BGALA_PENSQ
ID BGALA_PENSQ Reviewed; 1011 AA.
AC Q700S9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Beta-galactosidase A {ECO:0000305};
DE EC=3.2.1.23 {ECO:0000269|PubMed:11053867};
DE AltName: Full=Lactase A;
DE Flags: Precursor;
GN Name=lacA;
OS Penicillium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF
RP 41-1011 IN COMPLEX WITH GALACTOSE, GLYCOSYLATION AT ASN-374; ASN-456;
RP ASN-625; ASN-707; ASN-763; ASN-780 AND ASN-917, AND DISULFIDE BONDS.
RX PubMed=15491613; DOI=10.1016/j.jmb.2004.09.012;
RA Rojas A.L., Nagem R.A., Neustroev K.N., Arand M., Adamska M.,
RA Eneyskaya E.V., Kulminskaya A.A., Garratt R.C., Golubev A.M.,
RA Polikarpov I.;
RT "Crystal structures of beta-galactosidase from Penicillium sp. and its
RT complex with galactose.";
RL J. Mol. Biol. 343:1281-1292(2004).
RN [2]
RP CRYSTALLIZATION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11053867; DOI=10.1107/s0907444900011756;
RA Neustroev K.N., de Sousa E.A., Golubev A.M., Brandao Neto J.R.,
RA Eneyskaya E.V., Kulminskaya A.A., Polikarpov I.;
RT "Purification, crystallization and preliminary diffraction study of beta-
RT galactosidase from Penicillium sp.";
RL Acta Crystallogr. D 56:1508-1509(2000).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans. Has high in vitro
CC transglycosylation activity with p-nitrophenyl-beta-D-
CC galactopyranoside, methyl-beta-D-galactopyranoside or lactose as a
CC donor and galactose as an acceptor. {ECO:0000269|PubMed:11053867}.
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:0000269|PubMed:11053867};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11053867}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11053867}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {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; AJ629057; CAF32457.1; -; Genomic_DNA.
DR PDB; 1TG7; X-ray; 1.90 A; A=41-1011.
DR PDB; 1XC6; X-ray; 2.10 A; A=41-1011.
DR PDBsum; 1TG7; -.
DR PDBsum; 1XC6; -.
DR AlphaFoldDB; Q700S9; -.
DR SMR; Q700S9; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR iPTMnet; Q700S9; -.
DR PRIDE; Q700S9; -.
DR EvolutionaryTrace; Q700S9; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
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; IPR019801; Glyco_hydro_35_CS.
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.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1011
FT /note="Beta-galactosidase A"
FT /id="PRO_5000072460"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 299
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT DISULFID 205..206
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT DISULFID 267..316
FT /evidence="ECO:0000269|PubMed:15491613,
FT ECO:0007744|PDB:1XC6"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 429..437
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 485..500
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 503..510
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 583..586
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 605..614
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 628..634
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 681..685
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 721..724
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 731..738
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 745..751
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 777..784
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 793..800
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 821..827
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 832..834
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 843..846
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 851..853
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 855..857
FT /evidence="ECO:0007829|PDB:1TG7"
FT HELIX 862..865
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 866..869
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 887..900
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 911..915
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 925..931
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 934..940
FT /evidence="ECO:0007829|PDB:1TG7"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 948..951
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 960..970
FT /evidence="ECO:0007829|PDB:1TG7"
FT STRAND 981..985
FT /evidence="ECO:0007829|PDB:1TG7"
SQ SEQUENCE 1011 AA; 109750 MW; A8A5BD48354F791A CRC64;
MKLLSSWVVA ALAAQAAGAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE HSIFVNGERL
MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA LLEGNPGHYS AEGIFDLQPF
FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVDGILR TSDEAYLKAT DNYASNIAAT
IAKAQITNGG PIILYQPENE YSGACCGYNG FPDGSYMQYI EDHARDAGIV VPFISNDAWA
AGHNAPGTGA GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFHTSHEQQS PSTPYSLVEF
QGGAFDPWGG VGFAKCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN WGNLGHPGGY
TSYDYGSAIS ESRNITREKY SELKLLGNFA KVSPGYLVAN PGDLSTSTYT NTADLTVTPL
LGSNSSASSF FVIRHSDYSS QASVEYKLTV PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY
DVAGTNILYS TAEVFTWKKF NNEKVLVLYG GPGEHHEFAV SGASSSSVVE GSSSGISSKK
VGKALVVAWD VSTARRIVQV GSLKVFLLDR NSAYNYWVPQ VPTKGTAPGY SNQETTASSI
IVKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK NLVINGKKTQ TKVDKNGIWS
ASVAYTAPKV QLPSLKSLKW KSVDTLPEAK NTYDDSAWTS ADHAYTNNSA HSLQTPTSLF
ASDYGYHTGA LLFRGHFTAN GKEKTFFVQT KGGTAYGHSI WINETYVGSW AGTSINDNNN
ATYTLPTLQS GKNYVITVVI DNMGLDEDWT IGSEDMKNPR GIIQYSLSGQ EASAISWKLT
GNLGGENYRD TVRGPLNEGG LYAERQGFHQ PQPPTQKWDS SSPFTGLTKP GIRFYSTSFD
LDLPSGYDIP LYFNFGNSTS TPAAYRVQLY VNGYQYGKYV NNIGPQTSFP VPEGILNYHG
TNWLALSLWA QEDNGAKLDS FELINTTPVL TSLGEVKSVN QPKYQARKGA Y
