ID D8RFL8_SELML Unreviewed; 313 AA.
AC D8RFL8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Isopentenyl phosphate kinase {ECO:0000256|ARBA:ARBA00017267};
DE EC=2.7.4.26 {ECO:0000256|ARBA:ARBA00012908};
GN ORFNames=SELMODRAFT_92970 {ECO:0000313|EMBL:EFJ28888.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ28888.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate;
CC Xref=Rhea:RHEA:33963, ChEBI:CHEBI:30616, ChEBI:CHEBI:65078,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=2.7.4.26;
CC Evidence={ECO:0000256|ARBA:ARBA00000538};
CC -!- SIMILARITY: Belongs to the isopentenyl phosphate kinase family.
CC {ECO:0000256|ARBA:ARBA00010540}.
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DR EMBL; GL377578; EFJ28888.1; -; Genomic_DNA.
DR RefSeq; XP_002969764.1; XM_002969718.1.
DR AlphaFoldDB; D8RFL8; -.
DR STRING; 88036.D8RFL8; -.
DR EnsemblPlants; EFJ28888; EFJ28888; SELMODRAFT_92970.
DR Gramene; EFJ28888; EFJ28888; SELMODRAFT_92970.
DR KEGG; smo:SELMODRAFT_92970; -.
DR eggNOG; ENOG502QQ1X; Eukaryota.
DR HOGENOM; CLU_070213_0_0_1; -.
DR InParanoid; D8RFL8; -.
DR OMA; LEMTACH; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102043; F:isopentenyl phosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04241; AAK_FomA-like; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR024192; Fosfomycin_R_FomA-type.
DR NCBIfam; NF040647; IPPK_Arch; 1.
DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1.
DR PANTHER; PTHR43654:SF1; ISOPENTENYL PHOSPHATE KINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF016496; Kin_FomA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR016496-
KW 1}; Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR016496-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..283
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-1"
FT SITE 24
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR016496-2"
SQ SEQUENCE 313 AA; 33779 MW; 36948C78572A989D CRC64;
MESSSRKHHV RCIVKLGGAA ITFKDKLEAL NRESLSRTSL QLHEAMGGGV SFNMDWSKNL
EVPDPIDMEL HQKHAFVVVH GAGSFGHFQA SISGVNKGGL DNSLLVNAGF VATRLSVTKL
NHKVIRALAS QGIPAVGMPP FAAGWSTHKR IVGSSFLDVV LRIFVDAGFV PVLHGDAVRD
SHQGCCILSG DVIVRRLAEE LQPSYVVFLT NVPGVFDRPP SEENAVLLQE IVVYEDGTWS
IARPRLEAPV KTEMASHDTT GGMATKIAEA ASISRLGMDV YIVEAGTEHA LQALKGNIEQ
NWIGTIVRKA NST
//
