Beta-galactosidase precursor - Aspergillus niger

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P29853 (BGAL_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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

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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
EC=3.2.1.23

Alternative name(s):
Lactase-N
Short name=Lactase
INN=Tilactase

Gene names

Name:

lacA

Organism

Aspergillus niger

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	1006 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.
Pharmaceutical use	Capable of effecting hydrolysis of lactose in situ in the gastrointestinal tract of lactase-deficient subjects when given as replacement therapy at mealtime.
Sequence similarities	Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Pharmaceutical
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

19

Potential

Chain

987

Beta-galactosidase

PRO_0000012192

Sites

Active site

1

Proton donor Potential

Active site

1

Nucleophile Potential

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

S → C in CAA00105. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P29853 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 7157B28A83805488
Show »

1,006

109,161

        10         20         30         40         50         60 
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI 

        70         80         90        100        110        120 
MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGKPGEYR ADGIFDLEPF 

       130        140        150        160        170        180 
FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT 

       190        200        210        220        230        240 
IAKYQITNGG PIILYQPENE YTSGCSGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS 

       250        260        270        280        290        300 
GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ 

       310        320        330        340        350        360 
GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT 

       370        380        390        400        410        420 
SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL 

       430        440        450        460        470        480 
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS AGSVTIPQLG GTLTLNGRDS KIHVTDHNVS 

       490        500        510        520        530        540 
GTNIIYSTAE VFTWKKFADG KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS 

       550        560        570        580        590        600 
SVVVGWDVST TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK 

       610        620        630        640        650        660 
AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV DKNGIWSATV 

       670        680        690        700        710        720 
DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL KQTKNTLRSL TTPTSLYSSD 

       730        740        750        760        770        780 
YGFHTGYLLY RGHFTATGNE STFAIDTQGG SAFGSSVWLN GTYLGSWTGL YANSDYNATY 

       790        800        810        820        830        840 
NLPQLQAGKT YVITVVIDNM GLEENWTVGE DLMKSPRGIS TSCLPDGQAA PISWKLTGNL 

       850        860        870        880        890        900 
GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL 

       910        920        930        940        950        960 
PKDGMSHCSS TSVTALRHPR TACRSTSTDI VCEIHKQHRT SDQLPCPRGN PELSRNELVG 

       970        980        990       1000 
GDPVALDSAG GKLESLELSY TTPVLTALGE VESVDQPKYK KRKGAY

References

[1]	"Saccharomyces cerevisiae cells secreting an Aspergillus niger beta-galactosidase grow on whey permeate." Kumar V., Ramakrishnan S., Teeri T.T., Knowles J.K., Hartley B.S. Biotechnology (N.Y.) 10:82-85(1992) [PubMed: 1368193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: VTT D-80144.
[2]	"DNA construct and modified yeast." Hartley B.S., Ramakrishnan S., Kumar V. Patent number WO9010703, 20-SEP-1990 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHARMACEUTICAL USE. Strain: VTT D-80144.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06037 Genomic DNA. Translation: AAA32696.1. S37150 mRNA. Translation: AAC60538.1. A00968 Unassigned DNA. Translation: CAA00105.1.
PIR	T31685.
3D structure databases
ProteinModelPortal	P29853.
SMR	P29853. Positions 41-1006.
ModBase	Search...
Protein family/group databases
CAZy	GH35. Glycoside Hydrolase Family 35.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16612.
Family and domain databases
InterPro	IPR018954. Beta-galactosidase_domain-2. IPR008979. Galactose-bd-like. IPR019801. Glyco_hydro_35_CS. IPR013781. Glyco_hydro_subgr_catalytic. IPR001944. Glycoside_Hdrlase_35. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.102.20.10. Beta-galactosidase_domain-2. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR23421. Glyco_hydro_35. 1 hit.
Pfam	PF10435. BetaGal_dom2. 1 hit. PF01301. Glyco_hydro_35. 1 hit. [Graphical view]
PRINTS	PR00742. GLHYDRLASE35.
SMART	SM01029. BetaGal_dom2. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS01182. GLYCOSYL_HYDROL_F35. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGAL_ASPNG

Accession

Primary (citable) accession number: P29853

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

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