ID BGAL_CLOC7 Reviewed; 659 AA. AC D9SM34; Q8GEE3; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 56. DE RecName: Full=Beta-galactosidase BgaA; DE Short=Beta-gal {ECO:0000250|UniProtKB:P19668}; DE EC=3.2.1.23; DE AltName: Full=Alpha-L-arabinopyranosidase {ECO:0000303|PubMed:12446636}; GN Name=bgaA; OrderedLocusNames=Clocel_2022; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN05452.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-5, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBSTRATE SPECIFICITY, AND SUBUNIT. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B; RX PubMed=12446636; DOI=10.1128/jb.184.24.6859-6865.2002; RA Kosugi A., Murashima K., Doi R.H.; RT "Characterization of two noncellulosomal subunits, ArfA and BgaA, from RT Clostridium cellulovorans that cooperate with the cellulosome in plant cell RT wall degradation."; RL J. Bacteriol. 184:6859-6865(2002). RN [2] {ECO:0000312|EMBL:ADL51765.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000312|EMBL:ADL51765.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium cellulovorans 743B."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in plant cell wall degradation in cooperation with CC cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside CC (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher CC activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl- CC beta-D-fucopyranoside (pNPFp), but not against p-nitrophenyl-alpha-L- CC arabinofuranoside (pNPAf), o-nitrophenyl-beta-D-galactopyranoside CC (oNPGp), p-nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl- CC beta-D-glucopyranoside (pNPGLp), p-nitrophenyl-beta-D- CC cellobiopyranoside (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) CC or p-nitrophenyl-alpha-galactopyranoside (pNPalphaGp). No detectable CC activity against arabinan or arabinoxylan, but activity against CC arabinogalactan can be detected. Increases degradation activity of CC alpha-L-arabinofuranosidase (ArfA) and endo-1,4-beta-xylanase (XynA) CC when corn fiber gum and corn stem powder are used as substrates. CC {ECO:0000269|PubMed:12446636}. 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:12446636}; CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), Hg(2+) and Zn(2+). No effect CC with Ca(2+), Mg(2+), Mn(2+) or excess EDTA (10 mM). CC {ECO:0000269|PubMed:12446636}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.51 mM for pNPAp (at 37 degrees Celsius and pH 6.0) CC {ECO:0000269|PubMed:12446636}; CC KM=6.06 mM for pNPGp (at 37 degrees Celsius and pH 6.0) CC {ECO:0000269|PubMed:12446636}; CC Vmax=10.4 umol/min/mg enzyme with pNPAp as substrate (at 37 degrees CC Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; CC Vmax=2.5 umol/min/mg enzyme with pNPGp as substrate (at 37 degrees CC Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; CC pH dependence: CC Optimum pH is 6.0 for activities against both pNPAp and pNPGp. Stable CC in the range of pH 6.0-8.0. {ECO:0000269|PubMed:12446636}; CC Temperature dependence: CC Optimum temperature is 30-40 degrees Celsius for activities against CC both pNPAp and pNPGp when incubated 10 minutes at pH 6.0. Both CC activities completely lost after heating at 50 degrees Celsius for 20 CC minutes. {ECO:0000269|PubMed:12446636}; CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:12446636}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}. 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; AY128945; AAN05452.1; -; Genomic_DNA. DR EMBL; CP002160; ADL51765.1; -; Genomic_DNA. DR RefSeq; WP_010077016.1; NC_014393.1. DR AlphaFoldDB; D9SM34; -. DR SMR; D9SM34; -. DR STRING; 573061.Clocel_2022; -. DR CAZy; GH42; Glycoside Hydrolase Family 42. DR KEGG; ccb:Clocel_2022; -. DR eggNOG; COG1874; Bacteria. DR HOGENOM; CLU_012430_1_0_9; -. DR OrthoDB; 9800974at2; -. DR Proteomes; UP000002730; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR013739; Beta_galactosidase_C. DR InterPro; IPR013738; Beta_galactosidase_Trimer. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR003476; Glyco_hydro_42. DR InterPro; IPR013529; Glyco_hydro_42_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1. DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1. DR Pfam; PF02449; Glyco_hydro_42; 1. DR Pfam; PF08533; Glyco_hydro_42C; 1. DR Pfam; PF08532; Glyco_hydro_42M; 1. DR PIRSF; PIRSF001084; B-galactosidase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1..659 FT /note="Beta-galactosidase BgaA" FT /id="PRO_0000407687" FT ACT_SITE 142 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O69315" FT ACT_SITE 298 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 103 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:O69315" FT BINDING 307 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O69315" SQ SEQUENCE 659 AA; 76464 MW; 30C0DB5C33848BF2 CRC64; MRIGVDYYPE HWDRQLWEKD AQLMKEIGVK VVRLAEFAWC KLEPIEGQYD FKWLDDVIEI FSVRNIEIVL GTPTNTPPLW LYEKYPDAIQ VNESGERQFI GIRGHRCYNS SSMRKYTKAI VEAMTERYAN NKAVIGWQID NELDATHCCC DNCTEKFRGW LKNKYSTLEN INKEYGNVVW SGEYSAWSQV TAPLGGSPFL NPSYLLDYNR FASDSMVEYI DFQREIIRKN CPSQFITTNT WFTGNLPNFY DAFENLDFVS YDNYPTTNEI TDEEELHSHA FHCDLMRGIK KKNFWIMEQL SGTPGCWMPM QRTPKPGMIK GYSFQAIGRG AETVVHFRWR NAIIGAEMFW HGILDHSNVK GRRFYEFAEL CREVNKINEE IPDYKINNEV AILYSSDQDF AFKIQPQVEG LYYLQQLKAF HNALIRLGVG TDIINWSESL NKYKVVIAPT LYLTDDNVTT ELYRFVEAGG TLILTNRTGV KNMNNVCLME QMPSNLKECA GVVVKEYDPI GHSIHTIKDE AGKVYQCKQW CDILEPTTAK VIATYNDDFY IDEAAVTVNK YKKGNVYYLG TVFNSDYYIE LLSKILDEKE LPYYKKLPYG LELSVLENEN GKYLMVFNNS NEIKCFEGKH EGKSIIRNEL DGKSFTLEPY GIEVLQLVE //