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Conserved domains on  [gi|16129598|ref|NP_416157|]
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anhydro-N-acetylmuramic acid kinase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

anhydro-N-acetylmuramic acid kinase( domain architecture ID 10508667)

anhydro-N-acetylmuramic acid kinase catalyzes hydrolysis of 1,6-anhydro bond of anyhydro-N-acetylmuramic acid (anhMurNAc) and phosphorylates anhMurNAc to produce N-acetyl-muramate-6-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
4-367 0e+00

Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.


:

Pssm-ID: 397660  Cd Length: 364  Bit Score: 613.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598     4 GRFIGVMSGTSLDGVDVVLATIDEHRVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALLKE 83
Cdd:pfam03702   1 MRYIGLMSGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598    84 QNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERR 163
Cdd:pfam03702  81 QNLSPEQIRAIGCHGQTVRHEPEGAVPFTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEALFAAPNETR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   164 MVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKSTGR 243
Cdd:pfam03702 161 AVLNIGGIANVSVLPPGAPVLGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADPYFALPAPKSTGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   244 EYFNYGWLERHLRHFPgVDPRDVQATLAELTAVTISEQVLLSG-GCERLMVCGGGSRNPLLMARLAALLPGTEVTTTDAV 322
Cdd:pfam03702 241 ELFNLPWLETHLAKHP-VAAADVQATLAELTAVTIVDALLQAQpDCERLLVCGGGARNPLLMARLAALLPGVQVASTDAY 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 16129598   323 GISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPA 367
Cdd:pfam03702 320 GLDPDYMEAMAFAWLAARTLNGLPGNLPSVTGASRARSLGAIYPA 364
 
Name Accession Description Interval E-value
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
4-367 0e+00

Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.


Pssm-ID: 397660  Cd Length: 364  Bit Score: 613.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598     4 GRFIGVMSGTSLDGVDVVLATIDEHRVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALLKE 83
Cdd:pfam03702   1 MRYIGLMSGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598    84 QNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERR 163
Cdd:pfam03702  81 QNLSPEQIRAIGCHGQTVRHEPEGAVPFTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEALFAAPNETR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   164 MVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKSTGR 243
Cdd:pfam03702 161 AVLNIGGIANVSVLPPGAPVLGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADPYFALPAPKSTGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   244 EYFNYGWLERHLRHFPgVDPRDVQATLAELTAVTISEQVLLSG-GCERLMVCGGGSRNPLLMARLAALLPGTEVTTTDAV 322
Cdd:pfam03702 241 ELFNLPWLETHLAKHP-VAAADVQATLAELTAVTIVDALLQAQpDCERLLVCGGGARNPLLMARLAALLPGVQVASTDAY 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 16129598   323 GISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPA 367
Cdd:pfam03702 320 GLDPDYMEAMAFAWLAARTLNGLPGNLPSVTGASRARSLGAIYPA 364
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
3-367 0e+00

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 567.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598    3 SGRFIGVMSGTSLDGVDVVLATIDEHR--VAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNAL 80
Cdd:PRK09585   1 SMRYIGLMSGTSLDGVDAALVEIDGEGtkVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   81 LKEQNLQARDIVAIGCHGQTVWHEPTgvAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:PRK09585  81 LAEAGLSPEDIDAIGSHGQTVRHRPG--EGFTLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQALFGHPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  161 ERRMVLNIGGIANLSLLIPG-QPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPK 239
Cdd:PRK09585 159 ETRAVLNIGGIANITLLPPGgGPVIGFDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLAHPYFALPPPK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  240 STGREYFNYGWLERHLRHFPgVDPRDVQATLAELTAVTISEQVL-LSGGCERLMVCGGGSRNPLLMARLAALLPgTEVTT 318
Cdd:PRK09585 239 STGRELFNLAWLERQLAGFG-LSPEDVQATLTELTAASIARAVRrLPPGPDELLVCGGGARNPTLMERLAALLP-TEVAT 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 16129598  319 TDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPA 367
Cdd:PRK09585 317 TDALGIDGDAKEALAFAWLAVRTLRGLPGNLPSVTGASGPVVLGAIYPA 365
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-363 0e+00

1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441944  Cd Length: 363  Bit Score: 566.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   2 KSGRFIGVMSGTSLDGVDVVLATIDEH-RVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNAL 80
Cdd:COG2377   1 KPMLVIGLMSGTSLDGIDAALVEFDGEgKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAVLAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  81 LKEQNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:COG2377  81 LAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAFHQALFSDPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 161 ERRMVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKS 240
Cdd:COG2377 161 EPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLLADPYFALPPPKS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 241 TGREYFNYGWLERHLRHFpGVDPRDVQATLAELTAVTISEQV-LLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVTTT 319
Cdd:COG2377 241 TGRELFNLAWLEQLLAGF-GLSPEDVQATLTELTAASIADAIrRLPPPPDRVLVCGGGAHNPTLMERLQALLPGVPVVTT 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 16129598 320 DAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGA 363
Cdd:COG2377 320 DELGIDPDAKEALAFAWLAVRTLRGLPGNLPSVTGAKRPVILGA 363
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-366 0e+00

nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.


