ID A0A1M7DWI8_9RHOB Unreviewed; 303 AA.
AC A0A1M7DWI8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN ORFNames=SAMN05444398_10682 {ECO:0000313|EMBL:SHL83816.1};
OS Roseovarius pacificus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=337701 {ECO:0000313|EMBL:SHL83816.1, ECO:0000313|Proteomes:UP000183974};
RN [1] {ECO:0000313|EMBL:SHL83816.1, ECO:0000313|Proteomes:UP000183974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29589 {ECO:0000313|EMBL:SHL83816.1,
RC ECO:0000313|Proteomes:UP000183974};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for O(2)-independent ubiquinone (coenzyme Q)
CC biosynthesis. Together with UbiU, is essential for the C6-hydroxylation
CC reaction in the oxygen-independent ubiquinone biosynthesis pathway.
CC {ECO:0000256|HAMAP-Rule:MF_02233}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02233};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02233}.
CC -!- SUBUNIT: Forms an heterodimer with UbiU. {ECO:0000256|HAMAP-
CC Rule:MF_02233}.
CC -!- SIMILARITY: Belongs to the peptidase U32 family. UbiV subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02233}.
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; FRBR01000006; SHL83816.1; -; Genomic_DNA.
DR RefSeq; WP_073035004.1; NZ_FRBR01000006.1.
DR AlphaFoldDB; A0A1M7DWI8; -.
DR STRING; 337701.SAMN05444398_10682; -.
DR OrthoDB; 8523349at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000183974; 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_02233; UbiV; 1.
DR InterPro; IPR001539; Peptidase_U32.
DR InterPro; IPR043693; UbiV.
DR PANTHER; PTHR30217; PEPTIDASE U32 FAMILY; 1.
DR PANTHER; PTHR30217:SF11; UBIQUINONE BIOSYNTHESIS PROTEIN UBIV; 1.
DR Pfam; PF01136; Peptidase_U32; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02233};
KW Hydrolase {ECO:0000313|EMBL:SHL83816.1};
KW Iron {ECO:0000256|HAMAP-Rule:MF_02233};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02233};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02233};
KW Protease {ECO:0000313|EMBL:SHL83816.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183974};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ SEQUENCE 303 AA; 33429 MW; A37A6BFCD20C89CD CRC64;
MELTLGPLAY HWTVERKRDF YARIADEAPV DTVYLGEVIC SKRAPFFERE MPQVIERLQR
GGKRVVLCSL AEVMLKRERQ ATADLMESED HEIEINNAAG LLARDGRSHR VGPFLNAYNE
ATITWMADQG ATHVCLPTEM PGEAVGIAAK AARDLDLGVE VQVFGRAPLA VSARCYHARA
HGRTKDNCQF ICEDDPDGMP LATRDDQPIL RVNGIQTQSE SYIELLAELP EMKALGITHA
RLLPQNVDMV AVAQVFNDVL NSGLDADDGR SRLSTICAGT AFSNGFWHGV AGYRHINRKA
VAA
//