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O07012

- BGAL2_BACSU

UniProt

O07012 - BGAL2_BACSU

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Protein

Beta-galactosidase GanA

Gene

ganA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Enzyme regulationi

Inhibited by zinc, cobalt and copper ions.1 Publication

pH dependencei

Optimum pH is 6-0-6.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Thermolabile above 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051SubstrateBy similarity
Metal bindingi109 – 1091ZincBy similarity
Binding sitei143 – 1431SubstrateBy similarity
Active sitei144 – 1441Proton donorSequence Analysis
Metal bindingi149 – 1491ZincBy similarity
Metal bindingi151 – 1511ZincBy similarity
Metal bindingi154 – 1541ZincBy similarity
Active sitei308 – 3081NucleophileSequence Analysis
Binding sitei316 – 3161SubstrateBy similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. galactose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU34130-MONOMER.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase GanA (EC:3.2.1.23)
Short name:
Beta-gal
Alternative name(s):
Beta-1,4-galactooligomerase
Galactooligomerase
Gene namesi
Name:ganA
Synonyms:galO, lacA, yvfN
Ordered Locus Names:BSU34130
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU34130. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672Beta-galactosidase GanAPRO_0000367026Add
BLAST

Proteomic databases

PaxDbiO07012.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

STRINGi224308.BSU34130.

Structurei

3D structure databases

ProteinModelPortaliO07012.
SMRiO07012. Positions 2-670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 3594Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Curated

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000117811.
InParanoidiO07012.
KOiK12308.
OrthoDBiEOG6GTZGG.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFiPIRSF001084. B-galactosidase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

O07012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLHGGDYNPD QWLDRPDILA DDIKLMKLSH TNTFSVGIFA WSALEPEEGV
60 70 80 90 100
YQFEWLDDIF ERIHSIGGRV ILATPSGARP AWLSQTYPEV LRVNASRVKQ
110 120 130 140 150
LHGGRHNHCL TSKVYREKTR HINRLLAERY GHHPALLMWH ISNEYGGDCH
160 170 180 190 200
CDLCQHAFRE WLKSKYDNSL KTLNHAWWTP FWSHTFNDWS QIESPSPIGE
210 220 230 240 250
NGLHGLNLDW RRFVTDQTIS FYENEIIPLK ELTPDIPITT NFMADTPDLI
260 270 280 290 300
PYQGLDYSKF AKHVDAISWD AYPVWHNDWE STADLAMKVG FINDLYRSLK
310 320 330 340 350
QQPFLLMECT PSAVNWHNVN KAKRPGMNLL SSMQMIAHGS DSVLYFQYRK
360 370 380 390 400
SRGSSEKLHG AVVDHDNSPK NRVFQEVAKV GETLERLSEV VGTKRPAQTA
410 420 430 440 450
ILYDWENHWA LEDAQGFAKA TKRYPQTLQQ HYRTFWEHDI PVDVITKEQD
460 470 480 490 500
FSPYKLLIVP MLYLISEDTV SRLKAFTADG GTLVMTYISG VVNEHDLTYT
510 520 530 540 550
GGWHPDLQAI FGVEPLETDT LYPKDRNAVS YRSQIYEMKD YATVIDVKTA
560 570 580 590 600
SVEAVYQEDF YARTPAVTSH EYQQGKAYFI GARLEDQFQR DFYEGLITDL
610 620 630 640 650
SLSPVFPVRH GKGVSVQARQ DQDNDYIFVM NFTEEKQLVT FDQSVKDIMT
660 670
GDILSGDLTM EKYEVRIVVN TH
Length:672
Mass (Da):77,499
Last modified:March 24, 2009 - v2
Checksum:i324242C5D45E35BD
GO

Sequence cautioni

The sequence CAB08008.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAB15418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z94043 Genomic DNA. Translation: CAB08008.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB15418.1. Different initiation.
PIRiB69649.
RefSeqiNP_391293.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15418; CAB15418; BSU34130.
GeneIDi936313.
KEGGibsu:BSU34130.
PATRICi18978828. VBIBacSub10457_3577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z94043 Genomic DNA. Translation: CAB08008.1 . Different initiation.
AL009126 Genomic DNA. Translation: CAB15418.1 . Different initiation.
PIRi B69649.
RefSeqi NP_391293.1. NC_000964.3.

3D structure databases

ProteinModelPortali O07012.
SMRi O07012. Positions 2-670.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU34130.

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Proteomic databases

PaxDbi O07012.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15418 ; CAB15418 ; BSU34130 .
GeneIDi 936313.
KEGGi bsu:BSU34130.
PATRICi 18978828. VBIBacSub10457_3577.

Organism-specific databases

GenoListi BSU34130. [Micado ]

Phylogenomic databases

eggNOGi COG1874.
HOGENOMi HOG000117811.
InParanoidi O07012.
KOi K12308.
OrthoDBi EOG6GTZGG.

Enzyme and pathway databases

BioCyci BSUB:BSU34130-MONOMER.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProi IPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view ]
PIRSFi PIRSF001084. B-galactosidase. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the lacA gene encoding beta-galactosidase in Bacillus subtilis and a regulator gene, lacR."
    Daniel R.A., Haiech J., Denizot F., Errington J.
    J. Bacteriol. 179:5636-5638(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    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.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases."
    Shipkowski S., Brenchley J.E.
    Appl. Environ. Microbiol. 72:7730-7738(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiBGAL2_BACSU
AccessioniPrimary (citable) accession number: O07012
Secondary accession number(s): Q795J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: October 29, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3