ID A0A2I8DL84_9BURK Unreviewed; 298 AA.
AC A0A2I8DL84;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN ORFNames=C2U31_19435 {ECO:0000313|EMBL:AUT47980.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT47980.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
RL Submitted (JAN-2018) 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; CP026124; AUT47980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DL84; -.
DR KEGG; achr:C2U31_19435; -.
DR OrthoDB; 8523349at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000236176; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT BINDING 179
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"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ SEQUENCE 298 AA; 32443 MW; F02671BCEECF042E CRC64;
MNATPAFSIS VGPLLYYWPR QQTLDFYADL ADGPADIIYV GETVCSRRHE LRAEDWLDLA
RDLRATGKTV VLSGRTLIET GSEAGALRKL CEQQDFLIEA GEVGALRHLG GRPFVAGPHM
NAYHGGTLDW LASRGAVRFV APLEMDSATL ARLLAEKPAA LECEVMVWGR MALAFSARCF
TARHFRLKKD DCGFRCIEHP DGLDLRTRES RDFLAINGIQ VQSAACLDLL DQAMELAVMG
ARVLRVSPQS TGTQAAIAAL DATRHGAPAA EVAPPAGMER CNGYYYGHAG IDLLREPA
//