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Asparagine synthetase B [glutamine-hydrolyzing] (AS-B) (EC 6.3.5.4)

 ASNB_ECOLI              Reviewed;         554 AA.
P22106;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 152.
RecName: Full=Asparagine synthetase B [glutamine-hydrolyzing];
Short=AS-B;
EC=6.3.5.4;
Name=asnB; OrderedLocusNames=b0674, JW0660;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1973930;
Scofield M.A., Lewis W.S., Schuster S.M.;
"Nucleotide sequence of Escherichia coli asnB and deduced amino acid
sequence of asparagine synthetase B.";
J. Biol. Chem. 265:12895-12902(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE,
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-2; HIS-30;
ASP-34; HIS-81 AND ALA-105.
STRAIN=K12;
PubMed=7907328;
Boehlein S.K., Richards N.G., Schuster S.M.;
"Glutamine-dependent nitrogen transfer in Escherichia coli asparagine
synthetase B. Searching for the catalytic triad.";
J. Biol. Chem. 269:7450-7457(1994).
[6]
FUNCTION IN ASPARAGINE BIOSYNTHESIS.
STRAIN=K12;
PubMed=6102982;
Humbert R., Simoni R.D.;
"Genetic and biomedical studies demonstrating a second gene coding for
asparagine synthetase in Escherichia coli.";
J. Bacteriol. 142:212-220(1980).
[7]
ENZYME REGULATION, AND INHIBITION STUDIES.
PubMed=8691431; DOI=10.1021/jm9601009;
Parr I.B., Boehlein S.K., Dribben A.B., Schuster S.M., Richards N.G.;
"Mapping the aspartic acid binding site of Escherichia coli asparagine
synthetase B using substrate analogs.";
J. Med. Chem. 39:2367-2378(1996).
[8]
KINETIC PARAMETERS.
STRAIN=K12;
PubMed=12706338; DOI=10.1016/S0003-9861(03)00118-8;
Tesson A.R., Soper T.S., Ciustea M., Richards N.G.;
"Revisiting the steady state kinetic mechanism of glutamine-dependent
asparagine synthetase from Escherichia coli.";
Arch. Biochem. Biophys. 413:23-31(2003).
[9]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-349, AND KINETIC
MODEL.
STRAIN=K12;
PubMed=20853825; DOI=10.1021/bi1010688;
Meyer M.E., Gutierrez J.A., Raushel F.M., Richards N.G.;
"A conserved glutamate controls the commitment to acyl-adenylate
formation in asparagine synthetase.";
Biochemistry 49:9391-9401(2010).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-554 OF MUTANT ALA-2 IN
COMPLEX WITH AMP AND L-GLUTAMINE, AND SUBUNIT.
STRAIN=K12;
PubMed=10587437; DOI=10.1021/bi9915768;
Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J.,
Thoden J.B., Holden H.M., Rayment I.;
"Three-dimensional structure of Escherichia coli asparagine synthetase
B: a short journey from substrate to product.";
Biochemistry 38:16146-16157(1999).
[11]
ERRATUM.
PubMed=10852734; DOI=10.1021/bi005109y;
Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J.,
Thoden J.B., Holden H.M., Rayment I.;
Biochemistry 39:7330-7330(2000).
-!- FUNCTION: Catalyzes the ATP-dependent conversion of aspartate into
asparagine, using glutamine as a source of nitrogen. Can also use
ammonia as the nitrogen source in vitro, albeit with lower
efficiency. As nucleotide substrates, ATP and dATP are utilized at
a similar rate in both the glutamine- and ammonia-dependent
reactions, whereas GTP utilization is only 15% that of ATP, and
CTP, UTP, ITP and XTP are very poor or not substrates. Also
exhibits glutaminase activity. {ECO:0000269|PubMed:20853825,
ECO:0000269|PubMed:6102982, ECO:0000269|PubMed:7907328}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + L-glutamine + H(2)O = AMP
+ diphosphate + L-asparagine + L-glutamate.
{ECO:0000269|PubMed:20853825, ECO:0000269|PubMed:7907328}.
-!- ENZYME REGULATION: Glutamine-dependent asparagine synthesis
activity can be inhibited by aspartic acid analogs (such as a
sulfinate derivative and (2S,3R)-2-amino-3-methylsuccinate) in
vitro; the inhibition is competitive with respect to aspartate.
