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Database: UniProt
Entry: B1Y7Z7_LEPCP
LinkDB: B1Y7Z7_LEPCP
Original site: B1Y7Z7_LEPCP 
ID   B1Y7Z7_LEPCP            Unreviewed;       317 AA.
AC   B1Y7Z7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Ubiquinone biosynthesis protein UbiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   Name=ubiV {ECO:0000256|HAMAP-Rule:MF_02233};
GN   OrderedLocusNames=Lcho_1471 {ECO:0000313|EMBL:ACB33739.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB33739.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB33739.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) 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; CP001013; ACB33739.1; -; Genomic_DNA.
DR   RefSeq; WP_012346501.1; NC_010524.1.
DR   AlphaFoldDB; B1Y7Z7; -.
DR   STRING; 395495.Lcho_1471; -.
DR   MEROPS; U32.A01; -.
DR   KEGG; lch:Lcho_1471; -.
DR   eggNOG; COG0826; Bacteria.
DR   HOGENOM; CLU_056172_0_0_4; -.
DR   OMA; CCIKYPT; -.
DR   OrthoDB; 8523349at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001693; 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:UP000001693};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_02233}.
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         207
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
FT   BINDING         211
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02233"
SQ   SEQUENCE   317 AA;  33983 MW;  2C66D1FB54D42EC0 CRC64;
     MTSHSTPLDL TVGPLQYWWP RATLINFYAE LADSPARRIV LGEVICSRRN EFSTEDWLAL
     ARDLTAAGKT VLLASMPLLM SEAELRTLRR IAEQDEFAVE AGDASALQVL ARRPAEQAAR
     HPITLGPHLN IYSHGALIEH AALGADRWVA PLELSLDAIA RINPPDAPVP GVAGPVASEV
     FGFGRMPLAF SARCFTARHH RLNKDECDFR CRDDADGLLL SSTEGQPFLV LNGIQTQSAG
     LQCLIGDAAA MRAAGVSSVR LSPCGQGFAR VLTLFDQVLN HGEPAADAIA ELATLGLPGA
     LVNGYAHRQP GLEEISA
//
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