UBIX_AQUAE
ID UBIX_AQUAE Reviewed; 189 AA.
AC O66811;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=aq_528;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06774.1; -; Genomic_DNA.
DR PIR; G70347; G70347.
DR RefSeq; NP_213371.1; NC_000918.1.
DR RefSeq; WP_010880309.1; NC_000918.1.
DR PDB; 2EJB; X-ray; 2.15 A; A=1-189.
DR PDBsum; 2EJB; -.
DR AlphaFoldDB; O66811; -.
DR SMR; O66811; -.
DR STRING; 224324.aq_528; -.
DR EnsemblBacteria; AAC06774; AAC06774; aq_528.
DR KEGG; aae:aq_528; -.
DR PATRIC; fig|224324.8.peg.433; -.
DR eggNOG; COG0163; Bacteria.
DR HOGENOM; CLU_074522_0_0_0; -.
DR InParanoid; O66811; -.
DR OMA; GATHIQD; -.
DR OrthoDB; 1384786at2; -.
DR EvolutionaryTrace; O66811; -.
DR Proteomes; UP000000798; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Prenyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..189
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134954"
FT BINDING 10..12
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 36
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 91..94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 126
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 156
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 172
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:2EJB"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2EJB"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:2EJB"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:2EJB"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:2EJB"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2EJB"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:2EJB"
SQ SEQUENCE 189 AA; 21256 MW; 2EC4B4B65319CF85 CRC64;
MQKIALCITG ASGVIYGIKL LQVLEELDFS VDLVISRNAK VVLKEEHSLT FEEVLKGLKN
VRIHEENDFT SPLASGSRLV HYRGVYVVPC STNTLSCIAN GINKNLIHRV GEVALKERVP
LVLLVREAPY NEIHLENMLK ITRMGGVVVP ASPAFYHKPQ SIDDMINFVV GKLLDVLRIE
HNLYKRWRG
