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Database: UniProt
Entry: H3GH59_PHYRM
LinkDB: H3GH59_PHYRM
Original site: H3GH59_PHYRM 
ID   H3GH59_PHYRM            Unreviewed;       322 AA.
AC   H3GH59;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000256|ARBA:ARBA00012586};
DE            EC=3.2.1.99 {ECO:0000256|ARBA:ARBA00012586};
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase A {ECO:0000256|ARBA:ARBA00042202};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra75228, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra75228}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra75228};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC         (1->5)-arabinans.; EC=3.2.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000375};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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DR   EMBL; DS566008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GH59; -.
DR   STRING; 164328.H3GH59; -.
DR   EnsemblProtists; Phyra75228; Phyra75228; Phyra75228.
DR   EnsemblProtists; Phyra75232; Phyra75232; Phyra75232.
DR   VEuPathDB; FungiDB:PSURA_75228; -.
DR   VEuPathDB; FungiDB:PSURA_75232; -.
DR   eggNOG; ENOG502QTQG; Eukaryota.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   InParanoid; H3GH59; -.
DR   OMA; LIYHYYT; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18831; GH43_AnAbnA-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..322
FT                   /note="arabinan endo-1,5-alpha-L-arabinosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010118862"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            151
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   322 AA;  35044 MW;  A18689847BA9069C CRC64;
     MKLWPVLRGL PFLLSAGLVA GYVNPETCTG TCTNAHDPSI IRRSDGTYFR FSTGNKIAVH
     SAPDIVGPWT YLGAAVPDGS TIDLDGNDDL WAPDVHLVGD EYYLYYSVST FGSQNSAIGL
     TRSSTMAIGT WTDYGSTGIT SSSSKDYNAI DPNLIDVDGT YYLNFGSYWQ DIYQAEMKSI
     PTAHSGSASQ IAFTSDYEVL EGSYMFQYGD YYYLFLSKGQ CCSYDTSKPA SGKEYRILVC
     RSSSATGSFV DKDGTACTSG GGSIVLESHE EVYGPGGQGV YDDPTYGPVL YYHYVNTTIG
     YADGDKRFGW NYLDFSSGWP AV
//
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