ID   XGHA_NEOFI              Reviewed;         406 AA.
AC   A1DBT5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xghA; ORFNames=NFIA_099610;
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: 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}.
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DR   EMBL; DS027694; EAW20325.1; -; Genomic_DNA.
DR   RefSeq; XP_001262222.1; XM_001262221.1.
DR   AlphaFoldDB; A1DBT5; -.
DR   SMR; A1DBT5; -.
DR   STRING; 331117.A1DBT5; -.
DR   EnsemblFungi; EAW20325; EAW20325; NFIA_099610.
DR   GeneID; 4588576; -.
DR   KEGG; nfi:NFIA_099610; -.
DR   VEuPathDB; FungiDB:NFIA_099610; -.
DR   eggNOG; ENOG502QTHU; Eukaryota.
DR   HOGENOM; CLU_016031_1_3_1; -.
DR   OMA; FKPGANY; -.
DR   OrthoDB; 1028572at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..406
FT                   /note="Probable endo-xylogalacturonan hydrolase A"
FT                   /id="PRO_0000394702"
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        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   406 AA;  42278 MW;  63C9E35F62235C8C CRC64;
     MLYYRNLALL SLLSLSSAAP SQVERSPDAV FKPRAVCTPT AGGSSSIDDV PAIRKAISSC
     GNGGTIVFPA GSTYYLNSVL DLAGCSNCDI QVEGLLMFSG STEYWGGKTA MININKINAL
     KLRSLTGSGV IDGNGQNAYD LFASNSDYER PTLLYITGGS NIEVSGLRQR NPPNVFNSVK
     GDAKDVTFTN LRMDATSRSD NPPKNTDGFD IGSSTHVTIS SVSVSNDDDC VALKPGCNYV
     TVENVTCTGS HGISVGSLGK SSADTVQNVY AHRITMIDST KAAGIKTYPS GNGHGLSTVK
     NVTFSDFNVR GCDYAFQIQS CYGESASYCA SHPGNAILQD IIVKGFSGTT SGKDDWVVAD
     LNCGARGTCD VSMSDFSVKA PSGKATVLCA NTPSSLGVTC TSGASG