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Database: UniProt
Entry: V2WKT4_MONRO
LinkDB: V2WKT4_MONRO
Original site: V2WKT4_MONRO 
ID   V2WKT4_MONRO            Unreviewed;       310 AA.
AC   V2WKT4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=Moror_11599 {ECO:0000313|EMBL:ESK87473.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87473.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK87473.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87473.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK87473.1}.
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DR   EMBL; AWSO01000779; ESK87473.1; -; Genomic_DNA.
DR   RefSeq; XP_007853224.1; XM_007855033.1.
DR   AlphaFoldDB; V2WKT4; -.
DR   STRING; 1381753.V2WKT4; -.
DR   KEGG; mrr:Moror_11599; -.
DR   HOGENOM; CLU_009397_5_1_1; -.
DR   OrthoDB; 2418563at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000017559; 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; cd08998; GH43_Arb43a-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:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..310
FT                   /note="arabinan endo-1,5-alpha-L-arabinosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004711050"
FT   ACT_SITE        33
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            149
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   310 AA;  32824 MW;  FBEE3FCD6A9D0ACB CRC64;
     MRPSSFAYGL VLAAVARAQV GPGTVTGDTA VHDPTMCKDK NGKYWVFSTG QGIPIRSSTD
     RTAFKLEGKV WPNGASWTDQ YTGVSNGDLW APDCYYSGGT FHLFYAASSF GSQNSGIFYA
     KSTTGLPGSF SNEGLVLSTS GSNNFNAIDP NLLVVGNTWY LSLGSFWTGI KSVTLNPSTG
     KPNTSTITSL AQRTANGGAI EASNVFKNGN YYYLFTSWDN CCRGTSSTYN IRVGRSSNPN
     GGFVDKSGVA LTSGGGTLVL QTHGNIIGPG GQDLMDDGDG PILIYHYYTP SGSFLGINRL
     DFSSGWPVVV
//
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