ID Q4L3R7_STAHJ Unreviewed; 327 AA.
AC Q4L3R7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00012296};
DE EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296};
GN Name=mvaD {ECO:0000313|EMBL:BAE05710.1};
GN OrderedLocusNames=SH2401 {ECO:0000313|EMBL:BAE05710.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE05710.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE05710.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE05710.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00008831}.
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DR EMBL; AP006716; BAE05710.1; -; Genomic_DNA.
DR RefSeq; WP_011276656.1; NC_007168.1.
DR AlphaFoldDB; Q4L3R7; -.
DR GeneID; 58061569; -.
DR KEGG; sha:SH2401; -.
DR eggNOG; COG3407; Bacteria.
DR HOGENOM; CLU_040369_0_0_9; -.
DR OrthoDB; 5498344at2; -.
DR Proteomes; UP000000543; 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: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 92..149
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 179..318
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 327 AA; 36440 MW; 6AB023871A99B2A8 CRC64;
MKKNGKARAH TNIALIKYWG KADEALIIPM NNSLSVTLDR FYTETRVTFD ETLTEDQLIL
NGEAVNAKES AKIQRYMEMI RKEAGISEHA LIESENFVPT AAGLASSASA YAALAGACNE
ALQLGLSDKD LSRLARRGSG SASRSIYGGF AEWEKGNDDE TSFAHRVEAD GWENELAMVF
VVINNKSKKV SSRSGMSLTR DTSRFYQYWL DNVEPDLKEI KEAIAQKDFK RMGEVIEANG
LRMHATNLGA QPPFTYLVPE SYDAMRIVHE CREAGLPCYF TMDAGPNVKV LIEKKNQQAI
VDKFLQEFDQ SQIITSDITQ SGVEIIK
//
