UBIX_METJA
ID UBIX_METJA Reviewed; 184 AA.
AC Q57566;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=MJ0102;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98082.1; -; Genomic_DNA.
DR PIR; F64312; F64312.
DR RefSeq; WP_010869594.1; NC_000909.1.
DR PDB; 6M8V; X-ray; 2.22 A; A=1-184.
DR PDBsum; 6M8V; -.
DR AlphaFoldDB; Q57566; -.
DR SMR; Q57566; -.
DR STRING; 243232.MJ_0102; -.
DR EnsemblBacteria; AAB98082; AAB98082; MJ_0102.
DR GeneID; 1450941; -.
DR KEGG; mja:MJ_0102; -.
DR eggNOG; arCOG01703; Archaea.
DR HOGENOM; CLU_074522_0_0_2; -.
DR InParanoid; Q57566; -.
DR OMA; GATHIQD; -.
DR OrthoDB; 112962at2157; -.
DR PhylomeDB; Q57566; -.
DR Proteomes; UP000000805; 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..184
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134978"
FT BINDING 9..11
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 34
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 85..88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 150
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984"
FT BINDING 166
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:6M8V"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:6M8V"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:6M8V"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:6M8V"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6M8V"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6M8V"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:6M8V"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:6M8V"
SQ SEQUENCE 184 AA; 20643 MW; F3EDBFE5B48A82C5 CRC64;
MKIIVCITGA SGVIYAKRLL EVLKDRAEVN LIISNSAKKI IKEELDIDWK EIKKLATDYY
ENDDFFSPLA SGSNKFDAVV VVPCSMKTLS AIANGYSANL IVRVCDIALK ERRKLIIMPR
EMPFNSIHLE NMLKLSNLGA IVMPPIPAFY NKPKNVNDII NFVVGRVLDI LGIDNSLFKR
WGTV
