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Conserved domains on  [gi|126030358|pdb|2E2Q|A]
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Chain A, HEXOKINASE

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_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
 2-289 1.27e-155

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: 436.08  E-value: 1.27e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        2 MIIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG-EADVVGMGVAGLDSKFDWENFT 80
Cdd:cd24080   1 MIILGVDGGGTKTEAVAYDCKGRFLGYGLAGPGNIHNVGLESAIENVKEAVKRALKGgRADVAVLGFAGADSKKDWEKFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       81 P-LASLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNG-KEFLRVGGRGWLLSDDGSAYWVGRKALRKVLKM 158
Cdd:cd24080  81 ElLSKIIAKKVIVQHDGEIALIAETRGSPGVMVIAGTGSIVEGYDGrGRVVRVGGWGWLLGDEGSGYWIGREALRALLRM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      159 MDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVYLARKI 238
Cdd:cd24080 161 LDGRENKTILAEKVLKTLNVEDFDELVEWIYSSLCPVDLIASLAKAVDEAAEEGDTVARDILKRAAEELASAAVALARKI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
2E2Q_A      239 GTNKVYLKGGMFRSNIYHKFFTLYLEKEGIISDLGKRSPEIGAVILAYKEV 289
Cdd:cd24080 241 GPVKVYLKGGMFNSKIFHKFFTRYLEKEGIISSGGKFSPVVGALLLALKEL 291
 
Name Accession Description Interval E-value
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
 2-289 1.27e-155

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: 436.08  E-value: 1.27e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        2 MIIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG-EADVVGMGVAGLDSKFDWENFT 80
Cdd:cd24080   1 MIILGVDGGGTKTEAVAYDCKGRFLGYGLAGPGNIHNVGLESAIENVKEAVKRALKGgRADVAVLGFAGADSKKDWEKFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       81 P-LASLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNG-KEFLRVGGRGWLLSDDGSAYWVGRKALRKVLKM 158
Cdd:cd24080  81 ElLSKIIAKKVIVQHDGEIALIAETRGSPGVMVIAGTGSIVEGYDGrGRVVRVGGWGWLLGDEGSGYWIGREALRALLRM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      159 MDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVYLARKI 238
Cdd:cd24080 161 LDGRENKTILAEKVLKTLNVEDFDELVEWIYSSLCPVDLIASLAKAVDEAAEEGDTVARDILKRAAEELASAAVALARKI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
2E2Q_A      239 GTNKVYLKGGMFRSNIYHKFFTLYLEKEGIISDLGKRSPEIGAVILAYKEV 289
Cdd:cd24080 241 GPVKVYLKGGMFNSKIFHKFFTRYLEKEGIISSGGKFSPVVGALLLALKEL 291
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
 2-291 5.06e-88

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 264.82  E-value: 5.06e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        2 MIIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAK-----GEADVVGMGVAGLDSKFDW 76
Cdd:COG2971   1 PYILGVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAaagdpADIEAVGFGLAGAGTPEDA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       77 ENFTPLASLIAP--KVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGK-EFLRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:COG2971  81 EALEAALRELFPfaRVVVVNDALAALAGALGGEDGIVVIAGTGSIAAGRDGDgRTARVGGWGYLLGDEGSGAWLGREALR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      154 KVLKMMDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:COG2971 161 AALRALDGRGPPTALTEAVLAEFGLDDPEELIAWVYRGPAPPADLASLAPLVFEAAEAGDPVARAILEEAADELAELARA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
2E2Q_A      234 LARKiGTNKVYLKGGMFRSN-IYHKFFTLYLEKEGIISDLGKRSPEIGAVILAYKEVGC 291
Cdd:COG2971 241 LLER-GALPVVLAGGVAAAQpLLREALRARLAAGGAEIVPPAGDPVDGALLLALRLLGA 298
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-285 3.87e-46

