BGAL2_BACSU
ID BGAL2_BACSU Reviewed; 672 AA.
AC O07012; Q795J9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Beta-galactosidase GanA;
DE Short=Beta-gal;
DE EC=3.2.1.23 {ECO:0000269|PubMed:17056685, ECO:0000269|PubMed:27501980};
DE AltName: Full=Beta-1,4-galactooligomerase;
DE AltName: Full=Galactooligomerase;
GN Name=ganA {ECO:0000303|PubMed:27501980};
GN Synonyms=galO {ECO:0000303|PubMed:17056685}, lacA, yvfN;
GN OrderedLocusNames=BSU34130;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9287030; DOI=10.1128/jb.179.17.5636-5638.1997;
RA Daniel R.A., Haiech J., Denizot F., Errington J.;
RT "Isolation and characterization of the lacA gene encoding beta-
RT galactosidase in Bacillus subtilis and a regulator gene, lacR.";
RL J. Bacteriol. 179:5636-5638(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NOMENCLATURE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=17056685; DOI=10.1128/aem.01306-06;
RA Shipkowski S., Brenchley J.E.;
RT "Bioinformatic, genetic, and biochemical evidence that some glycoside
RT hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer
RT hydrolases.";
RL Appl. Environ. Microbiol. 72:7730-7738(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=27501980; DOI=10.1128/jb.00468-16;
RA Watzlawick H., Morabbi Heravi K., Altenbuchner J.;
RT "Role of the ganSPQAB operon in degradation of galactan by Bacillus
RT subtilis.";
RL J. Bacteriol. 198:2887-2896(2016).
CC -!- FUNCTION: Involved in galactan degradation (PubMed:27501980).
CC Hydrolyzes galactooligosaccharides released by the endo-beta-1,4-
CC galactanase GanB from galactan (PubMed:17056685, PubMed:27501980).
CC Degrades galactotetraose, galactotriose and galactobiose, generating
CC galactose as the end product (PubMed:27501980). It is unable to use
CC lactose (PubMed:17056685). In vitro, shows maximal activity with o-
CC nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-
CC galactopyranoside (PNPG) as substrates, trace activity with p-
CC nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-
CC fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-
CC D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside, o-
CC nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-mannopyranoside
CC or p-nitrophenyl-alpha-L-arabinofuranoside as substrates
CC (PubMed:17056685). {ECO:0000269|PubMed:17056685,
CC ECO:0000269|PubMed:27501980}.
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:17056685, ECO:0000269|PubMed:27501980};
CC -!- ACTIVITY REGULATION: Inhibited by zinc, cobalt and copper ions.
CC {ECO:0000269|PubMed:17056685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:17056685};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Thermolabile above 50
CC degrees Celsius. {ECO:0000269|PubMed:17056685};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17056685}.
CC -!- INDUCTION: Repressed by the transcriptional regulator GanR and induced
CC by galactobiose. Also repressed by glucose.
CC {ECO:0000269|PubMed:27501980}.
CC -!- DISRUPTION PHENOTYPE: No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-
CC galactopyranoside (X-Gal) hydrolyzation. Reduces beta-galactosidase
CC activity observed with polygalacturonic acid, citrus and apple pectins,
CC galactan and soy flour. {ECO:0000269|PubMed:17056685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB08008.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB15418.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z94043; CAB08008.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15418.1; ALT_INIT; Genomic_DNA.
DR PIR; B69649; B69649.
DR RefSeq; NP_391293.1; NC_000964.3.
DR RefSeq; WP_010886616.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O07012; -.
DR SMR; O07012; -.
DR STRING; 224308.BSU34130; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR PaxDb; O07012; -.
DR PRIDE; O07012; -.
DR EnsemblBacteria; CAB15418; CAB15418; BSU_34130.
DR GeneID; 936313; -.
DR KEGG; bsu:BSU34130; -.
DR PATRIC; fig|224308.43.peg.3577; -.
DR eggNOG; COG1874; Bacteria.
DR InParanoid; O07012; -.
DR BioCyc; BSUB:BSU34130-MON; -.
DR Proteomes; UP000001570; 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; 2.60.40.1180; -; 1.
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; IPR013780; Glyco_hydro_b.
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 Glycosidase; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..672
FT /note="Beta-galactosidase GanA"
FT /id="PRO_0000367026"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356..359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 672 AA; 77499 MW; 324242C5D45E35BD CRC64;
MLHGGDYNPD QWLDRPDILA DDIKLMKLSH TNTFSVGIFA WSALEPEEGV YQFEWLDDIF
ERIHSIGGRV ILATPSGARP AWLSQTYPEV LRVNASRVKQ LHGGRHNHCL TSKVYREKTR
HINRLLAERY GHHPALLMWH ISNEYGGDCH CDLCQHAFRE WLKSKYDNSL KTLNHAWWTP
FWSHTFNDWS QIESPSPIGE NGLHGLNLDW RRFVTDQTIS FYENEIIPLK ELTPDIPITT
NFMADTPDLI PYQGLDYSKF AKHVDAISWD AYPVWHNDWE STADLAMKVG FINDLYRSLK
QQPFLLMECT PSAVNWHNVN KAKRPGMNLL SSMQMIAHGS DSVLYFQYRK SRGSSEKLHG
AVVDHDNSPK NRVFQEVAKV GETLERLSEV VGTKRPAQTA ILYDWENHWA LEDAQGFAKA
TKRYPQTLQQ HYRTFWEHDI PVDVITKEQD FSPYKLLIVP MLYLISEDTV SRLKAFTADG
GTLVMTYISG VVNEHDLTYT GGWHPDLQAI FGVEPLETDT LYPKDRNAVS YRSQIYEMKD
YATVIDVKTA SVEAVYQEDF YARTPAVTSH EYQQGKAYFI GARLEDQFQR DFYEGLITDL
SLSPVFPVRH GKGVSVQARQ DQDNDYIFVM NFTEEKQLVT FDQSVKDIMT GDILSGDLTM
EKYEVRIVVN TH
