ID   R9PKP9_PSEHS            Unreviewed;      1125 AA.
AC   R9PKP9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=PHSY_006289 {ECO:0000313|EMBL:GAC98695.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC98695.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
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}.
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DR   EMBL; DF238821; GAC98695.1; -; Genomic_DNA.
DR   RefSeq; XP_012192282.1; XM_012336892.1.
DR   AlphaFoldDB; R9PKP9; -.
DR   STRING; 1305764.R9PKP9; -.
DR   GeneID; 24111561; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000014071; 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; IPR036833; BetaGal_dom3_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; SSF117100; Beta-galactosidase LacA, domain 3; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1125
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004478330"
FT   DOMAIN          428..602
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
FT   REGION          33..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  126495 MW;  4D939DD388F66A19 CRC64;
     MRLSTASLIG CIAAGFASLL HVASASQAPF SIEPAEERTD SSPSPKSAAP HSSKWTLPRD
     SNNSAVVFDK YSLALAGGQQ RLFVFAAEFH PWRLPVPSLW RDVLQKIRAA GFNTVSIYTH
     WGLIQPSAHA DSIDLTVVND LDYFLTVAKQ VRLFVIVRPG PYINAETTVG GMAPWTVNID
     AVLRTNDTAW QEAWKPYIEA ISQVVVKHQL VYDPSKSDHL TGGSVILVQA DNEYKTGKAE
     RAYMKELVTT LKGHGISVPI TYNDPGRDNN FVDLVDLYGL DSYPQRFDCS HPTTWVPFRD
     DYLQYHMETN PDQPFYIPEF QGGSYDPYGG PGYEACGRMT NASFTRVANQ ALIAQRVTLL
     SLYMVYGGTN WGGLAEPDVY TSYDYGAALN EHRQTTEKYT ELKRQGNFLS TFPDLAMTEQ
     IFDKPGFNIS QAMDLDTNQT VDATIFRSTV LENPETKSKF YIVRYDNTTE SRRIRFALEI
     ESLGETILLG DRSNPNSPWV GNNYLDGRDS HIVPVDQKLP GGLLLRFSTV NVYRIASFAN
     YVLVSLDYMP NQLIEYSLTV QDPKNRFTEM QMFTLDGVTA TLQEADEDER ERVMRMHSAI
     KGEPRNVRGS IPTSDDQEPN RRYVAYKTFE GIWIILQFTP TSETQRDFAA PASYQEQTSR
     LAMQLRRKPD NVINHFFGLT DETVILLDVD LLRNATYSTT SRPLDTIHLW GSVSNETTTA
     MMALPGLKNV YWNGKQIETS PQDDNGWFYT LELPGPPQAA LDWKPPDLSD LDWRWQDCIP
     EAQAAFDDTD WVDANKTNSF NPYAHDPSLD THGVVLFASE YGFHANNILW RGHFSTPSHA
     PSDVYVKVEG GRSSAFSVWL NGVYLGSAES NREKSASGAS FSIPPQTLHA KDEENVITVL
     QDHMGIEMEA GQLPIGFADE DRALEAVKLP RGIVAFNFPS LRTTERSDPE VRWKVQGNFR
     GESAPDHVRR SLNEGGLRAE VEGWHLPGFD TADWPSVKDS RGERGRVVFY RTTFSLDVAE
     DIDLGLTFAF RKAQGKKFRA QLYVNGWQMG KYVNHLGPQR RFPVHSGVVE LRGENEVGVS
     VWSLDEKELE WDPREGLRLE VGHLMSGEPR DGYTLDAGGW DELRS
//