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Database: UniProt
Entry: A0A0W8J9R9_9VIBR
LinkDB: A0A0W8J9R9_9VIBR
Original site: A0A0W8J9R9_9VIBR 
ID   A0A0W8J9R9_9VIBR        Unreviewed;       488 AA.
AC   A0A0W8J9R9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase {ECO:0000256|ARBA:ARBA00018597, 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|ARBA:ARBA00030393, ECO:0000256|HAMAP-Rule:MF_01636};
GN   Name=ubiD {ECO:0000256|HAMAP-Rule:MF_01636};
GN   ORFNames=VRK_38200 {ECO:0000313|EMBL:KUI96965.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI96965.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI96965.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI96965.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-2015) 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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|ARBA:ARBA00004749, ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643,
CC       ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202,
CC       ECO:0000256|HAMAP-Rule:MF_01636}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|HAMAP-Rule:MF_01636}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000256|ARBA:ARBA00010021,
CC       ECO:0000256|HAMAP-Rule:MF_01636}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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:KUI96965.1}.
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DR   EMBL; LQIY01000037; KUI96965.1; -; Genomic_DNA.
DR   RefSeq; WP_059122893.1; NZ_KQ947476.1.
DR   AlphaFoldDB; A0A0W8J9R9; -.
DR   STRING; 1761910.VRK_38200; -.
DR   PATRIC; fig|1761910.3.peg.3877; -.
DR   OrthoDB; 9809841at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000054473; 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};
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         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   488 AA;  55308 MW;  9C4057F8B466377E CRC64;
     MIFKDLRDFI DYLEKHGQLK RIQHPIDPQY EMTEICDRTL RAGGPALLFE NPVGYDIPVL
     TNLFGTPQRV AMGMGRVDVS ELREIGQLLA YLKEPEPPKG FKDALDKLPV FKQVLNMPVK
     RLKKAPCQEI IWQGDDVDLD KIPVMRCWPG DVAPLLTWGL TITKGPTKKR QNLGIYRQQK
     LSKNKVIMRW FQHRGGALDF RDWQVEHPGE PFPVSVAFGA DPATILGAVT PVPDTLSEYA
     FAGLLRGSKT EVVQSISNDL EVPASAEIVL EGYIDPNEYA DEGPYGDHTG YFNEVERHHV
     FTVTHVTMRK QPIYHSTYTG RPPDEPAVLG EALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RMAVVTIKKQ YPGHAKRVMM GVWSFLRQFM YTKFVIVCDD DINARDWKDV IWAITTRMDP
     ARDTTMVEST PIDSLDFASP VSGLGSKMGL DATNKWEGET AREWGKEIRK DPEVVSKIDA
     IWDELGIL
//
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