ID   GANA_NEOFI              Reviewed;         356 AA.
AC   A1D3T4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=NFIA_017780;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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}.
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DR   EMBL; DS027688; EAW23077.1; -; Genomic_DNA.
DR   RefSeq; XP_001264974.1; XM_001264973.1.
DR   AlphaFoldDB; A1D3T4; -.
DR   SMR; A1D3T4; -.
DR   STRING; 331117.A1D3T4; -.
DR   EnsemblFungi; EAW23077; EAW23077; NFIA_017780.
DR   GeneID; 4591274; -.
DR   KEGG; nfi:NFIA_017780; -.
DR   VEuPathDB; FungiDB:NFIA_017780; -.
DR   eggNOG; ENOG502QU6R; Eukaryota.
DR   HOGENOM; CLU_011259_0_0_1; -.
DR   OMA; GVNTVRQ; -.
DR   OrthoDB; 828182at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome;
KW   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_0000394952"
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;  39095 MW;  CFF0E268EF4DDA54 CRC64;
     MLGKMILLPL FVLLCHSLAS ASLAYRGADI SSLLIEEKAG IKYKDVNGQA QPLENILKAN
     GVNSVRQRVW VNPSDGSYNL DYNVKLAKRV KAAGMSVYLD LHFSDTWADP SHQTTPRGWS
     TNDIGTLTWQ VYNYTKEVCD TFASNGIDVS IVAIGNEIRN GLLWPLGKPN NYANIANILH
     SAAFGVKDST LSPKPKIMIH LDNGWDWSAQ KFFYDSVLSS GAKLVKSDFD LIGVSYYPFY
     NPSATLSALT TSLKNLRSTY GKDVLVVETD WPVSCPNPAY AFPSDLKDIP FSVAGQKTFV
     QRVANVVAQT PGGIGLYYWE PAWVQNAALG SSCADNLMVD WRTDQARTSL SVFGTI