI:128769; Evidence={ECO:0000269|PubMed:34864834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesyl
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:48128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:88226, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:34864834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+)
CC + phosphate; Xref=Rhea:RHEA:47944, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:88107; Evidence={ECO:0000269|PubMed:34864834};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:34864834};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.5 uM for dimethylallyl diphosphate (DMAPP) (at pH 8.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:34864834};
CC KM=27.8 uM for isopentenyl diphosphate (IPP) (at pH 8.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:34864834};
CC KM=152 uM for geranyl diphosphate (GPP) (at pH 8.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:34864834};
CC KM=99.8 uM for farnesyl diphosphate (FPP) (at pH 8.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:34864834};
CC Note=kcat is 0.139 sec(-1) with DMAPP as substrate. kcat is 0.681
CC sec(-1) with as IPP substrate. kcat is 0.395 sec(-1) with GPP as
CC substrate. kcat is 0.298 sec(-1) with FPP as substrate.
CC {ECO:0000269|PubMed:34864834};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:34864834};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Stable at 30 degrees
CC Celsius. More than half of its activity is lost after 30 min of
CC treatment at 35 degrees Celsius. Activity is lost by 30 min of
CC treatment above 40 degrees Celsius. {ECO:0000269|PubMed:34864834};
CC -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000305|PubMed:34864834}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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; AE008384; AAM32278.1; -; Genomic_DNA.
DR RefSeq; WP_011034497.1; NC_003901.1.
DR SMR; Q8PTX6; -.
DR STRING; 192952.MM_2582; -.
DR EnsemblBacteria; AAM32278; AAM32278; MM_2582.
DR GeneID; 24865255; -.
DR KEGG; mma:MM_2582; -.
DR PATRIC; fig|192952.21.peg.2962; -.
DR eggNOG; arCOG01082; Archaea.
DR HOGENOM; CLU_131901_0_0_2; -.
DR OMA; LFKIPCI; -.
DR BioCyc; MetaCyc:MON-21849; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..170
FT /note="Nudix hydrolase MM_2582"
FT /id="PRO_0000455562"
FT DOMAIN 25..155
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 59..83
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P65556"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P65556"
SQ SEQUENCE 170 AA; 19676 MW; 99D9F10440670BAD CRC64;
MISEVDMDDN FLGLRARDEF YSGKHIHRAS QLILLDPENR ILLQKRSPGK FWFPNRYTYS
VSGTVADESY EACIAREMLE EIGISVPFRR LFKIPCIREN KGAYHTIFSG RCSEEAASLI
RHDLEEATSI EWVELEELHR AVKAEPGNYT PALREGIIKI FKEGCEKYLF
