BGAL_CLOC7
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 03-AUG-2022, entry version 51.
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; Firmicutes; 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 {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}.
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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 EnsemblBacteria; ADL51765; ADL51765; Clocel_2022.
DR KEGG; ccb:Clocel_2022; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_0_9; -.
DR OMA; IGYLPRP; -.
DR OrthoDB; 831762at2; -.
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 Gene3D; 3.40.50.880; -; 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; PTHR36447; 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; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 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
