(data stored in ACNUC7421 zone)

SWISSPROT: UBID_EDWI9

ID   UBID_EDWI9              Reviewed;         495 AA.
AC   C5BCB4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   05-JUL-2017, entry version 55.
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=NT01EI_0150;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67405.1; -; Genomic_DNA.
DR   RefSeq; WP_015869621.1; NC_012779.2.
DR   ProteinModelPortal; C5BCB4; -.
DR   SMR; C5BCB4; -.
DR   STRING; 634503.NT01EI_0150; -.
DR   EnsemblBacteria; ACR67405; ACR67405; NT01EI_0150.
DR   GeneID; 7958750; -.
DR   KEGG; eic:NT01EI_0150; -.
DR   PATRIC; fig|634503.3.peg.141; -.
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; UP000001485; Chromosome.
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; C5BCB4.
DR   SWISS-2DPAGE; C5BCB4.
KW   Cell membrane; Complete proteome; Decarboxylase; Lyase; Manganese;
KW   Membrane; Metal-binding; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN         1    495       3-octaprenyl-4-hydroxybenzoate carboxy-
FT                                lyase.
FT                                /FTId=PRO_1000215808.
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   495 AA;  55772 MW;  A5C280C26D9C82EA CRC64;
     MKYRDLREFI ALLEQRGELK RIQQSIDPYL EMTEIADRTL RVGGPALLFE NPKGYDIPVL
     CNLFGTPQRV ALGMGQEEVG ALRDVGKLLA FLKEPDPPKG FRDLVEKLPQ FKQILNMPTK
     RLSKAPCQEQ VLQGDDVDLA TLPVMHCWPQ DVAPLVSWGL TVTRGPCKSR QNLGIYRQQV
     LGKNKLIMRW LSHRGGALDF QDWCQAHPGE RFPVAVALGA DPATLLAAVT PVPDSLSEYA
     FAGLLRGHKS EVVKCLSCDL EVPASAEIVL EGYIEPGETA PEGPYGDHTG YYNEVERFPV
     FTVTHLTQRD RPIYHSTYTG RPPDEPAVLG LALNEVFVPL LQKQFPEIVD FYLPPEGCSY
     RMAVVTMKKQ YPGHAKRVMM GVWSFLRQFM YTKFVIVCDD DINARDWQDV IWALTTRMDP
     ARDTLLIENT PIDYLDFASP VSGLGSKMGL DATNKWPGET QREWGHPIVM DEAVRARVDT
     LWNELDIFAN DKDAQ
//

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