GenomeNet

Database: UniProt
Entry: H2J2T7_MARPK
LinkDB: H2J2T7_MARPK
Original site: H2J2T7_MARPK 
ID   H2J2T7_MARPK            Unreviewed;       242 AA.
AC   H2J2T7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN   OrderedLocusNames=Marpi_0073 {ECO:0000313|EMBL:AEX84531.1};
OS   Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Marinitoga.
OX   NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX84531.1, ECO:0000313|Proteomes:UP000007161};
RN   [1] {ECO:0000313|EMBL:AEX84531.1, ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RX   PubMed=23045491; DOI=10.1128/JB.01430-12;
RA   Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA   Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT   "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT   Bacterium Marinitoga piezophila KA3.";
RL   J. Bacteriol. 194:5974-5975(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14283 / JCM 11233 / KA3
RC   {ECO:0000313|Proteomes:UP000007161};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA   Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT   "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
CC       {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01139}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003257; AEX84531.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2J2T7; -.
DR   STRING; 443254.Marpi_0073; -.
DR   KEGG; mpz:Marpi_0073; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_0; -.
DR   OMA; PRTEGHK; -.
DR   Proteomes; UP000007161; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   NCBIfam; TIGR00055; uppS; 1.
DR   PANTHER; PTHR10291:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE 2; 1.
DR   PANTHER; PTHR10291; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007161};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01139}.
FT   ACT_SITE        16
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         17..20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         61..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         184..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   242 AA;  27870 MW;  435A4F1D8A79BED3 CRC64;
     MTAIRKIPTH VGIIMDGNGR WAKQRGLKRT MGHEKGAKVA EDVIQWASDF GIKYLTLYSF
     STENWKRPPE EVKYLFSLMV RYLESRLNKI VRENVRVRFL GRIEELPENV YKVCKKIEEK
     SKNNTKIQVI LAVNYGGRQE IVDSVNKLIS SGKKEISIDD ISTNLYLPDV PDPELIIRTS
     GEIRISNFLL WQLAYSELYF TDILWPDFTK NDLEKALIDY SNRDRRFGGI SSDEGSGNIG
     SK
//
DBGET integrated database retrieval system