ID   XGHA_ASPFC              Reviewed;         406 AA.
AC   B0Y9F8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xghA; ORFNames=AFUB_080880;
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: Pectinolytic enzyme involved in the degradation of
CC       xylogalacturonan (xga), a galacturonan backbone heavily substituted
CC       with xylose, and which is one important component of the hairy regions
CC       of pectin. Activity requires a galacturonic acid backbone substituted
CC       with xylose (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP48651.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS499600; EDP48651.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B0Y9F8; -.
DR   SMR; B0Y9F8; -.
DR   PhylomeDB; B0Y9F8; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SMART; SM00710; PbH1; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..406
FT                   /note="Probable endo-xylogalacturonan hydrolase A"
FT                   /id="PRO_0000394696"
FT   REPEAT          183..213
FT                   /note="PbH1 1"
FT   REPEAT          214..235
FT                   /note="PbH1 2"
FT   REPEAT          237..257
FT                   /note="PbH1 3"
FT   REPEAT          299..320
FT                   /note="PbH1 4"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   406 AA;  42284 MW;  95511C3D2942DAF1 CRC64;
     MLYPRNLALF SLLSLSSAAP SQVERSPDAV LKPRAVCTPT AGGSPSIDDV PAIRKAIASC
     GNGGTIVFPA GSTYYLNSVL DLAGCSNCDI QVEGVLKFSG STEYWGGKTA MLNIDMINGL
     RLRSLTGSGV IDGNGQNAYD RFASDKNYKR PTLLYITGGS NIEVSGLRQK NPPNVFNSVK
     GDTQHVTFKN LRMDATSNSQ NPPKNTDGFD IGASTHVTIS SVSVTNDDDC VAFKPGSNYV
     TVEDVTCTGS HGISVGSLGK SGTDVVQNIL AHRINMIEST KAAGIKTYPS GNGHGLSTVK
     NVTFSDFNVR GCDYAFQIES CYGESESYCE SNPGNAILQG IVVKGFSGTT SGKYDPVVAN
     LNCGARGTCD VSMSAFSVKA PSGKATVLCD NTPSSLGVSC TSGASG