ID A0A0C5WTW3_9GAMM Unreviewed; 291 AA.
AC A0A0C5WTW3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN ORFNames=H744_2c3173 {ECO:0000313|EMBL:AJR09817.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR09817.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR09817.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR09817.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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; CP005974; AJR09817.1; -; Genomic_DNA.
DR RefSeq; WP_044624167.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WTW3; -.
DR STRING; 658445.H744_2c3173; -.
DR KEGG; pgb:H744_2c3173; -.
DR PATRIC; fig|658445.3.peg.5241; -.
DR HOGENOM; CLU_056172_0_0_6; -.
DR OrthoDB; 8523349at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000032303; Chromosome 2.
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:AJR09817.1};
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:AJR09817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ SEQUENCE 291 AA; 32780 MW; 4295EE11AA056D1D CRC64;
MKYSLGPLLY FWPKMDVEAF YQQAKDANTD IIYLGETVCS KRREMKPAHW FDIAKELSAS
GKQVVLSTMA LLEAPSEVNV MKKYIDNGDF AIEANDVSAI QLAHQNKVPF VVGPAVNCYN
AQTLNLFLKK GMIRWCMPVE LSRQWLQNVA NECEQMGIRD QFETEVFSYG YLPLAYSARC
FTARAEDRAK DDCETCCIKY PTGITVNSQE EQKVFTLNGI QTQSGYCYNL INDQPGMAGL
VDVVRLSPLG IDTLSLVDTF RANQHGGHQH KLEGGHHCNG YWHNLAGLNI E
//
