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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984}; EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984};
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MyHits synonymsUBIX_VIBCH , Q9KP38 , 11D78C878DEB1F22
match map segment
ihamap:ubiX_pad ipfam:Flavoprotein  
Legends: 1, BINDING FMN. {ECO:0000255|HAMAP-Rule:MF_01984}; 2, BINDING DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}; 3, NP_BIND FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
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   30-NOV-2016, entry version 75.
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};
GN   OrderedLocusNames=VC_2541;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; 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.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   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
CC       the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-
CC       polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase
CC       is metal-independent and links a dimethylallyl moiety from
CC       dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms
CC       of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl phosphate + FMNH(2) = prenylated
CC       FMNH(2) + phosphate. {ECO:0000255|HAMAP-Rule:MF_01984}.
CC   -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01984}.
DR   EMBL; AE003852; AAF95682.1; -; Genomic_DNA.
DR   PIR; G82063; G82063.
DR   RefSeq; NP_232169.1; NC_002505.1.
DR   RefSeq; WP_001883898.1; NC_002505.1.
DR   ProteinModelPortal; Q9KP38; -.
DR   STRING; 243277.VC2541; -.
DR   DNASU; 2615558; -.
DR   EnsemblBacteria; AAF95682; AAF95682; VC_2541.
DR   GeneID; 2615558; -.
DR   KEGG; vch:VC2541; -.
DR   PATRIC; 20084105; VBIVibCho83274_2419.
DR   eggNOG; ENOG4108UMA; Bacteria.
DR   eggNOG; COG0163; LUCA.
DR   KO; K03186; -.
DR   OMA; QGLVPRW; -.
DR   BioCyc; VCHO:VC2541-MONOMER; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; ISS:TIGR.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009108; P:coenzyme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:TIGR.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   HAMAP; MF_01984; ubiX_pad; 1.
DR   InterPro; IPR003382; Flavoprotein.
DR   InterPro; IPR004507; UbiX_Pad1.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR00421; ubiX_pad; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Flavoprotein; FMN; Prenyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    211       Flavin prenyltransferase UbiX.
FT                                /FTId=PRO_0000134975.
FT   NP_BIND      15     17       FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
FT   NP_BIND     106    109       FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
FT   BINDING      41     41       FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
FT   BINDING     141    141       FMN. {ECO:0000255|HAMAP-Rule:MF_01984}.
FT   BINDING     171    171       DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}.
FT   BINDING     187    187       DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         7    204       ihamap:ubiX_pad [T]
FT   MYHIT         8    183       ipfam:Flavoprotein [T]
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
//