ID A0A084A3A6_9GAMM Unreviewed; 331 AA.
AC A0A084A3A6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=yhbU_1 {ECO:0000313|EMBL:KEY59785.1};
GN Synonyms=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=SRDD_13640 {ECO:0000313|EMBL:KEY59785.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59785.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY59785.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59785.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEY59785.1}.
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DR EMBL; AYKS02000041; KEY59785.1; -; Genomic_DNA.
DR RefSeq; WP_023489007.1; NZ_AYKS02000041.1.
DR AlphaFoldDB; A0A084A3A6; -.
DR STRING; 1410619.SRDD_13640; -.
DR eggNOG; COG0826; Bacteria.
DR OrthoDB; 9807498at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000017810; 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; IPR036206; ThiamineP_synth_sf.
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.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR PROSITE; PS01276; PEPTIDASE_U32; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_02232};
KW Hydrolase {ECO:0000313|EMBL:KEY59785.1};
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:KEY59785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02232}.
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02232"
SQ SEQUENCE 331 AA; 36929 MW; 803AD957B160C85E CRC64;
MELLCPAGNL PALKAAVDNG ADAIYIGLKD DTNARHFAGL NFTEKKLQEA VDYVHRHGRK
LHIAINTFAH PDGYVRWQRA VDVAAQLGAD ALILADLAML EYAAERYPQV ERHVSVQASA
TNEEAIRFYQ RHFDVARVVL PRVLSMHQVK QLSRTSPVPL EVFAFGSLCI MAEGRCYLSS
YLTGESPNTI GACSPARFVR WQQTAQGMES RLNNVLIDRY QDGENAGYPT LCKGRYLVDN
VLYHPLEEPT SLNTLELLPE LLAANIASVK IEGRQRSPAY VSQVARVWRQ AIDRCIANPA
TYQPDAAWME TLGAMSEGTQ TTLGAYHRKW Q
//
