ID GANA_THETO Reviewed; 332 AA. AC P83692; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 22-FEB-2023, entry version 76. DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase; DE EC=3.2.1.89; DE AltName: Full=Endo-1,4-beta-galactanase; DE Short=Galactanase; OS Thermothelomyces thermophilus (Myceliophthora thermophila). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces. OX NCBI_TaxID=78579; RN [1] {ECO:0000305, ECO:0000312|PDB:1HJS} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY, GLYCOSYLATION AT RP ASN-111, AND MUTAGENESIS OF 90-ASP-HIS-91. RX PubMed=12761390; DOI=10.1110/ps.0300103; RA Le Nours J., Ryttersgaard C., Lo Leggio L., Oestergaard P.R., RA Borchert T.V., Christensen L.L.H., Larsen S.; RT "Structure of two fungal beta-1,4-galactanases: searching for the basis for RT temperature and pH optimum."; RL Protein Sci. 12:1195-1204(2003). 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 Evidence={ECO:0000269|PubMed:12761390}; CC -!- MISCELLANEOUS: Has a pH range of 5.5-8.5 with optimum of 7.0; and a CC temperature optimum of 65 degrees Celsius at pH 6.5. CC {ECO:0000269|PubMed:12761390}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. CC {ECO:0000269|PubMed:12761390}. 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 PDB; 1HJS; X-ray; 1.87 A; A/B/C/D=1-332. DR PDB; 1HJU; X-ray; 2.15 A; A/B/C/D=1-332. DR PDBsum; 1HJS; -. DR PDBsum; 1HJU; -. DR AlphaFoldDB; P83692; -. DR SMR; P83692; -. DR CAZy; GH53; Glycoside Hydrolase Family 53. DR CLAE; GAN53A_MYCTH; -. DR iPTMnet; P83692; -. DR VEuPathDB; FungiDB:MYCTH_43163; -. DR EvolutionaryTrace; P83692; -. DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB. DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; TAS: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 1: Evidence at protein level; KW 3D-structure; Glycoprotein; Glycosidase; Hydrolase. FT CHAIN 1..332 FT /note="Arabinogalactan endo-beta-1,4-galactanase" FT /id="PRO_0000057706" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P48841" FT ACT_SITE 245 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P48841" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12761390" FT MUTAGEN 90..91 FT /note="AH->SD: Lowers pH profile by 0.5 units." FT /evidence="ECO:0000269|PubMed:12761390" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 12..17 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 32..38 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 59..71 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 102..122 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 128..135 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 150..165 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 174..180 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 185..196 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 223..237 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 270..285 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 290..296 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:1HJS" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:1HJS" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:1HJS" FT HELIX 324..330 FT /evidence="ECO:0007829|PDB:1HJS" SQ SEQUENCE 332 AA; 36812 MW; 71CA092FDB1D43DC CRC64; ALTYRGVDWS SVVVEERAGV SYKNTNGNAQ PLENILAANG VNTVRQRVWV NPADGNYNLD YNIAIAKRAK AAGLGVYIDF HYSDTWADPA HQTMPAGWPS DIDNLSWKLY NYTLDAANKL QNAGIQPTIV SIGNEIRAGL LWPTGRTENW ANIARLLHSA AWGIKDSSLS PKPKIMIHLD NGWDWGTQNW WYTNVLKQGT LELSDFDMMG VSFYPFYSSS ATLSALKSSL DNMAKTWNKE IAVVETNWPI SCPNPRYSFP SDVKNIPFSP EGQTTFITNV ANIVSSVSRG VGLFYWEPAW IHNANLGSSC ADNTMFSQSG QALSSLSVFQ RI //