ID   GANA_ASPFC              Reviewed;         356 AA.
AC   B0XPR3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 53.
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=AFUB_007290;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP56027.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DS499594; EDP56027.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B0XPR3; -.
DR   SMR; B0XPR3; -.
DR   PhylomeDB; B0XPR3; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..356
FT                   /note="Probable arabinogalactan endo-beta-1,4-galactanase
FT                   A"
FT                   /id="PRO_0000394944"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   356 AA;  39132 MW;  C36E62DABE9805D5 CRC64;
     MLGKTVLLPL LVLLCHSLAS ASLVYRGADI SSLLIEEKAG IEYKNVNGQT QPLENILKAN
     GVNSVRQRVW VNPSDGSYNL DYNVKLAKRV KAAGMSVYLD LHFSDTWADP SHQTTPRGWS
     TNDIGTLTWQ VYNYTMEVCN TFASNGIDVS IVAIGNEIRN GLLWPLGKPD NYANIANILH
     SAAFGVKDST LSPKPKIMIH LDNGWDWSAQ KFFYDRVLSS GANLVKSDFD LIGVSYYPFY
     NPSATLSALT TSLKNLRSTY GKDVLVVETD WPVLCPNPAY AFPSDLKDIP FSVAGQTTFV
     QRVANIVAQT PGGIGLYYWE PAWVQNAALG SSCADNLMVD WSTRQARTSL SVFATI