ID   XGHA_ASPOR              Reviewed;         406 AA.
AC   Q2UBD8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xghA; ORFNames=AO090102000011;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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}.
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DR   EMBL; AP007162; BAE61127.1; -; Genomic_DNA.
DR   RefSeq; XP_001822260.1; XM_001822208.1.
DR   AlphaFoldDB; Q2UBD8; -.
DR   SMR; Q2UBD8; -.
DR   STRING; 510516.Q2UBD8; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; BAE61127; BAE61127; AO090102000011.
DR   GeneID; 5994305; -.
DR   KEGG; aor:AO090102000011; -.
DR   VEuPathDB; FungiDB:AO090102000011; -.
DR   HOGENOM; CLU_016031_1_3_1; -.
DR   OMA; FKPGANY; -.
DR   Proteomes; UP000006564; Chromosome 4.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
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_0000394699"
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          266..289
FT                   /note="PbH1 4"
FT   REPEAT          299..320
FT                   /note="PbH1 5"
FT   REPEAT          368..390
FT                   /note="PbH1 6"
FT   REGION          20..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
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;  42332 MW;  476C864B23DDF4CD CRC64;
     MISLNSIFLL SLVGLSRAAP SRSETSPDRT IKPRAACTPT AGGSSSTDDV PAIQEAITSC
     GDGGIIIIPA DTTYYLNSVL DFKGCSNCDF QVEGLLQFTS STDYWNGKTA MITVSDIDGL
     KLRSVTGSGV IDGNGQESWD KFAEDSSYKR PTLLYITGGS NIEVSGLRQK NPPNVFISVK
     GDTSNAQFTS LTMDATSNSD NLPKNTDAFD IGASTYVTIS SVAITNDDDC VAFKPGANYV
     TVENVSCTGS HGISVGSLGK SSDDTVQNVY ARNITMINSS KAAGIKTYPS GGDHGLSTVK
     NATFEDFIVD GCDYAFQIQS CYGEDDTYCE ENPGDAVLEG IVVKGFTGTT SDKEDPVVAN
     LNCGSKGTCD VTISGFEVKA PSGDAKILCG NTPSDLGVTC SSGASG