DBD23_ASPNG
ID DBD23_ASPNG Reviewed; 292 AA.
AC P80346;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=2,3-dihydroxybenzoate decarboxylase;
DE Short=2,3-DHBA decarboxylase;
DE Short=DHBD;
DE EC=4.1.1.46;
DE AltName: Full=o-pyrocatechuate decarboxylase;
DE Flags: Fragments;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7601088; DOI=10.1111/j.1432-1033.1995.0104i.x;
RA Santha R., Savithri H.S., Rao N.A., Vaidyanathan C.S.;
RT "2,3-dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel
RT decarboxylase.";
RL Eur. J. Biochem. 230:104-110(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoate + H(+) = catechol + CO2;
CC Xref=Rhea:RHEA:21492, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:36654; EC=4.1.1.46;
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation.
CC -!- SUBUNIT: Homotetramer.
CC -!- MISCELLANEOUS: The MW of the complete protein is about 38 kDa (345
CC residues).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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 PIR; S65362; S65362.
DR AlphaFoldDB; P80346; -.
DR VEuPathDB; FungiDB:An07g02050; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1157716; -.
DR VEuPathDB; FungiDB:ATCC64974_44650; -.
DR VEuPathDB; FungiDB:M747DRAFT_265980; -.
DR UniPathway; UPA00156; -.
DR GO; GO:0050150; F:o-pyrocatechuate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 3.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Direct protein sequencing; Lyase.
FT CHAIN 1..>292
FT /note="2,3-dihydroxybenzoate decarboxylase"
FT /id="PRO_0000079886"
FT ACT_SITE 263
FT UNSURE 247
FT /note="P or G"
FT UNSURE 250
FT /note="H or G"
FT NON_CONS 32..33
FT /evidence="ECO:0000305"
FT NON_CONS 66..67
FT /evidence="ECO:0000305"
FT NON_CONS 88..89
FT /evidence="ECO:0000305"
FT NON_CONS 121..122
FT /evidence="ECO:0000305"
FT NON_CONS 150..151
FT /evidence="ECO:0000305"
FT NON_CONS 160..161
FT /evidence="ECO:0000305"
FT NON_CONS 170..171
FT /evidence="ECO:0000305"
FT NON_CONS 183..184
FT /evidence="ECO:0000305"
FT NON_CONS 194..195
FT /evidence="ECO:0000305"
FT NON_CONS 207..208
FT /evidence="ECO:0000305"
FT NON_CONS 214..215
FT /evidence="ECO:0000305"
FT NON_CONS 224..225
FT /evidence="ECO:0000305"
FT NON_CONS 229..230
FT /evidence="ECO:0000305"
FT NON_CONS 236..237
FT /evidence="ECO:0000305"
FT NON_CONS 240..241
FT /evidence="ECO:0000305"
FT NON_CONS 247..248
FT /evidence="ECO:0000305"
FT NON_CONS 255..256
FT /evidence="ECO:0000305"
FT NON_CONS 264..265
FT /evidence="ECO:0000305"
FT NON_TER 292
SQ SEQUENCE 292 AA; 33001 MW; EF78074854BAD925 CRC64;
MLGKIALEEA FALPRFEEKT RWWASLFSVD PEIEHADKYG VGYQILSYTA PGVQDIWDPV
EAQAGEVGVD RILSIDYPFE TFEDAAVVLR RDVQTYGFIG ALVNDTQRTG PMGNNQEEAY
NINDYIAEQI RDKPDRFGAF TLSMHNPQEA GRDNAARLFE RNPTGTIYEK LGAFRDYDAK
VKAEITDINK LRIENASWDI FWQTDTEAQA LAVEDADVWF DGAEFYDNAA MQYVIAYGAK
QADIYGPINH WFEDRLLGLA ETCKWLVGPD LSFAHGVSLH VLGMTVNGVF DR
