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Database: UniProt
Entry: Q46KX5_PROMT
LinkDB: Q46KX5_PROMT
Original site: Q46KX5_PROMT 
ID   Q46KX5_PROMT            Unreviewed;       202 AA.
AC   Q46KX5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000256|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000256|HAMAP-Rule:MF_01984};
GN   OrderedLocusNames=PMN2A_0361 {ECO:0000313|EMBL:AAZ57853.1};
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ57853.1, ECO:0000313|Proteomes:UP000002535};
RN   [1] {ECO:0000313|EMBL:AAZ57853.1, ECO:0000313|Proteomes:UP000002535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A {ECO:0000313|EMBL:AAZ57853.1,
RC   ECO:0000313|Proteomes:UP000002535};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the
CC       prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic
CC       acid decarboxylase UbiD. The prenyltransferase is metal-independent and
CC       links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to
CC       the flavin N5 and C6 atoms of FMN. {ECO:0000256|HAMAP-Rule:MF_01984}.
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_01984};
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01984}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01984}.
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DR   EMBL; CP000095; AAZ57853.1; -; Genomic_DNA.
DR   RefSeq; WP_011293895.1; NC_007335.2.
DR   AlphaFoldDB; Q46KX5; -.
DR   STRING; 59920.PMN2A_0361; -.
DR   KEGG; pmn:PMN2A_0361; -.
DR   HOGENOM; CLU_074522_0_1_3; -.
DR   OrthoDB; 9781577at2; -.
DR   PhylomeDB; Q46KX5; -.
DR   Proteomes; UP000002535; Chromosome.
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_01984};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01984};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW   Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000002535};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}.
FT   DOMAIN          2..186
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         10..12
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         36
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         101..104
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         136
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         166
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         182
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   202 AA;  22568 MW;  57B41513AB1477D0 CRC64;
     MKSIVIAITG ASAMQIAERS IQVLLENDQS VDLILSKGSY EVAKSERGIN IPVEPNTQEK
     FWRKKLEVQS GKLTCYRWND HSASIASGSH KTKGMVIVPC SMGTLGRIAS GFSLDLIERC
     ADVHLKENRR LIISPRESPL SLIHIENMKR LAIAGASIVP PIPAWYTNPR TIEDIIDFIV
     VRLFDSLGED LNYIKRWNGP IK
//
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