ID A0A1Z4NLB2_9CYAN Unreviewed; 219 AA.
AC A0A1Z4NLB2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=NIES3974_31570 {ECO:0000313|EMBL:BAZ06496.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ06496.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ06496.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ06496.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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}.
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DR EMBL; AP018254; BAZ06496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NLB2; -.
DR OrthoDB; 9781577at2; -.
DR Proteomes; UP000218621; Chromosome.
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:BAZ06496.1};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000218621};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01984}.
FT DOMAIN 8..191
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT BINDING 14..16
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 40
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 106..109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 171
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT BINDING 187
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ SEQUENCE 219 AA; 24198 MW; 3EEA0419019ACAD9 CRC64;
MSNSHLPLII GVTGASGLIY AVRTLKYLLA ADYTIELVAS KSTYMVWQSE NKIRMPVEPE
QQEQFWRHHA NVPIAGKLRC HPWGNVGANI ASGSFRTLGM MVIPCSMSTV AKLANGLSSD
LLERAADVQI KEGRKLVLVP RETPFSLIHL RNLTTLAETG VRIVPAIPAW YHHPQSIEDL
VDFVVARALD QFEIDCIPIE RWKGNEEGRG SGGNGEQGE
//
