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Conserved domains on  [gi|9506739|ref|NP_062415|]
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N-acetyl-D-glucosamine kinase isoform 1 [Mus musculus]

Protein Classification

N-acetylglucosamine kinase( domain architecture ID 1903937)

N-acetylglucosamine kinase of eukaryotic type similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
4-322 0e+00

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.


:

Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 538.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078   1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   84 VRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQA 163
Cdd:cd24078  81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAYWIAHRA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  164 VKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLG 243
Cdd:cd24078 161 IKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKSKIAGFCKKLAEGAAEGDPLCRHLFREAGEELA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506739  244 RHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgreQQAQNSFSSFTLMKLRHSSALGGASLGARH 322
Cdd:cd24078 241 RHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL-----KQRSDKIKKLSLVRLKESSALGAARLGAKE 314
 
Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
4-322 0e+00

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 538.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078   1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   84 VRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQA 163
Cdd:cd24078  81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAYWIAHRA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  164 VKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLG 243
Cdd:cd24078 161 IKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKSKIAGFCKKLAEGAAEGDPLCRHLFREAGEELA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506739  244 RHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgreQQAQNSFSSFTLMKLRHSSALGGASLGARH 322
Cdd:cd24078 241 RHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL-----KQRSDKIKKLSLVRLKESSALGAARLGAKE 314
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
7-324 2.36e-57

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 187.78  E-value: 2.36e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:COG2971   5 GVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAG--DPADIEAVGFGLAGAGTPEDAEA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   87 LIEELRHRFPNlsENYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVK 165
Cdd:COG2971  83 LEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIAAGRDGDGRTARVGGWGYLLGDEGSGAWLGREALR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  166 IVFDSIDNLEAAphdiGHVKQAMFDYFQVPDRLGILTHLYRD-FDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:COG2971 161 AALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPPADLASLAPLVFEAAEAGDPVARAILEEAADELAE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  245 HVVAVLPEIDPvlfqgelglPILCVGSVWKSWELLKEGFLLALTLGReqqaqnsfssFTLMKLRHSSALGGASLGARHIG 324
Cdd:COG2971 237 LARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAGG----------AEIVPPAGDPVDGALLLALRLLG 297
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-281 2.57e-12

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 66.22  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739      7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPlVPLRSLGLSLSG-GEQEDAVR 85
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEAGLKL-DDIEYMFLGLTGyGRAGVDGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739     86 LLIEELRHRFpnlsenyLITTDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAV 164
Cdd:pfam01869  81 FGKDIVREEI-------TVHADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    165 KIVFDSIDNLeaAPHdighvkqamfdyfqvpdrlgilTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:pfam01869 153 GAVVRELDGL--APK----------------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIAL 208
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 9506739    245 HVVAVLPEIdpvlfqGELGLPILCVGSVWKSWELLKE 281
Cdd:pfam01869 209 RVAALAKRL------GFVPDEVVLTGGVAKNAGLVKA 239
 
Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
4-322 0e+00

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 538.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078   1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   84 VRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQA 163
Cdd:cd24078  81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAYWIAHRA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  164 VKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLG 243
Cdd:cd24078 161 IKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKSKIAGFCKKLAEGAAEGDPLCRHLFREAGEELA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506739  244 RHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgreQQAQNSFSSFTLMKLRHSSALGGASLGARH 322
Cdd:cd24078 241 RHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL-----KQRSDKIKKLSLVRLKESSALGAARLGAKE 314
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
7-318 7.05e-71

nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466857 [Multi-domain]  Cd Length: 295  Bit Score: 222.57  E-value: 7.05e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:cd24007   3 GVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAG--SLGEIDAICLGLAGIDSEEDRER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   87 LIEELRHRFPnlSENYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVK 165
Cdd:cd24007  81 LRSALKELFL--SGRIIIVNDAEIALAAALGGGpGIVVIAGTGSVAYGRNGDGEEARVGGWGHLLGDEGSGYWIGRRALR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  166 IVFDSIDNLEaaPHDIghVKQAMFDYFQVPDRLGILTHLYR-DFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:cd24007 159 AALRALDGRG--PKTP--LLDAILKFLGLDSIEELITAIYRsSDRKKEIASLAPLVFEAAEEGDPVAQAILKEAAEELAK 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506739  245 HVVAVLpeidpVLFQGELGLPILCVGSVWKSWELLKEGFLLALTLGREqqaqnsfsSFTLMKLRHSSALGGASL 318
Cdd:cd24007 235 LVVALA-----KLLLLGEKLPLALSGGVFKNNYYLAEFLEELLKKKKP--------NAKVVEPKGSPVVGALLL 295
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
7-324 2.36e-57

