ID G6F041_9PROT Unreviewed; 476 AA.
AC G6F041;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phenolic acid decarboxylase {ECO:0000256|HAMAP-Rule:MF_01985};
DE Short=PAD {ECO:0000256|HAMAP-Rule:MF_01985};
DE EC=4.1.1.- {ECO:0000256|HAMAP-Rule:MF_01985};
GN ORFNames=CIN_09870 {ECO:0000313|EMBL:EHD14123.1};
OS Commensalibacter intestini A911.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14123.1, ECO:0000313|Proteomes:UP000005939};
RN [1] {ECO:0000313|EMBL:EHD14123.1, ECO:0000313|Proteomes:UP000005939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A911 {ECO:0000313|EMBL:EHD14123.1,
RC ECO:0000313|Proteomes:UP000005939};
RA Lee W.-J., Kim E.-K.;
RT "Genome Sequence of Commensalibacter intestini A911, isolated from
RT Drosophila gut.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC detoxification of phenolic derivatives. {ECO:0000256|HAMAP-
CC Rule:MF_01985}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01985};
CC -!- COFACTOR:
CC Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01985};
CC Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01985};
CC -!- SIMILARITY: Belongs to the UbiD family. YclC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01985}.
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:EHD14123.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGFR01000005; EHD14123.1; -; Genomic_DNA.
DR RefSeq; WP_008853977.1; NZ_AGFR01000005.1.
DR AlphaFoldDB; G6F041; -.
DR STRING; 1088868.CIN_09870; -.
DR PATRIC; fig|1088868.3.peg.991; -.
DR eggNOG; COG0043; Bacteria.
DR OrthoDB; 9809841at2; -.
DR Proteomes; UP000005939; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1670.10; UbiD C-terminal domain-like; 1.
DR HAMAP; MF_01985; UbiD_YclC; 1.
DR InterPro; IPR032902; BsdC.
DR InterPro; IPR002830; UbiD.
DR InterPro; IPR049381; UbiD-like_C.
DR InterPro; IPR049383; UbiD-like_N.
DR InterPro; IPR048304; UbiD_Rift_dom.
DR NCBIfam; TIGR00148; UbiD family decarboxylase; 1.
DR NCBIfam; NF041204; VdcC; 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 Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01985};
KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01985};
KW Detoxification {ECO:0000256|HAMAP-Rule:MF_01985};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01985};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01985};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01985};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_01985};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01985}.
FT DOMAIN 10..90
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20695"
FT DOMAIN 107..309
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-likw
FT Rift-related"
FT /evidence="ECO:0000259|Pfam:PF01977"
FT DOMAIN 315..438
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20696"
FT ACT_SITE 274
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
FT BINDING 161..166
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
FT BINDING 182..183
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01985"
SQ SEQUENCE 476 AA; 52823 MW; 4850CB356B5430BB CRC64;
MAYDDLRSFL KALEDYGQLL HIEEEVNAEP DIAAAANATG RIGDGAPAIS FTNIKGFKEA
HVVMNTIGSW KNHAISLSLP PNTTIRQQID EFIRRWDQYP VKPERRDNPA WAENVVDGEA
INLFDILPLF RLNDGDGGFY LDKACVVSRD PEDPEHFGKQ NVGIYRMEVK GKRKLGLQPI
PMHDIAIHLH KAEERGDDLP IAITLGNDPV ITLMGATPLR YDQSEYEMAG ALRESPYPIA
TAPLTGFDVP WGSEVILEGV IEGRKREIEG PFGEFTGHYS GGRNMTVVRI DKVSYRNNPI
FESLYLGMPW TEIDYLMGPA TCVPLYQQLK AEFPEVQAVN AMYTHGLLAI ISTKKRYGGF
ARAVGLRAMT TPHGLGYVKM VIMVDEDVDP FDLLQVMWAL SSKVNPAGDL VQLPNMSVLE
LDPGSSPAGI TDKLVIDATT PVAPDTRGHY SQPVKDLPET AEWVKKLNNL LANRKK
//
