ID BGALB_PENRW Reviewed; 1013 AA.
AC B6GW04;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 27-MAR-2024, entry version 77.
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=Pc06g00600;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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=CAP79053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM920421; CAP79053.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002556674.1; XM_002556628.1.
DR AlphaFoldDB; B6GW04; -.
DR SMR; B6GW04; -.
DR STRING; 500485.B6GW04; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GlyCosmos; B6GW04; 9 sites, No reported glycans.
DR GeneID; 8315677; -.
DR KEGG; pcs:Pc06g00600; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR BioCyc; PCHR:PC06G00600-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c06.
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; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 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:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1013
FT /note="Probable beta-galactosidase B"
FT /id="PRO_5000408640"
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 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 442
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 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..324
FT /evidence="ECO:0000250"
SQ SEQUENCE 1013 AA; 111429 MW; A4858AD5E5C13BB2 CRC64;
MTRILNCLLV LLACLGVSSK AEDQAVTQWP LQDNGLNTVV QWDHYSFQIN GQRIFIFSGE
FHYWRIPVPA LWRDILEKIK AAGFTAFAFY SSWAYHAPNN ATVDFTTGAR DITPIFELAK
ELGMYIIVRP GPYVNAEANA GGFPLWVTTG DYGTLRNDDT RYTNAWTPYF TEVTEITSRY
QVTDGHYSIV YQIENEYGNQ WLGDPTLRVP NETAIAYMEL LKANARDNGI TLPLTVNDPN
MKTHSWGKDW SDAGGNVDVA GLDSYPSCWT CDISQCTSTN GAYVPFQVLE YHDYFQESQP
SMPAFMPEFQ GGSYNPWGGP EGGCPGDIGD DFANLFYRWN IGQRVTAMSL YMMFGGQNPG
AMAAPVTASS YDYSAPISED RSIWSKYHET KLLALFTRSA KDLTMTELMG NGTQYTDNPA
VRAYELRNPE TNSAFYATFH SNTSISTNEP FHLKVNTSAG VLTVPKYAST IRLNGHQSKI
IVTDFTFGSK SLLYSTAEVL TYAVFDKKPT LVLWVPTGES GEFSIKGAKK GSIKKCQGCS
RVKFIKEHGG LTTSLTQSAG MTVLEFDDGV RVILLDRTSA YDFWAPALTN DPFVPETESV
LIQGPYLVRD AKLSGSKLAI TGDVVNATTL DVFAPKGVKS VTWNGKKVDT HSTEYGSLKG
SLDAPQSIKL PALASWKSKD SLPERFADYD DSGAAWVDAN HMTTLNPRTP TSLPVLYADQ
YGFHNGVRLW RGYFNGTATG AFINVQGGSA FGWSAWLNGE FLASHLGNAT TSQANLSLSF
TDATLHTDTP NVLLIVHDDT GHDQTTGALN PRGIMDAKLL GSDSGFTHWR LAGTAGGESD
LDPVRGVYNE DGLFAERVGW HLPGFDDSDW GEEGSAKDST TSVLSFEGAT VRFFRTTCPL
DIPAHTDVSI SFVLSTPAGA TTEYRAQLFV NGYQYGRYNP YIGNQVVYPV PVGILDYKGE
NTIGVAVWAQ SEEGASIGID WRVNYLADSS LDVASWDTKD LRPGWTEERV KYA
//