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: 156.36  E-value: 3.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A          5 VGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG----EADV-------VGMGVAGLDSK 73
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEaglkLDDIeymflglTGYGRAGVDGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A         74 FDWEnftplasLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGKEFLRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:pfam01869  81 FGKD-------IVREEITVHADGAVALAPGTRGEDGVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        154 KVLKMMDGLENKTILYnkvlktinvkdldELVMWSYtsscqidlVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:pfam01869 154 AVVRELDGLAPKTTLN-------------KGAINST--------CAVFAEQVVINALSGGETAEDILAGAARSIALRVAA 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
2E2Q_A        234 LARKIG--TNKVYLKGGMFRSNIYHKFFTLYLEK-----EGIISDLGKRSPEIGAVILA 285
Cdd:pfam01869 213 LAKRLGfvPDEVVLTGGVAKNAGLVKALRDYLKEnilgvKVNVHPDPQYAGAIGAALLA 271
 
Name Accession Description Interval E-value
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
 2-289 1.27e-155

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: 436.08  E-value: 1.27e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        2 MIIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG-EADVVGMGVAGLDSKFDWENFT 80
Cdd:cd24080   1 MIILGVDGGGTKTEAVAYDCKGRFLGYGLAGPGNIHNVGLESAIENVKEAVKRALKGgRADVAVLGFAGADSKKDWEKFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       81 P-LASLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNG-KEFLRVGGRGWLLSDDGSAYWVGRKALRKVLKM 158
Cdd:cd24080  81 ElLSKIIAKKVIVQHDGEIALIAETRGSPGVMVIAGTGSIVEGYDGrGRVVRVGGWGWLLGDEGSGYWIGREALRALLRM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      159 MDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVYLARKI 238
Cdd:cd24080 161 LDGRENKTILAEKVLKTLNVEDFDELVEWIYSSLCPVDLIASLAKAVDEAAEEGDTVARDILKRAAEELASAAVALARKI 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
2E2Q_A      239 GTNKVYLKGGMFRSNIYHKFFTLYLEKEGIISDLGKRSPEIGAVILAYKEV 289
Cdd:cd24080 241 GPVKVYLKGGMFNSKIFHKFFTRYLEKEGIISSGGKFSPVVGALLLALKEL 291
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
 4-284 3.91e-91

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: 272.64  E-value: 3.91e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAK-----GEADVVGMGVAGLDSKFDWEN 78
Cdd:cd24007   1 VLGVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSqagslGEIDAICLGLAGIDSEEDRER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       79 FTPL--ASLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGK-EFLRVGGRGWLLSDDGSAYWVGRKALRKV 155
Cdd:cd24007  81 LRSAlkELFLSGRIIIVNDAEIALAAALGGGPGIVVIAGTGSVAYGRNGDgEEARVGGWGHLLGDEGSGYWIGRRALRAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      156 LKMMDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVYLA 235
Cdd:cd24007 161 LRALDGRGPKTPLLDAILKFLGLDSIEELITAIYRSSDRKKEIASLAPLVFEAAEEGDPVAQAILKEAAEELAKLVVALA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
2E2Q_A      236 R---KIGTNKVYLKGGMFRSNIYHKFFTLYLEKEG---IISDLGKRSPEIGAVIL 284
Cdd:cd24007 241 KlllLGEKLPLALSGGVFKNNYYLAEFLEELLKKKkpnAKVVEPKGSPVVGALLL 295
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
 2-291 5.06e-88

