ID   XGHA_ASPFU              Reviewed;         406 AA.
AC   Q4WBT4;
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 endo-xylogalacturonan hydrolase A;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xghA; ORFNames=AFUA_8G06890;
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: 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=EAL85450.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000013; EAL85450.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_747488.1; XM_742395.1.
DR   AlphaFoldDB; Q4WBT4; -.
DR   SMR; Q4WBT4; -.
DR   STRING; 746128.CADAFUBP00007877; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GeneID; 3504762; -.
DR   KEGG; afm:AFUA_8G06890; -.
DR   eggNOG; ENOG502QTHU; Eukaryota.
DR   HOGENOM; CLU_016031_1_3_1; -.
DR   InParanoid; Q4WBT4; -.
DR   OrthoDB; 1028572at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
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_0000394698"
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;  42267 MW;  D8CE83F43B505733 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 SGPDVVQNIL AHRITMIEST KAAGIKTYPS GNGHGLSTVK
     NVTFSDFNVR GCDYAFQIES CYGESESYCE SNPGNAILQG IVVKGFSGTT SGKYDPVVAN
     LNCGARGTCD VSMSAFSVKA PSGKATVLCD NTPSSLGVSC TSGASG