ID A0A0M2GKJ7_9ACTN Unreviewed; 477 AA.
AC A0A0M2GKJ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=UK15_30450 {ECO:0000313|EMBL:KJK35678.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK35678.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KJK35678.1}.
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DR EMBL; JYJH01000028; KJK35678.1; -; Genomic_DNA.
DR RefSeq; WP_031142594.1; NZ_JYJH01000028.1.
DR AlphaFoldDB; A0A0M2GKJ7; -.
DR STRING; 284040.UK15_30450; -.
DR PATRIC; fig|284040.3.peg.4488; -.
DR Proteomes; UP000034786; 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 106..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 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 477 AA; 51950 MW; 2F796FC656A2BE7A CRC64;
MAYDDLRSFL AALDAEGQLL RVSDEVLPEP DLAAAANAAG RIGEGAPALY FDNVKGFTDA
RIALNVHGSW TNHALALGLP KHTPVKEQVE IFASRWDDFP IAPERREDAP WRENTQAGGD
VDLFSVLPLF RLNDGDGGFY LDKAAVVSRD PEAPDDFGKQ NVGTYRIQVI GPDRLAFQPV
PVHDVALHLH KAEEKGEDLP VAITLGNDPV MAIVSGMPMA YDQSEYEMAG ALRGAPAPIA
TSPLTGFDVP WGSEVVIEGV IESRKRQIEG PFGEFTGHYS GGRRMPVIRV DRVSYRTNPV
FESLYLGKPW TEVDYLVGPN TCVPLLKQLR AEFPEVQAVN AMYTHGMLVI ISTAKRFGGF
AKAVGMRAMT TRHGLGYVSQ VIVVDEDVDP FDLPQVMWAM SAKVDPREDV VVVPNLSVVE
LAPAAQPAGI TSKMIIDATT PVAPDVRGNF STPAKDLPET REWAARLQQL RTAASSR
//