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


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 264.82  E-value: 5.06e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        2 MIIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAK-----GEADVVGMGVAGLDSKFDW 76
Cdd:COG2971   1 PYILGVDGGGTKTRAVLVDADGEVLGRGRAGGANPQSVGLEEALASLREALEEALAaagdpADIEAVGFGLAGAGTPEDA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       77 ENFTPLASLIAP--KVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGK-EFLRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:COG2971  81 EALEAALRELFPfaRVVVVNDALAALAGALGGEDGIVVIAGTGSIAAGRDGDgRTARVGGWGYLLGDEGSGAWLGREALR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      154 KVLKMMDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:COG2971 161 AALRALDGRGPPTALTEAVLAEFGLDDPEELIAWVYRGPAPPADLASLAPLVFEAAEAGDPVARAILEEAADELAELARA 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
2E2Q_A      234 LARKiGTNKVYLKGGMFRSN-IYHKFFTLYLEKEGIISDLGKRSPEIGAVILAYKEVGC 291
Cdd:COG2971 241 LLER-GALPVVLAGGVAAAQpLLREALRARLAAGGAEIVPPAGDPVDGALLLALRLLGA 298
ASKHA_NBD_MurK-like cd24084
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ...
 4-287 5.48e-53

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: 175.24  E-value: 5.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIA------AKGEADVVGMGVAGLDSKFDWE 77
Cdd:cd24084   3 VIGIDGGGTKTHLKITDLNGNVVGEGFGGSSNLESNSLETVRENLKELFQDFyeqlgkSLKECGSICLGTAGASHQGAKE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       78 NFTPLASLIAP--KVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYN--GKEFlRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:cd24084  83 TLKDILTELGPdaKIEVVNDAEIALAAGLEGKPGIVLISGTGSICYGRNtdGETA-RAGGWGHLLGDEGSGYWIAMQALG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      154 KVLKMMDGLENKTILYNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:cd24084 162 AVLQAFDGRGPKTILTELLLEELKLSSPRELIDFIYSSDADKKEIASLARLVDEAADQGDEVAKEILEEAARELARLAIA 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2E2Q_A      234 LARKIGTN----KVYLKGGMFRSNIYHK-FFTLYLEKEG--IISDLGKRSPEIGAVILAYK 287
Cdd:cd24084 242 VAQKLLMKpkdfVVILGGSVLENCCVLRsKLSALILTKYpnAIVGLLKHDAAYGAVKLARE 302
ASKHA_NBD_GspK-like cd24082
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ...
 3-248 6.35e-53

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: 174.26  E-value: 6.35e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        3 IIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNvGLTRAIENIKEAVKIAAKgEADV---------VGMGVAGLDSK 73
Cdd:cd24082   1 YFIGIDGGGTKCRARLADADGTVLGEATGGPANLSS-DLDQAWASILAAIKQALA-QAGLdaaalsdlhAGLGLAGANVP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       74 FDWENFTPLASLIApKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGKEFLRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:cd24082  79 EARAAFLAALPPFA-SLVVVSDAHIACLGAHGGEDGAIIILGTGSVGAALDGGEVRQVGGWGFPLGDEGSGAWLGLRALR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      154 KVLKMMDGLENKTILYNKVLKTINVkDLDELVMWSYTSScQIDlVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:cd24082 158 HTLLALDGLAPSSPLTRAVLARFGG-DPAEIVAWANTAT-PAD-FAALAPLVFEAAEQGDPVALAILQEAAAYIERLLRA 234

                       250
                ....*....|....*
2E2Q_A      234 LARKiGTNKVYLKGG 248
Cdd:cd24082 235 LGAQ-GALPLCLLGG 248
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-285 3.87e-46

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: 156.36  E-value: 3.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A          5 VGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG----EADV-------VGMGVAGLDSK 73
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDGEVLGRAIAGSANFESVGVEAAERNLKDAITEALEEaglkLDDIeymflglTGYGRAGVDGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A         74 FDWEnftplasLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGKEFLRVGGRGWLLSDDGSAYWVGRKALR 153
Cdd:pfam01869  81 FGKD-------IVREEITVHADGAVALAPGTRGEDGVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        154 KVLKMMDGLENKTILYnkvlktinvkdldELVMWSYtsscqidlVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVY 233
Cdd:pfam01869 154 AVVRELDGLAPKTTLN-------------KGAINST--------CAVFAEQVVINALSGGETAEDILAGAARSIALRVAA 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
2E2Q_A        234 LARKIG--TNKVYLKGGMFRSNIYHKFFTLYLEK-----EGIISDLGKRSPEIGAVILA 285
Cdd:pfam01869 213 LAKRLGfvPDEVVLTGGVAKNAGLVKALRDYLKEnilgvKVNVHPDPQYAGAIGAALLA 271
ASKHA_NBD_KdgK-like cd24083
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
 4-284 6.03e-45

