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Conserved domains on  [gi|1958768880|ref|XP_038963274|]
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N-acetyl-D-glucosamine kinase isoform X3 [Rattus norvegicus]

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_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
4-157 6.54e-92

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24078:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 314  Bit Score: 270.22  E-value: 6.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078     1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768880  84 VRLLMEELRDRFPYLSESYFITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24078    81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAY 154
 
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; ...
4-157 6.54e-92

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: 270.22  E-value: 6.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078     1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768880  84 VRLLMEELRDRFPYLSESYFITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24078    81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAY 154
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
7-155 2.12e-32

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 117.29  E-value: 2.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:COG2971     5 GVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAG--DPADIEAVGFGLAGAGTPEDAEA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880  87 LMEELRDRFPYlsESYFITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:COG2971    83 LEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIAAGRDGDGRTARVGGWGYLLGDEGS 150
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-155 3.45e-09

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: 54.28  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPlVPLRSLGLSLSG-GEQEDAVR 85
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEAGLKL-DDIEYMFLGLTGyGRAGVDGH 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958768880  86 LLMEELRdrfpylsESYFITTDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:pfam01869  81 FGKDIVR-------EEITVHADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGS 143
 
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; ...
4-157 6.54e-92

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: 270.22  E-value: 6.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   4 LYGGVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPLVPLRSLGLSLSGGEQEDA 83
Cdd:cd24078     1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768880  84 VRLLMEELRDRFPYLSESYFITTDAAGSIATATPDGGIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24078    81 QEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNCQLINPDGSTAGCGGWGHMLGDEGSAY 154
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
7-155 3.04e-36

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: 127.42  E-value: 3.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:cd24007     3 GVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAG--SLGEIDAICLGLAGIDSEEDRER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880  87 LMEELRDRFPylSESYFITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:cd24007    81 LRSALKELFL--SGRIIIVNDAEIALAAALGGGpGIVVIAGTGSVAYGRNGDGEEARVGGWGHLLGDEGS 148
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
7-155 2.12e-32

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 117.29  E-value: 2.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGvdPLVPLRSLGLSLSGGEQEDAVRL 86
Cdd:COG2971     5 GVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAAAG--DPADIEAVGFGLAGAGTPEDAEA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880  87 LMEELRDRFPYlsESYFITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:COG2971    83 LEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIAAGRDGDGRTARVGGWGYLLGDEGS 150
ASKHA_NBD_MurK-like cd24084
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ...
7-157 1.73e-19

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: 83.18  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPlVPLRSLGLSLSGGEQEDAVRL 86
Cdd:cd24084     5 GIDGGGTKTHLKITDLNGNVVGEGFGGSSNLESNSLETVRENLKELFQDFYEQLGKSL-KECGSICLGTAGASHQGAKET 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958768880  87 LMEELRDRFPYLSesYFITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24084    84 LKDILTELGPDAK--IEVVNDAEIALAAGLEGKpGIVLISGTGSICYGRNTDGETARAGGWGHLLGDEGSGY 153
ASKHA_NBD_DdNAGK-like cd24081
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ...
7-155 1.00e-18

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: 81.21  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLS-----EDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVdPLVPLRSLGLSLSGGEQE 81
Cdd:cd24081     3 GIDGGGTKTTCVAVDaatlgDNLLVLGRAVAGSSNYNSVGEEAARRAIEEAIAGALKQAGV-PRSAVRAVCLGISGVDRP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958768880  82 DAVRLLMEELRDRFPyLSESYFITTDAAGSIATATpDG---GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:cd24081    82 ADAERVRSWLRELFP-ENVKVFVFNDAVAALASGT-AGklhGCVLIAGTGTIAYGFNEDGKRARAGGWGPLLGDRGS 156
ASKHA_NBD_GspK-like cd24082
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ...
7-155 2.84e-16

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: 74.10  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNhwlIGTG--TCVERINEMVDRAKRKAGVDPLVPLR-SLGLSLSGGEQEDA 83
Cdd:cd24082     4 GIDGGGTKCRARLADADGTVLGEATGGPAN---LSSDldQAWASILAAIKQALAQAGLDAAALSDlHAGLGLAGANVPEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958768880  84 VrllmEELRDRFPYLSeSYFITTDAAGSIATATpDG--GIVLISGTGSNC-RLINpdGSESGCGGWGHMMGDEGS 155
Cdd:cd24082    81 R----AAFLAALPPFA-SLVVVSDAHIACLGAH-GGedGAIIILGTGSVGaALDG--GEVRQVGGWGFPLGDEGS 147
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
7-157 5.61e-14

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: 68.22  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPLVplrslgLSLSGGEQEDAVRL 86
Cdd:cd24080     5 GVDGGGTKTEAVAYDCKGRFLGYGLAGPGNIHNVGLESAIENVKEAVKRALKGGRADVAV------LGFAGADSKKDWEK 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958768880  87 LMEELRDrfpYLSESYFITTDAAGSIATATPDG-GIVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24080    79 FTELLSK---IIAKKVIVQHDGEIALIAETRGSpGVMVIAGTGSIVEGYDGRGRVVRVGGWGWLLGDEGSGY 147
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
7-155 3.45e-09

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: 54.28  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSEDGQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPlVPLRSLGLSLSG-GEQEDAVR 85
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEAGLKL-DDIEYMFLGLTGyGRAGVDGH 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958768880  86 LLMEELRdrfpylsESYFITTDAAGSIATAT-PDGGIVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGS 155
Cdd:pfam01869  81 FGKDIVR-------EEITVHADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGS 143
ASKHA_NBD_KdgK-like cd24083
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
7-157 9.51e-09

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: 53.16  E-value: 9.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880   7 GVEGGGTRSKVLLLSED-GQILAEADGLSTNHWLIGTGTCVERINEMVDRAKRKAGVDPLvplRSLGLSLSG-GEQEDAV 84
Cdd:cd24083     3 GVDGGGTKTLAVLFDERqGEIVGIGISGPSNFTVVGRETARKNISDAINDALSDAGMDSI---DKATFGLAGiGDSYEAT 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958768880  85 RLLMEELRDRFPYLSesyfITTDAAGSIATATPDG-GIVLISGTGSNCrLINPDGSESGCGGWGHMMGDEGSVF 157
Cdd:cd24083    80 IMGEEIIRSGLKKFD----IYNDGEAAYYSGNGDDdGIVFAPGTGSVG-YIKDEGRVNRIGGWGWSLGDEGSAF 148
ASKHA_NBD_PG1100-like cd24079
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ...
76-155 9.61e-07

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: 47.59  E-value: 9.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958768880  76 SGGEQEDAVRLLMEELRDRFPylSESYFITTDAAGSI-ATATPDGGIVLISGTGSNCRLInpDGSE--SGCGGWGHMMGD 152
Cdd:cd24079    65 AGCGSPERAARIKRLLKKVFP--KAEIEVKSDLLGAArALCGDKKGIVCILGTGSNSCYY--DGEKihDQRPGLGYLLGD 140

                  ...
gi 1958768880 153 EGS 155
Cdd:cd24079   141 EGS 143
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
1-77 3.24e-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: 39.88  E-value: 3.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958768880   1 MAALYGGVEGGGTRSKVLLLSEDGQILAEADgLSTNHWLiGTGTCVERINEMVDRAKRKAGVDPlVPLRSLGLSLSG 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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