GenomeNet

Database: UniProt/TrEMBL
Entry: E1ZZY3_CAMFO
LinkDB: E1ZZY3_CAMFO
Original site: E1ZZY3_CAMFO 
ID   E1ZZY3_CAMFO            Unreviewed;       624 AA.
AC   E1ZZY3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=EAG_11415 {ECO:0000313|EMBL:EFN73255.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN73255.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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}.
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DR   EMBL; GL435531; EFN73255.1; -; Genomic_DNA.
DR   RefSeq; XP_011268594.1; XM_011270292.2.
DR   AlphaFoldDB; E1ZZY3; -.
DR   STRING; 104421.E1ZZY3; -.
DR   GeneID; 105258784; -.
DR   KEGG; cfo:105258784; -.
DR   InParanoid; E1ZZY3; -.
DR   OMA; RAHPDTW; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000000311; 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:UP000000311};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..624
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003156309"
FT   DOMAIN          40..360
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          406..512
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          539..599
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   624 AA;  69855 MW;  FB68843D4CF694C1 CRC64;
     MWSLVFVTTL ALSSAVSETV NLPSNDTWQY SFGVDYENNQ FLLDGKPFRY VSGSFHYFRA
     PRQYWRDRLR KMRAAGLNAV STYVEWSLHE PEPGQFNWAG DADLIEFLNI AQEEDLFVLL
     RPGPYICAER DLGGLPYWLL REAPDIKLRT KDAAFMKYAT AYLNQVLEKV KPLLRGNGGP
     IIMVQIENEY GSYNACDTEY TDMLKEIIVG KVGSKALLYT TDGASASLLR CGFVPGAYAT
     IDFGTSVNVT NSFQSMRLYQ PRGPLVNSEF YPGWLTHWGE TFQRVKTEAV TKTLREMLAL
     GASVNIYMFY GGTNFGFTSG ANGGVGAYSP QITSYDYDAP LTEAGDPTDK YFAIRDVIGQ
     YLPLPNISLP TESPKGNYGP VLLEPIQKLF DSESSFVISW ASSDKPRTFE HLSVNQGFVL
     YETDLPPPVF DPVILRATIK DRALVYVDGR LSGTLSRMDK IFTIPLENPY GRRLSLLIEN
     QGRLNFGNEI HDFKGISNVT LSGTPLINWN MTGYALSDVS FLQDVMTIDI ESGTLNNGPV
     FLRGRFTITG QPLDTFLDPT GWGKGVAFVN GHNLGRYWPL VGPQITLYVP APYLRTGENE
     LILLELEYIS QTRKMKFQSV PNLG
//
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