Tag | Content |
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CPLM ID | CPLM-001743 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 6-phosphogluconate dehydrogenase, decarboxylating |
Protein Synonyms/Alias | |
Gene Name | gnd |
Gene Synonyms/Alias | b2029; JW2011 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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38 | IFNRSREKTEEVIAE | acetylation | [1, 2] | 49 | VIAENPGKKLVPYYT | acetylation | [2] | 50 | IAENPGKKLVPYYTV | acetylation | [1, 2] | 58 | LVPYYTVKEFVESLE | acetylation | [1, 2] | 75 | RRILLMVKAGAGTDA | acetylation | [1] | 88 | DAAIDSLKPYLDKGD | acetylation | [2] | 93 | SLKPYLDKGDIIIDG | acetylation | [2] | 136 | GGEEGALKGPSIMPG | acetylation | [2] | 146 | SIMPGGQKEAYELVA | acetylation | [2] | 158 | LVAPILTKIAAVAED | acetylation | [1] | 242 | TKDIFTKKDEDGNYL | acetylation | [2] | 260 | ILDEAANKGTGKWTS | acetylation | [1, 2] | 264 | AANKGTGKWTSQSAL | acetylation | [1, 2] | 301 | DQRVAASKVLSGPQA | acetylation | [1, 2] | 314 | QAQPAGDKAEFIEKV | acetylation | [2] | 320 | DKAEFIEKVRRALYL | acetylation | [1, 2] | 358 | LNYGEIAKIFRAGCI | acetylation | [2] | 454 | YFGAHTYKRIDKEGV | acetylation | [1, 2] | 458 | HTYKRIDKEGVFHTE | acetylation | [2] |
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Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] 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 oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. |
Sequence Annotation | NP_BIND 10 15 NADP. NP_BIND 33 35 NADP. NP_BIND 74 76 NADP. REGION 128 130 Substrate binding. REGION 186 187 Substrate binding (By similarity). ACT_SITE 183 183 Proton acceptor. ACT_SITE 190 190 Proton donor. BINDING 102 102 NADP (By similarity). BINDING 102 102 Substrate. BINDING 191 191 Substrate (By similarity). BINDING 260 260 Substrate; via amide nitrogen. BINDING 287 287 Substrate. BINDING 445 445 Substrate; shared with dimeric partner. BINDING 451 451 Substrate; shared with dimeric partner. |
Keyword | 3D-structure; Complete proteome; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 468 AA |
Protein Sequence | MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF 60 VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF 120 NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH 180 YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT 240 KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS 300 KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF 360 RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT 420 FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD 468 |
Gene Ontology | GO:0050661; F:NADP binding; IEA:InterPro. GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:UniProtKB. GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |