GANA_ASPFU
ID GANA_ASPFU Reviewed; 356 AA.
AC Q4WJ80;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 83.
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=AFUA_1G06910;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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=EAL88402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAHF01000007; EAL88402.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_750440.1; XM_745347.1.
DR AlphaFoldDB; Q4WJ80; -.
DR SMR; Q4WJ80; -.
DR STRING; 330879.Q4WJ80; -.
DR GeneID; 3507699; -.
DR KEGG; afm:AFUA_1G06910; -.
DR eggNOG; ENOG502QU6R; Eukaryota.
DR HOGENOM; CLU_011259_0_0_1; -.
DR InParanoid; Q4WJ80; -.
DR OrthoDB; 828182at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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_0000394946"
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; 39105 MW; 810E74AD6F3BB001 CRC64;
MLGKTVLLPL LVLLCHSLAS ASLVYRGADI SSLLIEEKAG IEYKNVNGQT QPLENILKAN
GVNSVRQRVW VNPSDGSYNL DYNVKLAKRV KAAGMSVYLD LHFSDTWADP SHQTTPRGWS
TNDIGTLTWQ VYNYTMEVCN TFASNGIDVS IVAIGNEIRN GLLWPLGKPD NYANIANILH
SAAFGVKDST LSPKPKIMIH LDNGWDWSAQ KFFYNRVLSS GANLVKSDFD LIGVSYYPFY
NPSATLSALT TSLKNLRSTY GKDVLVVETD WPVSCPNPAY AFPSDLKDIP FSVAGQTTFV
QRVANIVAQT PGGIGLYYWE PAWVQNAALG SSCADNLMVD WSTRQARTSL SVFATI