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Conserved domains on  [gi|255958271|ref|NP_001157659|]
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N-acetyl-D-glucosamine kinase isoform 2 [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; ...
1-271 1.57e-163

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: 456.66  E-value: 1.57e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   1 MVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNC 80
Cdd:cd24078   49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078  129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 161 KFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgr 240
Cdd:cd24078  209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL---- 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 255958271 241 eQQAQNSFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078  285 -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; ...
1-271 1.57e-163

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: 456.66  E-value: 1.57e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   1 MVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNC 80
Cdd:cd24078   49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078  129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 161 KFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgr 240
Cdd:cd24078  209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL---- 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 255958271 241 eQQAQNSFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078  285 -KQRSDKIKKLSLVRLKESSALGAARLGAKE 314
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
2-273 6.18e-43

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 148.88  E-value: 6.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   2 VDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNlsENYLITTDAAGSIATATPDG-GIVLISGTGSNC 80
Cdd:COG2971   51 LEEALAAAG--DPADIEAVGFGLAGAGTPEDAEALEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAphdiGHVKQAMFDYFQVPDRLGILTHLYRD-FDK 159
Cdd:COG2971  127 AGRDGDGRTARVGGWGYLLGDEGSGAWLGREALRAALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPP 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 160 CKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPvlfqgelglPILCVGSVWKSWELLKEGFLLALTLG 239
Cdd:COG2971  203 ADLASLAPLVFEAAEAGDPVARAILEEAADELAELARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAG 273
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958271 240 ReqqaqnsfssFTLMKLRHSSALGGASLGARHIG 273
Cdd:COG2971  274 G----------AEIVPPAGDPVDGALLLALRLLG 297
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
55-230 2.42e-05

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: 45.04  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   55 TDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHdighv 133
Cdd:pfam01869  94 ADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELDGL--APK----- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  134 kqamfdyfqvpdrlgilTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIdpvlfqGELGL 213
Cdd:pfam01869 166 -----------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRL------GFVPD 222
                         170
                  ....*....|....*..
gi 255958271  214 PILCVGSVWKSWELLKE 230
Cdd:pfam01869 223 EVVLTGGVAKNAGLVKA 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; ...
1-271 1.57e-163

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: 456.66  E-value: 1.57e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   1 MVDRAKQKAGVDPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNLSENYLITTDAAGSIATATPDGGIVLISGTGSNC 80
Cdd:cd24078   49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGHVKQAMFDYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078  129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 161 KFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWKSWELLKEGFLLALtlgr 240
Cdd:cd24078  209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGL---- 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 255958271 241 eQQAQNSFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078  285 -KQRSDKIKKLSLVRLKESSALGAARLGAKE 314
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
1-267 2.73e-55

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: 180.58  E-value: 2.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   1 MVDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPnlSENYLITTDAAGSIATATPDG-GIVLISGTGSN 79
Cdd:cd24007   48 AVREALSQAG--SLGEIDAICLGLAGIDSEEDRERLRSALKELFL--SGRIIIVNDAEIALAAALGGGpGIVVIAGTGSV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  80 CRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEaaPHDIghVKQAMFDYFQVPDRLGILTHLYR-DFD 158
Cdd:cd24007  124 AYGRNGDGEEARVGGWGHLLGDEGSGYWIGRRALRAALRALDGRG--PKTP--LLDAILKFLGLDSIEELITAIYRsSDR 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 159 KCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLpeidpVLFQGELGLPILCVGSVWKSWELLKEGFLLALTL 238
Cdd:cd24007  200 KKEIASLAPLVFEAAEEGDPVAQAILKEAAEELAKLVVALA-----KLLLLGEKLPLALSGGVFKNNYYLAEFLEELLKK 274
                        250       260
                 ....*....|....*....|....*....
gi 255958271 239 GREqqaqnsfsSFTLMKLRHSSALGGASL 267
Cdd:cd24007  275 KKP--------NAKVVEPKGSPVVGALLL 295
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
2-273 6.18e-43

