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Database: UniProt
Entry: A0YH42_9GAMM
LinkDB: A0YH42_9GAMM
Original site: A0YH42_9GAMM 
ID   A0YH42_9GAMM            Unreviewed;       197 AA.
AC   A0YH42;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   ORFNames=GP2143_11979 {ECO:0000313|EMBL:EAW29810.1};
OS   marine gamma proteobacterium HTCC2143.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; BD1-7 clade.
OX   NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW29810.1, ECO:0000313|Proteomes:UP000004931};
RN   [1] {ECO:0000313|EMBL:EAW29810.1, ECO:0000313|Proteomes:UP000004931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW29810.1,
RC   ECO:0000313|Proteomes:UP000004931};
RX   PubMed=20601481; DOI=10.1128/JB.00683-10;
RA   Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT   isolated from the Oregon Coast.";
RL   J. Bacteriol. 192:4530-4531(2010).
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}.
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:EAW29810.1}.
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DR   EMBL; AAVT01000014; EAW29810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0YH42; -.
DR   STRING; 247633.GP2143_11979; -.
DR   eggNOG; COG0163; Bacteria.
DR   OrthoDB; 9781577at2; -.
DR   Proteomes; UP000004931; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, ECO:0000256|HAMAP-
KW   Rule:MF_01984}; Reference proteome {ECO:0000313|Proteomes:UP000004931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..180
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         18..20
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         44
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         95..98
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         130
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         160
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         176
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   197 AA;  21394 MW;  B7FF780A5C5C44C1 CRC64;
     MFNQSGTGDS RLIVGISGAS GIIYGVRLLQ MLKDLPIESH LVMSKSAEMT LGYELDIKLK
     QIHDLADHVY PVKNIGAAIS SGSFRTMGMV IAPCSVRSMS EIATGVTTSL LTRAADVVLK
     ERKKLVLMVR ETPLHTGHLR TMTALSEMGA IIAPPLPAFY IKPKTIDDMV DHSVGRVLDL
     FDIETGAVNR WGENATE
//
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