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Database: UniProt
Entry: A0A0M2VGD5_9GAMM
LinkDB: A0A0M2VGD5_9GAMM
Original site: A0A0M2VGD5_9GAMM 
ID   A0A0M2VGD5_9GAMM        Unreviewed;       214 AA.
AC   A0A0M2VGD5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=VT06_11020 {ECO:0000313|EMBL:KKO48615.1};
OS   Arsukibacterium sp. MJ3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Arsukibacterium.
OX   NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO48615.1, ECO:0000313|Proteomes:UP000034895};
RN   [1] {ECO:0000313|EMBL:KKO48615.1, ECO:0000313|Proteomes:UP000034895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ3 {ECO:0000313|EMBL:KKO48615.1,
RC   ECO:0000313|Proteomes:UP000034895};
RA   Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA   Stougaard P., Glaring M.A.;
RT   "Draft genome sequences of two protease-producing strains of
RT   Arsukibacterium isolated from two cold and alkaline environments.";
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 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:KKO48615.1}.
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DR   EMBL; LAHP01000013; KKO48615.1; -; Genomic_DNA.
DR   RefSeq; WP_046554363.1; NZ_LAHP01000013.1.
DR   AlphaFoldDB; A0A0M2VGD5; -.
DR   STRING; 1632859.VT06_11020; -.
DR   PATRIC; fig|1632859.4.peg.2279; -.
DR   OrthoDB; 9781577at2; -.
DR   Proteomes; UP000034895; Unassembled WGS sequence.
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:UP000034895};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}.
FT   DOMAIN          3..187
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         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   214 AA;  23052 MW;  178D5E05D77373B7 CRC64;
     MREITLAFTG ASGAPYGWRL LELLLQQDIR VHLLISSAAR VVFATEHNIK LAAAPEKCTA
     QIQAQFACKT GQLTVYGKDD WFSPVASGSA APRHMVICPC STGAVSAIAC GASNNLIERA
     ADVVIKEGGK LILVPRESPL SAIHLENLLK LARLGVTIMP AAPGFYHQPQ QISDLVDFMV
     ARILDQLGVS QQLTARWGYG GERSLNSNKT GERE
//
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