MBD_PICTO
ID MBD_PICTO Reviewed; 349 AA.
AC Q6L1T9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-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 OrderedLocusNames=PTO0478 {ECO:0000312|EMBL:AAT43063.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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. Shows no detectable
CC decarboxylase activity on mevalonate, mevalonate 3-phosphate,
CC mevalonate 5-phosphate or mevalonate 5-pyrophosphate.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 7.0 sec(-1). {ECO:0000269|PubMed:28004831};
CC pH dependence:
CC Optimum pH is 5-5.5. {ECO:0000269|PubMed:28004831};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {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}.
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; AE017261; AAT43063.1; -; Genomic_DNA.
DR RefSeq; WP_011177279.1; NC_005877.1.
DR PDB; 7T71; X-ray; 2.19 A; A/B=1-349.
DR PDBsum; 7T71; -.
DR AlphaFoldDB; Q6L1T9; -.
DR SMR; Q6L1T9; -.
DR STRING; 263820.PTO0478; -.
DR EnsemblBacteria; AAT43063; AAT43063; PTO0478.
DR GeneID; 2845318; -.
DR KEGG; pto:PTO0478; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_743187_0_0_2; -.
DR OMA; ISMRTDF; -.
DR OrthoDB; 54999at2157; -.
DR BRENDA; 4.1.1.110; 7518.
DR UniPathway; UPA00057; -.
DR Proteomes; UP000000438; 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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Reference proteome.
FT CHAIN 1..349
FT /note="Mevalonate 3,5-bisphosphate decarboxylase"
FT /id="PRO_0000444885"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7T71"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 72..85
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 119..132
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:7T71"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 257..277
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:7T71"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:7T71"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:7T71"
SQ SEQUENCE 349 AA; 40022 MW; 20BD470085E38FA8 CRC64;
MNDLNVYGEK IRNMLLELGI YNKSDDYSPD IKYNKTFHAN GYPITGLYKF LGYYDRDNNI
ANFPSISFTT NFSSCDVTCR VLRSGNDRII FNGKNNEKYY KRAEKALSFL RKKYRIDAAF
EFNIRINRRY RDAKGLGESA AVASATARAV AAAVFGMDAA KDRGFVSYLA RHVSGSGTRS
AAGNLSMWLS YPGIDDLSSI GFEIRKDDLF HFYAIPMRSR IETLNAHDYA SSSIFYNAWV
KSKFFDIIDI IENKFNTRMM LEYSMKDMYR LQALLISSGY IIYEKHYLDI IRKLRSSLNN
YKNVYFTSDT GTSIVVMSTS MNELSRFVND LDLDGISGNF PEKIIIEEL
