(data stored in ACNUC7421 zone)

SWISSPROT: UBID_PSEHT

ID   UBID_PSEHT              Reviewed;         488 AA.
AC   Q3IDJ8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 88.
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};
GN   OrderedLocusNames=PSHAa0105;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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: A 4-hydroxy-3-polyprenylbenzoate = a 2-
CC       polyprenylphenol + CO(2). {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       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   -!- 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-
CC       Rule:MF_01636}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01636}.
CC   -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01636}.
DR   EMBL; CR954246; CAI85214.1; -; Genomic_DNA.
DR   RefSeq; WP_011326832.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDJ8; -.
DR   SMR; Q3IDJ8; -.
DR   STRING; 326442.PSHAa0105; -.
DR   EnsemblBacteria; CAI85214; CAI85214; PSHAa0105.
DR   KEGG; pha:PSHAa0105; -.
DR   PATRIC; fig|326442.8.peg.104; -.
DR   eggNOG; ENOG4105D3H; Bacteria.
DR   eggNOG; COG0043; LUCA.
DR   HOGENOM; HOG000227663; -.
DR   KO; K03182; -.
DR   OMA; IDATNKW; -.
DR   OrthoDB; POG091H05QI; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01636; UbiD; 1.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR002830; UbiD.
DR   InterPro; IPR023677; UbiD_bacteria.
DR   Pfam; PF01977; UbiD; 1.
DR   SUPFAM; SSF50475; SSF50475; 1.
DR   TIGRFAMs; TIGR00148; TIGR00148; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IDJ8.
DR   SWISS-2DPAGE; Q3IDJ8.
KW   Cell membrane; Complete proteome; Decarboxylase; Lyase; Manganese;
KW   Membrane; Metal-binding; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN         1    488       3-octaprenyl-4-hydroxybenzoate carboxy-
FT                                lyase.
FT                                /FTId=PRO_0000267679.
FT   REGION      172    177       prenyl-FMN binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01636}.
FT   REGION      194    195       prenyl-FMN binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01636}.
FT   ACT_SITE    287    287       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01636}.
FT   METAL       172    172       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01636}.
FT   METAL       238    238       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01636}.
SQ   SEQUENCE   488 AA;  54990 MW;  38F88BF4478F9609 CRC64;
     MKYKDLRDFI DLLEKRGELK RITQEIDPYL EMTEIADRTL RAKGPALLFE NPKGYDIPVL
     ANLFGTPKRV AMGMGQEDVS ELREVGKLLA FLKEPEPPKG IKEALGQIPV YKQVLNMPAK
     EVKKAPCQEV ILQGDEVDLT KLPIQHCWPG DAAPLITWGL TVTKGPYKKR QNLGIYRQQL
     LGKNKIIMRW LSHRGGALDF QEWCKENPGQ PYPVSVALGA DPATILGAVT PVPDTLSEYA
     FAGLLRGSKT EVVKSISNDL QVPASAEIVL EGYIMPGEMA PEGPYGDHTG YYNEVDDFPV
     MTVTHMTHRK NPIYHSTFTG RPPDEPAILG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RMAIVTMKKQ YPGHAKRVMM GVWSYLRQFM YTKFVIVCDD DINARDWEDV IWAITTRMDP
     ARDTTLIENT PIDYLDFASP VSGLGSKMGM DATNKWPGET NREWGEPIEM DKATKDRVDD
     IWQSLNIL
//

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