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: 153.70  E-value: 6.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYD-CEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKG----EADVVGMGVAGL-DSKFDWE 77
Cdd:cd24083   1 ILGVDGGGTKTLAVLFDeRQGEIVGIGISGPSNFTVVGRETARKNISDAINDALSDagmdSIDKATFGLAGIgDSYEATI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       78 NFTPLASLIAPKVIIQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGKEFLRVGGRGWLLSDDGSAYWVGRKALRKVLK 157
Cdd:cd24083  81 MGEEIIRSGLKKFDIYNDGEAAYYSGNGDDDGIVFAPGTGSVGYIKDEGRVNRIGGWGWSLGDEGSAFWIAKQAIEAAMR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      158 MMDGLENKTILYNKVLKTInvKDLDELVMWSYTSSCQIDLVASIAKAVDEAANEGDTVAMDILKQGAELLASQAVYLARK 237
Cdd:cd24083 161 EMDGREEWTSLVVEVEKEF--KLSLRELVINISYEGIKRLVASLAKLVSQLAEKGDPVALAIFDEAASEIKKIINAHRLN 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
2E2Q_A      238 IGTN-KVYLKGGMFRS-NIYHKFFTLYLEKEGIISDLgkrSPEIGAVIL 284
Cdd:cd24083 239 FGPPiRVSLVGGVMQSgPIYLEKFIKSSYEISIFFGY---EPVIGAVLL 284
ASKHA_NBD_DdNAGK-like cd24081
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ...
 4-285 2.80e-42

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: 147.46  E-value: 2.80e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYDC-----EGNFIGEGSSGPGNYHNVGLT---RAIEN-IKEAVKIAAKGEADVVG--MGVAGLDS 72
Cdd:cd24081   1 VLGIDGGGTKTTCVAVDAatlgdNLLVLGRAVAGSSNYNSVGEEaarRAIEEaIAGALKQAGVPRSAVRAvcLGISGVDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       73 KFD------W--ENFTPlasliAPKVIIQHDGVIALFAETLGE-PGVVVIAGTGSVVEGYNGK-EFLRVGGRGWLLSDDG 142
Cdd:cd24081  81 PADaervrsWlrELFPE-----NVKVFVFNDAVAALASGTAGKlHGCVLIAGTGTIAYGFNEDgKRARAGGWGPLLGDRG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      143 SAYWVGRKALRKVLKMMDGLENKTILYNKVLKTINVKDLDELVMWSYTSScQIDLVASIAKAVDEAANEGDTVAMDILKQ 222
Cdd:cd24081 156 SGHAIGSQALTAVMRAEDGRGPPTSLTGAILKKLGLSSPDDLIGWAYDDT-SWARVAALVPLVKACAAAGDAVALGILED 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E2Q_A      223 GAELLASQAVYLARKI---GTNK------VYLKGGMFRSNIYHKFFTLYLE----KEGIISDLGKRSPEIGAVILA 285
Cdd:cd24081 235 AAEELALSVKAVVRKLglrGTDGsesfplVLVGGVLERNGGLDLFKELVKKlntgFPGAQIVIPKVEPAVGAALLA 310
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 3-288 5.06e-25

