(data stored in ACNUC16935 zone)

SWISSPROT: PGXB_EMENI

ID   PGXB_EMENI              Reviewed;         440 AA.
AC   Q873X6; C8VLS8; Q5AS39;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-JUL-2017, entry version 69.
DE   RecName: Full=Probable exopolygalacturonase B;
DE            EC=3.2.1.67;
DE   AltName: Full=Galacturan 1,4-alpha-galacturonidase B;
DE   AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase B;
DE   Flags: Precursor;
GN   Name=pgxB; ORFNames=AN8891;
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].
RA   Ray A., Mort A.J.;
RT   "Expression cloning of exopolygalacturonase from Aspergillus
RT   nidulans.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY237304; AAO61898.1; -; mRNA.
DR   EMBL; AACD01000164; EAA64105.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF84721.1; -; Genomic_DNA.
DR   RefSeq; XP_682160.1; XM_677068.1.
DR   ProteinModelPortal; Q873X6; -.
DR   SMR; Q873X6; -.
DR   STRING; 162425.CADANIAP00007978; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   EnsemblFungi; CADANIAT00007978; CADANIAP00007978; CADANIAG00007978.
DR   EnsemblFungi; EAA64105; EAA64105; AN8891.2.
DR   GeneID; 2868221; -.
DR   KEGG; ani:AN8891.2; -.
DR   HOGENOM; HOG000217379; -.
DR   InParanoid; Q873X6; -.
DR   KO; K01213; -.
DR   OMA; NGQRWWN; -.
DR   OrthoDB; EOG092C2CYK; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
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; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q873X6.
DR   SWISS-2DPAGE; Q873X6.
KW   Cell wall biogenesis/degradation; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    440       Probable exopolygalacturonase B.
FT                                /FTId=PRO_0000393681.
FT   ACT_SITE    260    260       Proton donor. {ECO:0000250}.
FT   ACT_SITE    283    283       {ECO:0000250}.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    190    190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    268    268       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    280    280       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    334    334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    412    412       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    262    279       {ECO:0000250}.
FT   DISULFID    397    403       {ECO:0000250}.
SQ   SEQUENCE   440 AA;  48661 MW;  51A8DF1D080E6ECB CRC64;
     MRLHFLPLVA LCATTASSLA FDSSTSQPPG AQVYSVNDAA GLKRIGAHHP KYHDRRTVTI
     RSSHNDTDDV SADFLWGIRR ANHGGRLLLK KGQKYVIGRK LDLSFLDNVE VQLDGELKFT
     DDVPYWQENN FYYDFQKSIS FWRWGGHDVR IFGRGTLNGN GQRWYNEFAG QEILDPDNTY
     YRPILFVAEN ATRLSVEGIT ELNSPCWTNF LVNSKDISFD NVFINAYSTN ASAEPKNTDG
     FDSLNVNGLS VTNTRVDIGD DCFSPKPNTT NIFVQNLWCN NTHGVSMGSI GQYPGVLDII
     EHAYIENVTL LNGENGARLK AWAGEDVGYG RINNITYKNI HVENTDYPIV LDQCYFNIPA
     DECASYPSQV NVTNIVFENV YGTSSGAEGN VVAELICSPN AICEDIKLKG INLTTPEGEK
     GVVVCDGISG GVGVECQSSE
//

If you have problems or comments...

PBIL Back to PBIL home page