PGLR_EMENI
ID PGLR_EMENI Reviewed; 380 AA.
AC Q5ATQ3; C8VE18; Q1HFQ7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Endopolygalacturonase AN8327;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase AN8327;
DE AltName: Full=Polygalacturonase AN8327;
DE Flags: Precursor;
GN ORFNames=AN8327;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in
CC the smooth region of the plant cell wall.
CC {ECO:0000269|PubMed:16844780}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.8. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; DQ490517; ABF50893.1; -; mRNA.
DR EMBL; AACD01000150; EAA66950.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF80314.1; -; Genomic_DNA.
DR RefSeq; XP_681596.1; XM_676504.1.
DR AlphaFoldDB; Q5ATQ3; -.
DR SMR; Q5ATQ3; -.
DR STRING; 162425.CADANIAP00002791; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; CBF80314; CBF80314; ANIA_08327.
DR EnsemblFungi; EAA66950; EAA66950; AN8327.2.
DR GeneID; 2868744; -.
DR KEGG; ani:AN8327.2; -.
DR VEuPathDB; FungiDB:AN8327; -.
DR eggNOG; ENOG502SHAF; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q5ATQ3; -.
DR OMA; GYCHGGH; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
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; 7.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..35
FT /evidence="ECO:0000255"
FT /id="PRO_0000393694"
FT CHAIN 36..380
FT /note="Endopolygalacturonase AN8327"
FT /id="PRO_0000393695"
FT REPEAT 147..169
FT /note="PbH1 1"
FT REPEAT 170..200
FT /note="PbH1 2"
FT REPEAT 201..222
FT /note="PbH1 3"
FT REPEAT 223..243
FT /note="PbH1 4"
FT REPEAT 252..273
FT /note="PbH1 5"
FT REPEAT 281..303
FT /note="PbH1 6"
FT REPEAT 315..338
FT /note="PbH1 7"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..57
FT /evidence="ECO:0000250"
FT DISULFID 217..233
FT /evidence="ECO:0000250"
FT DISULFID 345..350
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 39360 MW; E55F4F978BE10DC4 CRC64;
MFYALGPLAL FAFATEVMAT PVAYPMTTAS PTLAKRDSCT FSGSDGAASA SRSQTDCATI
TLSDITVPSG TTLDLSDLED DTTVIFEGTT SWEYEEWDGP LLQIKGNGIT IKGADGAKLN
PDGSRWWDGE GSNGGVTKPK FFYAHDLTDS TIQNLYIENT PVQAVSINGC DGLTITDMTI
DNSAGDDAGG HNTDGFDIGE SSNVVITGAK VYNQDDCVAV NSGTSITFSG GTCSGGHGLS
IGSVGGRDDN TVDTVTFKDS TVSNSVNGIR IKAKSGETGE IKGVTYSGIS LESISDYGIL
IEQNYDGGDL DGEVTSGIPI TDLTIENISG SGAVDSDGYN IVIVCGDDAC SNWTWSDVEV
TGGEDYGSCE NVPSVASCST
