ID A0A0P1GVH7_9RHOB Unreviewed; 327 AA.
AC A0A0P1GVH7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=yhbU_2 {ECO:0000313|EMBL:CUH86942.1};
GN Synonyms=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=PH5382_00861 {ECO:0000313|EMBL:CUH86942.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH86942.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH86942.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH86942.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSG01000003; CUH86942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1GVH7; -.
DR STRING; 1712645.PH5382_00861; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000050782; 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_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:CUH86942.1};
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:CUH86942.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 234
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 327 AA; 34721 MW; 7829D9FC4FCDB27E CRC64;
MVMEIVCPAG TPASLRAAVK AGAHTVYCGF NDVTNARNFP GLNFDRAEMR EGVAFAHAHG
AKVLVAINTF PRAGAEDIWQ RAVADAAAAG ADAVILADPG LLDYAARNHP QIRRHLSVQA
AAANADVINF YAETFGVKRV VLPRVLSVPE IAAINAETEV ETEVFVFGGL CVMAEGRCSL
SSYATGLSPN MNGVCSPASH VEYRDTGGVL DARLGGYTIH QVGKDEPAPY PTLCKGCFSA
SGKQGHLFED PVSLNAEQLI PQLQRAGVTA LKIEGRQRSR SYVAQVVRNF RAAVDALEAG
QPLPVGMLAR LSEGQATTTG AYKKTWR
//
