ID   GANA_ASPFN              Reviewed;         347 AA.
AC   B8NNI2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=AFLA_127930;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963481; EED48570.1; -; Genomic_DNA.
DR   RefSeq; XP_002381986.1; XM_002381945.1.
DR   AlphaFoldDB; B8NNI2; -.
DR   SMR; B8NNI2; -.
DR   STRING; 332952.B8NNI2; -.
DR   EnsemblFungi; EED48570; EED48570; AFLA_127930.
DR   VEuPathDB; FungiDB:AFLA_127930; -.
DR   eggNOG; ENOG502QU6R; Eukaryota.
DR   HOGENOM; CLU_011259_0_0_1; -.
DR   OMA; GVNTVRQ; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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; Secreted; 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_0000394945"
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;  38452 MW;  3FE2B51673D9AB41 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 FLQRLADTLT
     ATKASGFFYW EPAWTKNAGL GSSCEDNLLV DYNTNQVRSS VKAFGQV