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C8WV58

- BGAL_ALIAD

UniProt

C8WV58 - BGAL_ALIAD

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Protein

Beta-galactosidase BglY

Gene

bglY

Organism
Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.1 Publication

Enzyme regulationi

Ca2+, Mg2+ and EDTA have little effect on enzyme activity at 1-10 mM. Zn2+ at 3, 5, 7 or 10 mM inhibits activity by 20%, 30%, 40% and 65%, respectively.1 Publication

Kineticsi

  1. KM=6 mM for ONPG (at 60 degrees Celsius and pH 6.0)1 Publication
  2. KM=3.5 mM for PNPF (at 60 degrees Celsius and pH 6.0)1 Publication

pH dependencei

Optimum pH is 5.8. Approximately 80% of activity retained after incubating the enzyme for 40 minutes in buffers ranging from pH 5.0 to pH 10.5.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius. Retains 90% of activity when heated at 70 degrees Celsius for 30 minutes. Approximately 48% of lactose in milk is hydrolyzed following treatment with enzyme at 65 degrees Celsius over 60 minutes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181SubstrateBy similarity
Metal bindingi122 – 1221ZincBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Active sitei157 – 1571Proton donorBy similarity
Metal bindingi162 – 1621ZincBy similarity
Metal bindingi164 – 1641ZincBy similarity
Metal bindingi167 – 1671ZincBy similarity
Active sitei313 – 3131NucleophileBy similarity
Binding sitei321 – 3211SubstrateBy 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

BioCyciAACI521098:GCIO-2974-MONOMER.

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase BglY (EC:3.2.1.23)
Short name:
Beta-galBy similarity
Gene namesi
Name:bglY
Ordered Locus Names:Aaci_2891
OrganismiAlicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius)
Taxonomic identifieri521098 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus
ProteomesiUP000001917: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Biotechnological usei

Has potential use in hydrolyzing lactose in neutral pH dairy products such as whole milk or whey. Also could be used in milk lactose hydrolysis during pasteurization at high temperatures.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 688688Beta-galactosidase BglYPRO_0000407679Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi521098.Aaci_2891.

Structurei

3D structure databases

ProteinModelPortaliC8WV58.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 3644Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000117811.
KOiK12308.
OMAiCFLGGFP.
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.

C8WV58-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKHAPIFPN VQGFLHGGDY NPDQWLAYPD VLEQDVQLMR EAKWNVVSLG
60 70 80 90 100
IFSWVSLEPE EGLFTFEWLD EAIERLTHAG VRILLATPSG ARPAWLSAKY
110 120 130 140 150
PEVLRVGPDG RRNRHGGRHN HCYTSPIYRE KVRIINRKLA ERYAHHPGVI
160 170 180 190 200
GWHVSNEYGG ECHCPLCQEA FREWLKRKYK TLDALNHAWW TPFWSHTYTD
210 220 230 240 250
WSQIESPMPH GETSIHGLNL DWKRFVTDQT VDFCRHEIEP LKQVNPNLPV
260 270 280 290 300
TTNFMGTYPG LNYWRFRDVL DVISWDSYPR WHAHETLVPE AVHTAMVHDL
310 320 330 340 350
NRSILKKPFL LMESTPSVTN WQAVSKQKRP GVHVLVSLQA VAHGADSVQY
360 370 380 390 400
FQWRKSRGSY EKFHGAVVDH VGHANTRVFR DVQAVGEMLE RLAPMAGAEV
410 420 430 440 450
KADAAVIFDW ENRWALEDAK GPRNIGMHYE ETVVNHYAAL WRMGVPMDVI
460 470 480 490 500
DEEQPLDGYK LVVAPMLYMV RPGVAERMKA FVERGGSLVL TYWSGIVDEN
510 520 530 540 550
DLVFLGGFPG PLRELAGVWA EEIDALYDGE RVPVRVADGN PLGLAGHYEA
560 570 580 590 600
RELCEVVHLE GAEPIAVYGA DYYEGMPAAT VHRVGKGKVY YVAARLEDAF
610 620 630 640 650
LRDFFARVAA EAGVARAIER ELPDGVSAMV RSGDGVEYVM LMNFTPEARE
660 670 680
VALDEAEYKP LYGEAPTDGA VRLPAYGVSV LERPARNG
Length:688
Mass (Da):77,869
Last modified:November 3, 2009 - v1
Checksum:i686AFEA665822767
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti543 – 5442Missing AA sequence (PubMed:17914606)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ887754 Genomic DNA. Translation: ABI84370.1.
CP001727 Genomic DNA. Translation: ACV59895.1.
RefSeqiWP_012812096.1. NC_013205.1.
YP_003186284.1. NC_013205.1.

Genome annotation databases

EnsemblBacteriaiACV59895; ACV59895; Aaci_2891.
GeneIDi8426432.
KEGGiaac:Aaci_2891.
PATRICi20849346. VBIAliAci73240_2885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ887754 Genomic DNA. Translation: ABI84370.1 .
CP001727 Genomic DNA. Translation: ACV59895.1 .
RefSeqi WP_012812096.1. NC_013205.1.
YP_003186284.1. NC_013205.1.

3D structure databases

ProteinModelPortali C8WV58.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 521098.Aaci_2891.

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACV59895 ; ACV59895 ; Aaci_2891 .
GeneIDi 8426432.
KEGGi aac:Aaci_2891.
PATRICi 20849346. VBIAliAci73240_2885.

Phylogenomic databases

eggNOGi COG1874.
HOGENOMi HOG000117811.
KOi K12308.
OMAi CFLGGFP.
OrthoDBi EOG6GTZGG.

Enzyme and pathway databases

BioCyci AACI521098:GCIO-2974-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. "Heterologous expression of a gene encoding a thermostable beta-galactosidase from Alicyclobacillus acidocaldarius."
    Yuan T., Yang P., Wang Y., Meng K., Luo H., Zhang W., Wu N., Fan Y., Yao B.
    Biotechnol. Lett. 30:343-348(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8; 536-551 AND 637-649, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
    Strain: ATCC 27009 / DSM 446 / 104-1AImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27009 / DSM 446 / 104-1AImported.

Entry informationi

Entry nameiBGAL_ALIAD
AccessioniPrimary (citable) accession number: C8WV58
Secondary accession number(s): Q06GJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 3, 2009
Last modified: October 1, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3