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Database: UniProt
Entry: A0A1M7DWI8_9RHOB
LinkDB: A0A1M7DWI8_9RHOB
Original site: A0A1M7DWI8_9RHOB 
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}.
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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
//
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