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Conserved domains on  [gi|496082051|ref|WP_008806558|]
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MULTISPECIES: dihydroxyacetone kinase subunit DhaL [Klebsiella]

Protein Classification

dihydroxyacetone kinase subunit L( domain architecture ID 10013397)

dihydroxyacetone kinase subunit L (DhaL) is the ADP-binding subunit of dihydroxyacetone kinase, which catalyzes the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10005 PRK10005
dihydroxyacetone kinase ADP-binding subunit DhaL;
1-210 1.63e-157

dihydroxyacetone kinase ADP-binding subunit DhaL;


:

Pssm-ID: 182192 [Multi-domain]  Cd Length: 210  Bit Score: 433.78  E-value: 1.63e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   1 MSLNRTQIVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGAS 80
Cdd:PRK10005   1 MSLSRTQIVNWLTRCGDIFTEESDYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  81 GPLFGTFFIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACE 160
Cdd:PRK10005  81 GPLYGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPAALNAAVS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082051 161 VAERAAHATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:PRK10005 161 IAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQALALAAKE 210
 
Name Accession Description Interval E-value
PRK10005 PRK10005
dihydroxyacetone kinase ADP-binding subunit DhaL;
1-210 1.63e-157

dihydroxyacetone kinase ADP-binding subunit DhaL;


Pssm-ID: 182192 [Multi-domain]  Cd Length: 210  Bit Score: 433.78  E-value: 1.63e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   1 MSLNRTQIVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGAS 80
Cdd:PRK10005   1 MSLSRTQIVNWLTRCGDIFTEESDYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  81 GPLFGTFFIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACE 160
Cdd:PRK10005  81 GPLYGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPAALNAAVS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082051 161 VAERAAHATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:PRK10005 161 IAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQALALAAKE 210
dha_L_ycgS TIGR02365
dihydroxyacetone kinase, phosphoprotein-dependent, L subunit; Two types of dihydroxyacetone ...
8-205 4.77e-98

dihydroxyacetone kinase, phosphoprotein-dependent, L subunit; Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the subunit homologous to the E. coli YcgS subunit.


Pssm-ID: 274099 [Multi-domain]  Cd Length: 194  Bit Score: 282.70  E-value: 4.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051    8 IVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGASGPLFGTF 87
Cdd:TIGR02365   1 ILNWLKNCGDLIIENKEYLTELDRAIGDGDHGINMARGFSEVKEKLDAFKDKTIGEILKNTGMTLISKVGGASGPLYGTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   88 FIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQhlsiAAALDAACEVAERAAH 167
Cdd:TIGR02365  81 FLKASKALKDDEILDAEDLAEILQAGLEGIQSRGKATPGEKTMVDVWAPVVEALRKAADE----PDALAAAREAAEQGAE 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 496082051  168 ATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLA 205
Cdd:TIGR02365 157 ATKDMQATKGRASYLGERSIGHIDPGATSSYYLFQALA 194
DAK1 COG2376
Dihydroxyacetone kinase [Carbohydrate transport and metabolism]; Dihydroxyacetone kinase is ...
14-210 2.96e-79

Dihydroxyacetone kinase [Carbohydrate transport and metabolism]; Dihydroxyacetone kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441943 [Multi-domain]  Cd Length: 206  Bit Score: 235.48  E-value: 2.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  14 RCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPsIADKDIGFILKNTGMTLLSNVGGASGPLFGTFFIRAAQ 93
Cdd:COG2376    3 AVADVIAENRKFLNDLDAVVGDGDHGINMARGFDAVRAALD-AAPADPGVVLRAAGMKVASVVGGGSGGLVGTGFLDAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  94 VTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACEVAERAAHATITMQ 173
Cdd:COG2376   82 ALKGETSPTADQVAAALRAADEGIQGRGVAYTGDKTNFDAAAPAAEAIEEAVAAGTAAAAALDEAAAAAEKGAEATRSMG 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 496082051 174 ARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:COG2376  162 AALGRATYPGERSPGHPDPGATSVALLLNGLGASLDA 198
Dak2 pfam02734
DAK2 domain; This domain is the predicted phosphatase domain of the dihydroxyacetone kinase ...
33-206 3.96e-64

DAK2 domain; This domain is the predicted phosphatase domain of the dihydroxyacetone kinase family.


