RHGB_ASPFU
ID RHGB_ASPFU Reviewed; 521 AA.
AC Q4WV23;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=AFUA_5G10530;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
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DR EMBL; AAHF01000003; EAL91553.1; -; Genomic_DNA.
DR RefSeq; XP_753591.1; XM_748498.1.
DR AlphaFoldDB; Q4WV23; -.
DR SMR; Q4WV23; -.
DR STRING; 746128.CADAFUBP00005687; -.
DR EnsemblFungi; EAL91553; EAL91553; AFUA_5G10530.
DR GeneID; 3511456; -.
DR KEGG; afm:AFUA_5G10530; -.
DR VEuPathDB; FungiDB:Afu5g10530; -.
DR eggNOG; ENOG502R2FT; Eukaryota.
DR HOGENOM; CLU_016031_7_2_1; -.
DR InParanoid; Q4WV23; -.
DR OMA; PNCQPNI; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..521
FT /note="Probable rhamnogalacturonase B"
FT /id="PRO_0000394387"
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; 54977 MW; E15357769C684D35 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 ASDLSTDSGS
TKSIPIPTIP TSFYPGATPY SALMSKQSTK AAKARAVDMS VETPAAASRS EQVVQGAPQE
TGQSAPESAG PVPSGNPGPV PTGGSRPSRH RHGHHHFGSA I
