ID A0A081CKN8_PSEA2 Unreviewed; 899 AA.
AC A0A081CKN8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=PAN0_017d5461 {ECO:0000313|EMBL:GAK67234.1}, PSANT_05846
GN {ECO:0000313|EMBL:SPO48158.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK67234.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK67234.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK67234.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO48158.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO48158.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; DF830084; GAK67234.1; -; Genomic_DNA.
DR EMBL; OOIQ01000017; SPO48158.1; -; Genomic_DNA.
DR RefSeq; XP_014654521.1; XM_014799035.1.
DR AlphaFoldDB; A0A081CKN8; -.
DR GeneID; 26306333; -.
DR HOGENOM; CLU_004624_6_2_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:GAK67234.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 230..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 401..561
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 98143 MW; 5E91F85A7263BB43 CRC64;
MSGRRQRDST AGESYELPAS PPSVAVEEPL LVNTSFATDP DATDASLQRL ASPKWSRSNS
RYSAFDEGLE PDSGGRFLSA AAAYQFDPAL SHGHPTPMQE RPFTPPFARS DSRPTSLASS
HMLSVRSRSD YDSVYQLWRQ SGTPSSFRDF ADDGASSHYD RRGSQARDLE KIEQYRAGAY
DPHSPPTGNA AFQGLHQGEA GAKGPKDYRA VGLAKYGRGK DQRMSARKKW CIVLAVAAVI
AICVIAVVVP ITQVLLKDKS SDRQANTSGS NSSSGAGASA GNGANPTPAP EKVVATWGVN
GSVIDLGNGN NFTYINNFGG RWASQPLNNS AQAQNYTPPL DQEFDFARNR ILGVNLGGWL
VTEPFIVPAL YEPYENTSSP AVDEFTLSQR YLSEGGADNL RAKMTEHYET FITEQDFANI
AAAGLNWVRL PIGFWALETY SNEPFLEGVA WNYVLKAIQW ARKYGLRINL DLHAVPGSQN
AYNHSGRVGF INYLQGLMGK ANGQRTLDYI RQIAQFISQP EIRNVVPMFS VINEPYAISI
GQPALQSWYS EVYSILRSIA GTGAGNGPYM TIHDGFLPLS SWSGFLGGGD RVAWDTHPYL
CFGQQNNDPW DVQILKPCQQ FTGLLDNARS NMGVSMGGEM SLAINDCGLF LNGVRDGHRY
DGSYTGPTPG DFPYVGSCQP FDDWENYSDE MKRGLRRFAL TSMGSLRDFF FWTWKTGNSL
RTGKPTSPMW SYSLGLQQGW MPTNPLAESS GACAAQASRL GTSVPSATWG SAFQNWQTGR
ASSYSPNTAA YPWPPQSLVS ANRPVSQLPS YTPTMSITPV PTPTISVTAT VSGDPTPSPT
IGAWYNSDDS TPFYTRIAGC EYPSDQYNLG NWNPSGWPCS GGQQRRDEQP RALPTNPPQ
//
