ID W0I1X7_9GAMM Unreviewed; 331 AA.
AC W0I1X7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ubiquinone biosynthesis protein UbiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN Name=yhbU {ECO:0000313|EMBL:AHF78433.1};
GN Synonyms=ubiU {ECO:0000256|HAMAP-Rule:MF_02232};
GN ORFNames=Sant_3444 {ECO:0000313|EMBL:AHF78433.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF78433.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF78433.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF78433.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(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}.
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DR EMBL; CP006569; AHF78433.1; -; Genomic_DNA.
DR RefSeq; WP_025423567.1; NZ_CP006569.1.
DR AlphaFoldDB; W0I1X7; -.
DR KEGG; sod:Sant_3444; -.
DR PATRIC; fig|1239307.3.peg.3798; -.
DR HOGENOM; CLU_011540_3_2_6; -.
DR OrthoDB; 9807498at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000019028; 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_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 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 Reference proteome {ECO:0000313|Proteomes:UP000019028};
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; 36800 MW; D047431A96E9FB6A CRC64;
MELLCPAGNL PALKAAIDNG ADAVYIGLKD DTNARHFAGL NFTDQRLQEA ERYVHRHGRK
LHIAINTFAH PDGYARWQRA IDMAAQSGAD ALILADLAML AYAAERYPAI ERHVSVQASA
TNQAAIRFYQ QQFDVARVVL PRVLSIHQVK QLAQVSPVPL EVFAFGSLCI MAEGRCYLSS
YLTGESPNTV GACSPARFVR WQQTAAGMEA RLNNVLIDRY QPDENAGYPT LCKGRYLVDG
QRYHALEEPT SLNTLALLPA LFAANIASVK IEGRQRSPAY VSQVTRVWRQ AIDRCRANPD
AYRPEDAWNQ TLAAMSEGVQ TTLGAYHRRW Q
//