ID   RHGB_ASPFC              Reviewed;         521 AA.
AC   B0Y0Q3;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=AFUB_058150;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499597; EDP51794.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y0Q3; -.
DR   SMR; B0Y0Q3; -.
DR   EnsemblFungi; EDP51794; EDP51794; AFUB_058150.
DR   VEuPathDB; FungiDB:AFUB_058150; -.
DR   HOGENOM; CLU_016031_7_2_1; -.
DR   PhylomeDB; B0Y0Q3; -.
DR   Proteomes; UP000001699; 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; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 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..521
FT                   /note="Probable rhamnogalacturonase B"
FT                   /id="PRO_0000394386"
FT   REGION          462..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..521
FT                   /note="Basic 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        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   521 AA;  55037 MW;  005357769C795C28 CRC64;
     MRLHAFTLLS LLGLVPSFAA ASLSGSVGPL TSASAKAAKK TCNVLDYGAK ADKKTDLGPP
     LAAAFAACKS GGLVYIPAGD YAMSTWVKLA NGKAWALQID GVIYRTGTDG GNMIMIEHTS
     DFELYSSTSS GAMQGLGYEF HASNNWSGPR LLRLWDVSDF SVHDLILVDS PSFHFSIDTC
     SNGEVYNMAI RGGNHGGLDG VDVWSTNIWI HDLEVTNKDE CVTVKSPAKN ILVENIYCNL
     SGGCAMGSLG ADTDISDITY KNIYTWNSNQ MMMIKSNGGS GTVSNVVFEN FIGHGNAYSL
     DIDSFWSSMS AVSGDGVTLN NITIKNWKGT EANGAQRGPI KIICPDKVPC YNILIEDFAM
     WTETGSKQWY SCQSAYGSGF CLKSGSHHTS YAVTTTTVSS APSGYSAAKM ASDLSTDFGS
     TKSIPIPTIP TSFYPGATPY SALMSKQSTK AAKARAVDMS VETPAAASRS EQVVQGAPQE
     TGQSAPESAG PVPSGNPGPV PTGGSRPSRH RHGHHHFGSA I