Pssm-ID: 460668 [Multi-domain]  Cd Length: 175  Bit Score: 196.25  E-value: 3.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   33 IGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGASGPLFGTFFIRAAQVTQAHQSLTLDELYLMIRE 112
Cdd:pfam02734   2 VGDGDHGTNMARGFEAALKALEDLEPASLAEVLKALAMALLSGAGGNSGPLYGQFFRGAAKALKGKEELDAEDLAAALEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  113 GADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACEVAERAAHATITMQARKGRASYLGERSIGHQDP 192
Cdd:pfam02734  82 ALEAIQARGKARPGDKTMLDVLRPAAEALEAAAEAGEDLAEALEAAVKAAEEGAEATKELLAKLGRASYLGERSIGVVDP 161
                         170
                  ....*....|....
gi 496082051  193 GATSVLFMVQMLAA 206
Cdd:pfam02734 162 GATGLALILEALLE 175
 
Name Accession Description Interval E-value
PRK10005 PRK10005
dihydroxyacetone kinase ADP-binding subunit DhaL;
1-210 1.63e-157

dihydroxyacetone kinase ADP-binding subunit DhaL;


Pssm-ID: 182192 [Multi-domain]  Cd Length: 210  Bit Score: 433.78  E-value: 1.63e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   1 MSLNRTQIVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGAS 80
Cdd:PRK10005   1 MSLSRTQIVNWLTRCGDIFTEESDYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  81 GPLFGTFFIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACE 160
Cdd:PRK10005  81 GPLYGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPAALNAAVS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082051 161 VAERAAHATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:PRK10005 161 IAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQALALAAKE 210
dha_L_ycgS TIGR02365
dihydroxyacetone kinase, phosphoprotein-dependent, L subunit; Two types of dihydroxyacetone ...
8-205 4.77e-98

dihydroxyacetone kinase, phosphoprotein-dependent, L subunit; Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the subunit homologous to the E. coli YcgS subunit.


Pssm-ID: 274099 [Multi-domain]  Cd Length: 194  Bit Score: 282.70  E-value: 4.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051    8 IVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGASGPLFGTF 87
Cdd:TIGR02365   1 ILNWLKNCGDLIIENKEYLTELDRAIGDGDHGINMARGFSEVKEKLDAFKDKTIGEILKNTGMTLISKVGGASGPLYGTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   88 FIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQhlsiAAALDAACEVAERAAH 167
Cdd:TIGR02365  81 FLKASKALKDDEILDAEDLAEILQAGLEGIQSRGKATPGEKTMVDVWAPVVEALRKAADE----PDALAAAREAAEQGAE 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 496082051  168 ATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLA 205
Cdd:TIGR02365 157 ATKDMQATKGRASYLGERSIGHIDPGATSSYYLFQALA 194
DAK1 COG2376
Dihydroxyacetone kinase [Carbohydrate transport and metabolism]; Dihydroxyacetone kinase is ...
14-210 2.96e-79

Dihydroxyacetone kinase [Carbohydrate transport and metabolism]; Dihydroxyacetone kinase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441943 [Multi-domain]  Cd Length: 206  Bit Score: 235.48  E-value: 2.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  14 RCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPsIADKDIGFILKNTGMTLLSNVGGASGPLFGTFFIRAAQ 93
Cdd:COG2376    3 AVADVIAENRKFLNDLDAVVGDGDHGINMARGFDAVRAALD-AAPADPGVVLRAAGMKVASVVGGGSGGLVGTGFLDAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  94 VTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACEVAERAAHATITMQ 173
Cdd:COG2376   82 ALKGETSPTADQVAAALRAADEGIQGRGVAYTGDKTNFDAAAPAAEAIEEAVAAGTAAAAALDEAAAAAEKGAEATRSMG 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 496082051 174 ARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:COG2376  162 AALGRATYPGERSPGHPDPGATSVALLLNGLGASLDA 198
Dak2 pfam02734
DAK2 domain; This domain is the predicted phosphatase domain of the dihydroxyacetone kinase ...
33-206 3.96e-64

DAK2 domain; This domain is the predicted phosphatase domain of the dihydroxyacetone kinase family.


