ID A0A0S2JXK4_9GAMM Unreviewed; 512 AA.
AC A0A0S2JXK4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=PP2015_68 {ECO:0000313|EMBL:ALO40597.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO40597.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO40597.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO40597.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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=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}.
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DR EMBL; CP013187; ALO40597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2JXK4; -.
DR STRING; 161398.PP2015_68; -.
DR KEGG; pphe:PP2015_68; -.
DR PATRIC; fig|161398.10.peg.69; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000061457; 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: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:UP000061457};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_01636}.
FT DOMAIN 30..109
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20695"
FT DOMAIN 141..342
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT Rift-related"
FT /evidence="ECO:0000259|Pfam:PF01977"
FT DOMAIN 348..472
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20696"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT BINDING 195..197
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT BINDING 209..211
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT BINDING 214..215
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01636"
SQ SEQUENCE 512 AA; 57575 MW; 652B012BB6F347B4 CRC64;
MPFSPHLDIL RDNEKCPMPT MKYKDLRDFI TRLEEQGELV RVKQPISTKL EMTEIADRTL
RAGGPAILFE NPEGFDIPVL ANLFGTPKRV AMGMGQTDVS ELREVGKLLA FLKEPEPPKG
IKEALGQIPV FKQVLNMPAK EVRKAPCQQV ILSGDDVDLT KLPIQHCWPG DAAPLITWGL
TVTRGPYKKR QNLGIYRQQL LGKNKIIMRW LSHRGGALDY QEWCKEHPGE PYPVSVALGA
DPATILGAVT PVPDTLSEYA FAGLLRGSKT EVVKSVSNDL QVPASAEIVL EGYIEQDEMA
PEGPYGDHTG YYNEVDDFPV MTVTHITHRE NPIYHSTYTG RPPDEPAILG VALNEVFVPI
LQKQFPEIVD FYLPPEGCSY RMAVVTMKKQ YPGHAKRVMM GVWSFLRQFM YTKFVIVCDD
DVNARDWNDV IWAITTRMDP ARDTTMIEST PIDYLDFASP VSGLGSKMGM DATNKWPGET
DREWGESIVM DESTKQRVDE IWDSLNIMSL NK
//
