RPG13_RHIO9
ID RPG13_RHIO9 Reviewed; 363 AA.
AC I1BPS7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Exopolygalacturonase rpg13 {ECO:0000303|PubMed:18935968};
DE EC=3.2.1.67 {ECO:0000269|PubMed:18935968};
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase rpg13 {ECO:0000305};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase rpg13 {ECO:0000305};
DE Flags: Precursor;
GN Name=rpg13 {ECO:0000303|PubMed:18935968}; ORFNames=RO3G_02911;
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18935968; DOI=10.1016/j.fgb.2008.09.009;
RA Mertens J.A., Burdick R.C., Rooney A.P.;
RT "Identification, biochemical characterization, and evolution of the
RT Rhizopus oryzae 99-880 polygalacturonase gene family.";
RL Fungal Genet. Biol. 45:1616-1624(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RX PubMed=21161225; DOI=10.1007/s00284-010-9842-8;
RA Mertens J.A., Bowman M.J.;
RT "Expression and characterization of fifteen Rhizopus oryzae 99-880
RT polygalacturonase enzymes in Pichia pastoris.";
RL Curr. Microbiol. 62:1173-1178(2011).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. Has no activity towards
CC trigalacturonic acid. {ECO:0000269|PubMed:18935968,
CC ECO:0000269|PubMed:21161225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC Evidence={ECO:0000269|PubMed:18935968, ECO:0000269|PubMed:21161225};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:21161225};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:21161225};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18935968,
CC ECO:0000305|PubMed:21161225}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21161225}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; CH476733; EIE78207.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BPS7; -.
DR SMR; I1BPS7; -.
DR STRING; 936053.I1BPS7; -.
DR CLAE; PGX28M_RHIOR; -.
DR EnsemblFungi; EIE78207; EIE78207; RO3G_02911.
DR VEuPathDB; FungiDB:RO3G_02911; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR InParanoid; I1BPS7; -.
DR OMA; CENIASI; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..363
FT /note="Exopolygalacturonase rpg13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432724"
FT REPEAT 143..173
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 174..195
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 197..217
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 227..248
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 256..277
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REPEAT 328..354
FT /note="PbH1 6"
FT /evidence="ECO:0000255"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 211
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 190..207
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 322..328
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 363 AA; 37857 MW; DD35AFD1C79E85F0 CRC64;
MVKFLSLTSS VTALLLLSLG ANGVAAAATT CTVAKSGSDD TAAITKAFSD CKNGGTVVFS
KDTTYNLNGI LILSDLKNVN IELAGTIKLP GFDKAVKGLK SYIQLIGTNV KVYGGGVINA
NHSSVSDISI INSPRAHMGV TNATDVLINN ITLHTASTSS LRPKNTDALD VSRSSNVVFQ
NSKLTVGDDC LAINEEVTNV TLSKITCNGG HGFSVGSLGK GGANQHVKTV RIHDSVCNDC
QNGVRIKTWP GGKGSVSDIK FNNVELNNVE NPILITTHYC DKNQMNYCTN NDKTSLSISD
VVISDITGSA SNDGNPIVSI NCSTSTPCTD FTLSGVKITK ASNTPKNVCV NLDGSSKIAE
CSA
