ID A0A1Q7YSW0_9CYAN Unreviewed; 345 AA.
AC A0A1Q7YSW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=GHMP kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUI36_13610 {ECO:0000313|EMBL:OLE58365.1};
OS Cyanobacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1805101 {ECO:0000313|EMBL:OLE58365.1, ECO:0000313|Proteomes:UP000186010};
RN [1] {ECO:0000313|EMBL:OLE58365.1, ECO:0000313|Proteomes:UP000186010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE58365.1}.
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DR EMBL; MNHI01001772; OLE58365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7YSW0; -.
DR Proteomes; UP000186010; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.120; -; 1.
DR InterPro; IPR001174; Galkinase.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR014606; Heptose_7-P_kinase.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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 PIRSF; PIRSF036406; Hept_kin; 1.
DR PRINTS; PR00960; LMBPPROTEIN.
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};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 107..175
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 245..326
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 345 AA; 37331 MW; 59DD116AAA333F3D CRC64;
MPGKSAPSLQ PTITAHAPCR ADLAGGTIDL WPLYLFHPGA LTLNFAVEIL TSCRVTPLKG
QRIELCSIDT HCEETFTNLD ELIASRSHRH VLAAYLVRFF APERGLRVET DSQSPAGAGI
SGSSALMIAT TAALARFTGR DLDPETMRVI AQNVEAQVIR VPTGCQDYYP ALYGGVSAIH
LAPDGIRRAA VPVAPEEIEL RFVLAYTGAP RQSGINNWEV FKAHMNGDKH VFRNLEKIAA
IARDMHQALL RHDWQDVARL LREEWKLRRT NAPGITTPLI DKLISVSRKN GGRAAKVCGA
GGGGCVLMMV EEGAKEAVAQ AVAQAGGHIL PLRVARDGLR VETQA
//