{ECO:0000269|PubMed:8691431}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17 mM for ammonia {ECO:0000269|PubMed:12706338,
ECO:0000269|PubMed:7907328};
KM=0.53 mM for aspartate (when assaying the ammonia-dependent
synthetase reaction) {ECO:0000269|PubMed:12706338,
ECO:0000269|PubMed:7907328};
KM=0.85 mM for aspartate (when assaying the glutamine-dependent
synthetase reaction) {ECO:0000269|PubMed:12706338,
ECO:0000269|PubMed:7907328};
KM=0.26 mM for ATP (when assaying the glutamine-dependent
synthetase reaction) {ECO:0000269|PubMed:12706338,
ECO:0000269|PubMed:7907328};
KM=0.66 mM for glutamine (when assaying the glutamine-dependent
synthetase reaction) {ECO:0000269|PubMed:12706338,
ECO:0000269|PubMed:7907328};
pH dependence:
Optimum pH is 6.5-8. {ECO:0000269|PubMed:7907328};
-!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
asparagine from L-aspartate (L-Gln route): step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10587437}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-549123, EBI-549123;
-!- SIMILARITY: Belongs to the asparagine synthetase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J05554; AAA23498.1; -; Genomic_DNA.
EMBL; U00096; AAC73768.1; -; Genomic_DNA.
EMBL; AP009048; BAA35317.1; -; Genomic_DNA.
PIR; A36616; AJECN.
RefSeq; NP_415200.1; NC_000913.3.
RefSeq; WP_000337077.1; NZ_LN832404.1.
PDB; 1CT9; X-ray; 2.00 A; A/B/C/D=2-554.
PDBsum; 1CT9; -.
ProteinModelPortal; P22106; -.
SMR; P22106; -.
BioGrid; 4261812; 406.
DIP; DIP-9177N; -.
IntAct; P22106; 7.
MINT; MINT-1306603; -.
STRING; 316385.ECDH10B_0739; -.
MEROPS; C44.976; -.
PaxDb; P22106; -.
PRIDE; P22106; -.
EnsemblBacteria; AAC73768; AAC73768; b0674.
EnsemblBacteria; BAA35317; BAA35317; BAA35317.
GeneID; 945281; -.
KEGG; ecj:JW0660; -.
KEGG; eco:b0674; -.
PATRIC; fig|1411691.4.peg.1605; -.
EchoBASE; EB0090; -.
EcoGene; EG10092; asnB.
eggNOG; ENOG4105CAQ; Bacteria.
eggNOG; COG0367; LUCA.
HOGENOM; HOG000027493; -.
InParanoid; P22106; -.
KO; K01953; -.
PhylomeDB; P22106; -.
BioCyc; EcoCyc:ASNSYNB-MONOMER; -.
BioCyc; MetaCyc:ASNSYNB-MONOMER; -.
BRENDA; 6.3.5.4; 2026.
UniPathway; UPA00134; UER00195.
EvolutionaryTrace; P22106; -.
PRO; PR:P22106; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
GO; GO:0004071; F:aspartate-ammonia ligase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006529; P:asparagine biosynthetic process; IDA:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; IMP:EcoliWiki.
GO; GO:0009063; P:cellular amino acid catabolic process; IMP:EcoliWiki.
GO; GO:0006541; P:glutamine metabolic process; IMP:EcoliWiki.
GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd01991; Asn_Synthase_B_C; 1.
CDD; cd00712; AsnB; 1.
Gene3D; 3.40.50.620; -; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR006426; Asn_synth_AEB.
InterPro; IPR001962; Asn_synthase.
InterPro; IPR033738; AsnB_N.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF00733; Asn_synthase; 1.
Pfam; PF13537; GATase_7; 1.
PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
PROSITE; PS51278; GATASE_TYPE_2; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Asparagine biosynthesis;
ATP-binding; Complete proteome; Direct protein sequencing;
Glutamine amidotransferase; Ligase; Nucleotide-binding;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7907328}.
CHAIN 2 554 Asparagine synthetase B [glutamine-
hydrolyzing].
/FTId=PRO_0000056931.
DOMAIN 2 186 Glutamine amidotransferase type-2.
{ECO:0000255|PROSITE-ProRule:PRU00609}.
NP_BIND 347 348 ATP.
REGION 50 54 Glutamine binding.
REGION 75 77 Glutamine binding.
ACT_SITE 2 2 For GATase activity.
BINDING 99 99 Glutamine.
BINDING 233 233 ATP; via carbonyl oxygen.
BINDING 273 273 ATP; via amide nitrogen and carbonyl
oxygen.
SITE 349 349 Important for beta-aspartyl-AMP
intermediate formation.
MUTAGEN 2 2 C->A,S: Loss of glutamine-dependent
activity but no effect on ammonia-
dependent asparagine synthetase activity.
{ECO:0000269|PubMed:7907328}.
MUTAGEN 30 30 H->A: 4,5-fold decrease in glutamine
affinity. {ECO:0000269|PubMed:7907328}.
MUTAGEN 34 34 D->N,E: Little effect on the kinetic
properties. {ECO:0000269|PubMed:7907328}.
MUTAGEN 81 81 H->A: 5-fold decrease in glutamine
affinity. {ECO:0000269|PubMed:7907328}.
MUTAGEN 105 105 A->H: Little effect on the kinetic
properties. {ECO:0000269|PubMed:7907328}.
