UBIX_PSEAE
ID UBIX_PSEAE Reviewed; 209 AA.
AC Q9HX08;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000303|PubMed:26083743};
DE EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000269|PubMed:26083743};
GN Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000303|PubMed:26083743};
GN OrderedLocusNames=PA4019;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN.
RX PubMed=22102023; DOI=10.1107/s174430911102923x;
RA Kopec J., Schnell R., Schneider G.;
RT "Structure of PA4019, a putative aromatic acid decarboxylase from
RT Pseudomonas aeruginosa.";
RL Acta Crystallogr. F 67:1184-1188(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH FMN AND DMAP,
RP FUNCTION, MUTAGENESIS OF GLU-49, AND CATALYTIC ACTIVITY.
RX PubMed=26083743; DOI=10.1038/nature14559;
RA White M.D., Payne K.A., Fisher K., Marshall S.A., Parker D., Rattray N.J.,
RA Trivedi D.K., Goodacre R., Rigby S.E., Scrutton N.S., Hay S., Leys D.;
RT "UbiX is a flavin prenyltransferase required for bacterial ubiquinone
RT biosynthesis.";
RL Nature 522:502-506(2015).
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 ECO:0000269|PubMed:26083743}.
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 ECO:0000269|PubMed:26083743};
CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01984}.
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DR EMBL; AE004091; AAG07406.1; -; Genomic_DNA.
DR PIR; H83144; H83144.
DR RefSeq; NP_252708.1; NC_002516.2.
DR RefSeq; WP_003093227.1; NZ_QZGE01000038.1.
DR PDB; 3ZQU; X-ray; 1.50 A; A=1-209.
DR PDB; 4ZAF; X-ray; 1.71 A; A=1-209.
DR PDB; 4ZAG; X-ray; 1.68 A; A=1-209.
DR PDB; 4ZAL; X-ray; 1.62 A; A=1-209.
DR PDB; 4ZAN; X-ray; 1.76 A; A=1-209.
DR PDB; 4ZAV; X-ray; 1.40 A; A=1-209.
DR PDB; 4ZAW; X-ray; 1.89 A; A=1-209.
DR PDB; 4ZAX; X-ray; 1.61 A; A=1-209.
DR PDB; 4ZAY; X-ray; 1.54 A; A=1-209.
DR PDB; 4ZAZ; X-ray; 1.45 A; A=1-209.
DR PDBsum; 3ZQU; -.
DR PDBsum; 4ZAF; -.
DR PDBsum; 4ZAG; -.
DR PDBsum; 4ZAL; -.
DR PDBsum; 4ZAN; -.
DR PDBsum; 4ZAV; -.
DR PDBsum; 4ZAW; -.
DR PDBsum; 4ZAX; -.
DR PDBsum; 4ZAY; -.
DR PDBsum; 4ZAZ; -.
DR AlphaFoldDB; Q9HX08; -.
DR SMR; Q9HX08; -.
DR DIP; DIP-61586N; -.
DR STRING; 287.DR97_3848; -.
DR PaxDb; Q9HX08; -.
DR PRIDE; Q9HX08; -.
DR DNASU; 878992; -.
DR EnsemblBacteria; AAG07406; AAG07406; PA4019.
DR GeneID; 878992; -.
DR KEGG; pae:PA4019; -.
DR PATRIC; fig|208964.12.peg.4211; -.
DR PseudoCAP; PA4019; -.
DR HOGENOM; CLU_074522_0_0_6; -.
DR InParanoid; Q9HX08; -.
DR OMA; GATHIQD; -.
DR PhylomeDB; Q9HX08; -.
DR BioCyc; MetaCyc:MON-19454; -.
DR BioCyc; PAER208964:G1FZ6-4092-MON; -.
DR BRENDA; 2.5.1.129; 5087.
DR EvolutionaryTrace; Q9HX08; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0106141; F:flavin prenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:PseudoCAP.
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..209
FT /note="Flavin prenyltransferase UbiX"
FT /id="PRO_0000134970"
FT BINDING 13..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:22102023"
FT BINDING 39
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:22102023"
FT BINDING 104..107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:22102023"
FT BINDING 116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:22102023"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:22102023"
FT BINDING 169
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:26083743"
FT BINDING 185
FT /ligand="dimethylallyl phosphate"
FT /ligand_id="ChEBI:CHEBI:88052"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01984,
FT ECO:0000269|PubMed:26083743"
FT MUTAGEN 49
FT /note="E->Q: Severely compromises catalytic activity."
FT /evidence="ECO:0000269|PubMed:26083743"
FT MUTAGEN 169
FT /note="Y->F: Severely compromises catalytic activity."
FT /evidence="ECO:0000269|PubMed:26083743"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:4ZAV"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:4ZAV"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:4ZAV"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4ZAV"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:4ZAV"
SQ SEQUENCE 209 AA; 22367 MW; 01FD081CC495D3F6 CRC64;
MSGPERITLA MTGASGAQYG LRLLDCLVQE EREVHFLISK AAQLVMATET DVALPAKPQA
MQAFLTEYCG AAAGQIRVFG QNDWMAPPAS GSSAPNAMVI CPCSTGTLSA VATGACNNLI
ERAADVALKE RRPLVLVPRE APFSSIHLEN MLKLSNLGAV ILPAAPGFYH QPQSVEDLVD
FVVARILNTL GIPQDMLPRW GEQHLVSDE
