ID K7S776_ACIA4 Unreviewed; 363 AA.
AC K7S776;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=phosphomevalonate kinase {ECO:0000256|ARBA:ARBA00012958};
DE EC=2.7.4.2 {ECO:0000256|ARBA:ARBA00012958};
GN OrderedLocusNames=PACID_26710 {ECO:0000313|EMBL:AFV90442.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV90442.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV90442.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 2/3. {ECO:0000256|ARBA:ARBA00005017}.
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DR EMBL; CP003493; AFV90442.1; -; Genomic_DNA.
DR RefSeq; WP_015071339.1; NC_019395.1.
DR AlphaFoldDB; K7S776; -.
DR STRING; 1171373.PACID_26710; -.
DR KEGG; pbo:PACID_26710; -.
DR PATRIC; fig|1171373.8.peg.2628; -.
DR eggNOG; COG1577; Bacteria.
DR HOGENOM; CLU_017814_7_0_11; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004631; F:phosphomevalonate 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; IPR035102; Phosphomevalonate_kinase.
DR InterPro; IPR005917; Pmev_kinase_bact.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01220; Pmev_kin_Gr_pos; 1.
DR PANTHER; PTHR31814; -; 1.
DR PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFV90442.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:AFV90442.1}.
FT DOMAIN 100..170
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 285..342
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 363 AA; 39003 MW; E49784DCD4727C55 CRC64;
MIETSAPGKL YIAGEYAVVE PGEPSVLVAV DRRITVQLTP SAGMGRVHSS RYGHGPLTWV
RDEDDQIVAD HNPYDYVTAS ITVMERLRAE RGLAPRYFDL HISSELDDAS GSKFGLGSSA
AVTVAVVAAL DEFYGTGLSC DERFRLALLA TVEVAPRSSG GDVAASTFGG FIRYTSPDRA
RLRQAASQGT VTDALTDEGW EPCRITRLSP LNGLRLLVGW TGTPASTEGL VRRVSMSDAE
LDARYSNFLT LSREAVDQLV GAWDDDAQTV LSVIRRCRRL LQHLGQLRGT AIETDQLRIL
CNIAEQEGAA AKPSGAGGGD CGIAFVPEDH DVEPILEAWR TDGVLPLDLQ PHAATGEPIG
AER
//