ID A0A139I8Z3_9PEZI Unreviewed; 1031 AA.
AC A0A139I8Z3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=AC579_832 {ECO:0000313|EMBL:KXT11193.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT11193.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT11193.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT11193.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KXT11193.1}.
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DR EMBL; LFZO01000216; KXT11193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I8Z3; -.
DR STRING; 113226.A0A139I8Z3; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT DOMAIN 749..1031
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1031 AA; 116043 MW; B22DC8A6D6E97451 CRC64;
MADTTKPDWA NLEVLHRNTL EPRSYFYLYN SEQDAVSRDV SKAKAVSLSG SWRFHLSNSP
LEAPVGFETT EFDSTSWQTV QVPGMWQLQG FGRGPRYTNV NFPFNACPPL PPFNDNECGS
YLTSFTVPPH LQDHQLRLRF EGVDSGFHVW VNGKAVGYSQ GARNPSEFDI TGFVRQDQKN
SLAVRVYQFT DGSYIEDQDQ WWLSGIFRDV FLLGFPKQTR LEDLDVRTVL DKDYRDAVLE
VNALVAGSGN IAFKLLDAVG SEVGIARKSK IEPAPMTVSA AIPVQRPNKW TAETPYLYTL
VVSLEGQHTA HRVGFRQVEL KDGLIKVNGE KVVFKGANRH EHHPLHGRAV PYDFMKQDLV
LMKRHNLNAI RTCHQPSDPR LYDLADELGL WVMDEADLEC HGFETIADAA LPPEQQALPF
FERQKFTRTE AAKWTSDNPE WREAYLDRAK QLVHRDKLHP SVIIWSLGNE AFYGRNHTAM
TEWIKTFDGT RLVHYEPDLE AKHVDMHSRM YPDIDEIVAF GKDKSKVKPL VLCEYIHAMG
TGPGNIKEYV DAFYQYPVLQ GGWVWEWANH GLLTKTKDGK EFYGYGGDFG DVPNDYNFVL
DGVLNSDHSP RSGLVEYKKA VEPVQLVSSS GPDFTIINRL DFTTLDSLVC EWSVSDEAGD
HPGGDFELPI GLQPGATVSL AVPDDARSQT FVGEAFLNLR FCLKDNTPWA EKGHEVALLQ
VQLSSTPAAK TPDLTEAELK VEATPTTLLI IGVESRWQVD LVNGYLTSWD KAGKPLLADP
LQPSFYRALT DNDAPRDGKD WKERYLHLAK VQTRSSRWKT IDDGSVVVTF EQDFGPPILS
WSVKLNTELK FSPAGTIRVN VNGNPKGQNL PRTLPRIGVT LGLRNEFQNV TWFGRGPGES
YKDMNGQRIG LHSVPRIDDL WTSPEFPQEC SNRTDVRFLS ISDGRTKFTA QFESSSSSSE
RKTFDFMASH FDVKDIDAAQ HPHELDGAKK THVILRLDAD HHGIGTGSCG PKTLEQYALK
TGPFEFTILL Q
//
