ID   GANA_ASPOR              Reviewed;         347 AA.
AC   Q2UN61;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable arabinogalactan endo-beta-1,4-galactanase A;
DE            EC=3.2.1.89;
DE   AltName: Full=Endo-1,4-beta-galactanase A;
DE            Short=Galactanase A;
DE   Flags: Precursor;
GN   Name=galA; ORFNames=AO090001000492;
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).
CC   -!- FUNCTION: Endogalactanase involved in the degradation of plant cell
CC       wall polysaccharides, and more particularly of hairy regions of pectin.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic
CC         linkages in type I arabinogalactans.; EC=3.2.1.89;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
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DR   EMBL; AP007154; BAE57004.1; -; Genomic_DNA.
DR   RefSeq; XP_001819006.1; XM_001818954.1.
DR   AlphaFoldDB; Q2UN61; -.
DR   SMR; Q2UN61; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   EnsemblFungi; BAE57004; BAE57004; AO090001000492.
DR   GeneID; 5990977; -.
DR   KEGG; aor:AO090001000492; -.
DR   VEuPathDB; FungiDB:AO090001000492; -.
DR   HOGENOM; CLU_011259_0_0_1; -.
DR   OMA; GVNTVRQ; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; ISS:UniProtKB.
DR   GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR   InterPro; IPR011683; Glyco_hydro_53.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34983; PTHR34983; 1.
DR   Pfam; PF07745; Glyco_hydro_53; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..347
FT                   /note="Probable arabinogalactan endo-beta-1,4-galactanase
FT                   A"
FT                   /id="PRO_0000394948"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  38493 MW;  25CBB4D0A8B5DB41 CRC64;
     MLFSYLLATL PLLANAALTY KGADISSVFI EEKAGVAYKN LAGETQALEA ILTDNGVNSI
     RQRVWVKNGD YDLTYNVNLA KRVAATGASI YLDLHYSDDW ADPKHQTTPD GWSTDDINTL
     ADQIYQYTLS VCNTFAEEKI NVEIVSIGNE ITSGLLWPLG KTPNYENIAR LLHSGAWGVK
     DSKLATKPKI LIHLDNGWDW DQQKYFYDTA LGTGLLTSDD FDMIGVSYYP FYNEKATLAS
     LKTSLTNIQT TYGKEVAVVE TNWPVKCSSP EFAFPADLKD IPFSVDGQVT FLQRLAETLT
     ATKASGFFYW EPAWTKNAGL GSSCEDNLLV DYNTNQVRNS VKAFGQV