UBIX_ARCFU
ID UBIX_ARCFU Reviewed; 182 AA.
AC O29054;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=AF_1214;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90031.1; -; Genomic_DNA.
DR PIR; E69401; E69401.
DR RefSeq; WP_010878709.1; NC_000917.1.
DR PDB; 6M8T; X-ray; 1.67 A; A=1-182.
DR PDB; 6M8U; X-ray; 2.22 A; A=1-182.
DR PDBsum; 6M8T; -.
DR PDBsum; 6M8U; -.
DR AlphaFoldDB; O29054; -.
DR SMR; O29054; -.
DR STRING; 224325.AF_1214; -.
DR EnsemblBacteria; AAB90031; AAB90031; AF_1214.
DR GeneID; 24794819; -.
DR KEGG; afu:AF_1214; -.
DR eggNOG; arCOG01703; Archaea.
DR HOGENOM; CLU_074522_2_1_2; -.
DR OMA; GATHIQD; -.
DR OrthoDB; 112962at2157; -.
DR PhylomeDB; O29054; -.
DR Proteomes; UP000002199; Chromosome.
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..182
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134977"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 35
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 86..89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 121
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 151
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 167
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6M8T"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:6M8T"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:6M8T"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6M8T"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6M8T"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:6M8T"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:6M8T"
SQ SEQUENCE 182 AA; 19968 MW; 65F015F4ED130768 CRC64;
MRFVVALTGA SGQILGIRLI EKLTELGAEV YAVASRAAKI TLKAETDYDE GYVREIATKY
YDEDEIAAPF ASGSFRHDGM AVVPCSIKTA SSIAYGIADN LIARAADVTL KEKRRLVLAI
REAPLHSGHL KTLARLAEMG AVIFPPVLSF YTRPKSVDDL IEHTVSRIAE QLGVEVDYRR
WG
