ID A0A2G4F3R1_9CYAN Unreviewed; 209 AA.
AC A0A2G4F3R1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CP500_005535 {ECO:0000313|EMBL:PHX56378.1};
OS Tychonema bourrellyi FEM_GT703.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Tychonema.
OX NCBI_TaxID=2040638 {ECO:0000313|EMBL:PHX56378.1, ECO:0000313|Proteomes:UP000226442};
RN [1] {ECO:0000313|EMBL:PHX56378.1, ECO:0000313|Proteomes:UP000226442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX56378.1,
RC ECO:0000313|Proteomes:UP000226442};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHX56378.1, ECO:0000313|Proteomes:UP000226442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX56378.1,
RC ECO:0000313|Proteomes:UP000226442};
RA Tett A., Armanini F., Asnicar F., Boscaini A., Pasolli E., Zolfo M.,
RA Donati C., Salmaso N., Segata N.;
RT "Draft genome sequence of the planktic cyanobacteria Tychonema bourrellyi
RT isolated from alpine lentic freshwater.";
RL Submitted (NOV-2017) 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:PHX56378.1}.
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; NXIB02000021; PHX56378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4F3R1; -.
DR OrthoDB; 9781577at2; -.
DR Proteomes; UP000226442; Unassembled WGS sequence.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
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 Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000226442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01984}.
FT DOMAIN 12..196
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT BINDING 18..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 44
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 110..113
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 175
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 191
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ SEQUENCE 209 AA; 23065 MW; DBD55721405F1290 CRC64;
MTNSVSVPAQ PLIVGVTGAS GLIYAVRTLK YLLEADRAIE LVASKSTYMV WQSEQNIRMP
AEPTLQEEFW REQAGVPTMG KLRCHPWQDV GANIASGSFR TQGMIIIPCS MSTLGKLAAG
LSSDLLERAA DVQLKEGRKL VLVPRETPFS LIHLRNLTTL AEAGARIVPA IPAWYHNPQT
IEDLVDFVVA RTLDQLGIDC VPLKRWKED
//