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Database: UniProt
Entry: W3WZA6_PESFW
LinkDB: W3WZA6_PESFW
Original site: W3WZA6_PESFW 
ID   W3WZA6_PESFW            Unreviewed;      1034 AA.
AC   W3WZA6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=PFICI_10524 {ECO:0000313|EMBL:ETS78462.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS78462.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
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; KI912115; ETS78462.1; -; Genomic_DNA.
DR   RefSeq; XP_007837296.1; XM_007839105.1.
DR   AlphaFoldDB; W3WZA6; -.
DR   GeneID; 19275537; -.
DR   KEGG; pfy:PFICI_10524; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   InParanoid; W3WZA6; -.
DR   OMA; TNNDAIT; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000030651; 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; IPR025972; BetaGal_dom3.
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:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 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:UP000030651};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          436..615
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   1034 AA;  114319 MW;  AD5C26B852F2BA32 CRC64;
     MKGGAAHIRD QSESLPLLQH RKSLPPSKEG KNGGQCLGLS LIISKRLAIW LCTLTLLATF
     ALLSRQDHDG AYYTVPQAEQ PKEQPQNIVT WDERSLFIRG QRVMVMSGEL HPWRLVPSLY
     DDVFQKIKAL GFNCVSFYVM WALVEPAPGN FTATGVFAYE PFLEAASRAG IYLIARPGPY
     INAEVSFGGY PGWMQRVNGQ LRTRNPEYLA ATDNYIAQIG AIIAKAQITN DGPVILYQPE
     NEYTWGVPPR FPDGEYMQYV EDQARKAGIV VPIISNDAAP LGHNAPGTGA GEVDIYGHDD
     YPLKFDCSNP TSWPKGALNG LYHSIHEVQS PSTPFSILEF QGGAFDPWGG PGFENCALLL
     NEEFERVFYK NNLAAGVTIF NIYMVYGGTN WGNIGHPGGY TSYDYGSPIK EDFTVGRKKY
     SELKLLAQWL QMSPGYLTAK PGLAEVLTYC NDAAITVTRL KGDSTIGGGS FFIIRHSDYT
     STVSTNYKLE LPTSRGKVSI PALYGSLTLN GRDSKIAVTD YDVHGSTLIY STAEILTHQK
     YTDRVVLVVY TGPGETNELA IKTTHKPKIL VGDAVAVHHA GDLAIMTWDT SGERKVIRVG
     NLFIFATDRD SAYRYWVPSI GKTSAIILGP YLVRNASLHD YRTLSIQADF TENTTVEILG
     LSHLKSVIVN GVDTPFRDNN ITISLDIHYK SPQLKIPVLA SLKWRAADSL PELHSSYDDS
     QWPSADLSSN NTYQHQWTPT SLFASDYGFH AGVLVFRGHF VAQGTEESFD IQTQGGTAYG
     HTVWLNNTFL GSEIGKAGVS NARATYRIPD LLPGKPYVLT VIVDNMGLDE NGVAGVDSGK
     APRGILRYNL KSSWFRSTPI DWKLTGNLHG EDSVDRSRGP LNEGGLFAER QGWHLPKPPI
     GAFRKRSPLE PISEPGVWIF TSSFDLDLPS DYEIPLSFVL GGVTGGAARI QLYVNGWQYG
     KYISHIGPQT RFPVPEGILN YHGENWIALL IWTMEDQTTQ LEDFRLERGL PVYSGRSAVK
     LVDSPSWKRR DGAY
//
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