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 187.78  E-value: 2.36e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:COG2971   5 GVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAG--DPADIEAVGFGLAGAGTPEDAEA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   87 LIEELRHRFPNlsENYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVK 165
Cdd:COG2971  83 LEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIAAGRDGDGRTARVGGWGYLLGDEGSGAWLGREALR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  166 IVFDSIDNLEAAphdiGHVKQAMFDYFQVPDRLGILTHLYRD-FDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:COG2971 161 AALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPPADLASLAPLVFEAAEAGDPVARAILEEAADELAE 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  245 HVVAVLPEIDPvlfqgelglPILCVGSVWKSWELLKEGFLLALTLGReqqaqnsfssFTLMKLRHSSALGGASLGARHIG 324
Cdd:COG2971 237 LARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAGG----------AEIVPPAGDPVDGALLLALRLLG 297
ASKHA_NBD_MurK-like cd24084
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ...
7-318 1.49e-39

nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK) and similar proteins; The family includes a group of uncharacterized proteins similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK; EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase. It catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. MurK may have a role in the rescue of the murein sugars GlcNAc and MurNAc released from muropeptides during cell wall turnover in C.acetobutylicum.


Pssm-ID: 466934 [Multi-domain]  Cd Length: 302  Bit Score: 141.73  E-value: 1.49e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPlVPLRSLGLSLSGGEQEDAVRL 86
Cdd:cd24084   5 GIDGGGTKTHLKITDLNGNVVGEGFGGSSNLESNSLETVRENLKELFQDFYEQLGKSL-KECGSICLGTAGASHQGAKET 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   87 LIEELRHRFPNLSenYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVK 165
Cdd:cd24084  84 LKDILTELGPDAK--IEVVNDAEIALAAGLEGKpGIVLISGTGSICYGRNTDGETARAGGWGHLLGDEGSGYWIAMQALG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  166 IVFDSIDNleAAPHDIghVKQAMFDYFQVPDRLGILTHLYR-DFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:cd24084 162 AVLQAFDG--RGPKTI--LTELLLEELKLSSPRELIDFIYSsDADKKEIASLARLVDEAADQGDEVAKEILEEAARELAR 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506739  245 HVVAVLPEidpvLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgrEQQAQNSfssfTLMKLRHSSALGGASL 318
Cdd:cd24084 238 LAIAVAQK----LLMKPKDFVVILGGSVLENCCVLRSKLSALI----LTKYPNA----IVGLLKHDAAYGAVKL 299
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
7-287 5.34e-28

nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and similar proteins; The family includes a group of uncharacterized proteins similar to Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK). Hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of glucose to glucose 6-phosphate by using ATP as a phosphoryl donor. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. It differs from other known hexokinases and glucokinases in that its activity is strongly inhibited by ADP. It is distinct in its broad substrate specificity from the GlcNAc kinases, which are specific for GlcNAc.


Pssm-ID: 466930 [Multi-domain]  Cd Length: 291  Bit Score: 110.59  E-value: 5.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVP-LRSLGLSLSGGEQEDAVR 85
Cdd:cd24080   5 GVDGGGTKTEAVAYDCKGRFLGYGLAGPGNIHNVGLESAIENVKEAVKRALKGGRADVAVLgFAGADSKKDWEKFTELLS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   86 LLIeelrhrfpnlSENYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAV 164
Cdd:cd24080  85 KII----------AKKVIVQHDGEIALIAETRGSpGVMVIAGTGSIVEGYDGRGRVVRVGGWGWLLGDEGSGYWIGREAL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  165 KIVFDSIDNLEaaPHDIghVKQAMFDYFQVPDRLGILTHLYRDFDKC-KFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLG 243
Cdd:cd24080 155 RALLRMLDGRE--NKTI--LAEKVLKTLNVEDFDELVEWIYSSLCPVdLIASLAKAVDEAAEEGDTVARDILKRAAEELA 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 9506739  244 RHVVAVLPEIDPVLfqgelglpILCVGSVWKSwELLKEGFLLAL 287
Cdd:cd24080 231 SAAVALARKIGPVK--------VYLKGGMFNS-KIFHKFFTRYL 265
ASKHA_NBD_GspK-like cd24082
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ...
7-244 1.64e-27

nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.


Pssm-ID: 466932 [Multi-domain]  Cd Length: 279  Bit Score: 108.77  E-value: 1.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLiGTDQCVERINEMVDRAKQKAGVDPLVPLR-SLGLSLSGGEQEDAVR 85
Cdd:cd24082   4 GIDGGGTKCRARLADADGTVLGEATGGPANLSS-DLDQAWASILAAIKQALAQAGLDAAALSDlHAGLGLAGANVPEARA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   86 LLIEELrHRFPNLsenyLITTDAAGSIATATpDG--GIVLISGTGSNC-RLINpdGSESGCGGWGHMMGDEGSAYWIAHQ 162
Cdd:cd24082  83 AFLAAL-PPFASL----VVVSDAHIACLGAH-GGedGAIIILGTGSVGaALDG--GEVRQVGGWGFPLGDEGSGAWLGLR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  163 AVKIVFDSIDNLeaAPHDIGHvkQAMFDYFQVpDRLGILtHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEML 242
Cdd:cd24082 155 ALRHTLLALDGL--APSSPLT--RAVLARFGG-DPAEIV-AWANTATPADFAALAPLVFEAAEQGDPVALAILQEAAAYI 228

                ..
gi 9506739  243 GR 244
Cdd:cd24082 229 ER 230
ASKHA_NBD_DdNAGK-like cd24081
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ...
7-281 1.77e-27

nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; The family includes a group of uncharacterized proteins similar to Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK). NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, into GlcNAc 6-phosphate. It also has ManNAc kinase activity.


Pssm-ID: 466931 [Multi-domain]  Cd Length: 311  Bit Score: 109.33  E-value: 1.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLS-----EDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVdPLVPLRSLGLSLSGGEQE 81
Cdd:cd24081   3 GIDGGGTKTTCVAVDaatlgDNLLVLGRAVAGSSNYNSVGEEAARRAIEEAIAGALKQAGV-PRSAVRAVCLGISGVDRP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   82 DAVRLLIEELRHRFPnLSENYLITTDAAGSIATATpDG---GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYW 158
Cdd:cd24081  82 ADAERVRSWLRELFP-ENVKVFVFNDAVAALASGT-AGklhGCVLIAGTGTIAYGFNEDGKRARAGGWGPLLGDRGSGHA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  159 IAHQAVKIVFDSIDnlEAAPHDIGHvkQAMFDYFQV--PDRLgiLTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFR 236
Cdd:cd24081 160 IGSQALTAVMRAED--GRGPPTSLT--GAILKKLGLssPDDL--IGWAYDDTSWARVAALVPLVKACAAAGDAVALGILE 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 9506739  237 KAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWK---SWELLKE 281
Cdd:cd24081 234 DAAEELALSVKAVVRKLGLRGTDGSESFPLVLVGGVLErngGLDLFKE 281
ASKHA_NBD_KdgK-like cd24083
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
7-283 7.78e-23

nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and similar proteins; The family includes a group of uncharacterized proteins similar to Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK; EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase. It catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG.


