ID A0A2K8K9W4_9RHOB Unreviewed; 325 AA.
AC A0A2K8K9W4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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=BG454_07820 {ECO:0000313|EMBL:ATX65746.1};
OS Rhodobaca barguzinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobaca.
OX NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX65746.1, ECO:0000313|Proteomes:UP000228948};
RN [1] {ECO:0000313|EMBL:ATX65746.1, ECO:0000313|Proteomes:UP000228948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT alga05 Genome.";
RL Submitted (NOV-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}.
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DR EMBL; CP024899; ATX65746.1; -; Genomic_DNA.
DR RefSeq; WP_071480296.1; NZ_SODJ01000003.1.
DR AlphaFoldDB; A0A2K8K9W4; -.
DR STRING; 441209.GCA_001870665_01341; -.
DR KEGG; rbg:BG454_07820; -.
DR OrthoDB; 9758184at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000228948; 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW Hydrolase {ECO:0000313|EMBL:ATX65746.1};
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:ATX65746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000228948};
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 325 AA; 34152 MW; 43BDF75D997EC539 CRC64;
MELVCPAGTP AALRAAVDAG AHCIYCGFAD ETNARNFPGL NFSRAELAEA VGYAHARGAK
VLVAINTFPT AGQEALWHSA VADAERAGAD AVILADLGLL AYTAEHHPDL RRHLSVQAAA
ANPDAINFYA SAFDVRRVVL PRVLSVEEIA AINKEIDVET EVFVFGGLCV MAEGRCSLSS
YATGRSPNMN GVCSPPEHVD YATEGNESVA RLGGFTIHRT PKGGAAPYPT LCKGCFTSGD
KTGHVFEDAV SLDASALVPR LAQAGVTALK IEGRQRSKAY VAQIVRAFRA VTDALDEGRA
PPALALARLS EGQAATTGAY AKTWR
//
