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Conserved domains on  [gi|498064520|ref|WP_010378676|]
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anhydro-N-acetylmuramic acid kinase [Pseudoalteromonas piscicida]

Protein Classification

anhydro-N-acetylmuramic acid kinase( domain architecture ID 19234747)

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
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
19-385 1.77e-152

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: 434.65  E-value: 1.77e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  19 ILGLMSGTSLDGLDIALCKIEGVGKNTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNAL 98
Cdd:cd24050    1 YIGLMSGTSLDGIDAALVEIDGDGTELRVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  99 AEWQVAADTVDLIASHGQTLYHCPKQafadiENLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYLL 178
Cdd:cd24050   81 AKSGISPSDIDAIGSHGQTVWHRPEP-----ERVGFTLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 179 YSDTSIDRVLLNIGGISNLTYLPQNCAltQSMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLSHEF 258
Cdd:cd24050  156 FADPDETRAVLNIGGIANVTYLPPGSD--DVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 259 FDIPLPKSTGQELFNQTFVHHALD-GKDYNHEDIITTLTEFTAITIANAVNKLSTAEL-ELYVSGGGIHNVFLMERIESH 336
Cdd:cd24050  234 FALPPPKSTGRELFNLAWLEELLKrAPGLSPEDIVATLTAFTARSIADAYRKFVPPGPdEVIVCGGGAHNPTLMRRLREL 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498064520 337 LnNRVLIKDFSQLGINPDAKEAALFALLANETVSG--------DGDALPFSMGKISL 385
Cdd:cd24050  314 L-PGIKVKTTDELGISSDAKEAMAFAWLAYRTLNGlpgnlpsvTGASKPVVLGKIYP 369
 
Name Accession Description Interval E-value
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
19-385 1.77e-152

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: 434.65  E-value: 1.77e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  19 ILGLMSGTSLDGLDIALCKIEGVGKNTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNAL 98
Cdd:cd24050    1 YIGLMSGTSLDGIDAALVEIDGDGTELRVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  99 AEWQVAADTVDLIASHGQTLYHCPKQafadiENLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYLL 178
Cdd:cd24050   81 AKSGISPSDIDAIGSHGQTVWHRPEP-----ERVGFTLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 179 YSDTSIDRVLLNIGGISNLTYLPQNCAltQSMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLSHEF 258
Cdd:cd24050  156 FADPDETRAVLNIGGIANVTYLPPGSD--DVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 259 FDIPLPKSTGQELFNQTFVHHALD-GKDYNHEDIITTLTEFTAITIANAVNKLSTAEL-ELYVSGGGIHNVFLMERIESH 336
Cdd:cd24050  234 FALPPPKSTGRELFNLAWLEELLKrAPGLSPEDIVATLTAFTARSIADAYRKFVPPGPdEVIVCGGGAHNPTLMRRLREL 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498064520 337 LnNRVLIKDFSQLGINPDAKEAALFALLANETVSG--------DGDALPFSMGKISL 385
Cdd:cd24050  314 L-PGIKVKTTDELGISSDAKEAMAFAWLAYRTLNGlpgnlpsvTGASKPVVLGKIYP 369
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
15-371 2.21e-151

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


Pssm-ID: 441944  Cd Length: 363  Bit Score: 431.80  E-value: 2.21e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  15 KTKYILGLMSGTSLDGLDIALCKIEGvgkNTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLI 94
Cdd:COG2377    1 KPMLVIGLMSGTSLDGIDAALVEFDG---EGKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  95 NNALAEWQVAADTVDLIASHGQTLYHCPKQafadieNLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYG 174
Cdd:COG2377   78 LALLAKAGLSAEDIDAIGSHGQTVRHRPEG------RPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 175 DYLLYSDTSIDRVLLNIGGISNLTYLPQNCALtqsMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALL 254
Cdd:COG2377  152 HQALFSDPGEPRAVLNIGGIANITYLPPGGPV---IAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 255 SHEFFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIE 334
Cdd:COG2377  229 ADPYFALPPPKSTGRELFNLAWLEQLLAGFGLSPEDVQATLTELTAASIADAIRRLPPPPDRVLVCGGGAHNPTLMERLQ 308
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 498064520 335 SHLNNrVLIKDFSQLGINPDAKEAALFALLANETVSG 371
Cdd:COG2377  309 ALLPG-VPVVTTDELGIDPDAKEALAFAWLAVRTLRG 344
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
18-371 3.89e-145

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 416.06  E-value: 3.89e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  18 YILGLMSGTSLDGLDIALCKIEGVGknTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNA 97
Cdd:PRK09585   3 RYIGLMSGTSLDGVDAALVEIDGEG--TKVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  98 LAEWQVAADTVDLIASHGQTLYHCPKQAFadienlnsTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYL 177
Cdd:PRK09585  81 LAEAGLSPEDIDAIGSHGQTVRHRPGEGF--------TLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 178 LYSDTSIDRVLLNIGGISNLTYLPQNcaltQSMCS--DIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLS 255
Cdd:PRK09585 153 LFGHPDETRAVLNIGGIANITLLPPG----GGPVIgfDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 256 HEFFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIES 335
Cdd:PRK09585 229 HPYFALPPPKSTGRELFNLAWLERQLAGFGLSPEDVQATLTELTAASIARAVRRLPPGPDELLVCGGGARNPTLMERLAA 308
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 498064520 336 HLNNRVLIKDfsQLGINPDAKEAALFALLANETVSG 371
Cdd:PRK09585 309 LLPTEVATTD--ALGIDGDAKEALAFAWLAVRTLRG 342
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
18-377 9.86e-101

