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Database: UniProt
Entry: K9FCX6_PEND2
LinkDB: K9FCX6_PEND2
Original site: K9FCX6_PEND2 
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
//
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