ASPG1_ECOLI
ID ASPG1_ECOLI Reviewed; 338 AA.
AC P0A962; P18840;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=L-asparaginase 1;
DE EC=3.5.1.1;
DE AltName: Full=L-asparaginase I;
DE Short=L-ASNase I;
DE AltName: Full=L-asparagine amidohydrolase I;
GN Name=ansA; OrderedLocusNames=b1767, JW1756;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2670682; DOI=10.1016/0378-1119(89)90312-0;
RA Jerlstroem P.G., Bezjak D.A., Jennings M.P., Beacham I.R.;
RT "Structure and expression in Escherichia coli K-12 of the L-asparaginase I-
RT encoding ansA gene and its flanking regions.";
RL Gene 78:37-46(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5] {ECO:0007744|PDB:2HIM, ECO:0007744|PDB:2P2D, ECO:0007744|PDB:2P2N}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH ASPARAGINE, ACTIVE
RP SITE, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP THR-14; THR-91; GLN-118; THR-162 AND ARG-240.
RX PubMed=17451745; DOI=10.1016/j.jmb.2007.03.061;
RA Yun M.K., Nourse A., White S.W., Rock C.O., Heath R.J.;
RT "Crystal structure and allosteric regulation of the cytoplasmic Escherichia
RT coli L-asparaginase I.";
RL J. Mol. Biol. 369:794-811(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000269|PubMed:17451745};
CC -!- ACTIVITY REGULATION: Shows cooperative activation. Allosterically
CC activated by asparagine. {ECO:0000269|PubMed:17451745}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for L-asparagine;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17451745}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: E.coli contains two L-asparaginase isoenzymes: L-
CC asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-
CC asparaginase II, a high-affinity secreted enzyme.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M26934; AAA23446.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74837.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15558.1; -; Genomic_DNA.
DR PIR; G64936; XDEC1.
DR RefSeq; NP_416281.1; NC_000913.3.
DR RefSeq; WP_001170162.1; NZ_STEB01000009.1.
DR PDB; 2HIM; X-ray; 1.82 A; A/B/C/D=1-338.
DR PDB; 2P2D; X-ray; 1.89 A; A/B/C/D=1-338.
DR PDB; 2P2N; X-ray; 1.90 A; A/B/C/D=1-338.
DR PDB; 6NXC; X-ray; 1.74 A; A/B/C/D=1-337.
DR PDB; 6NXD; X-ray; 1.90 A; A/B/C/D=1-338.
DR PDBsum; 2HIM; -.
DR PDBsum; 2P2D; -.
DR PDBsum; 2P2N; -.
DR PDBsum; 6NXC; -.
DR PDBsum; 6NXD; -.
DR AlphaFoldDB; P0A962; -.
DR SMR; P0A962; -.
DR BioGRID; 4259141; 16.
DR BioGRID; 850636; 1.
DR DIP; DIP-9109N; -.
DR IntAct; P0A962; 6.
DR STRING; 511145.b1767; -.
DR jPOST; P0A962; -.
DR PaxDb; P0A962; -.
DR PRIDE; P0A962; -.
DR EnsemblBacteria; AAC74837; AAC74837; b1767.
DR EnsemblBacteria; BAA15558; BAA15558; BAA15558.
DR GeneID; 66674338; -.
DR GeneID; 946278; -.
DR KEGG; ecj:JW1756; -.
DR KEGG; eco:b1767; -.
DR PATRIC; fig|1411691.4.peg.487; -.
DR EchoBASE; EB0043; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_2_3_6; -.
DR InParanoid; P0A962; -.
DR OMA; AIVPKLM; -.
DR PhylomeDB; P0A962; -.
DR BioCyc; EcoCyc:ANSA-MON; -.
DR BioCyc; MetaCyc:ANSA-MON; -.
DR EvolutionaryTrace; P0A962; -.
DR PRO; PR:P0A962; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004067; F:asparaginase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; IMP:EcoCyc.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR CDD; cd08963; L-asparaginase_I; 1.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR InterPro; IPR006033; AsnA_fam.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR041725; L-asparaginase_I.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00519; asnASE_I; 1.
DR PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..338
FT /note="L-asparaginase 1"
FT /id="PRO_0000171079"
FT DOMAIN 4..329
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 14
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100,
FT ECO:0000269|PubMed:17451745"
FT BINDING 59..61
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0007744|PDB:2P2N"
FT BINDING 91..92
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0007744|PDB:2P2N"
FT BINDING 162
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:2P2N"
FT BINDING 240
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:2P2N"
FT BINDING 271..273
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0007744|PDB:2P2N"
FT MUTAGEN 14
FT /note="T->A,V: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17451745"
FT MUTAGEN 61
FT /note="S->Q: Loss of enzyme activity."
FT MUTAGEN 91
FT /note="T->A,V: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17451745"
FT MUTAGEN 118
FT /note="Q->D: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17451745"
FT MUTAGEN 162
FT /note="T->A: No effect on activity at saturating substrate
FT concentration. Abolishes cooperativity."
FT /evidence="ECO:0000269|PubMed:17451745"
FT MUTAGEN 240
FT /note="R->A: No effect on activity at saturating substrate
FT concentration. Reduced activity at lower substrate
FT concentrations."
FT /evidence="ECO:0000269|PubMed:17451745"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2P2D"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2P2D"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2P2D"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2P2D"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2P2D"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2P2D"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2P2D"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:6NXC"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:6NXC"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:6NXC"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6NXC"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:6NXC"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6NXC"
SQ SEQUENCE 338 AA; 37127 MW; 75D97E6D10E9F8DA CRC64;
MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS
SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP
LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL
LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR
SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM
TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD
