PMD_HALVD
ID PMD_HALVD Reviewed; 324 AA.
AC D4GXZ3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Phosphomevalonate decarboxylase;
DE Short=PMD;
DE EC=4.1.1.99 {ECO:0000269|PubMed:24375100};
DE AltName: Full=Mevalonate monophosphate decarboxylase;
GN Name=mvaD; OrderedLocusNames=HVO_1412; ORFNames=C498_11676;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=DS2 / DS70;
RX PubMed=24375100; DOI=10.1128/jb.01230-13;
RA Vannice J.C., Skaff D.A., Keightley A., Addo J.K., Wyckoff G.J.,
RA Miziorko H.M.;
RT "Identification in Haloferax volcanii of phosphomevalonate decarboxylase
RT and isopentenyl phosphate kinase as catalysts of the terminal enzyme
RT reactions in an archaeal alternate mevalonate pathway.";
RL J. Bacteriol. 196:1055-1063(2014).
CC -!- FUNCTION: Catalyzes the decarboxylation of mevalonate 5-phosphate
CC (MVAP) to isopentenyl phosphate (IP). Functions in an alternate
CC mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a
CC key precursor for the biosynthesis of isoprenoid compounds such as
CC archaeal membrane lipids. {ECO:0000269|PubMed:24375100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-phosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC phosphate + phosphate; Xref=Rhea:RHEA:40955, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58146,
CC ChEBI:CHEBI:65078, ChEBI:CHEBI:456216; EC=4.1.1.99;
CC Evidence={ECO:0000269|PubMed:24375100};
CC -!- ACTIVITY REGULATION: Is strongly inhibited by 6-fluoromevalonate
CC monophosphate but shows negligible inhibition by 6-fluoromevalonate
CC diphosphate (a potent inhibitor of the classical mevalonate pathway).
CC {ECO:0000269|PubMed:24375100}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=159 uM for (R,S)-5-phosphomevalonate
CC {ECO:0000269|PubMed:24375100};
CC KM=75 uM for (R)-5-phosphomevalonate {ECO:0000269|PubMed:24375100};
CC KM=289 uM for ATP {ECO:0000269|PubMed:24375100};
CC Vmax=5.6 umol/min/mg enzyme {ECO:0000269|PubMed:24375100};
CC Note=kcat is 3.5 sec(-1).;
CC pH dependence:
CC Optimum pH is about 7.5. {ECO:0000269|PubMed:24375100};
CC -!- SIMILARITY: Belongs to the phosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE02509.1; -; Genomic_DNA.
DR EMBL; AOHU01000090; ELY28351.1; -; Genomic_DNA.
DR RefSeq; WP_004043526.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; D4GXZ3; -.
DR SMR; D4GXZ3; -.
DR STRING; 309800.C498_11676; -.
DR EnsemblBacteria; ADE02509; ADE02509; HVO_1412.
DR EnsemblBacteria; ELY28351; ELY28351; C498_11676.
DR GeneID; 8926402; -.
DR KEGG; hvo:HVO_1412; -.
DR PATRIC; fig|309800.29.peg.2226; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_040369_0_0_2; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 50204at2157; -.
DR BioCyc; MetaCyc:MON-18695; -.
DR BRENDA; 4.1.1.99; 2561.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR041431; Mvd1_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..324
FT /note="Phosphomevalonate decarboxylase"
FT /id="PRO_0000429253"
SQ SEQUENCE 324 AA; 35417 MW; C6C56D0BE9D629A1 CRC64;
MKATAKAHPI QGLVKYHGMR DTERRMPYHD SISVCTAPSH TQTTVEFRPD ADEDVYVIGG
EEVEGRGAER IQAVVDRVRE LAGFDHRVRL ESENSFPSNI GFGSSASGFA AAAMALAEAA
DLDMTRPEVS TIARRGSASA ARAVTGAFSH LYSGMNDTDC RSERIETDLE DDLRIVAAHV
PAYKETEQAH AEAADSHMFQ ARMAHIHAQI DDMRDALYDG DFDAAFELAE HDSLSLAATT
MTGPAGWVYW QPRTIAVFNA VRKLRNEEDV PVYFSTDTGA SVYINTTEEH VDRVEEAVAD
CGVETDVWGV GGPAEVLDES EALF
