ID BGAL1_BACSU Reviewed; 663 AA.
AC O31529;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Beta-galactosidase YesZ;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Probable rhamnogalacturonan beta-galactosidase;
GN Name=yesZ; OrderedLocusNames=BSU07080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP 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 [3]
RP FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, AND INDUCTION.
RC STRAIN=168;
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF GLU-145.
RX PubMed=17485082; DOI=10.1016/j.febslet.2007.04.053;
RA Shaikh F.A., Muellegger J., He S., Withers S.G.;
RT "Identification of the catalytic nucleophile in family 42 beta-
RT galactosidases by intermediate trapping and peptide mapping: YesZ from
RT Bacillus subtilis.";
RL FEBS Lett. 581:2441-2446(2007).
CC -!- FUNCTION: May play a role in the degradation of rhamnogalacturonan
CC derived from plant cell walls. {ECO:0000269|PubMed:17449691}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 mM for p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:17485082};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- DISRUPTION PHENOTYPE: No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-
CC galactopyranoside (X-Gal) hydrolyzation. {ECO:0000269|PubMed:17056685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 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; AL009126; CAB12527.1; -; Genomic_DNA.
DR PIR; A69798; A69798.
DR RefSeq; NP_388589.1; NC_000964.3.
DR RefSeq; WP_003242572.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31529; -.
DR SMR; O31529; -.
DR STRING; 224308.BSU07080; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR PaxDb; 224308-BSU07080; -.
DR EnsemblBacteria; CAB12527; CAB12527; BSU_07080.
DR GeneID; 936080; -.
DR KEGG; bsu:BSU07080; -.
DR PATRIC; fig|224308.179.peg.768; -.
DR eggNOG; COG1874; Bacteria.
DR InParanoid; O31529; -.
DR OrthoDB; 9800974at2; -.
DR PhylomeDB; O31529; -.
DR BioCyc; BSUB:BSU07080-MONOMER; -.
DR SABIO-RK; O31529; -.
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 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 Glycosidase; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..663
FT /note="Beta-galactosidase YesZ"
FT /id="PRO_0000367024"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:17485082"
FT ACT_SITE 296
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:17485082"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 345..348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 145
FT /note="E->A: Hydrolysis of the covalent glycosyl-enzyme
FT intermediate is slowed."
FT /evidence="ECO:0000269|PubMed:17485082"
SQ SEQUENCE 663 AA; 74099 MW; 7E5799B02C0C5238 CRC64;
MRKLYHGACY YPELWDEETI QQDIDIMREV GVNVVRIGEF AWSVMEPEEG KIDVGFFKEI
IARLYDSGIE TIMCTPTPTP PIWFSHGRPE RMHANEKREI MGHGSRQHAC TNNPYFRKKA
AIITTAIAKE LGRLPGLIGW QLDNEFKCHV AECMCETCLR LWHDWLKNRY GVIERLNEAW
GTDVWSETYQ TFEQVPQPGP APFLHHASLR TMYQLFSMEM IASFADEQAK IIRCYSDAPI
THNGSVMFSV DNERMFQNLD FASYDTYASQ ENASAFLLNC DLWRNLKQGR PFWILETSPS
YAASLESSAY PHADGYLQAE AVSSYALGSQ GFCYWLWRQQ RSGSEISHGS VLSAWGEPTI
GYQNVLAVER ARKEIEPIIL STEPVQAEAA MTYSDRAKAF IKTEPHRGLR HRSLVTHFYE
RILNTGIHRD LIPEGAPLDG YRLLFTPFVP YLSSEFIKKA SAFAEAGGIW ITGPLTGGRT
CEHTIHTDCG LGELEKTSGI KTLFTFPMNE NVNTGKAFGI TAPLGLWSAV FDTESGNTLG
TVEAGPGAGH AFLTERNYGE GKIVMLGSLP SGKEGDAMLE ALVRHYAEEA VISSRSDVTP
GTIVAPRIGE NGLVWIVVNM DGKGGSVTLP ESGTDLLTHR LEKAGRLAVG PHEYRVIQFD
NHS
//
