ID A0A2H3IKK9_9EURO Unreviewed; 384 AA.
AC A0A2H3IKK9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=mannan endo-1,4-beta-mannosidase {ECO:0000256|ARBA:ARBA00012706};
DE EC=3.2.1.78 {ECO:0000256|ARBA:ARBA00012706};
GN ORFNames=PENO1_059540 {ECO:0000313|EMBL:PCG98175.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG98175.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG98175.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG98175.1,
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 -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans.
CC {ECO:0000256|ARBA:ARBA00002993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001678};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:PCG98175.1}.
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DR EMBL; NPFK01000168; PCG98175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IKK9; -.
DR STRING; 290292.A0A2H3IKK9; -.
DR OrthoDB; 2717493at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProt.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR PANTHER; PTHR31451:SF60; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:PCG98175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 90..351
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 40646 MW; 6B0FAFC516EC5363 CRC64;
MCLGICTATT TTSSTLTTTT SKSTSSTSKT TSSSTTTSAP TSTGFSKVNG LNFTIDGKTS
YFVGTNTYWL AFLNNNSDVD LVLSDIAASG MKILRVWGFN DVNSVPSAGT VYFQLLANGT
ATINTGADGL EKLDYVVSSA EAHGIKLIIP FVNNWSDYGG MAAYVTAFGG SQTTWYTNAA
AQAAYQAYIK AVVSRYSSSP AILAWELGNE PRCNGCNTSV LTEWAETTSA YIKSLDSNHM
VTTGIEGFGL DAGSDGSYPY TYGEGTNFTA LLSIPDIDFG TIHLYPDSWG EALSWGSSWV
STHGAACASI GKPCILEEFG TSTNQCANEA PWQATSLDTK GMAADMYWQY GDTLSTGQSP
NDGNTIYYGT DTFTCIVTDH IAAI
//
