| Tag | Content |
|---|
| CPLM ID | CPLM-013302 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing) |
Protein Synonyms/Alias | ATP-dependent dihydroxyacetone kinase; DHA kinase; Glycerone kinase; Triokinase; Triose kinase; FAD-AMP lyase (cyclizing); FAD-AMP lyase (cyclic FMN forming); FMN cyclase |
Gene Name | Dak |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 46 | RSDLDSLKGRVALLS | acetylation | [1] | | 179 | MGLEEITKKVSVIAK | acetylation | [1] | | 341 | KAWPHMSKVSVTGRN | acetylation | [1] | | 413 | STHSRAAKAIQGWLK | acetylation | [1] | | 420 | KAIQGWLKEGPTPAS | acetylation | [1] | | 522 | SLLPVLTKAVKSAEA | acetylation | [1] | | 525 | PVLTKAVKSAEAAAE | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. |
Sequence Annotation | DOMAIN 9 336 DhaK.
DOMAIN 372 571 DhaL.
NP_BIND 401 404 ATP (By similarity).
NP_BIND 446 447 ATP (By similarity).
NP_BIND 494 495 ATP (By similarity).
NP_BIND 556 558 ATP (By similarity).
REGION 56 59 Dihydroxyacetone binding (By similarity).
ACT_SITE 221 221 Tele-hemiaminal-histidine intermediate
BINDING 109 109 Dihydroxyacetone (By similarity).
BINDING 114 114 Dihydroxyacetone (By similarity).
BINDING 486 486 ATP; via carbonyl oxygen (By similarity). |
Keyword | ATP-binding; Cobalt; Complete proteome; FAD; Kinase; Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 578 AA |
Protein Sequence | MSSKKMVNSV EGCAGDALAG FVACNPDLQL LQGYRVALRS DLDSLKGRVA LLSGGGSGHE 60
PAHAGFIGKG MLTGVIAGAV FASPAVGSIL AAIRAVAQAG TAGTLLIVKN YTGDRLNFGL 120
AMEQAKAEGI SVEMVVIEDD SAFTVLKKAG RRGLCGTILI HKVAGALAEE GMGLEEITKK 180
VSVIAKAIGT LGVSLSPCSV PGTKPTFELA ADEMELGLGI HGEAGVRRIK LVPVDQIVTL 240
MLDHMTDTSN ISHVPVKSGS SVVLMVNNLG GLSFLELGII ADAAIRLLEG RGVKVARALV 300
GTFMSALEMR GVSLTLMLVD EPLLKLIDAE TNAKAWPHMS KVSVTGRNRI RAAPTEPAEA 360
PEATAAGGVA SKQMTLVLDR ISTTLIGLEE HLNALDRAAG DGDCGSTHSR AAKAIQGWLK 420
EGPTPASPAQ VLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKANTDLPA WSAAMDAGLK 480
AMQKYGKAAP GDRTMLDSLW AAAQELQAWK SPGASLLPVL TKAVKSAEAA AEATKNMEAG 540
AGRASYISSA QLDQPDPGAV AAAAIFRAIL EVLQTKAA 578 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IEA:EC. GO:0004371; F:glycerone kinase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0050354; F:triokinase activity; IEA:EC. GO:0006071; P:glycerol metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |