ID A0A110A860_9CORY Unreviewed; 251 AA.
AC A0A110A860;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN ORFNames=AYJ05_03495 {ECO:0000313|EMBL:OAH26524.1}, BA700_04140
GN {ECO:0000313|EMBL:ASJ18335.1};
OS Corynebacterium stationis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1705 {ECO:0000313|EMBL:OAH26524.1, ECO:0000313|Proteomes:UP000076947};
RN [1] {ECO:0000313|EMBL:OAH26524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-15 {ECO:0000313|EMBL:OAH26524.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-15 {ECO:0000313|Proteomes:UP000076947};
RA Kaur G., Nair G.R., Mayilraj S.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ASJ18335.1, ECO:0000313|Proteomes:UP000197343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21170 {ECO:0000313|EMBL:ASJ18335.1,
RC ECO:0000313|Proteomes:UP000197343};
RA Yang J., Yang S.;
RT "Genome sequence of Corynebacterium stationis ATCC 21170.";
RL Submitted (JUN-2016) 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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01139}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC Rule:MF_01139}.
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DR EMBL; CP016326; ASJ18335.1; -; Genomic_DNA.
DR EMBL; LSTQ01000023; OAH26524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A110A860; -.
DR STRING; 1705.CA21670_03300; -.
DR Proteomes; UP000076947; Unassembled WGS sequence.
DR Proteomes; UP000197343; 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; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10291:SF48; DITRANS,POLYCIS-UNDECAPRENYL-DIPHOSPHATE SYNTHASE ((2E,6E)-FARNESYL-DIPHOSPHATE SPECIFIC); 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01139};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01139}; Reference proteome {ECO:0000313|Proteomes:UP000076947};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 30
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 31..34
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 251 AA; 29062 MW; 68A4C2E267F733C5 CRC64;
MVITPDPNRV LHPPEIPAEF LPRHIAMVMD GNGRWAQERG MKRTEGHKRG EAVLLDVVDA
CLALGVPYLS AYAFSTENWR RSPDEVRFLM GFNRDVLRRQ REWLHERGVR VVWVGRRPRL
WRSVIKELEA AEELTKDNTR MTLAMCVNYG GRAELADAFK KMSEDVQNGT LNPATVTEKT
ISQYMYDPTM PDVDLFLRPS GEKRTSNFLV WQSAYAEMVY QDKLFPDFTP EDLFAAVEEY
ARRDRRFGGT K
//
