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PR00139

Identifier
ASNGLNASE  [View Relations]  [View Alignment]  
Accession
PR00139
No. of Motifs
3
Creation Date
05-FEB-1994  (UPDATE 27-JUN-1999)
Title
Asparaginase/glutaminase family signature
Database References

PROSITE; PS00144 ASN_GLN_ASE_1; PS00917 ASN_GLN_ASE_2
BLOCKS; BL00144
PFAM; PF00710 Asparaginase
INTERPRO; IPR000267
PDB; 3ECA
SCOP; 3ECA
CATH; 3ECA
Literature References
1. MINTON, N.P., BULLMAN, H.M.S., SCAWEN, M.D., ATKINSON, T. AND
GILBERT, H.J.
Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066
L-asparaginase gene.
GENE 46(1) 25-35 (1986).
 
2. JENNINGS, M.P. AND BEACHAM, I.R.
Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB
and its regulation by cyclic AMP receptor and fnr proteins.
J.BACTERIOL. 172(3) 1491-1498 (1990).
 
3. TANAKA, S., ROBINSON, E.A., APELLA, E., MILLER, M., AMMON, H.L.,
ROBERTS, J., WEBER, I.T. AND WLODAWER, A.
Structures of aminohydrolases - amino acid sequence of a glutaminase-
asparaginase from Acinetobacter glutaminasificans and preliminary 
crystallographic data for an asparaginase from Erwinia chrysanthemi.
J.BIOL.CHEM. 263(18) 8583-8591 (1988).

Documentation
Asparaginase, which is found in various plant, animal and bacterial cells,
catalyses the deamination of asparagine to yield aspartic acid and an
ammonium ion, resulting in a depletion of free circulatory asparagine in
plasma [1]. The enzyme is effective in the treatment of human malignant
lymphomas, which have a diminished capacity to produce asparagine
synthetase: in order to survive, such cells absorb asparagine from blood
plasma [2,3] - if Asn levels have been depleted by injection of
asparaginase, the lymphoma cells die. Glutaminase, a similar enzyme,
catalyses the deaminination of glutamine to glutamic acid and an ammonium
ion [2]. Both enzymes are homotetramers [1]: two threonine residues in the
N-terminal half of the proteins are involved in the catalytic activity.
 
ASNGLNASE is a 3-element fingerprint that provides a signature for the 
asparaginase/glutaminase family. The fingerprint was derived from an
initial alignment of 4 sequences: the motifs were drawn from conserved
regions spanning virtually the full alignment length, motifs 1 and 2
including the regions encoded by PROSITE patterns ASN_GLN_ASE_1 (PS00144)
and ASN_GLN_ASE_2 (PS00917), which contain the 2 catalytically-important
Thr residues. Two iterations on OWL22.1 were required to reach convergence,
at which point a true comprising 7 sequences was identified. A single
partial match was also found, ASG2_YEAST, an asparaginase that fails to
make a significant match with motif 3.
 
