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 03-AUG-2022, entry version 73.
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;
OC Aspergillus subgen. Circumdati.
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., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA 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. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU34200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476600; EAU34200.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001214309.1; XM_001214309.1.
DR AlphaFoldDB; Q0CMF3; -.
DR SMR; Q0CMF3; -.
DR STRING; 341663.Q0CMF3; -.
DR PRIDE; Q0CMF3; -.
DR GeneID; 4320669; -.
DR eggNOG; KOG0496; Eukaryota.
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; 2.60.390.10; -; 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; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1022
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395227"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..324
FT /evidence="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
