ID   RHGB_ASPNG              Reviewed;         558 AA.
AC   P87161;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Rhamnogalacturonase B;
DE            Short=RGase B;
DE            Short=RHG B;
DE            EC=3.2.1.171;
DE   Flags: Precursor;
GN   Name=rhgB;
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 4.1. {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; X94221; CAA63912.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87161; -.
DR   SMR; P87161; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   CLAE; RHG28B_ASPNG; -.
DR   VEuPathDB; FungiDB:An14g04200; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1141671; -.
DR   VEuPathDB; FungiDB:ATCC64974_3630; -.
DR   VEuPathDB; FungiDB:M747DRAFT_3040; -.
DR   eggNOG; ENOG502R2FT; Eukaryota.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..558
FT                   /note="Rhamnogalacturonase B"
FT                   /id="PRO_0000394388"
FT   REGION          503..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        372..381
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   558 AA;  57903 MW;  34665B5E66ED0655 CRC64;
     MLLDKLSVLS FLGLAPIFAA AQLSGSVGPL TSASTKAATK TCNVLDYGAK ADKSTDLGAP
     LASAFADCKS GGLVYVPSGD YALSTWARLS GGEAWALQID GIIYRTGTDG GNMIYIEHSS
     DFELFSSTSE GAMQGLGYEF HADDNWSGPR LLRLYEVTDF SVHDFILVDS PSFHFSLDTC
     TNGEIYNMAI RGGNHGGLDG IDVWSNNIWV HDVEVTNKDE CVTVKGPSKN ILIESIYCNW
     SGGCGMGSFG SDTNVSDITY RNIYTWSSNN MMLIKSNGGS GFVENVLLEN FIGHGNAYSL
     DIDSYWASMS AVDGDGVQLS NITVKNWKGT EAYGAERGPV KVVCADGAPC YDITIEDFAM
     WTEEGDSQWY SCESAYGSGY CLQDSDDHVS YSVTTSTVSS APSGYSATSM AADLTTDFGS
     TVSIPIPTIP TSFYPGATPY SALMANSAST AAASSIASHA TVHSSSASVA ASVPSAVAPS
     ESIPAATSAV VSSAAAIAPS PAVGAQEGST TSAPSFAAPS GAGNSPQGPT GASGFGEKGQ
     QGEQGEQGEQ GEQGVCYV