RPG14_RHIO9
ID RPG14_RHIO9 Reviewed; 372 AA.
AC I1BYN5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Exopolygalacturonase rpg14 {ECO:0000303|PubMed:18935968};
DE EC=3.2.1.67 {ECO:0000269|PubMed:18935968};
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase rpg14 {ECO:0000305};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase rpg14 {ECO:0000305};
DE Flags: Precursor;
GN Name=rpg14 {ECO:0000303|PubMed:18935968}; ORFNames=RO3G_06020;
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.
CC {ECO:0000269|PubMed:18935968, 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 30 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; CH476735; EIE81315.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BYN5; -.
DR SMR; I1BYN5; -.
DR STRING; 936053.I1BYN5; -.
DR CLAE; PGX28N_RHIOR; -.
DR EnsemblFungi; EIE81315; EIE81315; RO3G_06020.
DR VEuPathDB; FungiDB:RO3G_06020; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR InParanoid; I1BYN5; -.
DR OMA; CINISAQ; -.
DR OrthoDB; 1028572at2759; -.
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; 5.
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..372
FT /note="Exopolygalacturonase rpg14"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432726"
FT REPEAT 152..183
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 184..205
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 207..227
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 237..258
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 303..350
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 221
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 200..217
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 332..338
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 372 AA; 39623 MW; 8593A345F13397A9 CRC64;
MVRFISLNIS VTALLLFSFR THLTTAASTN TCVVAKDSSD DAITIAKAFE DCKTDGTVVF
SKNTTYSLKS VLELSGLQNV NVDLAGTIEL PARNTSYSTT SAFIHFEGSN INLYDALDHT
APPTILVSAN DSSFGSFRIV NAPRAHMRIK NSNNILVHNV TFHTASSNIC YLPKNTDALQ
ITQSSNIVFK DSYLTVGDDC TAINGGVTNV TVSNIICNGG HGFSVGSLGK GGSTDVVRQV
RVRDSTCNGC ENGVRIKTWP GGQGSVSDVN YNNIILNNVD NPILVTTHYC DPNVIEYCNS
NDTISLTISD VHFKDITGSV SALGNPVVNI NCSSLTPCSD FTLSGVDITR VTTTSNNVCE
NLNGSSDISV CS
