PGLRB_EMENI
ID PGLRB_EMENI Reviewed; 364 AA.
AC Q5B508; C8V8X1; Q1HFT2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Endopolygalacturonase B;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase B;
DE AltName: Full=Polygalacturonase B;
DE Flags: Precursor;
GN Name=pgaB; Synonyms=pecB; ORFNames=AN4372;
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 5.1. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 38 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF77661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA60289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490492; ABF50868.1; -; mRNA.
DR EMBL; AACD01000076; EAA60289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF77661.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_661976.1; XM_656884.1.
DR AlphaFoldDB; Q5B508; -.
DR SMR; Q5B508; -.
DR STRING; 162425.CADANIAP00006086; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; EAA60289; EAA60289; AN4372.2.
DR GeneID; 2872172; -.
DR KEGG; ani:AN4372.2; -.
DR VEuPathDB; FungiDB:AN4372; -.
DR eggNOG; ENOG502QTAW; Eukaryota.
DR HOGENOM; CLU_040116_0_0_1; -.
DR InParanoid; Q5B508; -.
DR OrthoDB; 601945at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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; 6.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..29
FT /evidence="ECO:0000255"
FT /id="PRO_0000393654"
FT CHAIN 30..364
FT /note="Endopolygalacturonase B"
FT /id="PRO_0000393655"
FT REPEAT 159..188
FT /note="PbH1 1"
FT REPEAT 189..210
FT /note="PbH1 2"
FT REPEAT 211..231
FT /note="PbH1 3"
FT REPEAT 240..261
FT /note="PbH1 4"
FT REPEAT 269..291
FT /note="PbH1 5"
FT REPEAT 303..348
FT /note="PbH1 6"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..47
FT /evidence="ECO:0000250"
FT DISULFID 205..221
FT /evidence="ECO:0000250"
FT DISULFID 331..336
FT /evidence="ECO:0000250"
FT DISULFID 355..364
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 37857 MW; DB54DC4FFEE92897 CRC64;
MHFLQNSLIA AAMGAALVAA APAADLDARS SCTFTSASAA KSGASKCSTV TLKSIQVPAG
ETLDLTGLKS GATVIFEGET TFGYKEWKGP LISMSGDKIT VKQASGAKIN CDGARWWDTK
GSNGGKTKPK FFSAHKLNNS KIQGLKIYNT PVQGFSIQSD HLTISDVTID NSAGTSKGHN
TDAFDIGSST YITIDGATVY NQDDCIAINS GEHITFTNGY CSGGHGLSIG SVGGRSDNTV
KSVTISNSKV VDSQNGVRIK TVYKATGSVT DVTFQDIELS GITKYGLIVE QDYENGSPTG
TPTNGVEVED ITFKKITGSV DSSATRVNIL CGSGSCKDWT WSGVDITGGK KSSKCKNVPS
GASC
