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PR00743

Identifier
GLHYDRLASE36  [View Relations]  [View Alignment]  
Accession
PR00743
No. of Motifs
8
Creation Date
11-JUN-1997  (UPDATE 07-JUN-1999)
Title
Glycosyl hydrolase family 36 signature
Database References

PROSITE; PS00512 ALPHA_GALACTOSIDASE
BLOCKS; BL00512
INTERPRO; IPR002252
Literature References
1. HENRISSAT, B. AND BAIROCH, A.
New families in the classification of glycosyl hydrolases based on amino
acid sequence similarities.
BIOCHEM.J. 293 781-788 (1993).
 
2. HENRISSAT, B.
A classification of glycosyl hydrolases based on amino acid sequence
similarities.
BIOCHEM.J. 280 309-316 (1991).
 
3. DAVIES, G. AND HENRISSAT, B.
Structures and mechanisms of glycosyl hydrolases.
STRUCTURE 3 853-859 (1995).
 
4. HENRISSAT, B. AND BAIROCH, A.
Updating the sequence-based classification of glycosyl hydrolases.
BIOCHEM.J. 316 695-696 (1996).
 
5. TURAKAINEN, H., KRISTO, P. AND KORHOLA, M. 
Consideration of the evolution of the Saccharomyces cerevisiae MEL gene
family on the basis of the nucleotide sequences of the genes and their
flanking regions.
YEAST 10(12) 1559-1568 (1994). 
 
6. ASLANIDIS C., SCHMID K., SCHMITT R.
Nucleotide sequences and operon structure of plasmid-borne genes mediating
uptake and utilization of raffinose in Escherichia coli.
J.BACTERIOL. 171 6753-6763 (1989).

Documentation
O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that
hydrolyse the glycosidic bond between two or more carbohydrates, or between
a carbohydrate and a non-carbohydrate moiety. A classification system for
glycosyl hydrolases, based on sequence similarity, has led to the definition
of up to 60 different families [1-4] (http://expasy.hcuge.ch/cgi-bin/lists?
glycosid.txt). Family 36 encompasses alpha-galactosidases.
 
Alpha-galactosidase (melibiase) catalyses the hydrolysis of melibiose into
galactose and glucose [5]. In man, deficiency in the enzyme results in
Fabry's disease (X-linked sphingolipidosis). An E.coli plasmid-encoded
alpha-galactosidase (rafA) [6] contains a region of about 50 amino acids
that is similar to a domain of the eukaryotic alpha-galactosidases.
 
GLHYDRLASE36 is an 8-element fingerprint that provides a signature for
family 36 glycosyl hydrolases. The fingerprint was derived from an initial
alignment of 4 sequences: the motifs were drawn from conserved regions 
spanning the central portion of the alignment - motif 4 includes the
region encoded by PROSITE pattern ALPHA_GALACTOSIDASE (PS00512), which
contains two conserved Asp residues that may be involved in the catalytic
mechanism. Two iterations on OWL29.3 were required to reach convergence, at
which point a true set comprising 5 sequences was identified. A single 
partial match was found, TEMELA, an alpha-galactosidase that matches motifs
3 and 6.
 
An update on SPTR37_9f identified a true set of 5 sequences.
Summary Information
5 codes involving  8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
855555555
700000000
600000000
500000000
400000000
300000000
200000000
12345678
True Positives
AGA1_PEDPE    AGA2_PEDPE    AGAL_STRMU    Q92457        
RAFA_ECOLI
Sequence Titles
AGA1_PEDPE  ALPHA-GALACTOSIDASE 1 (EC 3.2.1.22) (MELIBIASE) - PEDIOCOCCUS PENTOSACEUS. 
AGA2_PEDPE ALPHA-GALACTOSIDASE 2 (EC 3.2.1.22) (MELIBIASE) - PEDIOCOCCUS PENTOSACEUS.
AGAL_STRMU ALPHA-GALACTOSIDASE (EC 3.2.1.22) (MELIBIASE) - STREPTOCOCCUS MUTANS.
Q92457 ALPHA-GALACTOSIDASE PRECURSOR (EC 3.2.1.22) (MELIBIASE) - TRICHODERMA REESEI (HYPOCREA JECORINA).
RAFA_ECOLI ALPHA-GALACTOSIDASE (EC 3.2.1.22) (MELIBIASE) - ESCHERICHIA COLI.
Scan History
OWL29_3    2  50   NSINGLE    
SPTR37_9f 2 6 NSINGLE
Initial Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
EFSGDAYGFNLVYSGN AGA1_PEDPE 243 243 -
EFYGEALALQLIYSGN AGAL_STRMU 235 235 -
EQQGEVWAVHLGWSGN RAFA_ECOLI 205 205 -
ELAGTVIGCALAWSGN AGA2_PEDPE 239 239 -

Motif 2 width=21
Element Seqn Id St Int Rpt
TPEVLMVYTNKGLNAMSQAYH AGA1_PEDPE 294 35 -
TPVALITYTDKGLTDLTQESH AGAL_STRMU 286 35 -
TPWLYACHSADGLNGMSQQYH RAFA_ECOLI 256 35 -
TPEAVLTWTNTGFNGMSQVFH AGA2_PEDPE 290 35 -

Motif 3 width=15
Element Seqn Id St Int Rpt
PIVVNNWEATFFDFN AGA1_PEDPE 332 17 -
PILINNWEATYFDFN AGAL_STRMU 324 17 -
PVHLNTWEGIYFNHN RAFA_ECOLI 293 16 -
PSVLNTWETLTFAVS AGA2_PEDPE 324 13 -

