ID   RHGA_ASPNG              Reviewed;         446 AA.
AC   P87160;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Rhamnogalacturonase A;
DE            Short=RGase A;
DE            Short=RHG A;
DE            EC=3.2.1.171;
DE   Flags: Precursor;
GN   Name=rhgA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=9212401; DOI=10.1128/aem.63.7.2507-2515.1997;
RA   Suykerbuyk M.E., Kester H.C., Schaap P.J., Stam H., Musters W., Visser J.;
RT   "Cloning and characterization of two rhamnogalacturonan hydrolase genes
RT   from Aspergillus niger.";
RL   Appl. Environ. Microbiol. 63:2507-2515(1997).
CC   -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC       pectine lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-
CC       alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions
CC       of pectins. {ECO:0000269|PubMed:9212401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic
CC         bond in the rhamnogalacturonan I backbone with initial inversion of
CC         anomeric configuration releasing oligosaccharides with beta-D-GalA at
CC         the reducing end.; EC=3.2.1.171;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.6. {ECO:0000269|PubMed:9212401};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; X94220; CAA63911.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87160; -.
DR   SMR; P87160; -.
DR   STRING; 5061.CADANGAP00009366; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; RHG28A_ASPNG; -.
DR   VEuPathDB; FungiDB:An12g00950; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1118594; -.
DR   VEuPathDB; FungiDB:ATCC64974_39800; -.
DR   VEuPathDB; FungiDB:M747DRAFT_295514; -.
DR   eggNOG; ENOG502R2FT; Eukaryota.
DR   BRENDA; 3.2.1.171; 518.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0046576; F:rhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase 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; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..446
FT                   /note="Rhamnogalacturonase A"
FT                   /id="PRO_0000394383"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        218..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        341..347
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..378
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  47045 MW;  D3772360D4464FA7 CRC64;
     MPALPILALA LAPLLVNGQL SGSVGPLTSA HSKAATKTCN VLDYGAVADN STDIGSALSE
     AWDACSDGGL IYIPPGDYAM DTWVSLSGGK ATAIILDGTI YRTGTDGGNM ILVENSSDFE
     LYSNSSSGAV QGFGYVYHRE GDLDGPRILR LQDVSNFAVH DIILVDAPAF HFVMDDCSDG
     EVYNMAIRGG NSGGLDGIDV WGSNIWVHDV EVTNKDECVT VKGPANNILV ESIYCNWSGG
     CAMGSLGADT DITDILYRNV YTWSSNQMYM IKSNGGSGTV NNTLLENFIG RGNRYSLDVD
     SYWSSMTAVD GDGVQLSNIT FKNWKGTEAD GAERGPIKVV CSDTAPCTDI TIEDFAMWTE
     SGDEQTYTCE SAYGDGFCLE DSDSTTSYTT TQTVTTAPSG YSATTMAADL TTDFGTTASI
     PIPTIPTSFY PGLTAISPLA SAATTA