RHGB_NEOFI
ID RHGB_NEOFI Reviewed; 516 AA.
AC A1DED1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=NFIA_076680;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027696; EAW17738.1; -; Genomic_DNA.
DR RefSeq; XP_001259635.1; XM_001259634.1.
DR AlphaFoldDB; A1DED1; -.
DR SMR; A1DED1; -.
DR STRING; 331117.A1DED1; -.
DR EnsemblFungi; EAW17738; EAW17738; NFIA_076680.
DR GeneID; 4585997; -.
DR KEGG; nfi:NFIA_076680; -.
DR VEuPathDB; FungiDB:NFIA_076680; -.
DR eggNOG; ENOG502R2FT; Eukaryota.
DR HOGENOM; CLU_016031_7_2_1; -.
DR OMA; KSNQMYM; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000006702; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..516
FT /note="Probable rhamnogalacturonase B"
FT /id="PRO_0000394391"
FT REGION 462..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..516
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 516 AA; 54800 MW; 01E6F33055552D6D CRC64;
MRLHAFTLLS LLGLVPSFAA ASLSGSVGPL TSASAKAAKK TCNVLDYGAK ADKKTDLGPP
LAAAFAACKS GGLVYIPAGN YAMSTWVKLA NGKAWALQID GVIYRTGTDG GNMIMIEHTS
DFELYSSTSS GAMQGLGYEL HAANNWSGPR LLRLWDVSDF SVHDLILVDS PSFHFSIDTC
SNGEVYNMAI RGGNHGGLDG VDVWSTNIWI HDVEVTNKDE CVTVKSPAKN ILVENIYCNL
SGGCGMGSLG ADTDISDITY KNIYTWNSNQ MMMIKSNGGS GTVSNVVLEN FIGHGNAYSL
DIDSYWSSMS AVSGDGVELS NITIKNWKGT EANGAQRGPI KIICPDKVPC YNILIEDFAM
WTETGSKQWY SCQSAYGSGF CLKSGSHHTS YAVTTTTVSS APSGYSAAKM PLDLSTDFGS
TQSIPIPTIP TSFYPGATPY SALMSKQSTK AAKARAVDMS VETPAAASRS EQVVQGASQE
TSQPAPESAG PVRSVPTGGN RPSRHRHGHH HFWIAA
