ID   GANA_HUMIN              Reviewed;         332 AA.
AC   P83691;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 69.
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   Humicola insolens (Soft-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX   NCBI_TaxID=34413;
RN   [1] {ECO:0000305, ECO:0000312|PDB:1HJQ}
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), CATALYTIC ACTIVITY, AND
RP   GLYCOSYLATION AT ASN-111.
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 6.5-9.5 with optimum of 8.5; 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; 1HJQ; X-ray; 2.55 A; A=1-332.
DR   PDBsum; 1HJQ; -.
DR   AlphaFoldDB; P83691; -.
DR   SMR; P83691; -.
DR   CAZy; GH53; Glycoside Hydrolase Family 53.
DR   CLAE; GAN53A_HUMIN; -.
DR   iPTMnet; P83691; -.
DR   EvolutionaryTrace; P83691; -.
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_0000057705"
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   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           12..17
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           102..123
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           150..165
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           185..198
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           223..237
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          240..245
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           270..286
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          290..296
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   TURN            304..307
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           324..327
FT                   /evidence="ECO:0007829|PDB:1HJQ"
FT   HELIX           328..331
FT                   /evidence="ECO:0007829|PDB:1HJQ"
SQ   SEQUENCE   332 AA;  37659 MW;  F6DA01D0F24CA702 CRC64;
     ALQYKGVDWS SVMVEERAGV RYKNVNGQEK PLEYILAENG VNMVRQRVWV NPWDGNYNLD
     YNIQLARRAK AAGLGLYINF HYSDTWADPA HQTTPAGWPS DINNLAWKLY NYTLDSMNRF
     ADAGIQVDIV SIGNEITQGL LWPLGKTNNW YNIARLLHSA AWGVKDSRLN PKPKIMVHLD
     NGWNWDTQNW WYTNVLSQGP FEMSDFDMMG VSFYPFYSAS ATLDSLRRSL NNMVSRWGKE
     VAVVETNWPT SCPYPRYQFP ADVRNVPFSA AGQTQYIQSV ANVVSSVSKG VGLFYWEPAW
     IHNANLGSSC ADNTMFTPSG QALSSLSVFH RI