ID K9FCX6_PEND2 Unreviewed; 202 AA.
AC K9FCX6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=PDIG_73730 {ECO:0000313|EMBL:EKV07099.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV07099.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV07099.1}.
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DR EMBL; AKCT01000266; EKV07099.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FCX6; -.
DR STRING; 1170229.K9FCX6; -.
DR eggNOG; ENOG502SI0E; Eukaryota.
DR HOGENOM; CLU_074522_3_0_1; -.
DR InParanoid; K9FCX6; -.
DR OMA; KTDGMIV; -.
DR OrthoDB; 5487130at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000009882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03197}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..184
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT BINDING 22..24
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 48
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 99..102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 164
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT BINDING 180
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
SQ SEQUENCE 202 AA; 22379 MW; 69EE8304EB24688B CRC64;
MPTIDHVPQP TRRRRIVVAM TGATGAILGI KALIALRRLN VETHLVISKW AEATIKYETD
YHPSNVKALA DHVHSINDMA APIASGSFKT DGMIVVPCSM KTLAAIRSGF CDDLISRSAD
VMLKERRKLV LVARETPLSD IHLSNMLEVS RAGAIIFPPV PAYYIRAASV DDLVNQTVGR
ILDLFDLDTG DFERWEGWQT EK
//