ISPT1_CORGL
ID ISPT1_CORGL Reviewed; 225 AA.
AC P38118;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Isoprenyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN Name=uppS1 {ECO:0000255|HAMAP-Rule:MF_01139};
GN OrderedLocusNames=Cgl0991, cg1130;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCRC 18310;
RX PubMed=8097175; DOI=10.1111/j.1574-6968.1993.tb06034.x;
RA Chen C.-C., Liao C.-C., Hsu W.-H.;
RT "The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-
RT deoxy-D-arabinoheptulosonate-7-phosphate synthase gene.";
RL FEMS Microbiol. Lett. 107:223-230(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC with allylic pyrophosphates generating different type of terpenoids.
CC {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01139};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_01139}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF19697.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L07603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BA000036; BAB98384.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19697.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_600218.1; NC_003450.3.
DR AlphaFoldDB; P38118; -.
DR SMR; P38118; -.
DR STRING; 196627.cg1130; -.
DR KEGG; cgb:cg1130; -.
DR KEGG; cgl:Cgl0991; -.
DR PATRIC; fig|196627.13.peg.975; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_2_0_11; -.
DR OMA; TKGQPDP; -.
DR Proteomes; UP000000582; 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; -; 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 PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..225
FT /note="Isoprenyl transferase 1"
FT /id="PRO_0000123605"
FT ACT_SITE 3
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 3
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 4..7
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 180..182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT CONFLICT 27..32
FT /note="KIGEMV -> RSRDG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..44
FT /note="DDVDVNLVT -> AGVMSRRQSRD (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="N -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="L -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..225
FT /note="RIDFLRAIRDYSQRSRRFGK -> PSTSSAPFATTRSAAEDSVNNLFSKERH
FT V (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 25423 MW; 871CDDDB967606E5 CRC64;
MCDGNRRWAR EAGFTDVSHG HRVGAKKIGE MVRWCDDVDV NLVTVYLLSM ENLGRSSEEL
QLLFDIIADV ADELARPETN CRVRLVGHLD LLPDPVACRL RKAEEATVNN TGIAVNMAVG
YGGRQEIVDA VQKLLTIGKD EGLSVDELIE SVKVDAISTH LYTSGQPDPD LVIRTSGEQR
LSGFMLWQSA YSEIWFTDTY WPAFRRIDFL RAIRDYSQRS RRFGK
