ID   RHGE_ASPFN              Reviewed;         449 AA.
AC   B8NKB9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable rhamnogalacturonase E;
DE            Short=RGase E;
DE            Short=RHG E;
DE            EC=3.2.1.171;
DE   Flags: Precursor;
GN   Name=rhgE; ORFNames=AFLA_089930;
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 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   -!- 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED48913.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EQ963480; EED48913.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002380814.1; XM_002380773.1.
DR   AlphaFoldDB; B8NKB9; -.
DR   SMR; B8NKB9; -.
DR   EnsemblFungi; EED48913; EED48913; AFLA_089930.
DR   eggNOG; ENOG502S379; Eukaryota.
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.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..449
FT                   /note="Probable rhamnogalacturonase E"
FT                   /id="PRO_0000394957"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        346..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..383
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  47920 MW;  4B4373D065CFC7CF CRC64;
     MRSKTFSVLS SCLLLIATVQ GQLSGSVGPS TSISDKKAVK TCNVLDYGAT NDNKTDVGQP
     IMDAFEDCGS GGVIYIPDGD YLIQEWVSLE NGTAFAIQLD GVIYRNGTTT SQGYMFGISG
     GSDFELYSST SKGAIQGSGY LYHMNGEFTA PRLLHISDVS HWSVHDIALV DAPMFHFVID
     DASNGEVYNM AIRGGNSGGL DGIDVSGDNI WIHDVMVTNK DECVTVKTGS HNFQIENIYC
     NWSGGCAMGS LGSGTNVSNI VYRNIYTWNS NQMYMIKSNG GDGEVSNLLF ENFIGHGNAY
     SLDLDSEWSS MDTVDGDGIF YRNITFKNWK GTETDGESRP SIRVICPEAT PCTDITIEDV
     DLWTEEGDSE TYVCKNAFGS GACLKSDSSS TATYATTTTV TSAPSGYSAT TMAADLTSAF
     GTDASIPIPT IPTSFYPGAT PYSALAGSS