ID   RHGE_ASPNG              Reviewed;         450 AA.
AC   Q1ZZM3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Probable rhamnogalacturonase E;
DE            Short=RGase E;
DE            Short=RHG E;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=rhgE;
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].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=16822232; DOI=10.1042/bj20060703;
RA   Martens-Uzunova E.S., Zandleven J.S., Benen J.A., Awad H., Kools H.J.,
RA   Beldman G., Voragen A.G., Van den Berg J.A., Schaap P.J.;
RT   "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus
RT   niger that are involved in pectin degradation.";
RL   Biochem. J. 400:43-52(2006).
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 (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; DQ417224; ABD67156.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1ZZM3; -.
DR   SMR; Q1ZZM3; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   VEuPathDB; FungiDB:An11g08700; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1160216; -.
DR   VEuPathDB; FungiDB:ATCC64974_93570; -.
DR   VEuPathDB; FungiDB:M747DRAFT_3040; -.
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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..450
FT                   /note="Probable rhamnogalacturonase E"
FT                   /id="PRO_0000394958"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        375..384
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  48425 MW;  A6F1FACCED625ED8 CRC64;
     MTWSTSFLSV HFFAFITTSI HAQLTGSVGP LTSVSDKAAV KTCNVLDYGA RSDNTTDVGQ
     PIIDAFADCG SGGLIYIPEG DYLLKNWISL ENGSAWAIQL DGVLYRDSSP SSQSYMFEIS
     GGRDFELFSS NATGAIQGSG YLYHRDDTYT GPRMLHISGV SDWSVHDLVL VDSPMFHFVI
     DGGYNGEVYN MAIRGADHGG LDGIDVYGDN MWIHDIMVTN KDECVTTKTN SHNFLIENIY
     CNSSGGCAIG SLGSGANVSN IVYRNVYTWD SNQMMMIKSN GGSGDVSNAV FENFIGHGNA
     YSLDLDSYWS SMDAIDGDGI YYHNITFQNW TGTAVDGETR PPIRVICPED TPCTEIALVQ
     IDLWVEEGGY DEYICKNAYG SGYCLDSATG TSTPYTTTTY VNSAPTGYEA PTMTDDLATA
     FGTSASIPIP TIPASFFPGV TPISAVAGSS