ID A0A261EU93_9BIFI Unreviewed; 329 AA.
AC A0A261EU93;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Mevalonate kinase {ECO:0000313|EMBL:OZG50430.1};
GN ORFNames=BOCO_0947 {ECO:0000313|EMBL:OZG50430.1};
OS Bombiscardovia coagulans.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bombiscardovia.
OX NCBI_TaxID=686666 {ECO:0000313|EMBL:OZG50430.1, ECO:0000313|Proteomes:UP000216004};
RN [1] {ECO:0000313|EMBL:OZG50430.1, ECO:0000313|Proteomes:UP000216004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22924 {ECO:0000313|EMBL:OZG50430.1,
RC ECO:0000313|Proteomes:UP000216004};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
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:OZG50430.1}.
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DR EMBL; MWWS01000004; OZG50430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261EU93; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000216004; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
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; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00549; mevalon_kin; 1.
DR PANTHER; PTHR43290; MEVALONATE KINASE; 1.
DR PANTHER; PTHR43290:SF2; MEVALONATE KINASE; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZG50430.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000216004};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZG50430.1}.
FT DOMAIN 109..170
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 239..318
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 329 AA; 34655 MW; 7A2B560E77296962 CRC64;
MGFAYGEDSQ EVSRKVQALP HEGYGQTWAK TILIGEHSVV YGHPALALPL HSLKMQAWAT
PIASGQQAQL EALDYSGSLE ESGGTFGGLK RAVEVTLNFL HHPQQAFNIR TQSDFPAGRG
LGSSAAASGA VIRAILDAYD VEVSREQLLD LTNQAEKITH GHPSGLDAAT TSGLKPVRLA
AGSMSTIQPQ GDAYLVIADT GVVGSTKEAV EGVRSRFQED PTGVGQLMDS LGEQSEAAIR
DLENGQMESL GHRMNEAQVL LNALQIGHPK LDLLVETARS CGALGAKLTG GGLGGCVLAL
ASTKEDADRI SKALRSDGAQ QVWLHQMVA
//