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 148.88  E-value: 6.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   2 VDRAKQKAGvdPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPNlsENYLITTDAAGSIATATPDG-GIVLISGTGSNC 80
Cdd:COG2971   51 LEEALAAAG--DPADIEAVGFGLAGAGTPEDAEALEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAphdiGHVKQAMFDYFQVPDRLGILTHLYRD-FDK 159
Cdd:COG2971  127 AGRDGDGRTARVGGWGYLLGDEGSGAWLGREALRAALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPP 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 160 CKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPvlfqgelglPILCVGSVWKSWELLKEGFLLALTLG 239
Cdd:COG2971  203 ADLASLAPLVFEAAEAGDPVARAILEEAADELAELARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAG 273
                        250       260       270
                 ....*....|....*....|....*....|....
gi 255958271 240 ReqqaqnsfssFTLMKLRHSSALGGASLGARHIG 273
Cdd:COG2971  274 G----------AEIVPPAGDPVDGALLLALRLLG 297
ASKHA_NBD_MurK-like cd24084
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ...
52-267 4.28e-32

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: 120.54  E-value: 4.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  52 LITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNleAAPHDI 130
Cdd:cd24084   98 EVVNDAEIALAAGLEGKpGIVLISGTGSICYGRNTDGETARAGGWGHLLGDEGSGYWIAMQALGAVLQAFDG--RGPKTI 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 131 ghVKQAMFDYFQVPDRLGILTHLYR-DFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEidpvLFQG 209
Cdd:cd24084  176 --LTELLLEELKLSSPRELIDFIYSsDADKKEIASLARLVDEAADQGDEVAKEILEEAARELARLAIAVAQK----LLMK 249
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255958271 210 ELGLPILCVGSVWKSWELLKEGFLLALtlgrEQQAQNSfssfTLMKLRHSSALGGASL 267
Cdd:cd24084  250 PKDFVVILGGSVLENCCVLRSKLSALI----LTKYPNA----IVGLLKHDAAYGAVKL 299
ASKHA_NBD_DdNAGK-like cd24081
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ...
2-230 2.85e-21

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: 91.22  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   2 VDRAKQKAGVdPLVPLRSLGLSLSGGEQEDAVRLLIEELRHRFPnLSENYLITTDAAGSIATATpDG---GIVLISGTGS 78
Cdd:cd24081   54 IAGALKQAGV-PRSAVRAVCLGISGVDRPADAERVRSWLRELFP-ENVKVFVFNDAVAALASGT-AGklhGCVLIAGTGT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  79 NCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDnlEAAPHDIGHvkQAMFDYFQV--PDRLgiLTHLYRD 156
Cdd:cd24081  131 IAYGFNEDGKRARAGGWGPLLGDRGSGHAIGSQALTAVMRAED--GRGPPTSLT--GAILKKLGLssPDDL--IGWAYDD 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255958271 157 FDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLFQGELGLPILCVGSVWK---SWELLKE 230
Cdd:cd24081  205 TSWARVAALVPLVKACAAAGDAVALGILEDAAEELALSVKAVVRKLGLRGTDGSESFPLVLVGGVLErngGLDLFKE 281
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
50-236 3.09e-20

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: 88.25  E-value: 3.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  50 NYLITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEaaPH 128
Cdd:cd24080   90 KVIVQHDGEIALIAETRGSpGVMVIAGTGSIVEGYDGRGRVVRVGGWGWLLGDEGSGYWIGREALRALLRMLDGRE--NK 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 129 DIghVKQAMFDYFQVPDRLGILTHLYRDFDKC-KFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPVLf 207
Cdd:cd24080  168 TI--LAEKVLKTLNVEDFDELVEWIYSSLCPVdLIASLAKAVDEAAEEGDTVARDILKRAAEELASAAVALARKIGPVK- 244
                        170       180
                 ....*....|....*....|....*....
gi 255958271 208 qgelglpILCVGSVWKSwELLKEGFLLAL 236
Cdd:cd24080  245 -------VYLKGGMFNS-KIFHKFFTRYL 265
ASKHA_NBD_KdgK-like cd24083
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
48-232 2.33e-19

