ID A0A0B5HTP6_ARCG5 Unreviewed; 330 AA.
AC A0A0B5HTP6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00012296};
DE EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296};
GN ORFNames=QT03_C0001G1032 {ECO:0000313|EMBL:AJF60518.1};
OS Archaeon GW2011_AR10.
OC Archaea.
OX NCBI_TaxID=1579370 {ECO:0000313|EMBL:AJF60518.1, ECO:0000313|Proteomes:UP000031777};
RN [1] {ECO:0000313|Proteomes:UP000031777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA Taylor R.C., Williams K.H., Banfield J.F.;
RT "Genomic expansion of domain archaea highlights roles for organisms from
RT new phyla in anaerobic carbon cycling.";
RL Curr. Biol. 25:690-701(2015).
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00008831}.
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DR EMBL; CP010424; AJF60518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5HTP6; -.
DR STRING; 1579370.QT03_C0001G1032; -.
DR KEGG; agw:QT03_C0001G1032; -.
DR HOGENOM; CLU_040369_0_0_2; -.
DR Proteomes; UP000031777; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01240; mevDPdecarb; 1.
DR PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AJF60518.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 89..147
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 178..310
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 330 AA; 36336 MW; 28C3D4FC3298B8D2 CRC64;
MKATARANAN IALVKYWGKR DDELILPMNG SISVTLSGLN TVTTVEFNEK LRNDVFVLNG
VEQKGDERKK LGNHLDLVRE KAKIKWNARV ESKNNFPTAA GLASSASGFA ALSVAAAKAA
HLELNEKELS ILARMGSGSA SRSIHGGFVE WQKGTKKDGS DSYAEQIAKP GHWENFRILT
TIVSGKEKKV KSRAGMKQTV QTSPMYKGWL ETVENDLENV RAGILKKNFS LVGETAEMNA
LKMHSTMLTT RPAIIYWEPE TIEIMHAVQE LREEGTECYF TIDAGPQVKV LCLQKNEAIV
TARLGEITGL QKIVPCKVGG KAETISEHFF
//
