ID A0A072PTW7_9EURO Unreviewed; 318 AA.
AC A0A072PTW7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A1O9_01542 {ECO:0000313|EMBL:KEF63564.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF63564.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF63564.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF63564.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF63564.1}.
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; AMGV01000001; KEF63564.1; -; Genomic_DNA.
DR RefSeq; XP_013266154.1; XM_013410700.1.
DR AlphaFoldDB; A0A072PTW7; -.
DR STRING; 1182545.A0A072PTW7; -.
DR GeneID; 25276488; -.
DR VEuPathDB; FungiDB:A1O9_01542; -.
DR HOGENOM; CLU_074522_1_1_1; -.
DR OrthoDB; 5487130at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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_03197};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03197};
KW Lyase {ECO:0000313|EMBL:KEF63564.1};
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:UP000027920};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03197}.
FT DOMAIN 78..246
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT REGION 32..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 111
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 162..165
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 197
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 227
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 243
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
SQ SEQUENCE 318 AA; 35513 MW; 38A3838C775FAAEC CRC64;
MLRLFAQPPA RGLAQSRRFV IPIAVHRCSH RRKSDYSNRS YQNPESHLQN VSESQPQPSG
PRTNEDRLIT LLPPRPRRIV VGITGATGTI YAIRMLEIMR QLGIETHLII SKWALATLKY
ETDLSEAHIR SLAHATYTAK DLSAPIASGS FQHDGVAIVP CSMKTLAAVR IGFCDDLISR
AADVSLKEGR KVLIAVRETP LSDIHLENML ALRRAGAIIF PPVPAFYTQP KSLDELVNQS
VGRMLDSLGI YINNFHRWNG FEKQNKNKLP RSVSADPSLN YSQVSNMRAK PEKQPDHSTN
STDYTELHND GPLRYASG
//
