GenomeNet

Database: UniProt
Entry: K9UNM8_CHAP6
LinkDB: K9UNM8_CHAP6
Original site: K9UNM8_CHAP6 
ID   K9UNM8_CHAP6            Unreviewed;       219 AA.
AC   K9UNM8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=Cha6605_5156 {ECO:0000313|EMBL:AFY96051.1};
OS   Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC   Chamaesiphon.
OX   NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY96051.1, ECO:0000313|Proteomes:UP000010366};
RN   [1] {ECO:0000313|EMBL:AFY96051.1, ECO:0000313|Proteomes:UP000010366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL   Submitted (MAY-2012) 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   ---------------------------------------------------------------------------
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; CP003600; AFY96051.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9UNM8; -.
DR   STRING; 1173020.Cha6605_5156; -.
DR   KEGG; cmp:Cha6605_5156; -.
DR   PATRIC; fig|1173020.3.peg.5914; -.
DR   eggNOG; COG0163; Bacteria.
DR   HOGENOM; CLU_074522_0_1_3; -.
DR   OrthoDB; 9781577at2; -.
DR   Proteomes; UP000010366; 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:UP000010366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01984}.
FT   DOMAIN          20..204
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   BINDING         27..29
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         53
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         119..122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         154
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         184
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
FT   BINDING         200
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   219 AA;  23961 MW;  D26F8DCEDF32F23E CRC64;
     MGTFKSQLPT PNSQLPLNKP LILGVTGASG LIYAIRAVKY LLAADYQIEL VASKSTYMVF
     QAEDQIRLPS EPEEQADFWR ELAGVPTAGK LRCHRWGDVG ANIASGSYRT QGMIIMPCSM
     STVGKLANGL SGDLLERAAD VQLKEGRKLV IVPRETPFSL IHLRNLTALA EAGAAIVPAC
     PAWYHKPQSI DDLVDFVVAR ALDRLDIDCI PINRWKTDS
//
DBGET integrated database retrieval system