MBD_THEAC
ID MBD_THEAC Reviewed; 405 AA.
AC Q9HJS1;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 OrderedLocusNames=Ta0893 {ECO:0000312|EMBL:CAC12022.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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:0000269|PubMed:28004831}.
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; AL445065; CAC12022.1; -; Genomic_DNA.
DR RefSeq; WP_010901303.1; NC_002578.1.
DR AlphaFoldDB; Q9HJS1; -.
DR SMR; Q9HJS1; -.
DR STRING; 273075.Ta0893; -.
DR DNASU; 1456429; -.
DR EnsemblBacteria; CAC12022; CAC12022; CAC12022.
DR GeneID; 1456429; -.
DR KEGG; tac:Ta0893; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_743187_0_0_2; -.
DR OMA; ISMRTDF; -.
DR OrthoDB; 54999at2157; -.
DR BioCyc; MetaCyc:MON-20539; -.
DR BRENDA; 4.1.1.110; 6324.
DR UniPathway; UPA00057; -.
DR Proteomes; UP000001024; 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;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Mevalonate 3,5-bisphosphate decarboxylase"
FT /id="PRO_0000444883"
SQ SEQUENCE 405 AA; 46288 MW; 7AED89D07080D771 CRC64;
MDTAGMEHSV SWISSNSDEL ILRSWISSRM DIAELHRAGD DIKEMMKSEG YYSEPSKYEA
ELSDGNITFA YSYPIKAFEK FLGYYDRENR IAFNPSISMR TDFSFCLAAC RYRKNGKTDT
VVLDGYADNK YYKKAKFALD KFRSEYSING SFDFYIKRYR RYQKAKGLSE SSAVAAAVSR
ALISNVFGDD AAKDDIFVSR YARLVSGSGT RAAHDGISMW LSYPGMDSRD CVAFKVGKSN
ENLNYGVFPK YSDVATDNAH SIAVNSVFYG TWVSEKFSNV KRLISDHFDI NDLLKIGEND
MLRLNSILMS GGLIIQTPDS LRILKEILKF KSKNEGFYFT ADTGPSIAIF SFDRSLIDEF
RENVNDEYIE GSYDFKGYNN RMRDFIREAQ EYFTQTPGED EEDRL