Pssm-ID: 460668 [Multi-domain]  Cd Length: 175  Bit Score: 196.25  E-value: 3.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   33 IGDADHGLNMHRGFSKVVEKLPSIADKDIGFILKNTGMTLLSNVGGASGPLFGTFFIRAAQVTQAHQSLTLDELYLMIRE 112
Cdd:pfam02734   2 VGDGDHGTNMARGFEAALKALEDLEPASLAEVLKALAMALLSGAGGNSGPLYGQFFRGAAKALKGKEELDAEDLAAALEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  113 GADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACEVAERAAHATITMQARKGRASYLGERSIGHQDP 192
Cdd:pfam02734  82 ALEAIQARGKARPGDKTMLDVLRPAAEALEAAAEAGEDLAEALEAAVKAAEEGAEATKELLAKLGRASYLGERSIGVVDP 161
                         170
                  ....*....|....
gi 496082051  193 GATSVLFMVQMLAA 206
Cdd:pfam02734 162 GATGLALILEALLE 175
PRK14479 PRK14479
dihydroxyacetone kinase; Provisional
7-210 1.53e-55

dihydroxyacetone kinase; Provisional


Pssm-ID: 237723 [Multi-domain]  Cd Length: 568  Bit Score: 185.01  E-value: 1.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051   7 QIVDWLYRCGDIFTKESDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIAD--KDIGFILKNTGMTLLSNVGGASGPLF 84
Cdd:PRK14479 363 NLVAALDAVAEALIDNEDELGELDAVAGDGDHGIGMARGSKAALAAARAAVEagAGAGSVLAAAGDAWADHAGGTSGPLW 442
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  85 GTFFIRAAQVTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQSSEQHLSIAAALDAACEVAER 164
Cdd:PRK14479 443 GTALRAAGKALGDKDEPTAADFAAAVRAAVDAIQELGGAQVGDKTMVDALVPFADALEAAAAAGADLAEAWAAAAEAAEE 522
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 496082051 165 AAHATITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLAAAAKE 210
Cdd:PRK14479 523 GAEATADLVPRMGRARYLGERSLGTPDAGAVSLALIFTAIAGSLKD 568
PTZ00375 PTZ00375
dihydroxyacetone kinase-like protein; Provisional
15-205 2.51e-32

dihydroxyacetone kinase-like protein; Provisional


Pssm-ID: 185583 [Multi-domain]  Cd Length: 584  Bit Score: 122.61  E-value: 2.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  15 CGDIFTKEsDFLTGLDKEIGDADHGLNMHRGFSKVVEKLPSIA-DKDIGFILKNTGMTLLSNVGGASGPLFGTFFIRAAQ 93
Cdd:PTZ00375 386 FETLIESE-NYLNELDAEVGDGDLGSGLERSSKAVLESLPYLPlEANVRKTLTLISKAVADAFGGSSGPLYGAFLLGGAN 464
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082051  94 --VTQAHQSLTLDELYLMIREGADGVVNRGKAEPGDKTMCDVWLPVADSLRQ--SSEQHLSIAAALDAACEVAERAAHAT 169
Cdd:PTZ00375 465 alAEALNGGNAVDAVRAALAAGSHSIQELGGARVGDRTMVDVLIPFAEALNScpSVNEAASSPELLKACSEEAREAAEAT 544
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496082051 170 ITMQARKGRASYLGERSIGHQDPGATSVLFMVQMLA 205
Cdd:PTZ00375 545 ALLPAKHGRSRYLEGKELGKKDPGAELVVAWVEALA 580
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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