ID A0A0N0NEC7_9ACTN Unreviewed; 223 AA.
AC A0A0N0NEC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Flavin prenyltransferase UbiX {ECO:0000256|HAMAP-Rule:MF_01984};
DE EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01984};
GN Name=ubiX {ECO:0000256|HAMAP-Rule:MF_01984};
GN ORFNames=OV320_2758 {ECO:0000313|EMBL:KPI31031.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI31031.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI31031.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI31031.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic
CC acid decarboxylase UbiD. The prenyltransferase is metal-independent and
CC links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to
CC the flavin N5 and C6 atoms of FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl phosphate + FMNH2 = phosphate + prenyl-FMNH2;
CC Xref=Rhea:RHEA:37743, ChEBI:CHEBI:43474, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:87467, ChEBI:CHEBI:88052; EC=2.5.1.129;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01984};
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP-
CC Rule:MF_01984}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01984}.
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:KPI31031.1}.
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DR EMBL; LJCX01000019; KPI31031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0NEC7; -.
DR PATRIC; fig|1592329.3.peg.1586; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR HAMAP; MF_01984; ubiX_pad; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR InterPro; IPR004507; UbiX-like.
DR NCBIfam; TIGR00421; ubiX_pad; 1.
DR PANTHER; PTHR43374; FLAVIN PRENYLTRANSFERASE; 1.
DR PANTHER; PTHR43374:SF1; FLAVIN PRENYLTRANSFERASE PAD1, MITOCHONDRIAL; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01984};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01984};
KW Lyase {ECO:0000313|EMBL:KPI31031.1};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01984}.
FT DOMAIN 1..200
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 35
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 180
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 196
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ SEQUENCE 223 AA; 23081 MW; A86176363005C985 CRC64;
MPWIVGVSGA SGTPYAAAVL RALLAAGESV DLVVSRASRL TLLDETGISF RDAHWRDDLR
EWLARGADGK PGTFDVDLGG EGAGDRVRYW AAGDLAAGPS SGSYATKGML IVPASTACVA
GVALGLSKDL LQRAASVTLK ERRPLVVAVR ETPLNGQTLR HLVALDEAGA SVVPASPAFY
AGATHIQDLV DFVAGRVLDA AGVGHGLYRR WKGEIGGGSR PPA
//
