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Database: UniProt
Entry: A0A011N1B6_9PROT
LinkDB: A0A011N1B6_9PROT
Original site: A0A011N1B6_9PROT 
ID   A0A011N1B6_9PROT        Unreviewed;       487 AA.
AC   A0A011N1B6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase {ECO:0000256|HAMAP-Rule:MF_01636};
DE            EC=4.1.1.98 {ECO:0000256|HAMAP-Rule:MF_01636};
DE   AltName: Full=Polyprenyl p-hydroxybenzoate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01636};
GN   Name=ubiD {ECO:0000256|HAMAP-Rule:MF_01636,
GN   ECO:0000313|EMBL:EXI68666.1};
GN   ORFNames=AW08_00978 {ECO:0000313|EMBL:EXI68666.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI68666.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI68666.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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:0000256|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:0000256|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01636};
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01636};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01636};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01636}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI68666.1}.
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DR   EMBL; JFAX01000004; EXI68666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011N1B6; -.
DR   STRING; 1454001.AW08_00978; -.
DR   PATRIC; fig|1454001.3.peg.924; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000020218; Unassembled WGS sequence.
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   Gene3D; 1.20.5.570; Single helix bin; 1.
DR   Gene3D; 3.40.1670.10; UbiD C-terminal domain-like; 1.
DR   HAMAP; MF_01636; UbiD; 1.
DR   InterPro; IPR002830; UbiD.
DR   InterPro; IPR049381; UbiD-like_C.
DR   InterPro; IPR049383; UbiD-like_N.
DR   InterPro; IPR023677; UbiD_bacteria.
DR   InterPro; IPR048304; UbiD_Rift_dom.
DR   NCBIfam; TIGR00148; UbiD family decarboxylase; 1.
DR   PANTHER; PTHR30108; 3-OCTAPRENYL-4-HYDROXYBENZOATE CARBOXY-LYASE-RELATED; 1.
DR   PANTHER; PTHR30108:SF17; FERULIC ACID DECARBOXYLASE 1; 1.
DR   Pfam; PF01977; UbiD; 1.
DR   Pfam; PF20696; UbiD_C; 1.
DR   Pfam; PF20695; UbiD_N; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR   SUPFAM; SSF143968; UbiD C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01636};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01636};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01636};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01636};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01636};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01636};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01636};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01636}; Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_01636}.
FT   DOMAIN          10..89
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20695"
FT   DOMAIN          123..322
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT                   Rift-related"
FT                   /evidence="ECO:0000259|Pfam:PF01977"
FT   DOMAIN          328..452
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20696"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT   BINDING         175..177
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT   BINDING         189..191
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT   BINDING         194..195
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
SQ   SEQUENCE   487 AA;  54815 MW;  F521BF671C6AC2C2 CRC64;
     MKYHDLRDFI AQLEGMGELR RIAVAVDPRF EMTEICDRVL RAGGPALLFE QPSGHDMPVL
     ANLFGTPRRV ALGMGQESVQ ALREVGKLLA YLKEPEPPRG LRDAWDKLPV LRQVLNMAPR
     LRSSAPCQEV VCDGRDVDLA RLPIQWCWPG DVAPLITWGL TVTRGPHKTR QNLGIYRQQV
     LAPNKLIMRW LAHRGGALDF REHCLQHPGQ RFPVAVALGA DPATILAAVT PVPDSLSEYQ
     FAGLLRGSRT EVVKCLGCEL QVPAAAEIVL EGFIDPQESA LEGPYGDHTG YYNEQARFPV
     FTVERMSMRR QPIYHSTYTG KPPDEPAMLG VALNEVFVPL LQKQFPEIVD FYLPPEGCSY
     RLAAVSLRKQ YPGHAKRVMF GIWSFLRQFM YTKFIIVVDE DVDVRDWKEV IWAMTTRVDA
     ARDTLIVENT PIDYLDFASP VAGLGSKMGI DATNKWPGET AREWGRPIVM DATVKRRVDE
     MWDQLGL
//
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