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Database: UniProt
Entry: A0A2A4K6F0_HELVI
LinkDB: A0A2A4K6F0_HELVI
Original site: A0A2A4K6F0_HELVI 
ID   A0A2A4K6F0_HELVI        Unreviewed;       666 AA.
AC   A0A2A4K6F0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=B5V51_1445 {ECO:0000313|EMBL:PCG79240.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG79240.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG79240.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG79240.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG79240.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:PCG79240.1}.
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DR   EMBL; NWSH01000130; PCG79240.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4K6F0; -.
DR   Proteomes; UP000218220; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
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; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..666
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011997500"
FT   DOMAIN          65..383
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          436..539
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          562..621
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   666 AA;  75263 MW;  2B736BCB31799396 CRC64;
     MRLQWSLFVA VSLWSFIIGL LTRVQASEVF DPMVVQVEQK RNERLSEPVA KTGQTSRQIN
     IVDDQFMVDG KPLRIVSGSL HYFRLPAAYW RDRLRKLKAA GLNSVATYVE WSYHEPEERQ
     YSFDGDRDIA NFIRIAAEEG LYVLLRVGPY ICAERDLGGL PYWLLGKYPN IRLRSTNKDF
     LEESRIWLEK LFEQVSPLLY GNGGPIILVQ VENEYGSYGS DMEYRLKARD MLQQHVASKA
     ILYTTDGNGL AFLRNGAIPD TLTTIDFNAY TDANRSFAEL RRFMPKGPLM NSEYYTGWLT
     HWGEHIASTD AADVVKTLGA MLDYGASVNF FMFYGGTNFE YTSGANYVST FLPDITSYDY
     DSPLTEAGDP TPKYYLIRDK LKQYNFVDDS IPIPRASAKG DYGPVSVTST INLLTTEGRA
     QLGKKYEDVT GPTLPTFEHL RQRGGLMLYE TELTEANSAL YIASPRDLIF VFVDGEFKGR
     LSRHHKTYSI PISAKNGSVL SLLVEHQGRI NFGNLLHDFK GILGQVEFNN NALDGKWKVT
     GFPLETFTTT PVPGQNNLRL GPTFYEGDLT LPAGQEPLDT FVDTSGWGKG YIWVNGHNLG
     RYWPSAGPQI TLYLPGLWLK PAPEKNHIQI LELDKPPQVL TIDFIDYPIL NRTGSIGLWK
     IQPRPS
//
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