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Database: UniProt
Entry: A0A1V9GA67_9BACT
LinkDB: A0A1V9GA67_9BACT
Original site: A0A1V9GA67_9BACT 
ID   A0A1V9GA67_9BACT        Unreviewed;       253 AA.
AC   A0A1V9GA67;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN   ORFNames=A3860_01415 {ECO:0000313|EMBL:OQP67450.1};
OS   Niastella vici.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP67450.1, ECO:0000313|Proteomes:UP000192796};
RN   [1] {ECO:0000313|EMBL:OQP67450.1, ECO:0000313|Proteomes:UP000192796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ57 {ECO:0000313|EMBL:OQP67450.1,
RC   ECO:0000313|Proteomes:UP000192796};
RA   Chen L., Wang D., Yang S., Wang G.;
RT   "Niastella vici sp. nov., isolated from farmland soil.";
RL   Submitted (MAR-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|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01139}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQP67450.1}.
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DR   EMBL; LVYD01000001; OQP67450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9GA67; -.
DR   STRING; 1703345.A3860_01415; -.
DR   OrthoDB; 4191603at2; -.
DR   Proteomes; UP000192796; Unassembled WGS sequence.
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:UP000192796};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01139}.
FT   ACT_SITE        22
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         23..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         27
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         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         67..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         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         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         196..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   253 AA;  29327 MW;  684E552E5D24EE1E CRC64;
     MQSLREQINL QRLPRHIAII MDGNGRWAKE QGQDRLYGHF HGVESVRNIV EGCAELGVEY
     LTLYAFSTEN WDRPQYEVTG LIELLVETIR KETETLNKNN IKLHVIGDVK MLPEYAQKEL
     NESLQITSQN TGLNLVMALS YSSRWELVQA VQHIAEDVKA GKIDPAAITQ NTLQQYLATS
     NFPDPELMIR TSGEYRISNF LLYQLAYAEL YFTNVRWPEF RKENLYEAIL DYQGRERRFG
     KTGDQIKKEH ING
//
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