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Streptococcus mutans Search Results

Record: 1 of 1  
MiniMap IGR1436 IGR1435 IGR1433 IGR1431 IGR1437 IGR1438 IGR1432 IGR1439 IGR1434 codY, - SMu1662 aroG, - SMu1672 alr, - SMu1670 yfbQ, - SMu1663 SMu1666 recG, - SMu1669 SMu1668 uspA, - SMu1665 yhfU,bioB, - SMu1664 aspG,ansB, - SMu1667 codY, - SMu1662 aroG, - SMu1672 alr, - SMu1670 yfbQ, - SMu1663 SMu1666 recG, - SMu1669 SMu1668 uspA, - SMu1665 yhfU,bioB, - SMu1664 aspG,ansB, - SMu1667 codY, - SMu1662 aroG, - SMu1672 alr, - SMu1670 yfbQ, - SMu1663 SMu1666 recG, - SMu1669 acpS, - SMu1671 acpS, - SMu1671 SMu1668 uspA, - SMu1665 yhfU,bioB, - SMu1664 aspG,ansB, - SMu1667


LANL Gene ID: SMu1667

GenBank Locus Tag: SMU.1831

DNA Molecule Name:
1  

GenBank ID:
24380193

Gene Name:
aspG  ansB  

Definition:
L-asparaginase

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
1727002

Gene Stop:
1727961

Gene Length:
960

Molecular Weight*:
34563

pI*:
6.40

Net Charge*:
-3.63

EC:
3.5.1.1  

Functional Class:
Amino acid biosynthesis; Aspartate family  

Gene Ontology:
Biological process
  GO:0006520    amino acid metabolic process
  GO:0008152    metabolic process
  GO:0016310    phosphorylation

Cellular component
  GO:0005622    intracellular

Molecular function
  GO:0016301    kinase activity
  GO:0016774    phosphotransferase activity, carboxyl group as acceptor


Pathway: pathway table
Alanine and aspartate metabolism
Cyanoamino acid metabolism
Nitrogen metabolism

Secondary Evidence:
Wang Y, Qian S, Meng G, Zhang S.
Cloning and expression of L-asparaginase gene in Escherichia coli.
Appl Biochem Biotechnol. 2001 Aug;95(2):93-101.
PMID: 11694066

Comment:
For other 'asp' genes see SMu1907 (aspS); SMu1199 (aspB), (aspC) and SMu1660 (aspS).



View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Matches in gapped BLAST to L-asparaginases. Residues 2-319 are 76% similar to 15901821 from S.pneumoniae. Residues 1-319 are 74% similar to 15675622 from S.pyogenes.





The best hit to the Streptococcus agalactiae 2603 V/R genome is to SAG1679 (1e-138).


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|24380193|ref|NP_722148.1|  putative L-asparaginase [Strep...   629   e-178
 gi|55821696|ref|YP_140138.1|  L-asparaginase [Streptococcus ...   497   e-139
 gi|15901821|ref|NP_346425.1|  L-asparaginase, putative [Stre...   486   e-136
 gi|148993138|ref|ZP_01822704.1|  L-asparaginase, putative [S...   486   e-136
 gi|149021949|ref|ZP_01835936.1|  L-asparaginase, putative [S...   486   e-135
 gi|148998530|ref|ZP_01825971.1|  L-asparaginase, putative [S...   485   e-135
 gi|149012413|ref|ZP_01833444.1|  L-asparaginase, putative [S...   483   e-135
 gi|149007474|ref|ZP_01831117.1|  L-asparaginase, putative [S...   483   e-134
 gi|116628410|ref|YP_821029.1|  L-asparaginase [Streptococcus...   481   e-134
 gi|157075006|gb|ABV09689.1|  asparaginase [Streptococcus gor...   481   e-134


InterPro Summary:  InterProScan

InterPro
IPR000890
Family
Acetate and butyrate kinase
PS01076 [4-21]? 0.0 PS01076 ACETATE_KINASE_2 ACETATE_KINASE_2
InterPro
IPR006034
Family
Asparaginase/glutaminase
PD003221 [6-229]T 0.0 PD003221 Asp/Glutamnse Asp/Glutamnse
PR00139 [4-15]T 2.1E-18 PR00139 ASNGLNASE[76-94]T 2.1E-18 PR00139 ASNGLNASE[249-267]T 2.1E-18 PR00139 ASNGLNASE ASNGLNASE
PIRSF001220 [1-319]T 2.90000000000029E-124 PIRSF001220 L-ASNase_gatD L-ASNase_gatD
PTHR11707 [48-318]T 2.2999842048855902E-91 PTHR11707 Asp/Glutamnse Asp/Glutamnse
PF00710 [3-314]T 0.0 PF00710 Asparaginase Asparaginase
PS00144 [6-14]? 0.0 PS00144 ASN_GLN_ASE_1 ASN_GLN_ASE_1
PS00917 [77-87]T 8.0E-5 PS00917 ASN_GLN_ASE_2 ASN_GLN_ASE_2
SSF53774 [1-319]T 1.0E-98 SSF53774 Asp/Glutamnse Asp/Glutamnse
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.1170 [1-207]T 3.8000069709354505E-62 G3DSA:3.40.50.1170 G3DSA:3.40.50.1170 G3DSA:3.40.50.1170
PIRSF500176 [1-319]T 2.0000000659507303E-126 PIRSF500176 L_ASNase L_ASNase
PTHR11707:SF4 [48-318]T 2.2999842048855902E-91 PTHR11707:SF4 PTHR11707:SF4 PTHR11707:SF4


