ID UBID_ECOL5 Reviewed; 498 AA.
AC Q0TAL3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=ECP_4056;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG72016.1; -; Genomic_DNA.
DR RefSeq; WP_000339823.1; NC_008253.1.
DR AlphaFoldDB; Q0TAL3; -.
DR SMR; Q0TAL3; -.
DR KEGG; ecp:ECP_4056; -.
DR HOGENOM; CLU_023348_4_1_6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009182; 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; Ubiquinone biosynthesis.
FT CHAIN 1..498
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT /id="PRO_0000267665"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 176
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 179..181
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 193..195
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 198..199
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ SEQUENCE 498 AA; 55832 MW; 299482D865544121 CRC64;
MDAMKYNDLR DFLTLLEQQG ELKRITLPVD PHLEITEIWL DRTLRAGGPA LLFENPKGYS
MPVLCNLFGT PKRVAMGMGQ EDVSALREVG KLLAFLKEPE PPKGFRDLFD KLPQFKQVLN
MPTKRLRGAP CQQKIVSGDD VDLNRIPIMT CWPEDAAPLI TWGLTVTRGP HKERQNLGIY
RQQLIGKNKL IMRWLSHRGG ALDYQEWCAA HPGERFPVSV ALGADPATIL GAVTPVPDTL
SEYAFAGLLR GTKTEVVKCI SNDLEVPASA EIVLEGYIEQ GETAPEGPYG DHTGYYNEVD
SFPVFTVTHI TQREDAIYHS TYTGRPPDEP AVLGVALNEV FVPILQKQFP EIVDFYLPPE
GCSYRLAVVT IKKQYAGHAK RVMMGVWSFL RQFMYTKFVI VCDDDVNARD WNDVIWAITT
RMDPARDTVL VENTPIDYLD FASPVSGLGS KMGLDATNKW PGETQREWGR PIKKDPDVVA
HIDAIWDELA IFNNGKSA
//
