ID A0A2H3I9F2_9EURO Unreviewed; 321 AA.
AC A0A2H3I9F2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Glycoside hydrolase, family 43 {ECO:0000313|EMBL:PCG90314.1};
GN ORFNames=PENO1_099770 {ECO:0000313|EMBL:PCG90314.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG90314.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG90314.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG90314.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:PCG90314.1}.
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DR EMBL; NPFK01000503; PCG90314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3I9F2; -.
DR STRING; 290292.A0A2H3I9F2; -.
DR OrthoDB; 1435052at2759; -.
DR Proteomes; UP000218381; 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:InterPro.
DR CDD; cd08999; GH43_ABN-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:PCG90314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..321
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013897625"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 148
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 321 AA; 33274 MW; 43DB03A86B1CB656 CRC64;
MSRSILPFAS VLALVGGAIA EPFLVLNSDF PDPSLIETSS GYYAFGTTGN GVNAQVASSP
DFNTWTLLSG TDALPGPFPS WVASSPQIWA PDVLVKADGT YVMYFSASAA SGSGKHCVGA
ATATSPEGPY TPVDSAVACP LDQGGAIDAN GFIDTDGTIY VVYKIDGNSL DGDGTTHPTP
IMLQQMEADG TTPAGSPIQL IDRSDLDGPL IEAPSLLLSN GIYYLSFSSN YYNTNYYDTS
YAYASSITGP WTKQSAPYAP LLVTGTETSN DGALSAPGGA DFSVDGTKIL FHANLNGQDI
SGGRALFASY ITEASDVVTL Q
//