Motif 4 width=16
Element Seqn Id St Int Rpt
LGIEMFVLDDGWFGHR AGA1_PEDPE 360 13 -
LGIELFVLDDGWFGHR AGAL_STRMU 352 13 -
LGVERFIIDDGWFKGR RAFA_ECOLI 321 13 -
LGLQMLVLDDGWFVNR AGA2_PEDPE 352 13 -

Motif 5 width=23
Element Seqn Id St Int Rpt
FGIWLEPEMISYDSKLYQQHPDY AGA1_PEDPE 410 34 -
FGLWFEPEMVSVDSKLYRAHPDW AGAL_STRMU 402 34 -
FGIWVEPEMINPDSDLFRLHPDW RAFA_ECOLI 371 34 -
FGLWVEPEMITTNSQLYQQHPDW AGA2_PEDPE 402 34 -

Motif 6 width=16
Element Seqn Id St Int Rpt
LLKSKQIDYIKWDMNR AGA1_PEDPE 468 35 -
LLTENTIDYVKWDYNR AGAL_STRMU 460 35 -
LLGEHPVDYVKWDMNR RAFA_ECOLI 429 35 -
LVQNNQLDYLKWDMNR AGA2_PEDPE 460 35 -

Motif 7 width=17
Element Seqn Id St Int Rpt
HILFEGCSGGGGRFDAG AGA1_PEDPE 522 38 -
KVLFESCSGGGGRNDLG AGAL_STRMU 513 37 -
HVEFESCASGGGRIDFE RAFA_ECOLI 477 32 -
KLIIENCSAGGGRFDFG AGA2_PEDPE 514 38 -

Motif 8 width=17
Element Seqn Id St Int Rpt
WASDNTDAVARLTIQYG AGA1_PEDPE 547 8 -
WSSDNTDAIARLPIQYG AGAL_STRMU 538 8 -
WASDNNDALERCTIQRG RAFA_ECOLI 502 8 -
WISDLTDPVDRATIENG AGA2_PEDPE 539 8 -
Final Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
EFSGDAYGFNLVYSGN AGA1_PEDPE 243 243 -
EFYGEALALQLIYSGN AGAL_STRMU 235 235 -
EQQGEVWAVHLGWSGN RAFA_ECOLI 205 205 -
ESQGEAWGFSLVYTGS Q92457 257 257 -
ELAGTVIGCALAWSGN AGA2_PEDPE 239 239 -

Motif 2 width=21
Element Seqn Id St Int Rpt
TPEVLMVYTNKGLNAMSQAYH AGA1_PEDPE 294 35 -
TPVALITYTDKGLTDLTQESH AGAL_STRMU 286 35 -
TPWLYACHSADGLNGMSQQYH RAFA_ECOLI 256 35 -
SPEAVAVFSTTGVGGMSRKFH Q92457 308 35 -
TPEAVLTWTNTGFNGMSQVFH AGA2_PEDPE 290 35 -

Motif 3 width=15
Element Seqn Id St Int Rpt
PIVVNNWEATFFDFN AGA1_PEDPE 332 17 -
PILINNWEATYFDFN AGAL_STRMU 324 17 -
PVHLNTWEGIYFNHN RAFA_ECOLI 293 16 -
PVLLNSWEGLGFDYN Q92457 346 17 -
PSVLNTWETLTFAVS AGA2_PEDPE 324 13 -

Motif 4 width=16
Element Seqn Id St Int Rpt
LGIEMFVLDDGWFGHR AGA1_PEDPE 360 13 -
LGIELFVLDDGWFGHR AGAL_STRMU 352 13 -
LGVERFIIDDGWFKGR RAFA_ECOLI 321 13 -
LGIKLFVLDDGWFGVK Q92457 374 13 -
LGLQMLVLDDGWFVNR AGA2_PEDPE 352 13 -

Motif 5 width=23
Element Seqn Id St Int Rpt
FGIWLEPEMISYDSKLYQQHPDY AGA1_PEDPE 410 34 -
FGLWFEPEMVSVDSKLYRAHPDW AGAL_STRMU 402 34 -
FGIWVEPEMINPDSDLFRLHPDW RAFA_ECOLI 371 34 -
FGLWFEPEMVNPNSTLYMEHPDW Q92457 434 44 -
FGLWVEPEMITTNSQLYQQHPDW AGA2_PEDPE 402 34 -

Motif 6 width=16
Element Seqn Id St Int Rpt
LLKSKQIDYIKWDMNR AGA1_PEDPE 468 35 -
LLTENTIDYVKWDYNR AGAL_STRMU 460 35 -
LLGEHPVDYVKWDMNR RAFA_ECOLI 429 35 -
ILSNASISYVKWDNNR Q92457 492 35 -
LVQNNQLDYLKWDMNR AGA2_PEDPE 460 35 -

Motif 7 width=17
Element Seqn Id St Int Rpt
HILFEGCSGGGGRFDAG AGA1_PEDPE 522 38 -
KVLFESCSGGGGRNDLG AGAL_STRMU 513 37 -
HVEFESCASGGGRIDFE RAFA_ECOLI 477 32 -
NVRWEGCASGGGRFDPG Q92457 538 30 -
KLIIENCSAGGGRFDFG AGA2_PEDPE 514 38 -

Motif 8 width=17
Element Seqn Id St Int Rpt
WASDNTDAVARLTIQYG AGA1_PEDPE 547 8 -
WSSDNTDAIARLPIQYG AGAL_STRMU 538 8 -
WASDNNDALERCTIQRG RAFA_ECOLI 502 8 -
WTSDDTDAVERIAIQFG Q92457 563 8 -
WISDLTDPVDRATIENG AGA2_PEDPE 539 8 -