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P94804

- BGAL_HALL2

UniProt

P94804 - BGAL_HALL2

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Protein
Beta-galactosidase BgaH
Gene
bgaH
Organism
Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax alicantei)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

When overexpressed, cleaves several different substrates including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and lactulose, but not lactose. Has also beta-D-fucosidase activity. No beta-L-fucosidase, beta-glucosidase, beta-arabinosidase or beta-xylosidase activity.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.2 Publications

Enzyme regulationi

Requires 4 M NaCl for maximal activity. Loss of activity if DTT or beta-mercaptoethanol is omitted from buffers. Addition of 5-20 mM EDTA, 1 mM Cu2+ or 1 mM Zn2+ results in loss of activity.1 Publication

Kineticsi

  1. KM=0.87 mM for ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)1 Publication

Vmax=110 µmol/min/mg enzyme with ONPG as substrate (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)

Temperature dependencei

Stable in 3 M NaCl for several days at room temperature, but approximately 18% and 50% of specific activity is lost when samples are stored overnight at 4 and -20 degrees Celsius, respectively. Activity is irreversibly lost within minutes in low salt buffers. Activity low, but detectable in 30% sorbitol in the complete absence of salt and it is stable in 30% sorbitol for at least four months at -20 degrees Celsius, but at room temperature approximately 20% of specific activity is lost after 48 hours.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031Substrate By similarity
Metal bindingi107 – 1071Zinc By similarity
Binding sitei141 – 1411Substrate By similarity
Active sitei142 – 1421Proton donor By similarity
Metal bindingi151 – 1511Zinc By similarity
Metal bindingi153 – 1531Zinc By similarity
Metal bindingi156 – 1561Zinc By similarity
Active sitei311 – 3111Nucleophile By similarity
Binding sitei319 – 3191Substrate By 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

Protein family/group databases

CAZyiGH42. Glycoside Hydrolase Family 42.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase BgaH (EC:3.2.1.23)
Short name:
Beta-gal
Gene namesi
Name:bgaH
OrganismiHaloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax alicantei)
Taxonomic identifieri1230452 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 663662Beta-galactosidase BgaH
PRO_0000407697Add
BLAST

Expressioni

Inductioni

Highest expression in cells grown on galactose. Glucose or glycerol, alone or in combination with galactose, gives an intermediate level of expression and peptone-containing media gives very low levels of expression.2 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP94804.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni359 – 3624Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR013780. Glyco_hydro_13_b.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P94804-1 [UniParc]FASTAAdd to Basket

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MTVGVCYFPE HWSRERWETD ISQMAEAGIE YVRMGEFAWR RIEPERGTFD    50
FAWLDEAVEL IGKFGMKAVL CTPTATPPKW LVDEHPDVRQ REQDGTPREW 100
GSRRFTCFNS PTYRSETERI VSVLTDRYAD NPHVAGWQTD NEFGCHETVT 150
CYCEDCGEAF SEWLADRYES VADLNDAWGT TFWSQQYDDF ESIDPPKPTP 200
AANHPSRVLA YERFSNDSVA EYNRLHAALI REANDEWFVT HNFMGGFSLD 250
AFRLAADLDF LSWDSYPTGF VQDRQPDTPT VDELRAGNPD QVSMNHDLQR 300
GAKGKPFWVM EQQPGDINWP PQSPQPADGA MRLWAHHAVA HGADAVVYFR 350
WRRCRQGQEQ YHAGLRRQDG SPDRGYREAS TAADELFDLD SVDASVALVH 400
DYESLWATRS QPLSPDWDYW NHLRTYYDAL RARGVQVDIV SPEATLERYD 450
AVVAPTLYLV GDELSTALTD YVDSGGCLLL GARTGEKDPY NRLHESLAPG 500
PLTALTGAQV ARHETLPDHV ETRLSYDGAT YEFRTWASWL APEVGVPRGE 550
YRTGEAAGNT AIVRNAAGDG SVTYCGCWPG DDLADALVTE LLDAAGVEYT 600
ERFPDGVRVM ERDGYTWALN FTSDPVTLTV PDSTGFLLGE STVDAFDTAV 650
LDGSIRGVGL ASE 663
Length:663
Mass (Da):74,460
Last modified:October 1, 2001 - v2
Checksum:i7ADF7634C5D13BE9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211I → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70664 Genomic DNA. Translation: AAB40123.2.
PIRiT44793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70664 Genomic DNA. Translation: AAB40123.2 .
PIRi T44793.

3D structure databases

ProteinModelPortali P94804.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
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.
IPR013780. Glyco_hydro_13_b.
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

  1. "Sequence and expression of a halobacterial beta-galactosidase gene."
    Holmes M.L., Dyall-Smith M.L.
    Mol. Microbiol. 36:114-122(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION.
    Strain: Aa 2.2 / SB1.
  2. Holmes M.L., Dyall-Smith M.L.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei."
    Holmes M.L., Scopes R.K., Moritz R.L., Simpson R.J., Englert C., Pfeifer F., Dyall-Smith M.L.
    Biochim. Biophys. Acta 1337:276-286(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26; 286-300; 410-424; 425-431 AND 493-512, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
    Strain: Aa 2.2 / SB1.

Entry informationi

Entry nameiBGAL_HALL2
AccessioniPrimary (citable) accession number: P94804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 1, 2001
Last modified: June 11, 2014
This is version 55 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

Direct protein sequencing

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

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