(data stored in ACNUC16935 zone)

SWISSPROT: PGLX2_EMENI

ID   PGLX2_EMENI             Reviewed;         449 AA.
AC   Q5ARN5; C8VKQ3; Q1HFQ3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 74.
DE   RecName: Full=Exopolygalacturonase X-2;
DE            Short=ExoPG;
DE            EC=3.2.1.67;
DE   AltName: Full=Galacturan 1,4-alpha-galacturonidase;
DE   AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase;
DE   Flags: Precursor;
GN   Name=pgaX-2; ORFNames=AN9045;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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
RT   enzymes 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC       polygalacturonic acid and oligogalacturonates.
CC       {ECO:0000269|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-galacturonide)(n) + H(2)O =
CC       ((1->4)-alpha-D-galacturonide)(n-1) + D-galacturonate.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC       {ECO:0000305}.
DR   EMBL; DQ490521; ABF50897.1; -; mRNA.
DR   EMBL; AACD01000168; EAA64377.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF84398.1; -; Genomic_DNA.
DR   RefSeq; XP_682314.1; XM_677222.1.
DR   STRING; 162425.CADANIAP00007808; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; CADANIAT00007808; CADANIAP00007808; CADANIAG00007808.
DR   EnsemblFungi; EAA64377; EAA64377; AN9045.2.
DR   GeneID; 2868155; -.
DR   KEGG; ani:AN9045.2; -.
DR   HOGENOM; HOG000217379; -.
DR   InParanoid; Q5ARN5; -.
DR   KO; K01213; -.
DR   OMA; DVWFNNI; -.
DR   OrthoDB; EOG092C2CYK; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
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; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q5ARN5.
DR   SWISS-2DPAGE; Q5ARN5.
KW   Cell wall biogenesis/degradation; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    449       Exopolygalacturonase X-2.
FT                                /FTId=PRO_0000393673.
FT   REPEAT      240    261       PbH1 1.
FT   REPEAT      263    283       PbH1 2.
FT   REPEAT      294    315       PbH1 3.
FT   ACT_SITE    254    254       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10052}.
FT   ACT_SITE    277    277       {ECO:0000255|PROSITE-ProRule:PRU10052}.
FT   CARBOHYD    136    136       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    172    172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    262    262       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    301    301       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    306    306       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    340    340       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    256    273       {ECO:0000250}.
FT   DISULFID    403    409       {ECO:0000250}.
SQ   SEQUENCE   449 AA;  49161 MW;  1BC2033F112CDDDB CRC64;
     MGFKRTIGLL LGILLALDQV SVLAQPGRPT FAKRPDIQPN PIQPYKAIPL HSRRNSHKVC
     YVKPSLNGGD DAGRVEAALR RCNNGGTIVL DKEYSICTPL DLRFLKHVDV ALTGKVEFCP
     ELEFWQQNVF QFHFQNASSW WVWGGEDIHL YGAGTGVIHG NGQPWWDAAA GNSSVRRPLL
     FITDGWHGGS ITGLKLRQSP NWHNFIANSS DLLISDMDIF SRSSSEAWAS NLDGWDTFRS
     DNVVIQNSVI NHDDDCVSFK PNSTNIIVQG LHCNGSHGIS VGSLGNYPYQ YDIVSDLYIY
     NNTMANTTTA ARLKVWPGAE AVKKGNPPWV GGGGKGYVRN VTYDLMINDN NDLAIQIDQC
     YGAINASECL DHPSGVILTN VLFKNMWGTS NGANDPVAGQ LICGSADSCD NIRAENVTLT
     NSSGQPSEWQ CRYMDEELLD LGGVGCIPA
//

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