| General Information |
| MoonProt ID | 455 |
| First appeared in release | 3.0 |
| Name(s) | ASPG2
L-asparaginase 2
Recommended name:
L-asparaginase 2 (EC:3.5.1.1)
Alternative name(s):
L-asparaginase II
Short name:
L-ASNase II
L-asparagine amidohydrolase II
INN: Colaspase |
| UniProt ID | P00805 |
| GO terms | GO:0016787 hydrolase activity
GO:0042597 periplasmic space
GO:0004067 asparaginase activity |
| Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
| Sequence length | 348 amino acids |
| FASTA sequence | >sp|P00805|ASPG2_ECOLI L-asparaginase 2 OS=Escherichia coli (strain K12) OX=83333 GN=ansB PE=1 SV=2
MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY |
| Structure Information |
| PDB ID | 6PA4 |
| Quaternary structure | Homotetramer |
| SCOP | class 1000002 Alpha and beta proteins (a/b);
fold 2000995 Glutaminase/Asparaginase;
superfamily 3001625 Glutaminase/Asparaginase;
family 4000833 Glutaminase/Asparaginase;
domain 8021094 This domain is represented by 1NNS A:1-326 L-asparaginase 2 Species Escherichia coli K-12. |
| CATH | |
| TM Helix Prediction | (7-29) signal sequence |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
moonID_455_uniID_P00805 is 348 residues long, with 0 residues (0.00%) predicted as disordered.The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | asparaginase |
| References for function | Palm GJ, Lubkowski J, Derst C, Schleper S, Röhm KH, Wlodawer A. A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant. FEBS Lett. 1996 Jul 22;390(2):211-6. doi: 10.1016/0014-5793(96)00660-6. PMID: 8706862. |
| E.C. number | 3.5.1.1 |
| Location of functional site(s) | |
| Cellular location of function | periplasm |
| Comments | |
| Function 2 |
| Function description | inhibits T-lymphocyte proliferation |
| References for function | Torres AN, Chamorro-Veloso N, Costa P, Cádiz L, Del Canto F, Venegas SA, López Nitsche M, Coloma-Rivero RF, Montero DA, Vidal RM. Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-Producing Escherichia coli. Microorganisms. 2020 Aug 4;8(8):E1184. doi: 10.3390/microorganisms8081184. PMID: 32759661; PMCID: PMC7464798. |
| E.C. number | |
| Location of functional site(s) | cell surface |
| Cellular location of function | |
| Comments | |