GenomeNet

Database: UniProt
Entry: A0A1B2R254_9BORD
LinkDB: A0A1B2R254_9BORD
Original site: A0A1B2R254_9BORD 
ID   A0A1B2R254_9BORD        Unreviewed;       254 AA.
AC   A0A1B2R254;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN   ORFNames=AKI39_10770 {ECO:0000313|EMBL:AOB31077.1};
OS   Bordetella sp. H567.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB31077.1, ECO:0000313|Proteomes:UP000093512};
RN   [1] {ECO:0000313|Proteomes:UP000093512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) 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; CP012334; AOB31077.1; -; Genomic_DNA.
DR   RefSeq; WP_066635464.1; NZ_CP012334.1.
DR   AlphaFoldDB; A0A1B2R254; -.
DR   STRING; 1697043.AKI39_10770; -.
DR   KEGG; boh:AKI39_10770; -.
DR   PATRIC; fig|1697043.4.peg.2224; -.
DR   OrthoDB; 4191603at2; -.
DR   Proteomes; UP000093512; 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:UP000093512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01139}.
FT   ACT_SITE        24
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         25..28
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         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         69..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         198..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   254 AA;  29231 MW;  44DA02C0404C624D CRC64;
     MTISSTQAVP QTSDIPQHVA IIMDGNGRWA TRRHLPRTAG HAKGVQAVRR VVEACGRRGV
     RYLTLFAFSS ENWRRPAEEV SLLMRLFVQA LEREVDKLDG QGVRLRVVGD LSPFEPRLRE
     LIEQAQARTA HNDRLHLSVC ANYGGRWDIL QAMRRMIVEN PDLAQAPDQI DEATLSRYLS
     MAWAPEPDLF IRTGGEQRIS NYLIWQLAYT ELFFTERYWP DFGGPELEEA FEWYRTRERR
     FGRTSAQVSA AGKR
//
DBGET integrated database retrieval system