CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005046
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Asparagine synthetase B [glutamine-hydrolyzing] 
Protein Synonyms/Alias
 AS-B 
Gene Name
 asnB 
Gene Synonyms/Alias
 b0674; JW0660 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
68QPLYNQQKTHVLAVNacetylation[1]
173VPVCRTIKEFPAGSYacetylation[1]
203WFDYDAVKDNVTDKNacetylation[1]
209VKDNVTDKNELRQALacetylation[1]
363GGYLYFHKAPNAKELacetylation[1]
493PYNTPTSKEAYLYREacetylation[1]
536IEWDEAFKKMDDPSGacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 2 186 Glutamine amidotransferase type-2.
 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  
Keyword
 3D-structure; Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 554 AA 
Protein Sequence
MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER LSIVDVNAGA 60
QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG 120
MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY 180
LWSQDGEIRS YYHRDWFDYD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS 240
SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF 300
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY 360
FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD 420
KMCGNGKMEK HILRECFEAY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET 480
ARFRFPYNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD 540
PSGRAVGVHQ SAYK 554 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0016597; F:amino acid binding; IDA:UniProtKB.
 GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
 GO:0004071; F:aspartate-ammonia ligase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0006529; P:asparagine biosynthetic process; IDA:UniProtKB.
 GO:0009063; P:cellular amino acid catabolic process; IMP:EcoliWiki.
 GO:0006541; P:glutamine metabolic process; IMP:EcoliWiki.
 GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006426; Asn_synth_AEB.
 IPR001962; Asn_synthase.
 IPR017932; GATase_2_dom.
 IPR000583; GATase_dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00733; Asn_synthase
 PF13537; GATase_7 
SMART
  
PROSITE
 PS51278; GATASE_TYPE_2 
PRINTS