GenomeNet

Database: UniProt
Entry: BGALB_ASPTN
LinkDB: BGALB_ASPTN
Original site: BGALB_ASPTN 
ID   BGALB_ASPTN             Reviewed;        1022 AA.
AC   Q0CMF3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=ATEG_05131;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU34200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH476600; EAU34200.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001214309.1; XM_001214309.1.
DR   ProteinModelPortal; Q0CMF3; -.
DR   SMR; Q0CMF3; -.
DR   STRING; 33178.CADATEAP00004534; -.
DR   GeneID; 4320669; -.
DR   EuPathDB; FungiDB:ATEG_05131; -.
DR   HOGENOM; HOG000181922; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   1022       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395227.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000255}.
FT   ACT_SITE    308    308       Nucleophile. {ECO:0000255}.
FT   BINDING      90     90       Substrate. {ECO:0000250}.
FT   BINDING     135    135       Substrate. {ECO:0000250}.
FT   BINDING     136    136       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     137    137       Substrate. {ECO:0000250}.
FT   BINDING     195    195       Substrate. {ECO:0000250}.
FT   BINDING     265    265       Substrate. {ECO:0000250}.
FT   BINDING     373    373       Substrate. {ECO:0000250}.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    411    411       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    456    456       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    626    626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    777    777       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    790    790       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    832    832       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    880    880       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    881    881       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    271    324       {ECO:0000250}.
SQ   SEQUENCE   1022 AA;  111471 MW;  032C051812784E46 CRC64;
     MARFPQLLFL LLASIGLLSA AQNHSDSEWP LHDNGLSTVV QWDHYSFHVH GQRIFVFSGE
     FHYWRIPVPG LWRDILEKIK AAGFTAFAFY SSWGYHAPNN HTVDFSTGAR DITPIYELAK
     ELGMYIIVRP GPYVNAEASA GGYPLWVTTG AYGSLRNDDA RYTAAWKPYF AKMSEITSQY
     QVTDGHNTFC YQIENEYGQQ WIGDPVDRNP NQTAVAYMEL LEASARENGI VVPLTANDPN
     MNTKSWGSDW SHAGGNVDVV GLDSYPSCWT CDVTQCTSTN GEYVPYKVMQ YYDYFQEVQP
     TMPGFMPEFQ GGSYNPWAGP EGGCPGDTGV DFANLFYRWN IAQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSSPISED RSIGSKYYET KLLALFTRSA TDLTMTDRIG NGTHYTNNPA
     VAAYELRNPV TNGAFYVTIH ADSTVGTDES FRLNVNTSAG ALTVPSKGSI RLNGHQSKII
     VTDFRFGPSH TLLYSTAEVL THAVMDKKAT LVLWVPTGES GEFAVKGAKS GKVERCPQCS
     NATFTRKKDV LVVNFTQAGG MSVLQLNNGV RVVLLDRAAA YKFWAPPLTD DPFAPETDLV
     LVQGPYLVRS ASLSGSTLAL RGDSANETAL EVFASKKVHT VTWNGKRIKT SRSSYGSLTA
     SLAAPPAVSL PALSSAQWKS QDSLPERLPS YDDSGPAWVD ANHMTTQNPR TPDTLPVLYA
     DEYGFHNGIR LWRGSFTDAA SGVYLNVQGG AAFGWSAYLN GHFLGSHLGT ATTSQANKTL
     LFPAGTLRKN TTNTILVIHD DTGHDQTTGA LNPRGILAAR LLAPSDSSTA PNFTQWRVAG
     TAGGESDLDP VRGVYNEDGL FAERMGWHLP GFDDADWPAN NSTTTRGAQV SLSVTGATVR
     FFRAVVPLHL PRGVDASISF MLGTPAGAST AYRAQLFVNG YQYGRFYPHI GNQVVYPVPA
     GVLDYDGENT IGVAVWAQSE AGAEMSLDWR VNYVADSSLD AVRVAAEGAL RPGWSEERLQ
     YA
//
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