Pssm-ID: 466900  Cd Length: 369  Bit Score: 559.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   6 FIGVMSGTSLDGVDVVLATIDEH----RVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALL 81
Cdd:cd24050   1 YIGLMSGTSLDGIDAALVEIDGDgtelRVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  82 KEQNLQARDIVAIGCHGQTVWHEPTG-VAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:cd24050  81 AKSGISPSDIDAIGSHGQTVWHRPEPeRVGFTLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYALFADPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 161 ERRMVLNIGGIANLSLLIPG-QPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPK 239
Cdd:cd24050 161 ETRAVLNIGGIANVTYLPPGsDDVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPYFALPPPK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 240 STGREYFNYGWLERHLRHFPGVDPRDVQATLAELTAVTISEQV--LLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVT 317
Cdd:cd24050 241 STGRELFNLAWLEELLKRAPGLSPEDIVATLTAFTARSIADAYrkFVPPGPDEVIVCGGGAHNPTLMRRLRELLPGIKVK 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 16129598 318 TTDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFP 366
Cdd:cd24050 321 TTDELGISSDAKEAMAFAWLAYRTLNGLPGNLPSVTGASKPVVLGKIYP 369
 
Name Accession Description Interval E-value
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
4-367 0e+00

Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.


Pssm-ID: 397660  Cd Length: 364  Bit Score: 613.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598     4 GRFIGVMSGTSLDGVDVVLATIDEHRVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALLKE 83
Cdd:pfam03702   1 MRYIGLMSGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598    84 QNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERR 163
Cdd:pfam03702  81 QNLSPEQIRAIGCHGQTVRHEPEGAVPFTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEALFAAPNETR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   164 MVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKSTGR 243
Cdd:pfam03702 161 AVLNIGGIANVSVLPPGAPVLGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADPYFALPAPKSTGR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   244 EYFNYGWLERHLRHFPgVDPRDVQATLAELTAVTISEQVLLSG-GCERLMVCGGGSRNPLLMARLAALLPGTEVTTTDAV 322
Cdd:pfam03702 241 ELFNLPWLETHLAKHP-VAAADVQATLAELTAVTIVDALLQAQpDCERLLVCGGGARNPLLMARLAALLPGVQVASTDAY 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 16129598   323 GISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPA 367
Cdd:pfam03702 320 GLDPDYMEAMAFAWLAARTLNGLPGNLPSVTGASRARSLGAIYPA 364
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
3-367 0e+00

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 567.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598    3 SGRFIGVMSGTSLDGVDVVLATIDEHR--VAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNAL 80
Cdd:PRK09585   1 SMRYIGLMSGTSLDGVDAALVEIDGEGtkVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   81 LKEQNLQARDIVAIGCHGQTVWHEPTgvAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:PRK09585  81 LAEAGLSPEDIDAIGSHGQTVRHRPG--EGFTLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQALFGHPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  161 ERRMVLNIGGIANLSLLIPG-QPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPK 239
Cdd:PRK09585 159 ETRAVLNIGGIANITLLPPGgGPVIGFDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLAHPYFALPPPK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  240 STGREYFNYGWLERHLRHFPgVDPRDVQATLAELTAVTISEQVL-LSGGCERLMVCGGGSRNPLLMARLAALLPgTEVTT 318
Cdd:PRK09585 239 STGRELFNLAWLERQLAGFG-LSPEDVQATLTELTAASIARAVRrLPPGPDELLVCGGGARNPTLMERLAALLP-TEVAT 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 16129598  319 TDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPA 367
Cdd:PRK09585 317 TDALGIDGDAKEALAFAWLAVRTLRGLPGNLPSVTGASGPVVLGAIYPA 365
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-363 0e+00

1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441944  Cd Length: 363  Bit Score: 566.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   2 KSGRFIGVMSGTSLDGVDVVLATIDEH-RVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNAL 80
Cdd:COG2377   1 KPMLVIGLMSGTSLDGIDAALVEFDGEgKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAVLAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  81 LKEQNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:COG2377  81 LAKAGLSAEDIDAIGSHGQTVRHRPEGRPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAFHQALFSDPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 161 ERRMVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKS 240
Cdd:COG2377 161 EPRAVLNIGGIANITYLPPGGPVIAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLLADPYFALPPPKS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 241 TGREYFNYGWLERHLRHFpGVDPRDVQATLAELTAVTISEQV-LLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVTTT 319
Cdd:COG2377 241 TGRELFNLAWLEQLLAGF-GLSPEDVQATLTELTAASIADAIrRLPPPPDRVLVCGGGAHNPTLMERLQALLPGVPVVTT 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 16129598 320 DAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGA 363
Cdd:COG2377 320 DELGIDPDAKEALAFAWLAVRTLRGLPGNLPSVTGAKRPVILGA 363
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-366 0e+00

nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.


