Beta-galactosidase BgaA - Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)

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D9SM34 (BGAL_CLOC7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 18. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) [Complete proteome] [HAMAP]

Taxonomic identifier

573061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=1.51 mM for pNPAp (at 37 degrees Celsius and pH 6.0) Ref.1 K_M=6.06 mM for pNPGp (at 37 degrees Celsius and pH 6.0) V_max=10.4 µmol/min/mg enzyme with pNPAp as substrate (at 37 degrees Celsius and pH 6.0) V_max=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
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	galactose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	beta-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 659

659

Beta-galactosidase BgaA

PRO_0000407687

Sites

Active site

142

Proton donor By similarity

Active site

298

Nucleophile By similarity

Metal binding

107

Zinc By similarity

Metal binding

148

Zinc By similarity

Metal binding

150

Zinc By similarity

Metal binding

153

Zinc By similarity

Binding site

103

Substrate By similarity

Binding site

141

Substrate By similarity

Binding site

307

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

D9SM34 [UniParc].

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

659

76,464

        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' referencesShow '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.
RefSeq	YP_003843529.1. NC_014393.1.
3D structure databases
ProteinModelPortal	D9SM34.
ModBase	Search...
Protein family/group databases
CAZy	GH42. Glycoside Hydrolase Family 42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADL51765; ADL51765; Clocel_2022.
GeneID	9608894.
KEGG	ccb:Clocel_2022.
PATRIC	41740234. VBICloCel81632203721_3817.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000117811.
KO	K12308.
Enzyme and pathway databases
BioCyc	CCEL573061:GIXD-2086-MONOMER.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR013739. 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]
Pfam	PF02449. Glyco_hydro_42. 1 hit. PF08533. Glyco_hydro_42C. 1 hit. PF08532. Glyco_hydro_42M. 1 hit. [Graphical view]
PIRSF	PIRSF001084. B-galactosidase. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BGAL_CLOC7

Accession

Primary (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:	May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents