(data stored in SCRATCH zone)

SWISSPROT: C3MHE7_SINFN

ID   C3MHE7_SINFN            Unreviewed;       319 AA.
AC   C3MHE7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS00711828};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS00336940};
DE   AltName: Full=4-HB polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635};
GN   Name=ubiA {ECO:0000256|HAMAP-Rule:MF_01635};
GN   OrderedLocusNames=NGR_c04790 {ECO:0000313|EMBL:ACP24275.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24275.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24275.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB)
CC       with an all-trans polyprenyl group. Mediates the second step in
CC       the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis,
CC       which is the condensation of the polyisoprenoid side chain with
CC       PHB, generating the first membrane-bound Q intermediate 3-
CC       octaprenyl-4-hydroxybenzoate. {ECO:0000256|HAMAP-Rule:MF_01635,
CC       ECO:0000256|SAAS:SAAS00711820}.
CC   -!- CATALYTIC ACTIVITY: 4-hydroxybenzoate + farnesylfarnesylgeraniol =
CC       3-octaprenyl-4-hydroxybenzoate. {ECO:0000256|HAMAP-Rule:MF_01635,
CC       ECO:0000256|SAAS:SAAS00711817}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01635, ECO:0000256|SAAS:SAAS00377743};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS00188628}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01635, ECO:0000256|SAAS:SAAS00711827}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01635,
CC       ECO:0000256|SAAS:SAAS00711827}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS00534287}.
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DR   EMBL; CP001389; ACP24275.1; -; Genomic_DNA.
DR   RefSeq; WP_012707060.1; NC_012587.1.
DR   RefSeq; YP_002825028.1; NC_012587.1.
DR   STRING; 394.NGR_c04790; -.
DR   EnsemblBacteria; ACP24275; ACP24275; NGR_c04790.
DR   GeneID; 7791705; -.
DR   KEGG; rhi:NGR_c04790; -.
DR   PATRIC; fig|394.7.peg.3286; -.
DR   eggNOG; ENOG4105C4G; Bacteria.
DR   eggNOG; COG0382; LUCA.
DR   HOGENOM; HOG000003697; -.
DR   KO; K03179; -.
DR   OMA; WTLGFDT; -.
DR   OrthoDB; POG091H03R0; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01635; UbiA; 1.
DR   InterPro; IPR031103; HB_octoprenylTrfase.
DR   InterPro; IPR006370; HB_polyprenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHE7.
DR   SWISS-2DPAGE; C3MHE7.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00711821};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00711823};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00711829};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00415574};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00415579, ECO:0000313|EMBL:ACP24275.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00415577};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00415562};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00414999}.
FT   TRANSMEM     46     65       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM     72     90       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    132    159       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    171    187       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    193    210       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    241    258       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    264    284       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    296    315       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
SQ   SEQUENCE   319 AA;  34986 MW;  E3409F3C0964AE90 CRC64;
     MNSSSVDSGR VHDAPSKNWV YRVLPRALWP YAQLARWDRP IGWQLLMWPC LWSAALAGGA
     AAALGSFSPA RFLFHVILFV AGAIAMRGAG CTYNDIVDHE IDMEVARTRS RPLPSGRVTR
     AQAKVFMVLQ ALVGLVVLLQ FNAFTVFLGI ASLGLVAIYP FAKRFTDWPQ FFLGLAFSWG
     AIMGWSAEFG SLSFAAVLLY AAAIAWTIGY DTIYAYQDRE DDALIGVRST ARRFGDNPRP
     WLIGLYGLTI LLMFLAFLAA GTGFFAHVGL VVAAVMLAYQ ILVLNIHDPE QCLALFKFNG
     VVGLIVFAGM VLALLPRLI
//

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