Pssm-ID: 466900  Cd Length: 369  Bit Score: 559.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   6 FIGVMSGTSLDGVDVVLATIDEH----RVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALL 81
Cdd:cd24050   1 YIGLMSGTSLDGIDAALVEIDGDgtelRVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  82 KEQNLQARDIVAIGCHGQTVWHEPTG-VAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPT 160
Cdd:cd24050  81 AKSGISPSDIDAIGSHGQTVWHRPEPeRVGFTLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYALFADPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 161 ERRMVLNIGGIANLSLLIPG-QPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPK 239
Cdd:cd24050 161 ETRAVLNIGGIANVTYLPPGsDDVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPYFALPPPK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 240 STGREYFNYGWLERHLRHFPGVDPRDVQATLAELTAVTISEQV--LLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVT 317
Cdd:cd24050 241 STGRELFNLAWLEELLKRAPGLSPEDIVATLTAFTARSIADAYrkFVPPGPDEVIVCGGGAHNPTLMRRLRELLPGIKVK 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 16129598 318 TTDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFP 366
Cdd:cd24050 321 TTDELGISSDAKEAMAFAWLAYRTLNGLPGNLPSVTGASKPVVLGKIYP 369
ASKHA_NBD_LGK cd24051
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
5-368 3.05e-85

nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom.


Pssm-ID: 466901  Cd Length: 409  Bit Score: 264.02  E-value: 3.05e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   5 RFIGVMSGTSLDGVDVVLA-----TID---EHRVAQLASLSWPIPvsLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADA 76
Cdd:cd24051   2 TVLGLNSGTSMDGIDCALChftqkTPDapmEFELIEYGEVPLAQP--IKQRVMSMILEDTTSPSELSEVNVILGETFADA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  77 VNALLKEQNLQARDIVAIGCHGQTVWHE---PTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHH 153
Cdd:cd24051  80 VRQFAAERNVDLSDIDAIASHGQTIWLLsmpEEGQVKSALTMGEGAIIAARTGITSVTDFRISDQAAGRQGAPLIAFFDA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 154 ALLAHPTERRMVLNIGGIANLSlLIPGQPVGG------YDTGPGNMLMDAWIwRQAG---KPYDKDAEWARAGKVILPLL 224
Cdd:cd24051 160 LLLHHPTKLRACQNIGGIANVC-FIPPDNDGRtdeyydFDTGPGNVFIDAVV-RHFTngeQEYDKDGAMGKRGKVDQELV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 225 QNMLSDPYFSQPAPKSTGREYFNYGWLERHLR--HFPGVDPRDVQATLAELTAVTISEQVLL---SGGCERLMVCGGGSR 299
Cdd:cd24051 238 DDFLKMPYFQLDPPKTTGREVFRDTLAHDLIRraEAKGLSPDDIVATTTRITAQSIVDHYRRyapSQEIDEIFMCGGGAF 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129598 300 NPLLMARLAALLPGTEVTTTDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPAN 368
Cdd:cd24051 318 NPNIVEFIQQSYPGTKIMMLDEAGVPAGAKEAITFAWQGMEALVGRSIPVPTRVETRQHTVLGKVSPGL 386
ASKHA_NBD_ANMK-like cd24005
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
7-364 9.06e-64

nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain family; The family includes anhydro-N-acetylmuramic acid kinase (ANMK) and levoglucosan kinase (LGK). ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. It is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom. The ANMK-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466855  Cd Length: 358  Bit Score: 207.26  E-value: 9.06e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598   7 IGVMSGTSLDGVDVVLAtideHRVAQLASLSW---PIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALLKE 83
Cdd:cd24005   2 LGLMSGTSLDGMDIVLI----EQGDRTTLLAShylPMPAGLREDILALCVPGPDEIARAAEVEQRWVALAAQGVRELLLQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598  84 QNLQARDIVAIGCHGQTVWHepTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERR 163
Cdd:cd24005  78 QQMSPDEVRAIGSHGQTIRH--EPARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGAPLVPAFHQALFGDDDTSR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 164 MVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKSTGR 243
Cdd:cd24005 156 AVLNIGGFSNVSLLSPGKPVRGFDCGPGNVLMDAWIHHQRGEHFDRDGAWAASGQVNHALLASLLADEFFAARGPKSTGR 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129598 244 EYFNYGWLERHLRHFPGVDPRDVQATLAELTAVTISEQV-LLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVTTTDAV 322
Cdd:cd24005 236 ERFNLPWLQEHLARHPALPAADIQATLLELSARSISESLlDAQPDCEEVLVCGGGAFNTALMKRLAMLMPEARVASTDEY 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 16129598 323 GISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAI 364
Cdd:cd24005 316 GIPPAWMEGMAFAWLAHRFLERLPGNCPDVTGALGPRTLGAL 357
 
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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