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
//