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Database: UniProt
Entry: A0A0F4GBU7_9PEZI
LinkDB: A0A0F4GBU7_9PEZI
Original site: A0A0F4GBU7_9PEZI 
ID   A0A0F4GBU7_9PEZI        Unreviewed;       355 AA.
AC   A0A0F4GBU7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=TI39_contig4274g00003 {ECO:0000313|EMBL:KJX93670.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93670.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX93670.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93670.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) 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:KJX93670.1}.
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DR   EMBL; LAFY01004233; KJX93670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GBU7; -.
DR   STRING; 1047168.A0A0F4GBU7; -.
DR   OrthoDB; 5487130at2759; -.
DR   Proteomes; UP000033647; 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:UP000033647};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03197}.
FT   DOMAIN          161..329
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         168..170
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT   BINDING         194
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT   BINDING         245..248
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT   BINDING         280
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT   BINDING         310
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
FT   BINDING         326
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03197"
SQ   SEQUENCE   355 AA;  38881 MW;  B30501FF0CDDAFE6 CRC64;
     MVLTSSDSVP GALTHADKSH YAAPFSPAGE AFGNQWALCI VPDECGQSSR SRLIVWPISG
     MSDVMIKRSR RWLPPGQGQI INEGRLTPLI TARHRHFPTL IAMRVKSNAI QQVQCFSNVL
     SASRRHQSTC VIRSLSPFPT QSSSPSARPR CISYVAPRPR RIVIGITGAT GTVYAIRLLE
     TLRQLDIETH LVMSKWALAT LKFETPLSAA DVASLATKSY SPRDVSADIA SGSYLHDGMI
     IVPCSMKTLA AVRCGFGDDL IARAADVTMK EGRRLVLVVR ETPLSEIHLE NMLSLRRAGA
     IIFPPMPAFY TKPQSMDELV NHSVGRMLDS MGIHVDNFER WTGFGKSGDQ AGKAR
//
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