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D9SM34 (BGAL_CLOC7) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase BgaA

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Alpha-L-arabinopyranosidase
Gene names
Name:bgaA
Ordered Locus Names:Clocel_2022
OrganismClostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) [Complete proteome] [HAMAP]
Taxonomic identifier573061 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in plant cell wall degradation in cooperation with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl-beta-D-fucopyranoside (pNPFp), but not against p-nitrophenyl-alpha-L-arabinofuranoside (pNPAf), o-nitrophenyl-beta-D-galactopyranoside (oNPGp), p-nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl-beta-D-glucopyranoside (pNPGLp), p-nitrophenyl-beta-D-cellobiopyranoside (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) or p-nitrophenyl-alpha-galactopyranoside (pNPalphaGp). No detectable activity against arabinan or arabinoxylan, but activity against arabinogalactan can be detected. Increases degradation activity of alpha-L-arabinofuranosidase (ArfA) and endo-1,4-beta-xylanase (XynA) when corn fiber gum and corn stem powder are used as substrates. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by Cu2+, Hg2+ and Zn2+. No effect with Ca2+, Mg2+, Mn2+ or excess EDTA (10 mM). Ref.1

Subunit structure

Dimer. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.51 mM for pNPAp (at 37 degrees Celsius and pH 6.0) Ref.1

KM=6.06 mM for pNPGp (at 37 degrees Celsius and pH 6.0)

Vmax=10.4 µmol/min/mg enzyme with pNPAp as substrate (at 37 degrees Celsius and pH 6.0)

Vmax=2.5 µmol/min/mg enzyme with pNPGp as substrate (at 37 degrees Celsius and pH 6.0)

pH dependence:

Optimum pH is 6.0 for activities against both pNPAp and pNPGp. Stable in the range of pH 6.0-8.0.

Temperature dependence:

Optimum temperature is 30-40 degrees Celsius for activities against both pNPAp and pNPGp when incubated 10 minutes at pH 6.0. Both activities completely lost after heating at 50 degrees Celsius for 20 minutes.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processgalactose 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: UniProtKB-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 – 659659Beta-galactosidase BgaA
PRO_0000407687

Sites

Active site1421Proton donor By similarity
Active site2981Nucleophile By similarity
Metal binding1071Zinc By similarity
Metal binding1481Zinc By similarity
Metal binding1501Zinc By similarity
Metal binding1531Zinc By similarity
Binding site1031Substrate By similarity
Binding site1411Substrate By similarity
Binding site3071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
D9SM34 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 30C0DB5C33848BF2

FASTA65976,464
        10         20         30         40         50         60 
MRIGVDYYPE HWDRQLWEKD AQLMKEIGVK VVRLAEFAWC KLEPIEGQYD FKWLDDVIEI 

        70         80         90        100        110        120 
FSVRNIEIVL GTPTNTPPLW LYEKYPDAIQ VNESGERQFI GIRGHRCYNS SSMRKYTKAI 

       130        140        150        160        170        180 
VEAMTERYAN NKAVIGWQID NELDATHCCC DNCTEKFRGW LKNKYSTLEN INKEYGNVVW 

       190        200        210        220        230        240 
SGEYSAWSQV TAPLGGSPFL NPSYLLDYNR FASDSMVEYI DFQREIIRKN CPSQFITTNT 

       250        260        270        280        290        300 
WFTGNLPNFY DAFENLDFVS YDNYPTTNEI TDEEELHSHA FHCDLMRGIK KKNFWIMEQL 

       310        320        330        340        350        360 
SGTPGCWMPM QRTPKPGMIK GYSFQAIGRG AETVVHFRWR NAIIGAEMFW HGILDHSNVK 

       370        380        390        400        410        420 
GRRFYEFAEL CREVNKINEE IPDYKINNEV AILYSSDQDF AFKIQPQVEG LYYLQQLKAF 

       430        440        450        460        470        480 
HNALIRLGVG TDIINWSESL NKYKVVIAPT LYLTDDNVTT ELYRFVEAGG TLILTNRTGV 

       490        500        510        520        530        540 
KNMNNVCLME QMPSNLKECA GVVVKEYDPI GHSIHTIKDE AGKVYQCKQW CDILEPTTAK 

       550        560        570        580        590        600 
VIATYNDDFY IDEAAVTVNK YKKGNVYYLG TVFNSDYYIE LLSKILDEKE LPYYKKLPYG 

       610        620        630        640        650 
LELSVLENEN GKYLMVFNNS NEIKCFEGKH EGKSIIRNEL DGKSFTLEPY GIEVLQLVE 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation."
Kosugi A., Murashima K., Doi R.H.
J. Bacteriol. 184:6859-6865(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-5, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.
[2]"Complete sequence of Clostridium cellulovorans 743B."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY128945 Genomic DNA. Translation: AAN05452.1.
CP002160 Genomic DNA. Translation: ADL51765.1.
RefSeqYP_003843529.1. NC_014393.1.

3D structure databases

ProteinModelPortalD9SM34.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL51765; ADL51765; Clocel_2022.
GeneID9608894.
KEGGccb:Clocel_2022.
PATRIC41740234. VBICloCel81632203721_3817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000117811.
KOK12308.
OMASDAPITH.

Enzyme and pathway databases

BioCycCCEL573061:GIXD-2086-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
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. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL_CLOC7
AccessionPrimary (citable) accession number: D9SM34
Secondary accession number(s): Q8GEE3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 5, 2010
Last modified: October 16, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries