ID A0A165NUJ2_EXIGL Unreviewed; 254 AA.
AC A0A165NUJ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:KZW01242.1};
DE Flags: Fragment;
GN ORFNames=EXIGLDRAFT_603246 {ECO:0000313|EMBL:KZW01242.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW01242.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW01242.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW01242.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043831};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC Class 3 subfamily. {ECO:0000256|ARBA:ARBA00043996}.
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DR EMBL; KV425895; KZW01242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165NUJ2; -.
DR STRING; 1314781.A0A165NUJ2; -.
DR InParanoid; A0A165NUJ2; -.
DR OrthoDB; 91669at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45856; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR45856:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZW01242.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 78..192
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZW01242.1"
SQ SEQUENCE 254 AA; 27773 MW; 183D6EB4DFFDE4E1 CRC64;
AVYDDLVHYY KYSCTAHALI LPGSALIPLF DLITDTHGYI ARDDKRQEIV VAFRGRCPSY
LLLVCSHHLT SHIEIGANSD CTFTAGTKVH MGFQAAWRSI APTLIATITA MLVSFPSYTI
VTTGHSLGGA LASFAAVSLQ MTFPTNKVRV YTYGAPRVGN KVFATWANTI LPLERAFRVV
HANDGVPTMA PEFEPFGYKH HGTEYWALSP HSPATTRICI APGELEDPEG SKKIFPSLGI
NPPHLVVRYG SHCV
//