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: 85.52  E-value: 2.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  48 SENYLITTDAAGSIATATPDG-GIVLISGTGSNCrLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEaa 126
Cdd:cd24083   90 LKKFDIYNDGEAAYYSGNGDDdGIVFAPGTGSVG-YIKDEGRVNRIGGWGWSLGDEGSAFWIAKQAIEAAMREMDGRE-- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 127 phDIGHVKQAMFDYFQVPDRLGILTHLYRdFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDPvl 206
Cdd:cd24083  167 --EWTSLVVEVEKEFKLSLRELVINISYE-GIKRLVASLAKLVSQLAEKGDPVALAIFDEAASEIKKIINAHRLNFGP-- 241
                        170       180
                 ....*....|....*....|....*.
gi 255958271 207 fqgelGLPILCVGSVWKSWELLKEGF 232
Cdd:cd24083  242 -----PIRVSLVGGVMQSGPIYLEKF 262
ASKHA_NBD_GspK-like cd24082
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ...
2-193 9.25e-17

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: 78.34  E-value: 9.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   2 VDRAKQKAGVDPLVPLR-SLGLSLSGGEQEDAVRLLIEELrHRFPNLsenyLITTDAAGSIATATpDG--GIVLISGTGS 78
Cdd:cd24082   49 IKQALAQAGLDAAALSDlHAGLGLAGANVPEARAAFLAAL-PPFASL----VVVSDAHIACLGAH-GGedGAIIILGTGS 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  79 NC-RLINpdGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHDIGHvkQAMFDYFQVpDRLGILtHLYRDF 157
Cdd:cd24082  123 VGaALDG--GEVRQVGGWGFPLGDEGSGAWLGLRALRHTLLALDGL--APSSPLT--RAVLARFGG-DPAEIV-AWANTA 194
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 255958271 158 DKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGR 193
Cdd:cd24082  195 TPADFAALAPLVFEAAEQGDPVALAILQEAAAYIER 230
ASKHA_NBD_PG1100-like cd24079
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ...
25-221 3.86e-11

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: 62.23  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  25 SGGEQEDAVRLLIEELRHRFPNlsENYLITTDAAGSI-ATATPDGGIVLISGTGSNCRLInpDGSE--SGCGGWGHMMGD 101
Cdd:cd24079   65 AGCGSPERAARIKRLLKKVFPK--AEIEVKSDLLGAArALCGDKKGIVCILGTGSNSCYY--DGEKihDQRPGLGYLLGD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271 102 EGSAYWIAHQAVKivfdsiDNLEA-APHDIghvKQAMFDYFQVpDRLGILTHLYRDFDKCKF-AGFCQKIAEgaHQGDPL 179
Cdd:cd24079  141 EGSGAYLGKLLLR------DYLYGqLPEEL---RKRFEEQFGL-NKEEILSRVYRSPDPNRYlASLSRFIAE--HLEHPY 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 255958271 180 SRYIFRKA-GEMLGRHVVAvlpeidpvlFQGELGLPILCVGSV 221
Cdd:cd24079  209 IRELIRESfREFFETHVLP---------YPDYKTLPIHFVGSV 242
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
55-230 2.42e-05

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: 45.04  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271   55 TDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHdighv 133
Cdd:pfam01869  94 ADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELDGL--APK----- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255958271  134 kqamfdyfqvpdrlgilTHLYRDFDKCKFAGFCQKIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIdpvlfqGELGL 213
Cdd:pfam01869 166 -----------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRL------GFVPD 222
                         170
                  ....*....|....*..
gi 255958271  214 PILCVGSVWKSWELLKE 230
Cdd:pfam01869 223 EVVLTGGVAKNAGLVKA 239
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
168-210 6.51e-03

ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; CYANR acts as transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl (CNN) degrading enzymes. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466923 [Multi-domain]  Cd Length: 304  Bit Score: 37.53  E-value: 6.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255958271 168 KIAEGAHQGDPLSRYIFRKAGEMLGRHVVAVLPEIDP--VLFQGE 210
Cdd:cd24073  207 DLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPelIIISGE 251
 
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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