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Database: UniProt
Entry: E9FBI0_METRA
LinkDB: E9FBI0_METRA
Original site: E9FBI0_METRA 
ID   E9FBI0_METRA            Unreviewed;       645 AA.
AC   E9FBI0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=MAA_09629 {ECO:0000313|EMBL:EFY94918.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY94918.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFY94918.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFY94918.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFY94918.1}.
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DR   EMBL; ADNJ02000009; EFY94918.1; -; Genomic_DNA.
DR   RefSeq; XP_007825818.1; XM_007827627.1.
DR   AlphaFoldDB; E9FBI0; -.
DR   GeneID; 19263915; -.
DR   KEGG; maj:MAA_09629; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000002498; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..645
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003239837"
FT   DOMAIN          40..363
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          408..520
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          545..606
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   645 AA;  69966 MW;  89CF61E957A4CE27 CRC64;
     MLVRGAAAAA AVFGWAAALL SLAKPLVAAH RGNFTYDRHN FLLDGVPIQL IGGQMDPQRI
     PPAYWTQRLQ MAKAMGLNTI FSYVFWNNIE PTEGSWDFDG RNDIARFLRL AQQEGLYVVL
     RPGPYICGEH EWGGFPSWLA QIPGMAVRQN NKPFLDASRN YLEQLGKHLA ATHISQGGPV
     LMTQLENEYG SFGKDKAYLR AMADMLKANF DGFLYTNDGG GKSYLDGGSL HGILAETDGD
     PKTGFAARDQ YVTDPTMLGP QLDGEYYVTW IDDWSSNSPY QYTSGRPDAT KRVLDDLDWI
     LAGNNSFSIY MFHGGTNWGF ENGGIWVDNR LNAVTTSYDY GAPLDESGRA TEIYRQIRDV
     ISKHVPAGTI PDVPHVPDLT TIDDFALEPA VALFDTRSDK PAVQAGSPVT MEKLGQAFGF
     VLYEHRVSAA VSGAIAPGDG PRDRVMVYVN GARVGVVDKT HAAPASVSVD LKQGDVLQLL
     VENLGRIDYG QQLREQQKGI VGNVTVGGDA ILEGWSAYSL PLTDLPAALA DENSETPEIK
     DGGAPVFYKG TFGLPAGVGN DLSGDTFLSL PNGVKGSVWV NGHHLGRYWV VGPQQSLYVP
     GAYLYGGNKP NHVVVLELEP KAGAGMVARG LATREWANHP DPDVA
//
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