ID   GANA_ASPTU              Reviewed;         350 AA.
AC   Q9Y7F8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 58.
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;
OS   Aspergillus tubingensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   DOI=10.1023/A:1008864118362;
RA   Vlugt-Bergmans C.J.B., van Ooyen A.J.J.;
RT   "Expression cloning in Kluyveromyces lactis.";
RL   Biotechnol. Tech. 13:87-92(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ012316; CAB40555.1; -; mRNA.
DR   AlphaFoldDB; Q9Y7F8; -.
DR   SMR; Q9Y7F8; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   CLAE; GAN53A_ASPTU; -.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_112383; -.
DR   OMA; GVNTVRQ; -.
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   2: Evidence at transcript 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="Probable arabinogalactan endo-beta-1,4-galactanase
FT                   A"
FT                   /id="PRO_0000394950"
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;  924E2C8E0F1D608A CRC64;
     MIYPLLLSAL PLLSSAALTY RGADISSLLI EEDAGISYKN LNGETQALED ILVNNGVNSI
     RQRVWVDPSD GSYDLDYNLK LAKRVQAAGM SIYLDLHLSD TWADPSDQTT PTGWSTTDID
     TLTWQLYNYT LEVCNTFAEN DIDVEIVSIG NEISSGLLWP LGKTSNYDNI AKLLHSGAWG
     VKDSDLTTTP KIMIHLDNGW DWDEQEYFYK TVLATGSLLS TDFDLMGVSY YPFYSSEATL
     SSLKTSLTNM QSNYDKPVVV VETNWPVSCP DPEYSFPSDL TSIPFSAAGQ EEFLEKLAEV
     VEGVTDGLGI YYWEPAWIDN AGLGSSCADN LMVDVNTDEV LESVTVFEDL