MBD_THEVO
ID MBD_THEVO Reviewed; 372 AA.
AC Q97BM8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Mevalonate 3,5-bisphosphate decarboxylase {ECO:0000303|PubMed:28004831};
DE Short=MBD {ECO:0000303|PubMed:28004831};
DE EC=4.1.1.110 {ECO:0000269|PubMed:28004831};
DE AltName: Full=Bisphosphomevalonate decarboxylase {ECO:0000305};
GN ORFNames=TVG0411662 {ECO:0000312|EMBL:BAB59569.1};
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28004831; DOI=10.1038/srep39737;
RA Vinokur J.M., Cummins M.C., Korman T.P., Bowie J.U.;
RT "An adaptation to life in acid through a novel mevalonate pathway.";
RL Sci. Rep. 6:39737-39737(2016).
CC -!- FUNCTION: Catalyzes the ATP-independent decarboxylation of (R)-
CC mevalonate 3,5-bisphosphate to isopentenyl phosphate. Functions in an
CC alternative mevalonate pathway, only present in extreme acidophiles of
CC the Thermoplasmatales order, which passes through mevalonate 3-
CC phosphate rather than mevalonate 5-phosphate.
CC {ECO:0000269|PubMed:28004831}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3,5-bisphosphomevalonate + H(+) = CO2 + isopentenyl
CC phosphate + phosphate; Xref=Rhea:RHEA:56500, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:43474, ChEBI:CHEBI:65078,
CC ChEBI:CHEBI:82774; EC=4.1.1.110;
CC Evidence={ECO:0000269|PubMed:28004831};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway. {ECO:0000305|PubMed:28004831}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HJS1}.
CC -!- MISCELLANEOUS: It is proposed that Thermoplasmatales adapted the
CC classical archaeal mevalonate pathway by replacing mevalonate 5-
CC phosphate decarboxylase (MMD) with two specialized enzymes (mevalonate-
CC 3-phosphate 5-kinase and mevalonate 3,5-bisphosphate decarboxylase) in
CC order to produce isoprenoids in extremely acidic environments. It was
CC found that at low pH, the dual function enzyme MMD is unable to carry
CC out the first phosphorylation step, yet retains its ability to perform
CC decarboxylation. {ECO:0000305|PubMed:28004831}.
CC -!- SIMILARITY: Belongs to the mevalonate 3,5-bisphosphate decarboxylase
CC family. {ECO:0000305}.
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DR EMBL; BA000011; BAB59569.1; -; Genomic_DNA.
DR AlphaFoldDB; Q97BM8; -.
DR SMR; Q97BM8; -.
DR STRING; 273116.14324642; -.
DR EnsemblBacteria; BAB59569; BAB59569; BAB59569.
DR KEGG; tvo:TVG0411662; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_743187_0_0_2; -.
DR OMA; ISMRTDF; -.
DR PhylomeDB; Q97BM8; -.
DR BRENDA; 4.1.1.110; 6326.
DR UniPathway; UPA00057; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Lyase.
FT CHAIN 1..372
FT /note="Mevalonate 3,5-bisphosphate decarboxylase"
FT /id="PRO_0000444884"
SQ SEQUENCE 372 AA; 42524 MW; CA9965D98E7BE7D7 CRC64;
MNIMEISKFQ SLGDKIRTML EDHGYLSENN DYEPNPIDGN ISISYAYPIK AFEKFLGYYD
VENRVAYNPS ISMRTDFSYC IAACRYNKNG NEDTVILDGV TDEKYLRKAK FALDYFRKEF
RIKGSFDFYI RRYRRYTKAK GLSESSAVAA AVSRALIKNV FGEGPALDDV FVSKYARLVS
GSGTRAAHSG ISIWLSYPGI NLRECAAFRV ADDPHDVYYG IFPKYTDIAT DSAHSVAVKS
IFYASWLEDK YANIKRLIEH NFDIDELLIS GENDMLKLNA ILFSGGLIIQ TGESLRILRA
IQDFKKNGDL FFTADTGPSI MVLSRDKSLI EELRQSVEDP YIEGTYNFNR HTRDLNNFTK
EANEYFLENK IE
