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Q9RFN0 (BGAL_CARML) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-galactosidase BgaB
Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bgaB
OrganismCarnobacterium maltaromaticum (Carnobacterium piscicola)
Taxonomic identifier2751 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Carnobacteriaceae › Carnobacterium

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) at low temperatures. pNP-beta-galactoside, pNP-beta-fucoside and pNP-beta-galacturonide are also hydrolyzed, but not pNP-beta-galactosidase, pNP-alpha-galactoside, pNP-beta-mannoside, pNP-beta-arabanoside, pNP-beta-xyloside, pNP-beta-glucuronide nor pNP-betacellobioside at 20 degrees Celsius. Ref.1

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.7 mM for o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 30 degrees Celsius) Ref.1

KM=1.04 mM for ONPG (at 25 degrees Celsius)

Vmax=450 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius)

Temperature dependence:

Optimum temperature is 30 degrees Celsius for activity with ONPG as substrate. Loses half of its activity at 30 degrees Celsius within 1 hour. Inactivated at 40 degrees Celsius in 10 minutes. In the absence of glycerol, the enzyme is extremely unstable even at low-temperature incubation, with an 85% loss of activity at 20 degrees Celsius after 1 hour.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionbeta-galactosidase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668Beta-galactosidase BgaB
PRO_0000407686

Regions

Region350 – 3534Substrate binding

Sites

Active site1481Proton donor By similarity
Active site3021Nucleophile By similarity
Metal binding1131Zinc By similarity
Metal binding1561Zinc By similarity
Metal binding1581Zinc By similarity
Metal binding1611Zinc By similarity
Binding site1091Substrate By similarity
Binding site1471Substrate By similarity
Binding site3101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RFN0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6B256F81C06C4F17

FASTA66876,789
        10         20         30         40         50         60 
MLQQKKLFYG GDYNPEQWSK AIILEDMRLM KKANVNYVSL NIFGWASIQP TEEGFDFSFL 

        70         80         90        100        110        120 
DEMLDLLWEN GIGIDLANGT ASPPAWLVKK HPEILPVTSQ GTPLVHGSRQ HYCPSNKVYR 

       130        140        150        160        170        180 
SYVIRLTEEV AKRYATHPGI VMWHVNNEYT CHISECYCES CEKSFRQWLQ MKYKKINTLN 

       190        200        210        220        230        240 
ECWSTKFWSQ SYSQWDEIFL PKEMPTFKNP AHQLDYKRFI SDQNLTLFKA EKKAIRSYSK 

       250        260        270        280        290        300 
DIPVMTNLMG LHKHVDGFAF AEEMDVVGWD SYPNPFEEKP YPQFLANDLT RSLKKKPFLV 

       310        320        330        340        350        360 
MEQAPSAVNW RRANGAKSPG QMRLWSYEAL AHGADGILFF QWRQSQGGAE KFHSGMVSHN 

       370        380        390        400        410        420 
QDTNSRIFKE VVQLGTEMSQ LDELVGTNYN AEVAIVFDWE NWWALELDAK PSGEINYIKQ 

       430        440        450        460        470        480 
MRDLYTIFHE LNIGVDFIHP KEDLSNYKLV LSIAQYLVTD DFSAKVKRYI KAGGHFLTTF 

       490        500        510        520        530        540 
FSGIVDEYDR VYLGGYPGAF KEVLGIYVEE FDPMPIGRKS QIKYGETYYT TELWKEVIHL 

       550        560        570        580        590        600 
QGAETIATFT EGYLMGQPAL TKFGYGKGKT YYMGTKLAKD GNMKFIQTIL AESKIQPLNQ 

       610        620        630        640        650        660 
VEIESENSKI SMTCRSNSSH DYIFLLNYGQ TSEKVKLKKG GQSLLDGSMV EGEVSVKAND 


VKIIKLTK

« Hide

References

[1]"Biochemical and phylogenetic analyses of a cold-active beta-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA."
Coombs J.M., Brenchley J.E.
Appl. Environ. Microbiol. 65:5443-5450(1999) [PubMed: 10584002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
Strain: BA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF184246 Genomic DNA. Translation: AAF16519.1.

3D structure databases

HSSPHSSP built from PDB template 1KWG based on UniProtKB O69315.
ProteinModelPortalQ9RFN0.
ModBaseSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFPIRSF001084. B-galactosidase. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL_CARML
AccessionPrimary (citable) accession number: Q9RFN0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 1, 2000
Last modified: May 31, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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