GANA_THETO
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 25-MAY-2022, entry version 73.
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}.
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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 PRIDE; 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 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 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
