ID   UBIX_VIBCH              Reviewed;         211 AA.
AC   Q9KP38;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984};
DE            EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984};
GN   Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984}; OrderedLocusNames=VC_2541;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_01984};
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01984}.
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DR   EMBL; AE003852; AAF95682.1; -; Genomic_DNA.
DR   PIR; G82063; G82063.
DR   RefSeq; NP_232169.1; NC_002505.1.
DR   AlphaFoldDB; Q9KP38; -.
DR   SMR; Q9KP38; -.
DR   STRING; 243277.VC_2541; -.
DR   DNASU; 2615558; -.
DR   EnsemblBacteria; AAF95682; AAF95682; VC_2541.
DR   KEGG; vch:VC_2541; -.
DR   PATRIC; fig|243277.26.peg.2419; -.
DR   eggNOG; COG0163; Bacteria.
DR   HOGENOM; CLU_074522_0_0_6; -.
DR   OMA; GATHIQD; -.
DR   BioCyc; VCHO:VC2541-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX-like.
DR   PANTHER; PTHR43374; PTHR43374; 2.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Prenyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..211
FT                   /note="Flavin prenyltransferase UbiX"
FT                   /id="PRO_0000134975"
FT   BINDING         15..17
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         41
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         106..109
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         171
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT   BINDING         187
FT                   /ligand="dimethylallyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:88052"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
SQ   SEQUENCE   211 AA;  22731 MW;  11D78C878DEB1F22 CRC64;
     MSMNNNRTIT LAWTGASGAP YGLRLLQCLL AADYQVYLLI SSAARVVLAT EHGLKLPANP
     EAAQAALVEH LGCASDKLVV CGKEDWFSPV ASGSAAPKQM VVCPCSAGSV AAIAHGMSDN
     LIERAADVVL KERGQLLLVV RETPFSTLHL ENMLKLSHMG VTIMPAAPGF YHQPQSIDDL
     VDFMVARILD HLGIEQALVP RWGYDQRVRG E