GANA_ASPNC
ID GANA_ASPNC Reviewed; 350 AA.
AC A2RB93;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
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; ORFNames=An18g05940;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
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DR EMBL; AM270410; CAK43317.1; -; Genomic_DNA.
DR AlphaFoldDB; A2RB93; -.
DR SMR; A2RB93; -.
DR CAZy; GH53; Glycoside Hydrolase Family 53.
DR PaxDb; A2RB93; -.
DR EnsemblFungi; CAK43317; CAK43317; An18g05940.
DR HOGENOM; CLU_011259_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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 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 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW 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_5000221354"
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; 38697 MW; 7BB458494EC916FE CRC64;
MIYSLLLSAL PLLSSAALTY RGADISSLLI EEDAGISYKN LNGETQALED ILVNNGVNSI
RQRVWVDPSD GSYDLDYNLK LAKRVQAAGM SIYLDLHLSD TWADPSDQTT PTGWSTTDID
TLTWQLYNYT LDVCNTFAEN DIDIEIVSIG NEISSGLLWP LGKTSNYDNI AKLLHSGAWG
VKDSNQATTP KIMIHLDNGW DWEEQEYFYK TVLATGSLLS TDFDLMGVSY YPFYSSEATL
SALQTSLTNM QSNYDKSVVV VETNWPVSCP DPEYSFPSDL SSIPFSAAGQ EEFLEKLAEV
VEGVTDGLGI YYWEPAWVDN AALGSSCADN LMVDIDTDEV LESVTVFEDL