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Endopolygalacturonase AN8327 (EC 3.2.1.15) (Pectinase AN8327) (Polygalacturonase AN8327)

 PGLR_EMENI              Reviewed;         380 AA.
Q5ATQ3; C8VE18; Q1HFQ7;
20-APR-2010, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
20-JUN-2018, entry version 79.
RecName: Full=Endopolygalacturonase AN8327;
EC=3.2.1.15;
AltName: Full=Pectinase AN8327;
AltName: Full=Polygalacturonase AN8327;
Flags: Precursor;
ORFNames=AN8327;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16844780; DOI=10.1073/pnas.0604632103;
Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
"Development and application of a suite of polysaccharide-degrading
enzymes for analyzing plant cell walls.";
Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
-!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate
in the smooth region of the plant cell wall.
{ECO:0000269|PubMed:16844780}.
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-alpha-D-
galactosiduronic linkages in pectate and other galacturonans.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 4.8. {ECO:0000269|PubMed:16844780};
Temperature dependence:
Optimum temperature is 48 degrees Celsius.
{ECO:0000269|PubMed:16844780};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
{ECO:0000305}.
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EMBL; DQ490517; ABF50893.1; -; mRNA.
EMBL; AACD01000150; EAA66950.1; -; Genomic_DNA.
EMBL; BN001305; CBF80314.1; -; Genomic_DNA.
RefSeq; XP_681596.1; XM_676504.1.
ProteinModelPortal; Q5ATQ3; -.
SMR; Q5ATQ3; -.
STRING; 162425.CADANIAP00002791; -.
CAZy; GH28; Glycoside Hydrolase Family 28.
EnsemblFungi; CBF80314; CBF80314; ANIA_08327.
EnsemblFungi; EAA66950; EAA66950; AN8327.2.
GeneID; 2868744; -.
KEGG; ani:AN8327.2; -.
HOGENOM; HOG000193107; -.
InParanoid; Q5ATQ3; -.
KO; K01184; -.
OMA; TTTWGYK; -.
OrthoDB; EOG092C33Y3; -.
Proteomes; UP000000560; Chromosome V.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0004650; F:polygalacturonase activity; IDA:UniProtKB.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR000743; Glyco_hydro_28.
InterPro; IPR006626; PbH1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
Pfam; PF00295; Glyco_hydro_28; 1.
SMART; SM00710; PbH1; 7.
SUPFAM; SSF51126; SSF51126; 1.
PROSITE; PS00502; POLYGALACTURONASE; 1.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Complete proteome; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Repeat;
Secreted; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 35 {ECO:0000255}.
/FTId=PRO_0000393694.
CHAIN 36 380 Endopolygalacturonase AN8327.
/FTId=PRO_0000393695.
REPEAT 147 169 PbH1 1.
REPEAT 170 200 PbH1 2.
REPEAT 201 222 PbH1 3.
REPEAT 223 243 PbH1 4.
REPEAT 252 273 PbH1 5.
REPEAT 281 303 PbH1 6.
REPEAT 315 338 PbH1 7.
ACT_SITE 215 215 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10052}.
ACT_SITE 237 237 {ECO:0000255|PROSITE-ProRule:PRU10052}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 57 {ECO:0000250}.
DISULFID 217 233 {ECO:0000250}.
DISULFID 345 350 {ECO:0000250}.
DISULFID 369 378 {ECO:0000250}.
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


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