(data stored in SCRATCH zone)

SWISSPROT: UBID_PSEU2

ID   UBID_PSEU2              Reviewed;         488 AA.
AC   Q4ZZP7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase {ECO:0000255|HAMAP-Rule:MF_01636};
DE            EC=4.1.1.98 {ECO:0000255|HAMAP-Rule:MF_01636};
DE   AltName: Full=Polyprenyl p-hydroxybenzoate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01636};
GN   Name=ubiD {ECO:0000255|HAMAP-Rule:MF_01636}; OrderedLocusNames=Psyr_0302;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy
CC       benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-
CC         trans-polyprenylphenol + CO2; Xref=Rhea:RHEA:41680, Rhea:RHEA-
CC         COMP:9514, Rhea:RHEA-COMP:9516, ChEBI:CHEBI:1269, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:78396; EC=4.1.1.98;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01636};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01636}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY35375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000075; AAY35375.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_233413.1; NC_007005.1.
DR   SMR; Q4ZZP7; -.
DR   STRING; 205918.Psyr_0302; -.
DR   PRIDE; Q4ZZP7; -.
DR   EnsemblBacteria; AAY35375; AAY35375; Psyr_0302.
DR   GeneID; 3365778; -.
DR   KEGG; psb:Psyr_0302; -.
DR   PATRIC; fig|205918.7.peg.304; -.
DR   eggNOG; ENOG4105D3H; Bacteria.
DR   eggNOG; COG0043; LUCA.
DR   HOGENOM; HOG000227663; -.
DR   KO; K03182; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; 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_01636; UbiD; 1.
DR   InterPro; IPR002830; UbiD.
DR   InterPro; IPR023677; UbiD_bacteria.
DR   PANTHER; PTHR30108; PTHR30108; 1.
DR   Pfam; PF01977; UbiD; 1.
DR   TIGRFAMs; TIGR00148; TIGR00148; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZP7.
DR   SWISS-2DPAGE; Q4ZZP7.
KW   Cell membrane; Decarboxylase; Flavoprotein; FMN; Lyase; Manganese;
KW   Membrane; Metal-binding; Ubiquinone biosynthesis.
FT   CHAIN           1..488
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_0000267684"
FT   REGION          175..177
FT                   /note="Prenyl-FMN binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   REGION          189..191
FT                   /note="Prenyl-FMN binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   REGION          194..195
FT                   /note="Prenyl-FMN binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   METAL           172
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   METAL           238
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ   SEQUENCE   488 AA;  54580 MW;  840FD7C2036DD00F CRC64;
     MKFKDLRDFV QQLEQRGELK RIQMPISPVL EMTEICDRTL RAKGPALLFE KPVGFDIPVL
     GNLFGTPERV AMGMGAEAVS ELREIGKLLA FLKEPEPPKG LKDAWSKLPI FRKVIAMAPK
     VVKDAPCQEV VIEGDDVDLG MLPVQTCWPG DVAPLITWGL TVTKGPNKER QNLGIYRQQV
     IGRNKIIMRW LSHRGGALDF RDWCVKHPGE PYPVAVALGA DPATILGAVT PVPDSLSEYA
     FAGLLRGSRT ELIKCRGSNL QVPASAEIVL EGVIHPGEMA DEGPYGDHTG YYNEVDSFPV
     LTVERITHRI KPIYHSTYTG RPPDEPAILG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RMAVVTIKKQ YPGHAKRVML GVWSFLRQFM YTKFVIVTDD DINARDWNDV IWAITTRMDP
     KRDTVMIDNT PIDYLDFASP VSGLGSKMGL DATNKWPGET SREWGRAIVK DEATTRRVDE
     IWTQLGID
//

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