ID Q6D8A4_PECAS Unreviewed; 474 AA.
AC Q6D8A4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
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 OrderedLocusNames=ECA1070 {ECO:0000313|EMBL:CAG73981.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG73981.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG73981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG73981.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) 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}.
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DR EMBL; BX950851; CAG73981.1; -; Genomic_DNA.
DR RefSeq; WP_011092668.1; NC_004547.2.
DR AlphaFoldDB; Q6D8A4; -.
DR STRING; 218491.ECA1070; -.
DR KEGG; eca:ECA1070; -.
DR PATRIC; fig|218491.5.peg.1074; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_3_2_6; -.
DR OrthoDB; 9809841at2; -.
DR Proteomes; UP000007966; Chromosome.
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|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01985}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007966}.
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 474 AA; 52087 MW; B38475072C9D2DD4 CRC64;
MAFDDLRGFL NALDENGQLL HIDEEVQAEP DLAAAANATG RIGEGAPALS FTNIKGFVDA
HVVMNTIGSW PNHAISMGLP GNTPVKQQID EFIRRWDNFP VAPERRENPP WAENALEGDG
INLFALLPLF RLNDGDGGFY LDKACVVSRD PDDPEHFGKQ NVGIYRMEVK GKRKLGLQPV
PMHDIAMHLR KAEERGEDLP IAITLGNDPI ITLMGATPLK YDQSEYEMAG ALRESPYPIS
TAPLTGFDVP WGSEVILEGV IESRKREIEG PFGEFTGHYS GGRSMPVVRI DKVSYRSKLI
FESLYLGMPW TEVDYLIGPA TCVPLYQQLK AEFPEVQAVN AMYTHGLLAI ISTKKRYGGF
ARAVGLRAMT TPHGLGYVKM VIMVDEDVDP FNLPQVMWAL SAKVNPAGDL VQLPNMPVLA
LDPSSSPAGI TDKLIIDATT PVAPDIRGHY SQSVKDLPEA KVWVEKLSAM LANR
//
