PGLRD_NEOFI
ID PGLRD_NEOFI Reviewed; 472 AA.
AC A1DBR6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=NFIA_099410;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027694; EAW20306.1; -; Genomic_DNA.
DR RefSeq; XP_001262203.1; XM_001262202.1.
DR AlphaFoldDB; A1DBR6; -.
DR SMR; A1DBR6; -.
DR STRING; 36630.CADNFIAP00008533; -.
DR EnsemblFungi; EAW20306; EAW20306; NFIA_099410.
DR GeneID; 4588514; -.
DR KEGG; nfi:NFIA_099410; -.
DR VEuPathDB; FungiDB:NFIA_099410; -.
DR eggNOG; ENOG502QW1P; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR OMA; QGDWYWE; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000006702; 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..472
FT /note="Probable endopolygalacturonase D"
FT /id="PRO_0000393664"
FT REPEAT 236..258
FT /note="PbH1 1"
FT REPEAT 259..297
FT /note="PbH1 2"
FT REPEAT 298..319
FT /note="PbH1 3"
FT REPEAT 349..370
FT /note="PbH1 4"
FT REPEAT 378..400
FT /note="PbH1 5"
FT REPEAT 412..433
FT /note="PbH1 6"
FT REPEAT 444..467
FT /note="PbH1 7"
FT ACT_SITE 312
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..144
FT /evidence="ECO:0000250"
FT DISULFID 314..330
FT /evidence="ECO:0000250"
FT DISULFID 439..444
FT /evidence="ECO:0000250"
FT DISULFID 462..469
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 48428 MW; 5A182761017C7E0A CRC64;
MKRGALLVPF VPLALACVDP GDSNHSCASV FSVSSAAAAS FCATFTVSAV TETTGVPAAL
LSNCDYKTKH LSSACSCLGP ATAAAPTQTS AVTPTVAPTT LKANAVAPTT EAPAPTKSST
FAGNGGTTCT VTEYAAISSA VASCSNILLS DVYAPPSSTI DLQNLQTGAA VIFAGTTTFG
DTPDDDFDPI VISGTDVTIT GADGHVIDGN GAAYWDGKGS NGGSSKPDHF IVAKHMYYSR
IENLNIQNWP VHCFDIEHTE NLIISGITLD NSAGDAPNSA SGSKPAAHNS DGFDIKSSTN
LTLQNSWVHN QDDCVAVSSG TDIVVDNMYC YGGHGLSIGS IGGKSDNTVD GVTFSNSQVI
NSSNGCRIKS NSGTTGEVSN IRYENITVSG ITDYGIDIQQ DYLNGGPTGK PTNGVKIENI
TFVDVTGTMS DGKDYYILCG DGSCSNFVFE NVGITGGSGD SCNYPTDTCL EA