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: 101.89  E-value: 5.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        3 IIVGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKiAAKGEADV--------VGMGVAGLDSKF 74
Cdd:cd24078   1 YFGGVEGGATHSKLVIMDEDGKILAESEGPGTNHWLIGLDECAKRINEMVQ-EAKKKAGLdpdtplksLGLSLSGAEQEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       75 DWENFTPLASLIAPKV----IIQHDGVIALFAeTLGEPGVVVIAGTGS--VVEGYNGKEFlRVGGRGWLLSDDGSAYWVG 148
Cdd:cd24078  80 AQEELIEGLRSRYPNLsesyYVTSDTVGAIAT-AFENGGIVLISGTGSncQLINPDGSTA-GCGGWGHMLGDEGSAYWIA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      149 RKALRKVLKMMDGLENK----TILYNKVLKTINVKDLDELVMWSYTSScQIDLVASIAKAVDEAANEGDTVAMDILKQGA 224
Cdd:cd24078 158 HRAIKAVFDAEDNFEPPphdiSYVKKAMFEYFKIEDRLDLLPHLYTNF-DKSKIAGFCKKLAEGAAEGDPLCRHLFREAG 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      225 ELLASQAVYLARKIGTNKVYLKGGM------------------FRSNIYH-----KFFTLYLEKEgiisdlgkrSPEIGA 281
Cdd:cd24078 237 EELARHVLAVLPKIDKALLEGEGGLpivcvgsvwkswdllkegFLEGLKQrsdkiKKLSLVRLKE---------SSALGA 307


                ....*..
2E2Q_A      282 VILAYKE 288
Cdd:cd24078 308 ARLGAKE 314
ASKHA_NBD_PG1100-like cd24079
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ...
 3-207 5.74e-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: 64.54  E-value: 5.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        3 IIVGvDAGGTKTKAVAYDCEGN---FIGEGSSgPgNYHNvglTRAIENIKEAVKIAAKGEADVV-----GMGVAGLDSKF 74
Cdd:cd24079   1 ILIA-DSGGTKTDWALVDGGGVikqFTTKGLN-P-FFLS---DEEIEQILALVLLPLLEESKIEevyfyGAGCGSPERAA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       75 DWENFtpLASLIAPKVI-IQHDGVIALFAETLGEPGVVVIAGTGSVVEGYNGKEFL-RVGGRGWLLSDDGSAYWVGRKAL 152
Cdd:cd24079  75 RIKRL--LKKVFPKAEIeVKSDLLGAARALCGDKKGIVCILGTGSNSCYYDGEKIHdQRPGLGYLLGDEGSGAYLGKLLL 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
2E2Q_A      153 RKVLKmmdGLENKTIlyNKVLKTINVKDLDELVMWSYTSSCQIDLVASIAKAVDE 207
Cdd:cd24079 153 RDYLY---GQLPEEL--RKRFEEQFGLNKEEILSRVYRSPDPNRYLASLSRFIAE 202
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 1-285 6.43e-06

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: 46.81  E-value: 6.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        1 MMIIVGVDAGGTKTKAVAYDCEGNFIGEGS---SGPGNYHNVgLTRAIENIKEAVKIAAKGEADV--VGMGVAG-LDSK- 73
Cdd:COG1940   4 AGYVIGIDIGGTKIKAALVDLDGEVLARERiptPAGAGPEAV-LEAIAELIEELLAEAGISRGRIlgIGIGVPGpVDPEt 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A       74 ---------FDWENFtPLASLIAPK----VIIQHDGVIALFAE-TLGEPG-----VVVIAGTG---SVVegYNGKefLRV 131
Cdd:COG1940  83 gvvlnapnlPGWRGV-PLAELLEERlglpVFVENDANAAALAEaWFGAGRgadnvVYLTLGTGiggGIV--INGK--LLR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      132 GGRGW-------LLSDDGSAYWVGRK----------ALRKVLKMMDGLENKTilynkvlktinvkdldelvmwsytsscq 194
Cdd:COG1940 158 GANGNageighmPVDPDGPLCGCGNRgcletyasgpALLRRARELGGAEKLT---------------------------- 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A      195 idlvasiAKAVDEAANEGDTVAMDILKQGAELLA---SQAVYLarkIGTNKVYLKGGMFRSN----------IYHKFFTL 261
Cdd:COG1940 210 -------AEELFAAARAGDPLALEVLDEAARYLGiglANLINL---LDPEVIVLGGGVSAAGdlllepireaLAKYALPP 279

