ID   GANA_ASPNG              Reviewed;         350 AA.
AC   Q8X168;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION,
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=12383257; DOI=10.1046/j.1432-1033.2002.03199.x;
RA   de Vries R.P., Paenicova L., Hinz S., Kester H.C.M., Benen J.A.E.,
RA   Beldman G.A., Visser J.;
RT   "Endogalactanase A from Aspergillus niger is specifically induced on L-
RT   arabinose and galacturonic acid and plays an important role in the
RT   degradation of pectic hairy regions.";
RL   Eur. J. Biochem. 269:4985-4993(2002).
CC   -!- FUNCTION: Endogalactanase involved in the degradation of plant cell
CC       wall polysaccharides, and more particularly of hairy regions of pectin.
CC       {ECO:0000250, ECO:0000269|PubMed:12383257}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 4.0 and 4.5. {ECO:0000269|PubMed:12383257};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12383257}.
CC   -!- INDUCTION: Specifically expressed on arabinose and galacturonic acid.
CC       {ECO:0000269|PubMed:12383257}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
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DR   EMBL; AJ305303; CAC83735.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X168; -.
DR   SMR; Q8X168; -.
DR   STRING; 5061.CADANGAP00013963; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   CLAE; GAN53A_ASPNG; -.
DR   VEuPathDB; FungiDB:An18g05940; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1147681; -.
DR   VEuPathDB; FungiDB:ATCC64974_107090; -.
DR   VEuPathDB; FungiDB:M747DRAFT_312025; -.
DR   eggNOG; ENOG502QU6R; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IDA: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; IDA: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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..350
FT                   /note="Arabinogalactan endo-beta-1,4-galactanase A"
FT                   /id="PRO_0000394947"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  38734 MW;  3353286DECB85DD6 CRC64;
     MIYPLLLSAL PLLSSAALTY RGADISSLLI EEDAGISYKN LNGETQALED ILVNNGVNSI
     RQRVWVDPSD GSYDLDYNLK LAKRVQAAGM SIYLDLHLSD TWADPSDQTT PTGWSTTDID
     TLTWQLYNYT LDVCNTFAEN DIDIEIVSIG NEISSGLLWP LGKTSNYDNI AKLLHSGAWG
     VKDSNQATTP KIMIHLDNGW DWEEQEYFYK TVLATGSLLS TDFDLMGVSY YPFYNSEATL
     SALQTSLTNM QSNYDKSVVV VETNWPVSCP DPEYSFPSDL SSIPFSAAGQ EEFLEKLAEV
     VEGVTDGLGI YYWEPAWVDN AALGSSCADN LMVDIDTDEV LESVTVFEDL