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 03-MAY-2023, entry version 61. 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 GlyCosmos; Q9Y7F8; 1 site, No reported glycans. DR VEuPathDB; FungiDB:ASPTUDRAFT_112383; -. DR OMA; KAQGMKL; -. 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 Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR011683; Glyco_hydro_53. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR34983; ARABINOGALACTAN ENDO-BETA-1,4-GALACTANASE A; 1. DR PANTHER; PTHR34983:SF1; ARABINOGALACTAN ENDO-BETA-1,4-GALACTANASE A; 1. DR Pfam; PF07745; Glyco_hydro_53; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 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 //