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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.2 Publications

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)1 Publication

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031SubstrateBy similarity
Metal bindingi107 – 1071ZincBy similarity
Binding sitei141 – 1411SubstrateBy similarity
Active sitei142 – 1421Proton donorBy similarity
Metal bindingi151 – 1511ZincBy similarity
Metal bindingi153 – 1531ZincBy similarity
Metal bindingi156 – 1561ZincBy similarity
Active sitei311 – 3111NucleophileBy similarity
Binding sitei319 – 3191SubstrateBy 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-galBy similarity
Gene namesi
Name:bgaHImported
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 BgaHPRO_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.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP94804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 42 family.Sequence Analysis

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

« Hide

        10         20         30         40         50
MTVGVCYFPE HWSRERWETD ISQMAEAGIE YVRMGEFAWR RIEPERGTFD
60 70 80 90 100
FAWLDEAVEL IGKFGMKAVL CTPTATPPKW LVDEHPDVRQ REQDGTPREW
110 120 130 140 150
GSRRFTCFNS PTYRSETERI VSVLTDRYAD NPHVAGWQTD NEFGCHETVT
160 170 180 190 200
CYCEDCGEAF SEWLADRYES VADLNDAWGT TFWSQQYDDF ESIDPPKPTP
210 220 230 240 250
AANHPSRVLA YERFSNDSVA EYNRLHAALI REANDEWFVT HNFMGGFSLD
260 270 280 290 300
AFRLAADLDF LSWDSYPTGF VQDRQPDTPT VDELRAGNPD QVSMNHDLQR
310 320 330 340 350
GAKGKPFWVM EQQPGDINWP PQSPQPADGA MRLWAHHAVA HGADAVVYFR
360 370 380 390 400
WRRCRQGQEQ YHAGLRRQDG SPDRGYREAS TAADELFDLD SVDASVALVH
410 420 430 440 450
DYESLWATRS QPLSPDWDYW NHLRTYYDAL RARGVQVDIV SPEATLERYD
460 470 480 490 500
AVVAPTLYLV GDELSTALTD YVDSGGCLLL GARTGEKDPY NRLHESLAPG
510 520 530 540 550
PLTALTGAQV ARHETLPDHV ETRLSYDGAT YEFRTWASWL APEVGVPRGE
560 570 580 590 600
YRTGEAAGNT AIVRNAAGDG SVTYCGCWPG DDLADALVTE LLDAAGVEYT
610 620 630 640 650
ERFPDGVRVM ERDGYTWALN FTSDPVTLTV PDSTGFLLGE STVDAFDTAV
660
LDGSIRGVGL ASE
Length:663
Mass (Da):74,460
Last modified:October 1, 2001 - v2
Checksum:i7ADF7634C5D13BE9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211I → F AA sequence (PubMed:9048905)Curated

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: October 1, 2014
This is version 56 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