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Database: UniProt
Entry: D8PT40_SCHCM
LinkDB: D8PT40_SCHCM
Original site: D8PT40_SCHCM 
ID   D8PT40_SCHCM            Unreviewed;       326 AA.
AC   D8PT40;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
DE            EC=3.2.1.99 {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
GN   ORFNames=SCHCODRAFT_232782 {ECO:0000313|EMBL:EFJ00450.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFJ00450.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
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         ECO:0000256|PIRNR:PIRNR026534};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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DR   EMBL; GL377303; EFJ00450.1; -; Genomic_DNA.
DR   RefSeq; XP_003035352.1; XM_003035306.1.
DR   AlphaFoldDB; D8PT40; -.
DR   STRING; 578458.D8PT40; -.
DR   GeneID; 9597164; -.
DR   KEGG; scm:SCHCO_02485552; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02485552; -.
DR   eggNOG; ENOG502QTQG; Eukaryota.
DR   HOGENOM; CLU_009397_5_1_1; -.
DR   InParanoid; D8PT40; -.
DR   OMA; YHYVRES; -.
DR   OrthoDB; 2418563at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000007431; 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, ECO:0000256|PIRNR:PIRNR026534};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..326
FT                   /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003120316"
FT   ACT_SITE        33
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            147
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   326 AA;  34921 MW;  B941AA8AC4F683F7 CRC64;
     MRLQWLAALF SLGVLASATP APLPGSEDIV VRDPAIWYNA DLGKYFVFAT REGIKIYTAP
     SLKGPWTREG SVLPNCSSIQ LDGNCKLWAP DVNYINGEYV LYYSVSTIGS QNSAVGVATS
     PSMEQGTWTD LGEVIRSQGG DQFNAIDPNI IDDNGLKLAF GSYWNGMYQV GLSDIKTRAS
     DLPGTHLAGG NGRAAEGGFV YKPQGSPYYF MFFSAGTTPL EGGDSRPPAG SEYKVLVGRG
     DSAVGPFRGQ AGHELTEQVD PPTGSLVLGS HDTVYAPGGQ SIFLDPVSGR DVIVYHYVRM
     EEVGGTSYLG INYLDFSSGW PVVVEE
//
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