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Database: UniProt
Entry: UBID_HAHCH
LinkDB: UBID_HAHCH
Original site: UBID_HAHCH 
ID   UBID_HAHCH              Reviewed;         488 AA.
AC   Q2SQ75;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   24-JAN-2024, entry version 96.
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=HCH_00286;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC27199.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000155; ABC27199.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2SQ75; -.
DR   SMR; Q2SQ75; -.
DR   STRING; 349521.HCH_00286; -.
DR   KEGG; hch:HCH_00286; -.
DR   eggNOG; COG0043; Bacteria.
DR   HOGENOM; CLU_023348_4_1_6; -.
DR   OrthoDB; 9809841at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000238; 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..488
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_0000267667"
FT   ACT_SITE        287
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   488 AA;  54948 MW;  066DEB9ABB406F4F CRC64;
     MQYRDLRDFI RILEQRGELK RITAEVDPHL EMTEICDRTL RREGPALLFE NPRGYSIPVL
     GNLFGTPGRV ALGMGAESVE SLREIGKLLA FLKEPEPPKG LRDAWSKLPI FKQVMNMGPK
     EVSSASCQEV IIEGDDVDLY QYPIQTCWPG DAGPLVTWPL VITRGPNKAR QNLGIYRQQL
     IGRNKLIMRW LSHRGGALDY REWREAHPME PFPVAVALGA DPATILGAVT PVPDTLSEYA
     FAGLLRGNKT EVVRCIGSDL QAPASAEIVL EGVIHPGEMA PEGPFGDHTG YYNEVDRFPV
     FTVERITQRK KPIYHSTYTG RPPDEPAVLG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RMAVVTMKKQ YPGHAKRVMM GVWSFLRQFM YTKFVIVTDD DVNARDWKDV IWAITTRMDP
     ARDTVMVENT PIDYLDFASP VSGLGSKMGL DATNKWPGET QREWGRTIQM DADVKARVDD
     LWSQLGID
//
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