ID   RHGB_ASPTN              Reviewed;         526 AA.
AC   Q0CFC7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable rhamnogalacturonase B;
DE            Short=RGase B;
DE            Short=RHG B;
DE            EC=3.2.1.171;
DE   Flags: Precursor;
GN   Name=rhgB; ORFNames=ATEG_07607;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476604; EAU31869.1; -; Genomic_DNA.
DR   RefSeq; XP_001216228.1; XM_001216228.1.
DR   AlphaFoldDB; Q0CFC7; -.
DR   SMR; Q0CFC7; -.
DR   EnsemblFungi; EAU31869; EAU31869; ATEG_07607.
DR   GeneID; 4322704; -.
DR   VEuPathDB; FungiDB:ATEG_07607; -.
DR   eggNOG; ENOG502R2FT; Eukaryota.
DR   HOGENOM; CLU_016031_7_2_1; -.
DR   OMA; PNCQPNI; -.
DR   OrthoDB; 1028572at2759; -.
DR   Proteomes; UP000007963; 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:0046576; F:rhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS: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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..526
FT                   /note="Probable rhamnogalacturonase B"
FT                   /id="PRO_0000394390"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        220..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..349
FT                   /evidence="ECO:0000250"
FT   DISULFID        371..380
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  55261 MW;  1FF3741862EDC215 CRC64;
     MHVNTLSVLS LVGLVPLAAA RLSGSVGPLT SASAKAATKT CNVLDYGAAA DKTTDLGAPL
     ASAFADCKTG GLVYVPPGDY ALESWAQLSG GKAWALQIDG TIYRTGTDGG NMIFIEHSSD
     FELFSSTSSG AMQGLGYEFH KDDNWSGPRL LRLYDVSDFA LHDFILVDSP SFHLSLDTCS
     NGEVYNMAIR GGNHGALDGV DVWSTNIWIH DVEVTNKDEC VTVKSPAQNI LVENIYCNWS
     GGCGMGSLGA DTNISDITYR NVYTWNSNQM MLIKSNGGSG TVSNVVLENF IGHGNAYSLD
     IDSAWSSMST QSGDGVEFSN FTIRNWKGTE ANGAERGPVK IICPNGAPCY EMYIEDFAMW
     TEEGDEQWYT CQSAFGSGFC LQSGSDYSSY EATTSTATSA PSGYSAPTMA SDLTRDFGST
     VSIPIPTIPT SFYPGATPYS ALMGAQSSAS ANVRAVAFGT SAVVSRAGSS SRPAQTGSFL
     TKSTTAAAGS IMGPTAAAVQ GVCAPPAGQG RGAARYGGHR RHGHRH