DBD23_ASPOR
ID DBD23_ASPOR Reviewed; 338 AA.
AC P80402; Q2USF4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 92.
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;
GN ORFNames=AO090005000447;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-20; 52-65 AND 244-252.
RX PubMed=8620029; DOI=10.1016/0167-4838(95)00242-1;
RA Santha R., Rao N.A., Vaidyanathan C.S.;
RT "Identification of the active-site peptide of 2,3-dihydroxybenzoic acid
RT decarboxylase from Aspergillus oryzae.";
RL Biochim. Biophys. Acta 1293:191-200(1996).
CC -!- FUNCTION: Has an absolute substrate specificity for 2,3-DHBA.
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 -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AP007151; BAE55511.1; -; Genomic_DNA.
DR RefSeq; XP_001817513.1; XM_001817461.2.
DR PDB; 7A19; X-ray; 1.21 A; A/B=1-338.
DR PDB; 7A1A; X-ray; 1.53 A; A/B=1-338.
DR PDBsum; 7A19; -.
DR PDBsum; 7A1A; -.
DR AlphaFoldDB; P80402; -.
DR SMR; P80402; -.
DR EnsemblFungi; BAE55511; BAE55511; AO090005000447.
DR GeneID; 5989458; -.
DR KEGG; aor:AO090005000447; -.
DR VEuPathDB; FungiDB:AO090005000447; -.
DR HOGENOM; CLU_039329_5_2_1; -.
DR OMA; FAQNIWI; -.
DR UniPathway; UPA00156; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase;
KW Reference proteome.
FT CHAIN 1..338
FT /note="2,3-dihydroxybenzoate decarboxylase"
FT /id="PRO_0000079887"
FT ACT_SITE 251
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:7A19"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:7A19"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:7A19"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:7A19"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:7A19"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:7A19"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:7A19"
SQ SEQUENCE 338 AA; 38857 MW; 31DCC0320E267165 CRC64;
MLGKIALEEA FALPRFEEKT RWWASLFSTD AETHVKEITD INKIRIEHAD KHGVGYQILS
YTAPGVQDIW DPVEAQALAV EINDYIAEQV RVNPDRFGAF ATLSMHNPKE AADELRRCVE
KYGFKGALVN DTQRAGPDGD DMIFYDNADW DIFWQTCTEL DVPFYMHPRN PTGTIYEKLW
ADRKWLVGPP LSFAHGVSLH VLGMVTNGVF DRHPKLQIIM GHLGEHVPFD MWRINHWFED
RKKLLGLAET CKKTIRDYFA ENIWITTSGH FSTTTLNFCM AEVGSDRILF SIDYPFETFS
DACEWFDNAE LNGTDRLKIG RENAKKLFKL DSYKDSSA
