PGLR_TOBAC
ID PGLR_TOBAC Reviewed; 396 AA.
AC Q05967;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase;
DE Flags: Precursor;
GN Name=PG1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 12-396,
RP AND VARIANTS VAL-154; SER-258; VAL-262; ARG-286; CYS-343 AND ASP-381.
RC STRAIN=cv. Havana; TISSUE=Pollen;
RX PubMed=8018876; DOI=10.1007/bf00023244;
RA Tebbutt S.J., Lonsdale D.M.;
RT "Characterization of a tobacco gene encoding a pollen-specific
RT polygalacturonase.";
RL Plant Mol. Biol. 25:283-297(1994).
CC -!- FUNCTION: May function in depolymerizing pectin during pollen
CC development, germination, and tube growth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall.
CC -!- TISSUE SPECIFICITY: Pollen.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; X71020; CAA50338.1; -; Genomic_DNA.
DR EMBL; X71017; CAA50335.1; -; mRNA.
DR EMBL; X71018; CAA50336.1; -; mRNA.
DR EMBL; X71016; CAA50334.1; -; mRNA.
DR EMBL; X71019; CAA50337.1; -; mRNA.
DR PIR; S46532; S46532.
DR PIR; S46533; S46533.
DR AlphaFoldDB; Q05967; -.
DR SMR; Q05967; -.
DR STRING; 4097.Q05967; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
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; 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.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 2: Evidence at transcript level;
KW Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..396
FT /note="Polygalacturonase"
FT /id="PRO_0000024813"
FT REPEAT 172..198
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 199..220
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 252..273
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 282..303
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 316..356
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT REGION 364..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 215..232
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 372..388
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT VARIANT 154
FT /note="I -> V"
FT /evidence="ECO:0000305|PubMed:8018876"
FT VARIANT 258
FT /note="R -> S"
FT /evidence="ECO:0000305|PubMed:8018876"
FT VARIANT 262
FT /note="F -> V"
FT /evidence="ECO:0000305|PubMed:8018876"
FT VARIANT 286
FT /note="H -> R"
FT /evidence="ECO:0000305|PubMed:8018876"
FT VARIANT 343
FT /note="R -> C (in clones G27W, G27X and G27Y)"
FT /evidence="ECO:0000305|PubMed:8018876"
FT VARIANT 381
FT /note="G -> D (in clone G27W)"
FT /evidence="ECO:0000305|PubMed:8018876"
SQ SEQUENCE 396 AA; 42469 MW; B3A486FB281E492B CRC64;
MDLKFKVHFA LVLLFLAHFG ESQTGVFDIT KYGANSNADI SEALLNAFKE ACQSTSPSTI
VIPKGTFTMN QVKLEGPCKS PLELQIQATL KAPSDPSQLK VGEWLTVNKL DQFTMSGGGI
LDGQAAAAWE CKQSKKCNKL PNNLSFNSLT NSTIKDITTL DSKSFHVNVN QCKNLTFIRF
NVSAPANSPN TDGIHVSRSS SVNITDSNFS TGDDCISVGD ETEQLYITRV TCGPGHGISV
GSLGGNPDEK PVVGVFVRNC TFTNTDNGVR IKTWPASHPG VVNDVHFEDI IVQNVSNPVV
IDQVYCPFNK CNKDLPSQVK ISKVSFQNIK GTSRTQDAVS LLRSKGVPCE GIEVGDIDIT
YSGKEGPAKS SCENIKPSLK GKQNPPVCTA SAASSS