COGS Summary:  COGS Search
BeTs to 9 clades of COG0252
COG name: L-asparaginase
Functional Class: E
The phylogenetic pattern of COG0252 is amtKY---EBrhuj-------
Number of proteins in this genome belonging to this COG is 1
Blocks Summary:  Blocks Search
***** IPB000267 (Asparaginase/glutaminase family) with a combined E-value of 1.1e-65.
    IPB000267A    1-17
    IPB000267B    30-68
    IPB000267C    76-120
    IPB000267D    127-168
    IPB000267E    291-317


 ProDom Summary:  Protein Domain Search
Residues 203-304 are 30% similar to a (L-ASPARAGINASE PROTEOME COMPLETE HYDROLASE) protein domain (PD344636 which is seen in O59132_PYRHO.

Residues 1-162 are 61% similar to a (L-ASPARAGINASE HYDROLASE COMPLETE PROTEOME L-ASPARAGINE) protein domain (PD003221 which is seen in Q9CHJ5_LACLA.

Residues 172-307 are 55% similar to a (L-ASPARAGINASE PROTEOME COMPLETE) protein domain (PD304321 which is seen in Q9CHJ5_LACLA.

Residues 203-315 are 28% similar to a (L-ASPARAGINASE HYDROLASE AMIDOHYDROLASE L-ASPARAGINE) protein domain (PD244538 which is seen in Q9V0T9_PYRAB.


Paralogs:  Local Blast Search
SMu1667 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 8 to 315 (E-value = 1.8e-64) place SMu1667 in the Asparaginase family which is described as Asparaginase (PF00710)

 Top PDB Hits:
pdb|3ECA|A Chain A, Asparaginase Type Ii (E.C.3.5.1.1) (Eca) >g... 145 7e-036
pdb|1HFJ|A Chain A, Asparaginase From Erwinia Chrysanthemi, Hex... 143 3e-035
pdb|4ECA|A Chain A, Asparaginase From E. Coli, Mutant T89v With... 141 1e-034

Gene Protein Sequence:
MKRILVLHTGGTISMHADKAGRVVPDSDNPMNHASVKLDDIQINAIDFLN
IPSPQITVEHMLLLTQKIRETAGLYDGVVITHGTDTLEETAYFLDTMILP
QIPIVLTGAMRSSNELGSDGVYNYLSALRVASHDNAADKGVLVVMNDEIH
AAKYVTKTHTTNVSTFQTPTHGPLGIIMKHDILFFKTAEPRVRFRLESLT
GTVPIIKAYAGMGDWLLNILDKSSIDGLVVEALGAGNLPPEAAQSITKLI
QEGIPVALVSRCFNGIAEPVYAYQGGGVKLQEAGVMFVRELNAPKARLKL
LIALNAGLKGQELKEYIEG

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAAGAATCCTTGTTTTACATACTGGAGGAACCATTTCCATGCATGC
TGATAAGGCTGGTAGGGTTGTTCCAGACAGTGATAACCCTATGAACCATG
CCAGTGTCAAACTTGATGATATTCAGATTAATGCTATTGATTTTTTAAAC
ATTCCCAGTCCGCAAATAACAGTGGAGCATATGCTTTTATTGACTCAAAA
AATTAGAGAAACAGCTGGCTTATACGATGGCGTGGTTATTACACATGGAA
CAGACACTTTAGAAGAGACTGCTTACTTCCTAGACACTATGATTTTGCCA
CAAATTCCCATTGTTTTGACTGGAGCTATGCGTTCTTCCAATGAGTTAGG
GAGTGATGGTGTTTACAATTACTTATCTGCCCTTCGTGTTGCCAGCCATG
ACAATGCTGCTGACAAGGGAGTCCTTGTCGTCATGAATGATGAAATTCAT
GCTGCCAAATACGTTACCAAAACACATACTACTAATGTTTCTACTTTTCA
AACACCTACACATGGACCGCTTGGTATCATTATGAAACATGATATTCTCT
TTTTCAAAACAGCTGAACCGCGGGTTCGTTTTCGCCTAGAATCTTTAACA
GGAACTGTTCCCATTATCAAGGCATACGCTGGTATGGGTGATTGGCTTTT
AAATATTTTAGATAAAAGCAGTATTGATGGTTTGGTTGTTGAAGCTCTAG
GTGCTGGTAACCTTCCACCCGAGGCTGCTCAAAGCATTACCAAGCTCATT
CAAGAAGGAATTCCTGTCGCTCTCGTCTCTCGATGTTTTAACGGGATTGC
AGAGCCTGTCTACGCTTACCAAGGTGGCGGTGTCAAACTGCAAGAAGCAG
GTGTCATGTTTGTTAGGGAACTCAATGCCCCTAAGGCCAGACTCAAACTT
CTCATTGCTCTCAACGCTGGCCTCAAGGGGCAAGAATTAAAAGAATACAT
AGAAGGTTAA

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