ID UBID_HERAR Reviewed; 494 AA.
AC A4G3Y4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 87.
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}; OrderedLocusNames=HEAR1041;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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:
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:0000255|HAMAP-Rule:MF_01636};
CC -!- COFACTOR:
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={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-Rule:MF_01636};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01636}.
CC -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000255|HAMAP-
CC Rule:MF_01636}.
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DR EMBL; CU207211; CAL61221.2; -; Genomic_DNA.
DR AlphaFoldDB; A4G3Y4; -.
DR SMR; A4G3Y4; -.
DR STRING; 204773.HEAR1041; -.
DR KEGG; har:HEAR1041; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_4_1_4; -.
DR OrthoDB; 9809841at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000006697; Chromosome.
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; Decarboxylase; Flavoprotein; FMN; Lyase; Manganese;
KW Membrane; Metal-binding; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..494
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT /id="PRO_1000186714"
FT ACT_SITE 294
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 175..177
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 189..191
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 194..195
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ SEQUENCE 494 AA; 55611 MW; 3733C335566F86CB CRC64;
MKYSDLRDFI SQLQQMGELK RINMPVSPYL EMTEICDRTL RAEGPALLFE NPTGHTIPVL
GNLFGTPQRV ALGMGATDVS ELRKIGHVLA MLKEPEPPKG FKDMLGLGSL VKSLWDMTPK
ERRDAPCHDI VWEGNDVDLA RLPIQHCWPG DIAPLITWGL VITKGPHKKR QNLGIYRQQV
IGRNKVIMRW LAQRGGALDF REHSIANRGQ PYPIAVALGA DPATILGAVT PVPDSLSEYQ
FAGLLRGSRT ELVKAIGSEL RVPASAEIVL EGHIYPDESH PSGYEHALEG PYGDHTGYYN
EQDTFPVFTI DRITMRRDPI YHSTYTGKPP DEPAILGVAL NEVFIPLLQK QFSEILDFYL
PPEGCSYRMA VVQMKKAYPG HAKRVMFGVW SFLRQFMYTK FIIVVDEDVN IRDWKEVIWA
ITTRVDPTRD TTLVDNTPID YLDFASPVSG LGSKMGIDAT NKWPGETDRE WGTTITMTPE
VKKRVDQIWQ ELGI
//