An update on SPTR37_9f identified a true set of 21 sequences, and 3
partial matches.
Summary Information
  21 codes involving  3 elements
3 codes involving 2 elements
Composite Feature Index
3212121
2231
123
True Positives
ASG1_ECOLI    ASG1_YEAST    ASG2_ECOLI    ASG2_HAEIN    
ASG2_YEAST ASPG_BACLI ASPG_BACSU ASPG_ERWCH
ASPG_METJA ASPG_WOLSU ASPQ_ACIGL ASPQ_PSES7
O25424 O26802 O29380 O34482
O59132 O68897 O88202 P87015
Q09164
True Positive Partials
Codes involving 2 elements
ASPG_MYCTU O57797 P90758
Sequence Titles
ASG1_ECOLI  L-ASPARAGINASE I (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE I) (L-ASNASE I) - ESCHERICHIA COLI. 
ASG1_YEAST L-ASPARAGINASE I (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE I) (ASP I) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
ASG2_ECOLI L-ASPARAGINASE II PRECURSOR (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE II) (L-ASNASE II) (COLASPASE) - ESCHERICHIA COLI.
ASG2_HAEIN PROBABLE L-ASPARAGINASE PERIPLASMIC PRECURSOR (EC 3.5.1.1) - HAEMOPHILUS INFLUENZAE.
ASG2_YEAST L-ASPARAGINASE II PRECURSOR (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE II) (ASP II) - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
ASPG_BACLI L-ASPARAGINASE (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) - BACILLUS LICHENIFORMIS.
ASPG_BACSU L-ASPARAGINASE (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) - BACILLUS SUBTILIS.
ASPG_ERWCH L-ASPARAGINASE PRECURSOR (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) (L-ASNASE) - ERWINIA CHRYSANTHEMI.
ASPG_METJA PROBABLE L-ASPARAGINASE (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) - METHANOCOCCUS JANNASCHII.
ASPG_WOLSU L-ASPARAGINASE (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) - WOLINELLA SUCCINOGENES.
ASPQ_ACIGL GLUTAMINASE-ASPARAGINASE (EC 3.5.1.38) - ACINETOBACTER GLUTAMINASIFICANS.
ASPQ_PSES7 GLUTAMINASE-ASPARAGINASE (EC 3.5.1.38) (PGA) - PSEUDOMONAS SP. (STRAIN 7A).
O25424 L-ASPARAGINASE II (ANSB) - HELICOBACTER PYLORI (CAMPYLOBACTER PYLORI).
O26802 L-ASPARAGINASE I - METHANOBACTERIUM THERMOAUTOTROPHICUM.
O29380 ASPARAGINASE (ASNA) - ARCHAEOGLOBUS FULGIDUS.
O34482 YCCC - BACILLUS SUBTILIS.
O59132 438AA LONG HYPOTHETICAL L-ASPARAGINASE - PYROCOCCUS HORIKOSHII.
O68897 L-ASPARAGINASE PRECURSOR (EC 3.5.1.1) - PSEUDOMONAS FLUORESCENS.
O88202 LYSOPHOSPHOLIPASE - RATTUS NORVEGICUS (RAT).
P87015 L-ASPARAGINASE PRECURSOR - SCHIZOSACCHAROMYCES POMBE (FISSION YEAST).
Q09164 CYCLOSPORIN SYNTHETASE (CYSYN) (EC 6.-.-.-) - TOLYPOCLADIUM INFLATUM.

ASPG_MYCTU PROBABLE L-ASPARAGINASE (EC 3.5.1.1) (L-ASPARAGINE AMIDOHYDROLASE) - MYCOBACTERIUM TUBERCULOSIS.
O57797 328AA LONG HYPOTHETICAL L-ASPARAGINASE - PYROCOCCUS HORIKOSHII.
P90758 HYPOTHETICAL PROTEIN C27A7.5A - CAENORHABDITIS ELEGANS.
Scan History
OWL22_1    2  100  NSINGLE    
OWL26_0 1 100 NSINGLE
SPTR37_9f 3 100 NSINGLE
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
IVILATGGTIAG ASPG_ERWCH 28 28 -
VVIVATGGTIAG ASPQ_ACIGL 4 4 -
VALITTGGTIAS ASPG_BACLI 5 5 -
IYVAYTGGTIGM ASG1_ECOLI 6 6 -

Motif 2 width=19
Element Seqn Id St Int Rpt
DGVVITHGTDTVEESAYFL ASPG_ERWCH 108 68 -
NGVVITHGTDTMEETAFFL ASPQ_ACIGL 84 68 -
DGAVVTHGTDTLEETAYFL ASPG_BACLI 81 64 -
DGFVILHGTDTMAYTASAL ASG1_ECOLI 83 65 -

Motif 3 width=19
Element Seqn Id St Int Rpt
AMEKGVVVIRSTRTGNGIV ASPG_ERWCH 287 160 -
HDEQGLQIVRSSRVAQGFV ASPQ_ACIGL 265 162 -
ALNQGVYIVITTSAEEGEV ASPG_BACLI 254 154 -
ASDRGIVVVNLTQCMSGKV ASG1_ECOLI 260 158 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
ITILATGGTIAG ASG2_ECOLI 26 26 -
IRILATGGTIAG O34482 53 53 -
ITILATGGTIAG ASG2_HAEIN 27 27 -
IVILATGGTIAG ASPG_ERWCH 28 28 -
VTILATGGTIAG ASPG_WOLSU 6 6 -
VVILATGGTIAG O68897 37 37 -
VVIVATGGTIAG ASPQ_ACIGL 4 4 -
IALLATGGTIAG O25424 8 8 -
VVILATGGTIAG ASPQ_PSES7 12 12 -
ISILSTGGTVAS ASPG_METJA 76 76 -
IKIFGTGGTIAS ASG2_YEAST 35 35 -
VALITTGGTIAS ASPG_BACLI 5 5 -
VTIIGTGGTIAS O59132 94 94 -
IKILGTGGTIAS ASG1_YEAST 56 56 -
VSIISTGGTVAS O26802 93 93 -
VKIISTGGTIAS O29380 83 83 -
IYVAYTGGTIGM ASG1_ECOLI 6 6 -
VTIFAMGGTIAG P87015 41 41 -
LLMLTTGGTIAS ASPG_BACSU 4 4 -
LLAIYTGGTIGM O88202 11 11 -
LDLLYTGGDRVG Q09164 6309 6309 -

