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Q9RFN0

- BGAL_CARML

UniProt

Q9RFN0 - BGAL_CARML

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Protein

Beta-galactosidase BgaB

Gene
bgaB
Organism
Carnobacterium maltaromaticum (Carnobacterium piscicola)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Kineticsi

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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Substrate By similarity
Metal bindingi113 – 1131Zinc By similarity
Binding sitei147 – 1471Substrate By similarity
Active sitei148 – 1481Proton donor By similarity
Metal bindingi156 – 1561Zinc By similarity
Metal bindingi158 – 1581Zinc By similarity
Metal bindingi161 – 1611Zinc By similarity
Active sitei302 – 3021Nucleophile By similarity
Binding sitei310 – 3101Substrate 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 BgaB (EC:3.2.1.23)
Short name:
Beta-gal
Gene namesi
Name:bgaB
OrganismiCarnobacterium maltaromaticum (Carnobacterium piscicola)
Taxonomic identifieri2751 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesCarnobacteriaceaeCarnobacterium

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Beta-galactosidase BgaBPRO_0000407686Add
BLAST

Proteomic databases

PRIDEiQ9RFN0.

Structurei

3D structure databases

ProteinModelPortaliQ9RFN0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni350 – 3534Substrate binding

Sequence similaritiesi

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.

Q9RFN0-1 [UniParc]FASTAAdd to Basket

« Hide

MLQQKKLFYG GDYNPEQWSK AIILEDMRLM KKANVNYVSL NIFGWASIQP    50
TEEGFDFSFL DEMLDLLWEN GIGIDLANGT ASPPAWLVKK HPEILPVTSQ 100
GTPLVHGSRQ HYCPSNKVYR SYVIRLTEEV AKRYATHPGI VMWHVNNEYT 150
CHISECYCES CEKSFRQWLQ MKYKKINTLN ECWSTKFWSQ SYSQWDEIFL 200
PKEMPTFKNP AHQLDYKRFI SDQNLTLFKA EKKAIRSYSK DIPVMTNLMG 250
LHKHVDGFAF AEEMDVVGWD SYPNPFEEKP YPQFLANDLT RSLKKKPFLV 300
MEQAPSAVNW RRANGAKSPG QMRLWSYEAL AHGADGILFF QWRQSQGGAE 350
KFHSGMVSHN QDTNSRIFKE VVQLGTEMSQ LDELVGTNYN AEVAIVFDWE 400
NWWALELDAK PSGEINYIKQ MRDLYTIFHE LNIGVDFIHP KEDLSNYKLV 450
LSIAQYLVTD DFSAKVKRYI KAGGHFLTTF FSGIVDEYDR VYLGGYPGAF 500
KEVLGIYVEE FDPMPIGRKS QIKYGETYYT TELWKEVIHL QGAETIATFT 550
EGYLMGQPAL TKFGYGKGKT YYMGTKLAKD GNMKFIQTIL AESKIQPLNQ 600
VEIESENSKI SMTCRSNSSH DYIFLLNYGQ TSEKVKLKKG GQSLLDGSMV 650
EGEVSVKAND VKIIKLTK 668
Length:668
Mass (Da):76,789
Last modified:May 1, 2000 - v1
Checksum:i6B256F81C06C4F17
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184246 Genomic DNA. Translation: AAF16519.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184246 Genomic DNA. Translation: AAF16519.1 .

3D structure databases

ProteinModelPortali Q9RFN0.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH42. Glycoside Hydrolase Family 42.

Proteomic databases

PRIDEi Q9RFN0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    Strain: BA.

Entry informationi

Entry nameiBGAL_CARML
AccessioniPrimary (citable) accession number: Q9RFN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 45 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

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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