PGLRD_EMENI
ID PGLRD_EMENI Reviewed; 514 AA.
AC Q5AYH4; C8V1E3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable endopolygalacturonase D;
DE Short=PGD;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase D;
DE AltName: Full=Polygalacturonase D;
DE Flags: Precursor;
GN Name=pgaD; ORFNames=AN6656;
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 [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 [2]
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 (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AACD01000110; EAA58185.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF71186.1; -; Genomic_DNA.
DR RefSeq; XP_664260.1; XM_659168.1.
DR AlphaFoldDB; Q5AYH4; -.
DR SMR; Q5AYH4; -.
DR STRING; 162425.CADANIAP00007439; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; CBF71186; CBF71186; ANIA_06656.
DR EnsemblFungi; EAA58185; EAA58185; AN6656.2.
DR GeneID; 2870420; -.
DR KEGG; ani:AN6656.2; -.
DR VEuPathDB; FungiDB:AN6656; -.
DR eggNOG; ENOG502QW1P; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q5AYH4; -.
DR OMA; QGDWYWE; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase activity; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; ISS: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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..514
FT /note="Probable endopolygalacturonase D"
FT /id="PRO_0000393663"
FT REPEAT 280..302
FT /note="PbH1 1"
FT REPEAT 303..341
FT /note="PbH1 2"
FT REPEAT 342..363
FT /note="PbH1 3"
FT REPEAT 364..384
FT /note="PbH1 4"
FT REPEAT 393..414
FT /note="PbH1 5"
FT REPEAT 422..444
FT /note="PbH1 6"
FT REPEAT 456..500
FT /note="PbH1 7"
FT REGION 134..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..188
FT /evidence="ECO:0000250"
FT DISULFID 358..374
FT /evidence="ECO:0000250"
FT DISULFID 483..488
FT /evidence="ECO:0000250"
FT DISULFID 506..513
FT /evidence="ECO:0000250"
SQ SEQUENCE 514 AA; 52732 MW; 90FD05384EA55A6F CRC64;
MKRCALLTPL LPLALACNNP NDPAHSCASI YSVSSDEAAS FCATFTASVV SEPTGVPDAF
LSACDSKIKH LSSACSCLGP VDSATATPVP ATSTVPASVP VITTSTATAT PSRIPVFVPS
SSSSSAVVTF KTQIKSSSPG PSSSFAAAAT TEAPTSTRAS PYTPYTGNGG TTCTVTDYAG
ISSAVASCSN IMLSDVYAPP SSTIDLQDLQ TGAAVIFAGK TTFGDTSDSD FDPIVISGTN
LTITGTEDHV IDGNGQAYWD GQGSNGGSDK PDHFIVLKHV YNSVVANLNI QNWPVHCFDI
ENTESLTLTG ITLDNSAGDE PNDSSDGDPA AHNSDGFDIK SSTDLILKDS NVYNQDDCVA
ITSGTNITVD NMYCSGGHGL SIGSIGGKSD NTVDGVVFSN SQVVNSQNGC RIKTNEGETG
EVSNIKYENI SLSGISKYGI VVQQDYLNGG PTGEPSNGVS ITNVEFTDVT GTMSGGKDYY
ILCGDGSCEN FTFSGVSITG GSDDSCNYPD SGCP
