GenomeNet

Database: UniProt
Entry: W0SE17_9PROT
LinkDB: W0SE17_9PROT
Original site: W0SE17_9PROT 
ID   W0SE17_9PROT            Unreviewed;       203 AA.
AC   W0SE17;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=ppcY {ECO:0000313|EMBL:BAO29464.1};
GN   Synonyms=ubiX {ECO:0000256|HAMAP-Rule:MF_01984};
GN   ORFNames=SUTH_01671 {ECO:0000313|EMBL:BAO29464.1};
OS   Sulfuritalea hydrogenivorans sk43H.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfuritalea.
OX   NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO29464.1, ECO:0000313|Proteomes:UP000031637};
RN   [1] {ECO:0000313|EMBL:BAO29464.1, ECO:0000313|Proteomes:UP000031637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM22779 {ECO:0000313|EMBL:BAO29464.1};
RX   PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA   Watanabe T., Kojima H., Fukui M.;
RT   "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT   skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT   sulfur oxidation pathway of betaproteobacteria.";
RL   Syst. Appl. Microbiol. 37:387-395(2014).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012547; BAO29464.1; -; Genomic_DNA.
DR   RefSeq; WP_041098481.1; NZ_AP012547.1.
DR   AlphaFoldDB; W0SE17; -.
DR   STRING; 1223802.SUTH_01671; -.
DR   KEGG; shd:SUTH_01671; -.
DR   HOGENOM; CLU_074522_0_1_4; -.
DR   OrthoDB; 9781577at2; -.
DR   Proteomes; UP000031637; 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:UP000031637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}.
FT   DOMAIN          1..171
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         9..11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         35
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         86..89
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         121
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         151
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         167
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   203 AA;  22177 MW;  2352EB195D165B4A CRC64;
     MKLVVGISGA SGAIYGLRML EVLKQAGVET HLVMSDSAKR TIVHETDYTI DAVRGLASQV
     HDINDIGASI ASGSFRHDGM VIAPCSIKTL SAVANSFTTN LLIRAADVTL KERRRLVLML
     RETPLHLGHL RLMAQAVEIG AVMVPPMPAF YHRPQTLDDI INQSVGKALD QFNLDIGPDL
     FKRWTGTEER QRARPQPGGD GNR
//
DBGET integrated database retrieval system