ID Q9HXA0_PSEAE Unreviewed; 331 AA.
AC Q9HXA0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN OrderedLocusNames=PA3913 {ECO:0000313|EMBL:AAG07300.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG07300.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG07300.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., 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., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Required for O(2)-independent ubiquinone (coenzyme Q)
CC biosynthesis. Together with UbiV, is essential for the C6-hydroxylation
CC reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02232}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02232};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02232}.
CC -!- SUBUNIT: Forms an heterodimer with UbiV. {ECO:0000256|HAMAP-
CC Rule:MF_02232}.
CC -!- SIMILARITY: Belongs to the peptidase U32 family. UbiU subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02232}.
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DR EMBL; AE004091; AAG07300.1; -; Genomic_DNA.
DR PIR; A83158; A83158.
DR RefSeq; NP_252602.1; NC_002516.2.
DR RefSeq; WP_003093020.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXA0; -.
DR STRING; 208964.PA3913; -.
DR PaxDb; 208964-PA3913; -.
DR DNASU; 878972; -.
DR GeneID; 77219538; -.
DR GeneID; 878972; -.
DR KEGG; pae:PA3913; -.
DR PATRIC; fig|208964.12.peg.4099; -.
DR PseudoCAP; PA3913; -.
DR HOGENOM; CLU_011540_3_2_6; -.
DR InParanoid; Q9HXA0; -.
DR OrthoDB; 9807498at2; -.
DR PhylomeDB; Q9HXA0; -.
DR BioCyc; PAER208964:G1FZ6-3986-MONOMER; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02232; UbiU; 1.
DR InterPro; IPR001539; Peptidase_U32.
DR InterPro; IPR043692; UbiU.
DR PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR PANTHER; PTHR30217:SF3; UBIQUINONE BIOSYNTHESIS PROTEIN UBIU; 1.
DR Pfam; PF01136; Peptidase_U32; 1.
DR PROSITE; PS01276; PEPTIDASE_U32; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW Hydrolase {ECO:0000313|EMBL:AAG07300.1};
KW Iron {ECO:0000256|HAMAP-Rule:MF_02232};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02232};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02232};
KW Protease {ECO:0000313|EMBL:AAG07300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 331 AA; 36025 MW; E0B697D9C4D17D84 CRC64;
MQLVCPAGSL PALKSALRQG ADAIYVGFRD DTNARHFAGL NLDERQLQEG LRRVHEAGRQ
LYVAVNTYSS AQGWERWQRA VDQAADLGVD ALIAADVAVL GYAAKRHPRL NLHLSVQGSA
TNAAALALYH ERYGIRRAVL PRVLSLAQVR QVAAGSPVPV EVFAFGSLCI MAEGRCHLSS
YVTGESPNLC GVCSPARAVR WSEEPEGLTS RLNEVLIDRY AAGEAAGYPT LCKGRFLVNG
QRFHALEEPT SLNTLDLVPQ LAEIGVAAVK IEGRQRSPAY VEQVTRVWRQ ALDSYASAPG
AYSVQPQWQR ALAGLSEGHQ TTLGAYHRSW Q
//
