ID A0A1X7J3Q0_9RHOB Unreviewed; 330 AA.
AC A0A1X7J3Q0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=SAMN02746000_01208 {ECO:0000313|EMBL:SMG22203.1};
OS Paracoccus sp. J56.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=935850 {ECO:0000313|EMBL:SMG22203.1, ECO:0000313|Proteomes:UP000193912};
RN [1] {ECO:0000313|Proteomes:UP000193912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J56 {ECO:0000313|Proteomes:UP000193912};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FXAQ01000006; SMG22203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7J3Q0; -.
DR STRING; 935850.SAMN02746000_01208; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000193912; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW Hydrolase {ECO:0000313|EMBL:SMG22203.1};
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:SMG22203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193912};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 170
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 330 AA; 34903 MW; 7AC6C212459192B9 CRC64;
MMELVCPAGT PAALRAAVDA GAHTVYCGFA DETNARNFPG LNFSREEMAQ GIAYAHARGA
KVLIAINTFP RAGDQALWHR AVSDAAGLDA DAVILADPGL IAHAAQTHPH LRLHLSVQAA
AANPDAINFH ARTFGIRRVV LPRVLSVEEI TAINREIDIE TEVFVFGGLC VMAEGRCSLS
SYATGLSPNM NGVCSPASHV AYADTGGNHE ARLGEFLIHR TPKGMPVPYP TLCKGCFTSP
GDGSSQTGHI FEDPVSLDAT RLIPALQKAG VTALKIEGRQ RSRAYVAQVV RAFRAAVEAA
DQGAPMPEGL LARLTEGQAA TTGAYAKTWR
//
