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Beta-galactosidase GanA (Beta-gal) (EC 3.2.1.23) (Beta-1,4-galactooligomerase) (Galactooligomerase)

 BGAL2_BACSU             Reviewed;         672 AA.
O07012; Q795J9;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 2.
05-DEC-2018, entry version 109.
RecName: Full=Beta-galactosidase GanA;
Short=Beta-gal;
EC=3.2.1.23;
AltName: Full=Beta-1,4-galactooligomerase;
AltName: Full=Galactooligomerase;
Name=ganA; Synonyms=galO, lacA, yvfN; OrderedLocusNames=BSU34130;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9287030; DOI=10.1128/jb.179.17.5636-5638.1997;
Daniel R.A., Haiech J., Denizot F., Errington J.;
"Isolation and characterization of the lacA gene encoding beta-
galactosidase in Bacillus subtilis and a regulator gene, lacR.";
J. Bacteriol. 179:5636-5638(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
NOMENCLATURE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
PubMed=17056685; DOI=10.1128/AEM.01306-06;
Shipkowski S., Brenchley J.E.;
"Bioinformatic, genetic, and biochemical evidence that some glycoside
hydrolase family 42 beta-galactosidases are arabinogalactan type I
oligomer hydrolases.";
Appl. Environ. Microbiol. 72:7730-7738(2006).
-!- FUNCTION: Hydrolyzes oligosaccharides released by the endo-1,4-
beta-galactosidase GalA from arabinogalactan type I, a pectic
plant polysaccharide. It is unable to use lactose as a sole carbon
source. Maximal activity with o-nitrophenyl-beta-D-
galactopyranoside (ONPG) and p-nitrophenyl-beta-D-
galactopyranoside (PNPG) as substrates, trace activity with p-
nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-
fucopyranoside as substrates, but no activity with p-nitrophenyl-
alpha-D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside,
o-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-
mannopyranoside or p-nitrophenyl-alpha-L-arabinofuranoside as
substrates. {ECO:0000269|PubMed:17056685}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
residues in beta-D-galactosides.; EC=3.2.1.23;
-!- ACTIVITY REGULATION: Inhibited by zinc, cobalt and copper ions.
{ECO:0000269|PubMed:17056685}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6-0-6.5. {ECO:0000269|PubMed:17056685};
Temperature dependence:
Optimum temperature is 50 degrees Celsius. Thermolabile above 50
degrees Celsius. {ECO:0000269|PubMed:17056685};
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17056685}.
-!- DISRUPTION PHENOTYPE: No chromogen 5-bromo-4-chloro-3-indolyl-
beta-D-galactopyranoside (X-Gal) hydrolyzation. Reduces beta-
galactosidase activity observed with polygalacturonic acid, citrus
and apple pectins, galactan and soy flour.
{ECO:0000269|PubMed:17056685}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB08008.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB15418.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; Z94043; CAB08008.1; ALT_INIT; Genomic_DNA.
EMBL; AL009126; CAB15418.1; ALT_INIT; Genomic_DNA.
PIR; B69649; B69649.
RefSeq; NP_391293.1; NC_000964.3.
RefSeq; WP_010886616.1; NZ_JNCM01000033.1.
ProteinModelPortal; O07012; -.
SMR; O07012; -.
STRING; 224308.Bsubs1_010100018506; -.
CAZy; GH42; Glycoside Hydrolase Family 42.
PaxDb; O07012; -.
PRIDE; O07012; -.
EnsemblBacteria; CAB15418; CAB15418; BSU34130.
GeneID; 936313; -.
KEGG; bsu:BSU34130; -.
PATRIC; fig|224308.43.peg.3577; -.
eggNOG; COG1874; LUCA.
HOGENOM; HOG000117811; -.
InParanoid; O07012; -.
KO; K12308; -.
BioCyc; BSUB:BSU34130-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
Gene3D; 2.60.40.1180; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR013739; Beta_galactosidase_C.
InterPro; IPR013738; Beta_galactosidase_Trimer.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR003476; Glyco_hydro_42.
InterPro; IPR013529; Glyco_hydro_42_N.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR36447; PTHR36447; 1.
Pfam; PF02449; Glyco_hydro_42; 1.
Pfam; PF08533; Glyco_hydro_42C; 1.
Pfam; PF08532; Glyco_hydro_42M; 1.
PIRSF; PIRSF001084; B-galactosidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF52317; SSF52317; 1.
1: Evidence at protein level;
Complete proteome; Glycosidase; Hydrolase; Metal-binding;
Reference proteome; Zinc.
CHAIN 1 672 Beta-galactosidase GanA.
/FTId=PRO_0000367026.
REGION 356 359 Substrate binding. {ECO:0000250}.
ACT_SITE 144 144 Proton donor. {ECO:0000255}.
ACT_SITE 308 308 Nucleophile. {ECO:0000255}.
METAL 109 109 Zinc. {ECO:0000250}.
METAL 149 149 Zinc. {ECO:0000250}.
METAL 151 151 Zinc. {ECO:0000250}.
METAL 154 154 Zinc. {ECO:0000250}.
BINDING 105 105 Substrate. {ECO:0000250}.
BINDING 143 143 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
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


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