ID A0A081CBI4_PSEA2 Unreviewed; 1114 AA.
AC A0A081CBI4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=PAN0_004c2239 {ECO:0000313|EMBL:GAK64030.1}, PSANT_02442
GN {ECO:0000313|EMBL:SPO44756.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64030.1, 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:GAK64030.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64030.1};
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:SPO44756.1, 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:SPO44756.1};
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF830071; GAK64030.1; -; Genomic_DNA.
DR EMBL; OOIQ01000004; SPO44756.1; -; Genomic_DNA.
DR RefSeq; XP_014657670.1; XM_014802184.1.
DR AlphaFoldDB; A0A081CBI4; -.
DR GeneID; 26303012; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAK64030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053758};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1114
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035397363"
FT DOMAIN 421..584
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1114 AA; 123601 MW; 49A84EEDB48DB958 CRC64;
MRVSTAAFWG CLAWGLALLP HPLGTRAAQI PFSVSTQPQH ATAPATKWTL PRGSNNTAVV
FDKYSLALGA GQQRLFVLAA EFHPWRLPVP SLWRDVLQKI RAAGFNTVSI YTHWGLIQPS
PDAETIDLTG VNDLDFFLAL AKEVGLFVIV RPGPYINAET TVGGMAPWTV NLDAVLRTND
TAWREAWRPY IDAISRVVVK HQLVHDASRP DELHGGSVIL VQADNEYKTG KAERAYMMEL
VAALKENGIT VPITYNDPGR EQNFVDLVDL YGLDSYPQRF DCSHPETWVP MRDDYLQYHM
DTNPDQPFYI PEFQAGSYDP YAGPGYEACA RMTNASFTRV ANQALIAQRV TLLSLYMVYG
GTNWGGLAEP DVYSSYDYGA ALNEHRQPND KYAELKRQAG FIAAFPDLAM TEQIADKPGL
NISQVGDLDD EGVSVDAASI RTTVLENPQT KSRFYVVRHN DTSVSRRTRF ALHFVSQGKT
EVIGARQDEE VEKRIGVNFL AGRDSHIIPV DQQLPGGLVM RWCTANVNLV TTIGDALLIS
LDWTPGQLVE YSLATSEDDY IESMHLLRVS EAGIQEIQNG EWDTFVAMHS DIQSDPTNIR
ARMSSGEAND RYVVYRTAKA AWIIIMFSET ALTSGLFSVP ARYTSGRAGL SLHRPDSGLV
SRFFGHSEDS VVVMHVDMLR NATYASTDSP LDTLYLCGSL SHESHTALNA LPDLKYVYWN
GERIDAQADE VSRRFYRIHL PGPSRAALEW SPPRSDQLDW RWRDSMPEAS AAFDDSTWVQ
ANKTQSANPY TRDPSLDTQG AILFASEYGF HANNIVWRGR FATPDHTQDA PCDVHVRVEG
GRSSAFSVWF NGVYLGSAAA DREKSAAGAT FSLPSNALQT SGDNVLTVLQ DHMGIEMEAG
ELPIGLQEQR GLEAVKLPRG IVAFNFPSLR TASRPEPKVT WRVQGNLGGE QARDTVRRSL
NEGGLHAEVQ GWHLPGYDAS TWHNTLTHQR GRVTMYRTSF KLNGPQDSDV GVSFVFATLP
GVELRAQLYV NGWQMGKFVN ALGPQTVFPV HSGVLNHRGD NILAVSVWML GDAEQEVPTW
DPRSHLKIDV AHRVSGEPRD GYVLDAPGWK QLRA
//
