RPG15_RHIO9
ID RPG15_RHIO9 Reviewed; 385 AA.
AC I1BYM7;
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 rpg15 {ECO:0000303|PubMed:18935968};
DE EC=3.2.1.67 {ECO:0000269|PubMed:18935968};
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase rpg15 {ECO:0000305};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase rpg15 {ECO:0000305};
DE Flags: Precursor;
GN Name=rpg15 {ECO:0000303|PubMed:18935968}; ORFNames=RO3G_06012;
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; EIE81307.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BYM7; -.
DR SMR; I1BYM7; -.
DR STRING; 936053.I1BYM7; -.
DR CLAE; PGX28O_RHIOR; -.
DR EnsemblFungi; EIE81307; EIE81307; RO3G_06012.
DR VEuPathDB; FungiDB:RO3G_06012; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR InParanoid; I1BYM7; -.
DR OMA; YSPQWYT; -.
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..385
FT /note="Exopolygalacturonase rpg15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432725"
FT REPEAT 165..195
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 196..217
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 219..241
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 249..270
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 350..376
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 212..229
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 344..350
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 385 AA; 41501 MW; 3BE73FE39B8F0583 CRC64;
MVRFISFTSP IAALLLLSFG VKHASTASTN TCIVANSDSD DAITIAEAFE KCKTGGTVVF
PKDSSYQLNS IVTTSDLKNV NINFAGTIHL PAREESYRNG DYYIQIKGTH IKMYGGGTIN
GHGQAWYDAL DHTAPSVLRI AANDSIIGGF TIINSPRAHL NVTNSTNLVL HDFTLHTVSN
NSYLPKNTDA LDLYHSSGIT FRDSMLTIGD DCVAIKEDVE KVIVSNVTCR GGHGYSIGSL
GIGGRKDYVK HVNFRNSTCI DCENGVRVKT WAGGKGIVED INYNDIILQN VDNPILVTTH
YCDPNVIEYC NGNDDNSLNI SSIHFKDITG TASALGNPIV NVNCSIESPC SDITFSGIDI
TKASNTTDNV CVYLEGSDEV SECSS