Pssm-ID: 466933 [Multi-domain]  Cd Length: 284  Bit Score: 96.30  E-value: 7.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    7 GVEGGGTRSKVLLLSED-GQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPlVPLRSLGLSLSGGEQEDAVR 85
Cdd:cd24083   3 GVDGGGTKTLAVLFDERqGEIVGIGISGPSNFTVVGRETARKNISDAINDALSDAGMDS-IDKATFGLAGIGDSYEATIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   86 llIEELRHRFPnlsENYLITTDAAGSIATATPDG-GIVLISGTGSNCrLINPDGSESGCGGWGHMMGDEGSAYWIAHQAV 164
Cdd:cd24083  82 --GEEIIRSGL---KKFDIYNDGEAAYYSGNGDDdGIVFAPGTGSVG-YIKDEGRVNRIGGWGWSLGDEGSAFWIAKQAI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  165 KIVFDSIDNLEaaphDIGHVKQAMFDYFQVPDRLGILTHLYRdFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:cd24083 156 EAAMREMDGRE----EWTSLVVEVEKEFKLSLRELVINISYE-GIKRLVASLAKLVSQLAEKGDPVALAIFDEAASEIKK 230
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 9506739  245 HVVAVLPEIDPvlfqgelGLPILCVGSVWKSWELLKEGF 283
Cdd:cd24083 231 IINAHRLNFGP-------PIRVSLVGGVMQSGPIYLEKF 262
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-281 2.57e-12

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 66.22  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739      7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPlVPLRSLGLSLSG-GEQEDAVR 85
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEAGLKL-DDIEYMFLGLTGyGRAGVDGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739     86 LLIEELRHRFpnlsenyLITTDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAV 164
Cdd:pfam01869  81 FGKDIVREEI-------TVHADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    165 KIVFDSIDNLeaAPHdighvkqamfdyfqvpdrlgilTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 244
Cdd:pfam01869 153 GAVVRELDGL--APK----------------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIAL 208
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 9506739    245 HVVAVLPEIdpvlfqGELGLPILCVGSVWKSWELLKE 281
Cdd:pfam01869 209 RVAALAKRL------GFVPDEVVLTGGVAKNAGLVKA 239
ASKHA_NBD_PG1100-like cd24079
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ...
8-272 3.50e-12

nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100) and similar proteins; The family includes a group of uncharacterized proteins similar to Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100; EC 2.7.1.59), which may convert GlcNAc to GlcNAc-6-phosphate, a component utilized in UDP-GlcNAc biosynthesis or energy metabolism.


Pssm-ID: 466929 [Multi-domain]  Cd Length: 276  Bit Score: 65.69  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739    8 VEGGGTRSKVLLLSEDGQILaEADGLSTNHWLIGTDQCVERINEMVDRAKQKAGVDPLVplrslgLSLSGGEQEDAVRLL 87
Cdd:cd24079   4 ADSGGTKTDWALVDGGGVIK-QFTTKGLNPFFLSDEEIEQILALVLLPLLEESKIEEVY------FYGAGCGSPERAARI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739   88 IEELRHRFPNlsENYLITTDAAGSI-ATATPDGGIVLISGTGSNCRLInpDGSE--SGCGGWGHMMGDEGSAYWIAHQAV 164
Cdd:cd24079  77 KRLLKKVFPK--AEIEVKSDLLGAArALCGDKKGIVCILGTGSNSCYY--DGEKihDQRPGLGYLLGDEGSGAYLGKLLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506739  165 KivfdsiDNLEA-APHDIghvKQAMFDYFQVpDRLGILTHLYRDFDKCKF-AGFCQKIAEgaHQGDPLSRYIFRKA-GEM 241
Cdd:cd24079 153 R------DYLYGqLPEEL---RKRFEEQFGL-NKEEILSRVYRSPDPNRYlASLSRFIAE--HLEHPYIRELIRESfREF 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 9506739  242 LGRHVVAvlpeidpvlFQGELGLPILCVGSV 272
Cdd:cd24079 221 FETHVLP---------YPDYKTLPIHFVGSV 242
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
1-77 2.25e-04

Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];


Pssm-ID: 441543 [Multi-domain]  Cd Length: 306  Bit Score: 42.58  E-value: 2.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506739    1 MAALYGGVEGGGTRSKVLLLSEDGQILAEADgLSTNHWLiGTDQCVERINEMVDRAKQKAGVDPlVPLRSLGLSLSG 77
Cdd:COG1940   3 DAGYVIGIDIGGTKIKAALVDLDGEVLARER-IPTPAGA-GPEAVLEAIAELIEELLAEAGISR-GRILGIGIGVPG 76
 
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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