Motif 2 width=19
Element Seqn Id St Int Rpt
DGFVITHGTDTMEETAYFL ASG2_ECOLI 103 65 -
DGIVVTHGTDTLEETAYFL O34482 133 68 -
DGFVITHGTDTMEETAYFL ASG2_HAEIN 104 65 -
DGVVITHGTDTVEESAYFL ASPG_ERWCH 108 68 -
EAVIITHGTDTMEETAFFL ASPG_WOLSU 85 67 -
DGIVITHGTDTLEETAYFL O68897 117 68 -
NGVVITHGTDTMEETAFFL ASPQ_ACIGL 84 68 -
QGVVITHGTDTLEESAYFL O25424 87 67 -
DGIVITHGTDTLEETAYFL ASPQ_PSES7 92 68 -
DGIVIAHGTDTMSYTASAL ASPG_METJA 152 64 -
AGAVVTHGTDTMEETAFFL ASG2_YEAST 114 67 -
DGAVVTHGTDTLEETAYFL ASPG_BACLI 81 64 -
SGVVVAHGTDTMGYTAAAL O59132 170 64 -
DGIVITHGTDTLSETAFFI ASG1_YEAST 133 65 -
DGVVVAHGTDTMHYTSAAL O26802 169 64 -
EGVIITHGTDTMHFSAAAL O29380 158 63 -
DGFVILHGTDTMAYTASAL ASG1_ECOLI 83 65 -
HGIVVTHGTDSLEETAMFL P87015 121 68 -
DGFVITHGTDTMAYTSAAL ASPG_BACSU 77 61 -
QGFVVIHGTDTMAFAASVL O88202 108 85 -
DSAVITQLTDEEEPELVAF Q09164 12016 5695 -

Motif 3 width=19
Element Seqn Id St Int Rpt
AAKTGTAVVRSSRVPTGAT ASG2_ECOLI 282 160 -
AVKKGVTVVRSTRTGNGVV O34482 311 159 -
AAKDSVVVVRSSRVPTGYT ASG2_HAEIN 283 160 -
AMEKGVVVIRSTRTGNGIV ASPG_ERWCH 287 160 -
AAKSGVVVARSSRVGSGST ASPG_WOLSU 264 160 -
LRKQGVQIIRSSHVNAGGF O68897 295 159 -
HDEQGLQIVRSSRVAQGFV ASPQ_ACIGL 265 162 -
ASQMGVVIVRSSRVNSGEI O25424 267 161 -
LRKTGTQIIRSSHVNQGGF ASPQ_PSES7 270 159 -
ATDKGVVVVMTTQTINGRV ASPG_METJA 335 164 -
YEEYGIPIVHSRRTADGTV ASG2_YEAST 297 164 -
ALNQGVYIVITTSAEEGEV ASPG_BACLI 254 154 -
ATEEGIAVCMTSQCIYGRV O59132 353 164 -
CMKLSLPIVYSKRSMDGMV ASG1_YEAST 310 158 -
AHDMGVPVAMTSQCLNGRV O26802 350 162 -
RVCEDSVVVMTSQCLWGRV O29380 339 162 -
ASDRGIVVVNLTQCMSGKV ASG1_ECOLI 260 158 -
ISNQSIPVVYSHRTMDGFS P87015 300 160 -
LIESGIVVVITTQCLEEGE ASPG_BACSU 253 157 -
AAERGLIIVNCTHCLQGAV O88202 286 159 -
ASPSTVAVTDSTSKLTYAE Q09164 14179 2144 -