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Database: UniProt
Entry: A0A0W8C4U0_PHYNI
LinkDB: A0A0W8C4U0_PHYNI
Original site: A0A0W8C4U0_PHYNI 
ID   A0A0W8C4U0_PHYNI        Unreviewed;       322 AA.
AC   A0A0W8C4U0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
GN   ORFNames=AM587_10011968 {ECO:0000313|EMBL:KUF79093.1}, AM588_10008462
GN   {ECO:0000313|EMBL:KUF98872.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF79093.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC   {ECO:0000313|EMBL:KUF79093.1}, race 1
RC   {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC   {ECO:0000313|EMBL:KUF98872.1};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF79093.1}.
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DR   EMBL; LNFO01004958; KUF79093.1; -; Genomic_DNA.
DR   EMBL; LNFP01000052; KUF98872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8C4U0; -.
DR   STRING; 4790.A0A0W8C4U0; -.
DR   EnsemblProtists; KUF79093; KUF79093; AM587_10011968.
DR   EnsemblProtists; KUF98872; KUF98872; AM588_10008462.
DR   OMA; LIYHYYT; -.
DR   OrthoDB; 2655644at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   Proteomes; UP000054636; 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:UP000052943};
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_5007439835"
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;  35010 MW;  C0ED997496E11B55 CRC64;
     MKVLSIFGAL PLLLSAPLVA GYANPETCTG ICTNAHDPSI IRRSDGTYFR FSTGGKIAVH
     SAPDIVGPWT YLGAAVPDGS VIDLDGNDDL WAPDVHLVGD EYYLYYSVST FGSQNSAIGL
     TRSSTMDIDS WTDNGSTGIA STSAKSYNAI DPNLIAVDGT YYLNFGSYWQ DIYQVEMKST
     PTKSTGSASQ IAFTSDYEVL EGAYMFKYGD YYYLFLSKGQ CCSYDTSKPA SGKEYRILVC
     RSSSATDDFV DQDGTSCRNG GGTIVLESHD EVYGPGGQGV YNDPTYGPVL YYHYVNTTIG
     YADGDKRFGW NYLDFSSGWP TV
//
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