ID A0A177D053_9PLEO Unreviewed; 339 AA.
AC A0A177D053;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Arabinanase/levansucrase/invertase {ECO:0000313|EMBL:OAG12339.1};
GN ORFNames=CC84DRAFT_112854 {ECO:0000313|EMBL:OAG12339.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12339.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG12339.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12339.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KV441548; OAG12339.1; -; Genomic_DNA.
DR RefSeq; XP_018042704.1; XM_018175800.1.
DR AlphaFoldDB; A0A177D053; -.
DR STRING; 1460663.A0A177D053; -.
DR GeneID; 28759286; -.
DR InParanoid; A0A177D053; -.
DR OrthoDB; 5470935at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT SITE 135
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 339 AA; 37616 MW; 74E68E22182230DE CRC64;
MADKKPFVTH LYTADPSAHV FNGKLYVYPS HDRETDIKNN DNGDQYDMND YHVFSMEEVG
GPVTDHGVVL KVEDVPWVSR QLWAPDAASK NGKYYLYFPA RDKDDIFRIG VAVGDKPEGP
FKAEPEHIKG TFSVDPAVFV DDDGQAYLYF GGLWGGQLQC YANGDFDKSQ LGANEPSKGS
ALHAKVAKLS DDMLSLAGDV SDVVIQDPTT KAPIAAEDHA RRFFEAAWLH KYNGKYYFSY
STGDTHLLAY AIGDTPLGPF TYGGTILEPV IGWTTHHSIA EFKGKWYLFY HDSSLSGGEN
HLRSAKIREI VYDGDGKIHL AEPQPQIKPP AARLEEEGS
//
