GANA_ASPAC
ID GANA_ASPAC Reviewed; 350 AA.
AC P48842;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
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;
DE Flags: Precursor;
GN Name=gal1;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-44.
RC STRAIN=KSM 510;
RX PubMed=7788716; DOI=10.1007/bf00313427;
RA Christgau S., Sandal T., Kofod L.V., Dalboege H.;
RT "Expression cloning, purification and characterization of a beta-1,4-
RT galactanase from Aspergillus aculeatus.";
RL Curr. Genet. 27:135-141(1995).
RN [2]
RP MUTAGENESIS OF ASP-198.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12484750; DOI=10.1021/bi026238c;
RA Ryttersgaard C., Lo Leggio L., Coutinho P.M., Henrissat B., Larsen S.;
RT "Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and
RT relations to other glycoside hydrolases in clan GH-A.";
RL Biochemistry 41:15135-15143(2002).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0-4.5.;
CC Temperature dependence:
CC Optimum temperature is 40-65 degrees Celsius.;
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
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DR EMBL; L34599; AAA32692.1; -; mRNA.
DR PIR; S51494; S51494.
DR PDB; 1FHL; X-ray; 2.30 A; A=17-350.
DR PDB; 1FOB; X-ray; 1.80 A; A=17-350.
DR PDB; 6Q3R; X-ray; 2.69 A; A/B=17-350.
DR PDBsum; 1FHL; -.
DR PDBsum; 1FOB; -.
DR PDBsum; 6Q3R; -.
DR AlphaFoldDB; P48842; -.
DR SMR; P48842; -.
DR CAZy; GH53; Glycoside Hydrolase Family 53.
DR CLAE; GAN53A_ASPAC; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_78476; -.
DR EvolutionaryTrace; P48842; -.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; Direct protein sequencing; Glycoprotein; Glycosidase;
KW Hydrolase; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:7788716"
FT CHAIN 17..350
FT /note="Arabinogalactan endo-beta-1,4-galactanase"
FT /id="PRO_0000012221"
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"
FT MUTAGEN 198
FT /note="D->N: Broadens pH profile by 1 unit towards the
FT basic end of the scale."
FT /evidence="ECO:0000269|PubMed:12761390"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 119..139
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1FOB"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 287..302
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1FOB"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:1FOB"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:1FOB"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1FOB"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:1FOB"
SQ SEQUENCE 350 AA; 38423 MW; 9074249DFAB24CAC CRC64;
MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET ILADAGINSI
RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD TWADPSDQTT PSGWSTTDLG
TLKWQLYNYT LEVCNTFAEN DIDIEIISIG NEIRAGLLWP LGETSSYSNI GALLHSGAWG
VKDSNLATTP KIMIHLDDGW SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL
ASLKTSLANL QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV
VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL
