ID   XGHA_ASPFN              Reviewed;         406 AA.
AC   B8NPS8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xghA; ORFNames=AFLA_001420;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963482; EED47501.1; -; Genomic_DNA.
DR   RefSeq; XP_002382343.1; XM_002382302.1.
DR   AlphaFoldDB; B8NPS8; -.
DR   SMR; B8NPS8; -.
DR   STRING; 332952.B8NPS8; -.
DR   EnsemblFungi; EED47501; EED47501; AFLA_001420.
DR   VEuPathDB; FungiDB:AFLA_001420; -.
DR   eggNOG; ENOG502QTHU; Eukaryota.
DR   HOGENOM; CLU_016031_1_3_1; -.
DR   OMA; FKPGANY; -.
DR   Proteomes; UP000001875; 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: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; 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_0000394697"
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;  42292 MW;  99C237E18731D6F8 CRC64;
     MISLNSIFLL SLVGLSRAAP SRSETSPDRT IKPRAACTPT AGGSSSTDDV PAIQEAITSC
     GDGGTIVIPA DTTYYLNSVL DFKGCSNCDF QVEGLLQFTS STDYWNGKTA MISVSDIDGL
     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