Tag | Content |
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CPLM ID | CPLM-006075 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutamate 5-kinase |
Protein Synonyms/Alias | GK; Gamma-glutamyl kinase |
Gene Name | PRO1 |
Gene Synonyms/Alias | YDR300C; D9740.12 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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297 | LNVPLHTKFIANDNK | acetylation | [1] |
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Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5- oxoproline. |
Sequence Annotation | DOMAIN 321 412 PUA. NP_BIND 175 176 ATP (By similarity). NP_BIND 219 225 ATP (By similarity). BINDING 56 56 Substrate (By similarity). BINDING 143 143 Substrate (By similarity). BINDING 155 155 Substrate; via amide nitrogen (By |
Keyword | Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 428 AA |
Protein Sequence | MKDANESKSY TIVIKLGSSS LVDEKTKEPK LAIMSLIVET VVKLRRMGHK VIIVSSGGIA 60 VGLRTMRMNK RPKHLAEVQA IAAIGQGRLI GRWDLLFSQF DQRIAQILLT RNDILDWTQY 120 KNAQNTINEL LNMGVIPIVN ENDTLSVREI KFGDNDTLSA ITSALIHADY LFLLTDVDCL 180 YTDNPRTNPD AMPILVVPDL SKGLPGVNTA GGSGSDVGTG GMETKLVAAD LATNAGVHTL 240 IMKSDTPANI GRIVEYMQTL ELDDENKVKQ AYNGDLTDLQ KREFEKLKAL NVPLHTKFIA 300 NDNKHHLKNR EFWILHGLVS KGAVVIDQGA YAALTRKNKA GLLPAGVIDV QGTFHELECV 360 DIKVGKKLPD GTLDPDFPLQ TVGKARCNYT SSELTKIKGL HSDQIEEELG YNDSEYVAHR 420 ENLAFPPR 428 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |