RPG16_RHIO9
ID RPG16_RHIO9 Reviewed; 385 AA.
AC I1BYN6;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Exopolygalacturonase rpg16 {ECO:0000303|PubMed:18935968};
DE EC=3.2.1.67 {ECO:0000269|PubMed:18935968};
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase rpg16 {ECO:0000305};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase rpg16 {ECO:0000305};
DE Flags: Precursor;
GN Name=rpg16 {ECO:0000303|PubMed:18935968}; ORFNames=RO3G_06021;
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; EIE81316.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BYN6; -.
DR SMR; I1BYN6; -.
DR STRING; 936053.I1BYN6; -.
DR CLAE; PGX28P_RHIOR; -.
DR EnsemblFungi; EIE81316; EIE81316; RO3G_06021.
DR VEuPathDB; FungiDB:RO3G_06021; -.
DR eggNOG; ENOG502QPPR; Eukaryota.
DR InParanoid; I1BYN6; -.
DR OMA; WVVFGNI; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 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 rpg16"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432727"
FT REPEAT 165..195
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 219..241
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 249..270
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 278..299
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 218
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 282
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 359
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; 41641 MW; B63F258B8ADBF3B1 CRC64;
MVRFTSFTSP FSAILLLSFG INKVATASTN TCVVAKSDSD DAITILEAFE KCKTGGTVVF
PKDSTYNLNS IVTTSGLKNV NINLAGTINL PVREESYRNG DYYIQIKGTN IKMYGGGTIN
GNGQAWWDAL DRTAPSVLRI AANDSSFGNF NIINSPRAHL NVTNSTNLLL HDFIIHTVSN
NSNPAKNTDA LDLYHSSGVI FRDSDLTIGD DCLAVKENVT KVTVSNITCR GGHGYSIGSL
GMGGRRDFVT QVNVYNSTCI DCQNGVRVKT WAGGKGFVED INFTDIYLEK AENPIIITTH
YCDKNEMGYC NNNYETSLDI AGVHFKNIHG SGSDKGKPII NLNCSTESPC SDVTLTNINI
SKASNNTKNV CVNLKGSDKI PECSS
