| Tag | Content |
|---|
| CPLM ID | CPLM-004001 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Adenylosuccinate lyase |
Protein Synonyms/Alias | ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor |
Gene Name | purB |
Gene Synonyms/Alias | purE; BSU06440 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 162 | ALWHEEMKRNLERFK | acetylation | [1] |
|
Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Influences the affinity of glutamyl--tRNA ligase for its substrates and increases its thermostability. |
Sequence Annotation | REGION 4 5 Substrate binding (By similarity).
REGION 67 69 Substrate binding (By similarity).
REGION 93 94 Substrate binding (By similarity).
REGION 268 270 Substrate binding (By similarity).
ACT_SITE 141 141 Proton donor/acceptor (By similarity).
ACT_SITE 262 262 Proton donor/acceptor (By similarity).
BINDING 212 212 Substrate (By similarity).
BINDING 276 276 Substrate (By similarity).
BINDING 301 301 Substrate (By similarity).
BINDING 306 306 Substrate (By similarity). |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Lyase; Purine biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 431 AA |
Protein Sequence | MIERYSRPEM SAIWTDENRF QAWLEVEILA CEAWAELGVI PKEDVKVMRE NASFDINRIL 60
EIEKDTRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT ALSYLLKQAN DILLKDLERF 120
VDIIKEKAKE HKYTVMMGRT HGVHAEPTTF GLKLALWHEE MKRNLERFKQ AKAGIEVGKI 180
SGAVGTYANI DPFVEQYVCE KLGLKAAPIS TQTLQRDRHA DYMATLALIA TSIEKFAVEI 240
RGLQKSETRE VEEFFAKGQK GSSAMPHKRN PIGSENMTGM ARVIRGYMMT AYENVPLWHE 300
RDISHSSAER IILPDATIAL NYMLNRFSNI VKNLTVFPEN MKRNMDRTLG LIYSQRVLLA 360
LIDTGLTREE AYDTVQPKAM EAWEKQVPFR ELVEAEEKIT SRLSPEKIAD CFDYNYHLKN 420
VDLIFERLGL A 431 |
Gene Ontology | GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:EC. GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:MGI. GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. GO:0006167; P:AMP biosynthetic process; IDA:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |