ID   GANA_ASPTN              Reviewed;         349 AA.
AC   Q0CTQ7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=ATEG_02927;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36201.1; -; Genomic_DNA.
DR   RefSeq; XP_001212105.1; XM_001212105.1.
DR   AlphaFoldDB; Q0CTQ7; -.
DR   SMR; Q0CTQ7; -.
DR   STRING; 341663.Q0CTQ7; -.
DR   EnsemblFungi; EAU36201; EAU36201; ATEG_02927.
DR   GeneID; 4317469; -.
DR   VEuPathDB; FungiDB:ATEG_02927; -.
DR   eggNOG; ENOG502QU6R; Eukaryota.
DR   HOGENOM; CLU_011259_0_0_1; -.
DR   OMA; GVNTVRQ; -.
DR   OrthoDB; 828182at2759; -.
DR   Proteomes; UP000007963; 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; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..349
FT                   /note="Probable arabinogalactan endo-beta-1,4-galactanase
FT                   A"
FT                   /id="PRO_0000394949"
FT   ACT_SITE        150
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   349 AA;  37806 MW;  AE98B70165ADE29F CRC64;
     MLLSFLPLLP LATAALTYRG ADISSLLIEE DAGIAYKNLN GQTQALESIL ADNGVNSIRQ
     RLWVNPSDGS YDLDYNLKLA KRAKAAGMSV YLDLHYSDTW ADPSHQTTPA GWSTDDIGTL
     AWQVYNYTKE VCDTFAANDI ALEMVSIGNE IRNGLLWPLG ATDSYPNIAR LLHSGAWGVK
     DSALATTPQI LLHLDNGWDW AAQKYFYDTV LAAGSELTSA DFDLIGVSYY PFYNADATLS
     ALKTSLGNLA SAYGKKVLVV ETNWPVACPN PEYQFPADLA DIPFSVDGQS TFLRRLGEVV
     AGTDGGAGVY YWEPAWTKNA GLGSSCQDNL LVDYNTDQVR ASISALGGI