ID A0A0R1KHR8_9LACO Unreviewed; 288 AA.
AC A0A0R1KHR8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00012296};
DE EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296};
GN ORFNames=FD03_GL001924 {ECO:0000313|EMBL:KRK80500.1};
OS Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK80500.1, ECO:0000313|Proteomes:UP000051248};
RN [1] {ECO:0000313|EMBL:KRK80500.1, ECO:0000313|Proteomes:UP000051248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK80500.1,
RC ECO:0000313|Proteomes:UP000051248};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00008831}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK80500.1}.
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DR EMBL; AZDZ01000003; KRK80500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1KHR8; -.
DR STRING; 1423775.FD03_GL001924; -.
DR PATRIC; fig|1423775.4.peg.1962; -.
DR eggNOG; COG3407; Bacteria.
DR Proteomes; UP000051248; Unassembled WGS sequence.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 57..113
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 144..276
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 288 AA; 31725 MW; 33B3E3F1D5204A0C CRC64;
MTLDRFYTDT KSEIIDSDKD QIRLNNELLD DAHSQRIVKY LDFARKYFDF NEHFIVETVN
HVPTSAGFAS SASGFAALAA SLNQTMKLNL SDRELSILAR NGSGSASRSI YGGFVEWISG
TSNDTSYAVP IDEHPDIDLS LLSVVINQDA KKVSSTNGME SSVKTSPFYD NWVTLVSSEI
HEIKQAIAQK DVQKIGELSE HNAMSMHALT LSADPSFTYF APETIQVIQL VKSLRNQGVF
AYVTIDAGPN VKIICTKEST PVVQKYIKDN LPAVTTVVAN IGNGIQYI
//