ID A0A1V6PSW8_9EURO Unreviewed; 214 AA.
AC A0A1V6PSW8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Flavin prenyltransferase PAD1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03197};
DE EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_03197};
GN Name=PAD1 {ECO:0000256|HAMAP-Rule:MF_03197};
GN ORFNames=PENANT_c039G00406 {ECO:0000313|EMBL:OQD80104.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD80104.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase
CC FDC1. The prenyltransferase is metal-independent and links a
CC dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the
CC flavin N5 and C6 atoms of FMN. {ECO:0000256|HAMAP-Rule:MF_03197}.
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_03197};
CC -!- SUBUNIT: Oligomer. {ECO:0000256|HAMAP-Rule:MF_03197}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03197}.
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03197}.
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:OQD80104.1}.
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DR EMBL; MDYN01000039; OQD80104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PSW8; -.
DR STRING; 416450.A0A1V6PSW8; -.
DR OrthoDB; 5487130at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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_03197};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03197};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03197};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW Rule:MF_03197}; Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03197}.
FT DOMAIN 49..197
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 113..116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 148
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 178
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 194
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
SQ SEQUENCE 214 AA; 23273 MW; 2E4CC23041FC03D6 CRC64;
MLSMLSGTHT PQSVGTSPAG SQTGASTPAE THLEQIQHAP THPPTKPRKR IVVAMTGATG
AILGIKATIK YETDYHPSNV RALADHIHNI NDMAAPISSG SFKTDGMIVV PCSMKTLAAI
HSGFCDDLIS RTADVMLKER RKLVLVARET PLSDIHLRNM LEITRSGAII FPPVPAYYIR
AASVDDLVDQ SVGRMLDLFE LDTGDFARWE GWEK
//
