DMD_SACS2
ID DMD_SACS2 Reviewed; 325 AA.
AC Q97UL5;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE Short=DMD;
DE EC=4.1.1.33;
GN OrderedLocusNames=SSO2989;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=23378249; DOI=10.1093/jb/mvt006;
RA Nishimura H., Azami Y., Miyagawa M., Hashimoto C., Yoshimura T., Hemmi H.;
RT "Biochemical evidence supporting the presence of the classical mevalonate
RT pathway in the thermoacidophilic archaeon Sulfolobus solfataricus.";
RL J. Biochem. 153:415-420(2013).
CC -!- FUNCTION: Catalyzes the decarboxylation of mevalonate 5-diphosphate
CC (MVAPP) to isopentenyl diphosphate (IPP). Functions in the mevalonate
CC (MVA) pathway leading to IPP, a key precursor for the biosynthesis of
CC isoprenoid compounds such as archaeal membrane lipids.
CC {ECO:0000269|PubMed:23378249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC Evidence={ECO:0000269|PubMed:23378249};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000269|PubMed:23378249}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK43094.1; -; Genomic_DNA.
DR PIR; G90479; G90479.
DR RefSeq; WP_009992640.1; NC_002754.1.
DR PDB; 4Z7C; X-ray; 2.20 A; A=2-325.
DR PDB; 4Z7Y; X-ray; 2.70 A; A/B/C/D/E/F=2-325.
DR PDB; 5GMD; X-ray; 1.50 A; A=1-325.
DR PDB; 5GME; X-ray; 1.70 A; A=1-325.
DR PDBsum; 4Z7C; -.
DR PDBsum; 4Z7Y; -.
DR PDBsum; 5GMD; -.
DR PDBsum; 5GME; -.
DR AlphaFoldDB; Q97UL5; -.
DR SMR; Q97UL5; -.
DR STRING; 273057.SSO2989; -.
DR EnsemblBacteria; AAK43094; AAK43094; SSO2989.
DR GeneID; 44128718; -.
DR KEGG; sso:SSO2989; -.
DR PATRIC; fig|273057.12.peg.3083; -.
DR eggNOG; arCOG02937; Archaea.
DR HOGENOM; CLU_040369_0_0_2; -.
DR InParanoid; Q97UL5; -.
DR OMA; LTLHAMM; -.
DR PhylomeDB; Q97UL5; -.
DR BRENDA; 4.1.1.33; 6163.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
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; IPR029765; Mev_diP_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.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isoprene biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..325
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000429454"
FT BINDING 18..21
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 75
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 139..144
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5GMD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5GMD"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5GMD"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 208..227
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 231..250
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:5GMD"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:5GMD"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5GMD"
SQ SEQUENCE 325 AA; 37028 MW; 01FB736096112177 CRC64;
MLKSVTVSAP SNIAVVKYWG KRGDERLNLP LNNSLSITLD DQLSVITKVT LNDKNIVIVN
DRILSEDEMK EYAGRVLDTF KKIVGKEFHV KVESKSKFPI NAGLASSAAG IAALAFSLNE
LLELNLKSEE LSKIARLGSG SACRSMFGGF VVWNKGERED GEDSYCYQIF RHDYWSELVD
IIPILSEKEK KISSRKGMIR SAETSELMEC RLKYIEKTFN EVIEAIRNRD EKKFYYLMMR
HSNSMHAVIL DSWPSFFYLN DTSIRIMEWI HDYGKAGYTF DAGPNPHIFT TERNIGDILE
FLKSLEIKRI IVSKVGDGPK VLSRE