                       330       340
                ....*....|....*....|....*
2E2Q_A      262 YLEKEGI-ISDLGKRSPEIGAVILA 285
Cdd:COG1940 280 AREDPRIvPASLGDDAGLLGAAALA 304
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
 4-135 8.66e-06

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.


Pssm-ID: 466935 [Multi-domain]  Cd Length: 262  Bit Score: 46.02  E-value: 8.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIgegssgpgnyHNVGLTRAIENIKEavKIAAKGEADVVGMGVAGLDSKFDWENFTPLA 83
Cdd:cd24085   1 KIGIDAGGTLTKIVLLENNGELK----------FKAFDSLKIEALVK--FLNELGINDIEKIAVTGGGASRLPENIDGIP 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
2E2Q_A       84 SLIAPKVIIQHDGVIALfAETLGEPGVVVIAGTGSVVEGYNGKEFLRVGGRG 135
Cdd:cd24085  69 IVKVDEFEAIGRGALYL-LGEILDDALVVSIGTGTSIVLAKNGTIRHVGGTG 119
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 4-69 1.79e-04

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY 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: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 42.55  E-value: 1.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGSSG-PGNYHNVG---------LTRAIENIKEAVKIAAKGEADVVGMGVAG 69
Cdd:cd00366   2 LLGIDIGTTSVKAALFDEDGNLVASASREyPLIYPQPGwaeqdpedwWQAVVEAIREVLAKAGIDPSDIAAIGISG 77
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
 4-69 4.10e-04

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 41.77  E-value: 4.10e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGS-------SGPGNY---HNVGLTRAIENIKEAVKIAAKGEADVVGMGVAG 69
Cdd:cd07802   2 LLGIDNGTTNVKAVLFDLDGREIAVASrptpvisPRPGWAerdMDELWQATAEAIRELLEKSGVDPSDIAGVGVTG 77
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 4-86 6.34e-04

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 41.00  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGS--------SGPGNYHNVG--LTRAIENIKEAVKIAAKGEADVVG-----MGVA 68
Cdd:cd07770   2 ILGIDIGTTSTKAVLFDEDGRVVASSSaeyplirpEPGWAEQDPEeiLEAVLEALKEVLAKLGGGEVDAIGfssamHSLL 81

                        90
                ....*....|....*...
2E2Q_A       69 GLDskfdwENFTPLASLI 86
Cdd:cd07770  82 GVD-----EDGEPLTPVI 94
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 4-69 3.76e-03

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 38.66  E-value: 3.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2E2Q_A        4 IVGVDAGGTKTKAVAYDCEGNFIGEGSSG-PGNYHNVG--------LTRAIEN-IKEAVKIAAKGEADVVGMGVAG 69
Cdd:COG1070   3 VLGIDIGTTSVKAVLFDADGEVVASASAEyPLSSPHPGwaeqdpedWWEAVVEaIRELLAKAGVDPEEIAAIGVSG 78
ASKHA_NBD_benz_CoA_BcrA_BadF cd24104
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
 5-66 5.93e-03

nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.


Pssm-ID: 466954  Cd Length: 253  Bit Score: 37.66  E-value: 5.93e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2E2Q_A        5 VGVDAGGTKTKAVAYDCEGNFIGEGSSGPGNYHNVGLTRAIENIKEAVKIAAKGEADVVGMG 66
Cdd:cd24104   2 AGVDVGSTQTKAVIIDEDGEIVGRGLTNTGANVVVAAERAFREAIEEAGIKEEEVEYVVGTG 63
 
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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