TAN_ASPOR
ID TAN_ASPOR Reviewed; 588 AA.
AC P78581; Q2TYX1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Tannase;
DE EC=3.1.1.20;
DE Contains:
DE RecName: Full=Tannase 33 kDa subunit;
DE Contains:
DE RecName: Full=Tannase 30 kDa subunit;
DE Flags: Precursor;
GN ORFNames=AO090103000074;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 19-43; 159-166;
RP 317-327; 424-426 AND 456-471, AND PYROGLUTAMATE FORMATION AT GLN-317.
RC STRAIN=TH;
RX PubMed=8917102; DOI=10.1016/0378-1119(96)00153-9;
RA Hatamoto O., Watarai T., Kikuchi M., Mizusawa K., Sekine H.;
RT "Cloning and sequencing of the gene encoding tannase and a structural study
RT of the tannase subunit from Aspergillus oryzae.";
RL Gene 175:215-221(1996).
RN [2]
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).
CC -!- FUNCTION: Hydrolyzes ester bonds of tannic acid to produce gallic acid
CC and glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=digallate + H2O = 2 3,4,5-trihydroxybenzoate + H(+);
CC Xref=Rhea:RHEA:16365, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16918, ChEBI:CHEBI:17866; EC=3.1.1.20;
CC -!- SUBUNIT: Heterooctamer of 4 33 kDa and 4 30 kDa subunits linked by
CC disulfide bond(s).
CC -!- PTM: The protein is glycosylated to a carbohydrate content of 22.7%.
CC -!- PTM: The N-terminus of the 30 kDa subunit is blocked.
CC {ECO:0000269|PubMed:8917102}.
CC -!- SIMILARITY: Belongs to the tannase family. {ECO:0000305}.
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DR EMBL; D63338; BAA09656.1; -; Genomic_DNA.
DR EMBL; AP007174; BAE65552.1; -; Genomic_DNA.
DR PIR; JC5087; JC5087.
DR RefSeq; XP_001826685.1; XM_001826633.1.
DR AlphaFoldDB; P78581; -.
DR SMR; P78581; -.
DR ESTHER; aspor-tan; Tannase.
DR EnsemblFungi; BAE65552; BAE65552; AO090103000074.
DR GeneID; 5998807; -.
DR KEGG; aor:AO090103000074; -.
DR VEuPathDB; FungiDB:AO090103000074; -.
DR HOGENOM; CLU_014819_2_1_1; -.
DR OMA; MLCQWPT; -.
DR BioCyc; MetaCyc:MON-16449; -.
DR BRENDA; 3.1.1.20; 522.
DR SABIO-RK; P78581; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050318; F:tannase activity; IEA:UniProtKB-EC.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011118; Tannase/feruloyl_esterase.
DR PANTHER; PTHR33938; PTHR33938; 1.
DR Pfam; PF07519; Tannase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8917102"
FT CHAIN 19..316
FT /note="Tannase 33 kDa subunit"
FT /id="PRO_0000033587"
FT CHAIN 317..588
FT /note="Tannase 30 kDa subunit"
FT /id="PRO_0000033588"
FT ACT_SITE 195
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT ACT_SITE 501
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT SITE 316..317
FT /note="Cleavage"
FT MOD_RES 317
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8917102"
FT DISULFID 25..71
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 194..502
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
FT DISULFID 261..278
FT /evidence="ECO:0000250|UniProtKB:Q2UP89"
SQ SEQUENCE 588 AA; 64095 MW; 24DB928DB02BE77D CRC64;
MRQHSRMAVA ALAAGANAAS FTDVCTVSNV KAALPANGTL LGISMLPSAV TANPLYNQSA
GMGSTTTYDY CNVTVAYTHT GKGDKVVIKY AFPKPSDYEN RFYVAGGGGF SLSSDATGGL
AYGAVGGATD AGYDAFDNSY DEVVLYGNGT INWDATYMFA YQALGEMTRI GKYITKGFYG
QSSDSKVYTY YEGCSDGGRE GMSQVQRWGE EYDGAITGAP AFRFAQQQVH HVFSSEVEQT
LDYYPPPCEL KKIVNATIAA CDPLDGRTDG VVSRTDLCKL NFNLTSIIGE PYYCAAGTST
SLGFGFSNGK RSNVKRQAEG STTSYQPAQN GTVTARGVAV AQAIYDGLHN SKGERAYLSW
QIASELSDAE TEYNSDTGKW ELNIPSTGGE YVTKFIQLLN LDNLSDLNNV TYDTLVDWMN
TGMVRYMDSL QTTLPDLTPF QSSGGKLLHY HGESDPSIPA ASSVHYWQAV RSVMYGDKTE
EEALEALEDW YQFYLIPGAA HCGTNSLQPG PYPENNMEIM IDWVENGNKP SRLNATVSSG
TYAGETQMLC QWPKRPLWRG NSSFDCVNDE KSIDSWTYEF PAFKVPVY
