GenomeNet

Database: UniProt/SWISS-PROT
Entry: BGAL_CLOC7
LinkDB: BGAL_CLOC7
Original site: 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   28-FEB-2018, entry version 36.
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 /
OS   743B).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; 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, ENZYME 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
RT   cell 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.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., 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
CC       with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-
CC       arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-
CC       galactopyranoside (pNPGp), with higher activity for pNPAp. Shows
CC       hydrolysis activity against p-nitrophenyl-beta-D-fucopyranoside
CC       (pNPFp), but not against p-nitrophenyl-alpha-L-arabinofuranoside
CC       (pNPAf), o-nitrophenyl-beta-D-galactopyranoside (oNPGp), p-
CC       nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl-beta-D-
CC       glucopyranoside (pNPGLp), p-nitrophenyl-beta-D-cellobiopyranoside
CC       (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) or p-
CC       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
CC       (XynA) when corn fiber gum and corn stem powder are used as
CC       substrates. {ECO:0000269|PubMed:12446636}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC       {ECO:0000269|PubMed:12446636}.
CC   -!- ENZYME REGULATION: Inhibited by Cu(2+), Hg(2+) and Zn(2+). No
CC       effect 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
CC         degrees Celsius and pH 6.0) {ECO:0000269|PubMed:12446636};
CC         Vmax=2.5 umol/min/mg enzyme with pNPGp as substrate (at 37
CC         degrees 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.
CC         Stable in the range of pH 6.0-8.0.
CC         {ECO:0000269|PubMed:12446636};
CC       Temperature dependence:
CC         Optimum temperature is 30-40 degrees Celsius for activities
CC         against both pNPAp and pNPGp when incubated 10 minutes at pH
CC         6.0. Both activities completely lost after heating at 50 degrees
CC         Celsius for 20 minutes. {ECO:0000269|PubMed:12446636};
CC   -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:12446636}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000255}.
DR   EMBL; AY128945; AAN05452.1; -; Genomic_DNA.
DR   EMBL; CP002160; ADL51765.1; -; Genomic_DNA.
DR   RefSeq; WP_010077016.1; NC_014393.1.
DR   ProteinModelPortal; 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; ENOG4105C4C; Bacteria.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000117811; -.
DR   KO; K12308; -.
DR   OMA; ARQIMDI; -.
DR   OrthoDB; POG091H0719; -.
DR   BioCyc; CCEL573061:G1GMK-2052-MONOMER; -.
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   Complete proteome; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN         1    659       Beta-galactosidase BgaA.
FT                                /FTId=PRO_0000407687.
FT   ACT_SITE    142    142       Proton donor.
FT                                {ECO:0000250|UniProtKB:O69315}.
FT   ACT_SITE    298    298       Nucleophile.
FT                                {ECO:0000250|UniProtKB:O69315}.
FT   METAL       107    107       Zinc. {ECO:0000250|UniProtKB:O69315}.
FT   METAL       148    148       Zinc. {ECO:0000250|UniProtKB:O69315}.
FT   METAL       150    150       Zinc. {ECO:0000250|UniProtKB:O69315}.
FT   METAL       153    153       Zinc. {ECO:0000250|UniProtKB:O69315}.
FT   BINDING     103    103       Substrate.
FT                                {ECO:0000250|UniProtKB:O69315}.
FT   BINDING     141    141       Substrate.
FT                                {ECO:0000250|UniProtKB:O69315}.
FT   BINDING     307    307       Substrate.
FT                                {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
//
DBGET integrated database retrieval system