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Database: UniProt
Entry: A0A2G9I4H9_9LAMI
LinkDB: A0A2G9I4H9_9LAMI
Original site: A0A2G9I4H9_9LAMI 
ID   A0A2G9I4H9_9LAMI        Unreviewed;       852 AA.
AC   A0A2G9I4H9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Non-lysosomal glucosylceramidase {ECO:0000256|PIRNR:PIRNR028944};
DE            Short=NLGase {ECO:0000256|PIRNR:PIRNR028944};
DE            EC=3.2.1.45 {ECO:0000256|PIRNR:PIRNR028944};
GN   ORFNames=CDL12_02614 {ECO:0000313|EMBL:PIN24651.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN24651.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
CC   -!- FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the
CC       hydrolysis of glucosylceramide (GlcCer) to free glucose and ceramide.
CC       {ECO:0000256|PIRNR:PIRNR028944}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC         acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC         ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC         ChEBI:CHEBI:52639; EC=3.2.1.45;
CC         Evidence={ECO:0000256|PIRNR:PIRNR028944};
CC   -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase family.
CC       {ECO:0000256|PIRNR:PIRNR028944}.
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:PIN24651.1}.
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DR   EMBL; NKXS01000380; PIN24651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9I4H9; -.
DR   STRING; 429701.A0A2G9I4H9; -.
DR   OrthoDB; 997839at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR014551; B_Glucosidase_GBA2-typ.
DR   InterPro; IPR006775; GH116_catalytic.
DR   InterPro; IPR024462; GH116_N.
DR   PANTHER; PTHR12654; BILE ACID BETA-GLUCOSIDASE-RELATED; 1.
DR   PANTHER; PTHR12654:SF27; NON-LYSOSOMAL GLUCOSYLCERAMIDASE; 1.
DR   Pfam; PF04685; DUF608; 1.
DR   Pfam; PF12215; Glyco_hydr_116N; 1.
DR   PIRSF; PIRSF028944; Beta_gluc_GBA2; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR028944, ECO:0000313|EMBL:PIN24651.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR028944, ECO:0000313|EMBL:PIN24651.1};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR028944};
KW   Membrane {ECO:0000256|PIRNR:PIRNR028944};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279}.
FT   DOMAIN          90..408
FT                   /note="Glycosyl-hydrolase family 116 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12215"
FT   DOMAIN          520..851
FT                   /note="Glycosyl-hydrolase family 116 catalytic region"
FT                   /evidence="ECO:0000259|Pfam:PF04685"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  94992 MW;  6155755310D31AC2 CRC64;
     MENGFIPEET VNSSDSPNKV DPGKPPLLTW QRTLNCISTI PTASFVRLRE IFHLLPLGLR
     LWRHVKEEAD KGTPSIMDPY HKRQVTCHHG VPLGGIGAGS IGRSFKGEFQ RFQLFPRVCE
     DTPNLANQFS VFVSRPKGGK SSTVLCSTSP NITEKNKGAG IDSWDWNLDG EKCTYHALFP
     RAWTVYDGLP DAEISIVCRQ ISPFIPHNYK ESSLPVAVFT FTLSNSGKTS ADATLLFTWA
     NSVGGDSGST GSHFNKRKMM QEGVHSVLLH HKTSNGRPPV TFAIAAQETD GVHVSECPCF
     LISGTSQIMT ANEMWKEIRE HSSFDCLKHQ ENQLPSEPGS SIGAAIAASV NIPPGSSRSM
     TFSLAWDCPE IRFPSGKTYH RRYTKFYGIN GNSAANIACD AILEHAKWEH QIEEWQRPIL
     EDRRLPEWYP ITLLNELYYL NAGSTIWTDG SLPTHCISTI GQQRFSLSNH ITGSDKSHKN
     DTSTDILERM QTVLERMHSP MASNSAFGPY LLQNAEENVG QLLYLEGIEY HMWNTYDVHF
     YSSFALLMLF PKLELSVQRD FAMAVMMHDP RKMKVMSNGT WVPRKVLGAV PHDIGLNDPW
     FEVNAYNFYD TDRWKDLNSK FVLQVYRDMI ATGDKSFAKA VWPAVFIAIA YMDQFDKDGD
     GMIENEGFPD QTYDAWTVKG VSSYCGGLWV AALQAASAMA SEIGDDSSAE YLWVKFEQAK
     SAYDRKLWNG SYFNYDSSNA KTSSSIQADQ LAGQWYARAC GLSPIADENK VRSALEKIYE
     FNVMKVRAGM CGAVNGMQPN GEVDLSALQS REIWSGVTYS VAAAMIQEGM VDMAFNTASG
     VYEAAWSEHG LG
//
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