MUTAGEN 349 349 E->A,Q: Loss of glutamine- and ammonia-
dependent synthetase activity, but still
exhibits glutaminase activity.
{ECO:0000269|PubMed:20853825}.
MUTAGEN 349 349 E->D: 5-fold increase in affinity for
asparate when assaying both the
glutamine- and ammonia-dependent
synthetase reactions, and 2-fold decrease
in kcat for these reactions. Modifies the
product glutamate/asparagine
stoichiometry.
{ECO:0000269|PubMed:20853825}.
STRAND 3 9 {ECO:0000244|PDB:1CT9}.
HELIX 14 26 {ECO:0000244|PDB:1CT9}.
HELIX 27 31 {ECO:0000244|PDB:1CT9}.
STRAND 35 40 {ECO:0000244|PDB:1CT9}.
STRAND 42 50 {ECO:0000244|PDB:1CT9}.
TURN 56 58 {ECO:0000244|PDB:1CT9}.
STRAND 61 64 {ECO:0000244|PDB:1CT9}.
STRAND 70 78 {ECO:0000244|PDB:1CT9}.
HELIX 81 88 {ECO:0000244|PDB:1CT9}.
TURN 89 91 {ECO:0000244|PDB:1CT9}.
HELIX 99 101 {ECO:0000244|PDB:1CT9}.
HELIX 102 110 {ECO:0000244|PDB:1CT9}.
TURN 111 114 {ECO:0000244|PDB:1CT9}.
HELIX 115 117 {ECO:0000244|PDB:1CT9}.
STRAND 120 128 {ECO:0000244|PDB:1CT9}.
TURN 129 132 {ECO:0000244|PDB:1CT9}.
STRAND 133 138 {ECO:0000244|PDB:1CT9}.
STRAND 147 150 {ECO:0000244|PDB:1CT9}.
STRAND 156 161 {ECO:0000244|PDB:1CT9}.
HELIX 162 164 {ECO:0000244|PDB:1CT9}.
TURN 165 168 {ECO:0000244|PDB:1CT9}.
STRAND 170 174 {ECO:0000244|PDB:1CT9}.
STRAND 179 182 {ECO:0000244|PDB:1CT9}.
TURN 183 185 {ECO:0000244|PDB:1CT9}.
STRAND 187 190 {ECO:0000244|PDB:1CT9}.
HELIX 195 197 {ECO:0000244|PDB:1CT9}.
HELIX 199 202 {ECO:0000244|PDB:1CT9}.
HELIX 209 223 {ECO:0000244|PDB:1CT9}.
STRAND 230 233 {ECO:0000244|PDB:1CT9}.
HELIX 238 250 {ECO:0000244|PDB:1CT9}.
STRAND 269 275 {ECO:0000244|PDB:1CT9}.
HELIX 279 291 {ECO:0000244|PDB:1CT9}.
STRAND 294 299 {ECO:0000244|PDB:1CT9}.
HELIX 302 316 {ECO:0000244|PDB:1CT9}.
HELIX 321 339 {ECO:0000244|PDB:1CT9}.
STRAND 344 346 {ECO:0000244|PDB:1CT9}.
HELIX 351 355 {ECO:0000244|PDB:1CT9}.
HELIX 359 363 {ECO:0000244|PDB:1CT9}.
HELIX 367 380 {ECO:0000244|PDB:1CT9}.
HELIX 381 383 {ECO:0000244|PDB:1CT9}.
HELIX 385 394 {ECO:0000244|PDB:1CT9}.
TURN 395 397 {ECO:0000244|PDB:1CT9}.
STRAND 399 401 {ECO:0000244|PDB:1CT9}.
HELIX 403 405 {ECO:0000244|PDB:1CT9}.
HELIX 407 415 {ECO:0000244|PDB:1CT9}.
HELIX 418 420 {ECO:0000244|PDB:1CT9}.
HELIX 431 437 {ECO:0000244|PDB:1CT9}.
HELIX 438 440 {ECO:0000244|PDB:1CT9}.
HELIX 443 446 {ECO:0000244|PDB:1CT9}.
HELIX 460 472 {ECO:0000244|PDB:1CT9}.
HELIX 475 479 {ECO:0000244|PDB:1CT9}.
HELIX 481 484 {ECO:0000244|PDB:1CT9}.
HELIX 493 505 {ECO:0000244|PDB:1CT9}.
HELIX 509 514 {ECO:0000244|PDB:1CT9}.
SEQUENCE 554 AA; 62659 MW; 9091B269112C9F5C CRC64;
MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER LSIVDVNAGA
QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG
MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY
LWSQDGEIRS YYHRDWFDYD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS
SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY
FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD
KMCGNGKMEK HILRECFEAY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET
ARFRFPYNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD
PSGRAVGVHQ SAYK


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