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: 303.15  E-value: 9.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520   18 YILGLMSGTSLDGLDIALCKIEGvgKNTQLTVEQFTTieYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNA 97
Cdd:pfam03702   2 RYIGLMSGTSLDGVDAALVDLDD--ARVELLASHFSP--MPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520   98 LAEWQVAADTVDLIASHGQTLYHCPKQAFAdienlnSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYL 177
Cdd:pfam03702  78 LQKQNLSPEQIRAIGCHGQTVRHEPEGAVP------FTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  178 LYSDTSIDRVLLNIGGISNLTYLPQNCALtqsMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLSHE 257
Cdd:pfam03702 152 LFAAPNETRAVLNIGGIANVSVLPPGAPV---LGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  258 FFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIESHL 337
Cdd:pfam03702 229 YFALPAPKSTGRELFNLPWLETHLAKHPVAAADVQATLAELTAVTIVDALLQAQPDCERLLVCGGGARNPLLMARLAALL 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 498064520  338 NNrVLIKDFSQLGINPDAKEAALFALLANETVSGDGDALP 377
Cdd:pfam03702 309 PG-VQVASTDAYGLDPDYMEAMAFAWLAARTLNGLPGNLP 347
 
Name Accession Description Interval E-value
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
19-385 1.77e-152

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: 434.65  E-value: 1.77e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  19 ILGLMSGTSLDGLDIALCKIEGVGKNTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNAL 98
Cdd:cd24050    1 YIGLMSGTSLDGIDAALVEIDGDGTELRVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  99 AEWQVAADTVDLIASHGQTLYHCPKQafadiENLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYLL 178
Cdd:cd24050   81 AKSGISPSDIDAIGSHGQTVWHRPEP-----ERVGFTLQIGDPAVIAERTGITVVSDFRRADMAAGGQGAPLVPAFDYAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 179 YSDTSIDRVLLNIGGISNLTYLPQNCAltQSMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLSHEF 258
Cdd:cd24050  156 FADPDETRAVLNIGGIANVTYLPPGSD--DVIGFDTGPGNMLIDAWVQRLTGLPYDKDGEIAASGKVDEALLARLLDDPY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 259 FDIPLPKSTGQELFNQTFVHHALD-GKDYNHEDIITTLTEFTAITIANAVNKLSTAEL-ELYVSGGGIHNVFLMERIESH 336
Cdd:cd24050  234 FALPPPKSTGRELFNLAWLEELLKrAPGLSPEDIVATLTAFTARSIADAYRKFVPPGPdEVIVCGGGAHNPTLMRRLREL 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498064520 337 LnNRVLIKDFSQLGINPDAKEAALFALLANETVSG--------DGDALPFSMGKISL 385
Cdd:cd24050  314 L-PGIKVKTTDELGISSDAKEAMAFAWLAYRTLNGlpgnlpsvTGASKPVVLGKIYP 369
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
15-371 2.21e-151

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


Pssm-ID: 441944  Cd Length: 363  Bit Score: 431.80  E-value: 2.21e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  15 KTKYILGLMSGTSLDGLDIALCKIEGvgkNTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLI 94
Cdd:COG2377    1 KPMLVIGLMSGTSLDGIDAALVEFDG---EGKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  95 NNALAEWQVAADTVDLIASHGQTLYHCPKQafadieNLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYG 174
Cdd:COG2377   78 LALLAKAGLSAEDIDAIGSHGQTVRHRPEG------RPGFTLQIGDGALLAELTGIPVVADFRSRDVAAGGQGAPLVPAF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 175 DYLLYSDTSIDRVLLNIGGISNLTYLPQNCALtqsMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALL 254
Cdd:COG2377  152 HQALFSDPGEPRAVLNIGGIANITYLPPGGPV---IAFDTGPGNALLDAWVQRHGGKPYDKDGAWAASGKVDEALLARLL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 255 SHEFFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIE 334
Cdd:COG2377  229 ADPYFALPPPKSTGRELFNLAWLEQLLAGFGLSPEDVQATLTELTAASIADAIRRLPPPPDRVLVCGGGAHNPTLMERLQ 308
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 498064520 335 SHLNNrVLIKDFSQLGINPDAKEAALFALLANETVSG 371
Cdd:COG2377  309 ALLPG-VPVVTTDELGIDPDAKEALAFAWLAVRTLRG 344
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
18-371 3.89e-145

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 416.06  E-value: 3.89e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  18 YILGLMSGTSLDGLDIALCKIEGVGknTQLTVEQFTTIEYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNA 97
Cdd:PRK09585   3 RYIGLMSGTSLDGVDAALVEIDGEG--TKVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  98 LAEWQVAADTVDLIASHGQTLYHCPKQAFadienlnsTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYL 177
Cdd:PRK09585  81 LAEAGLSPEDIDAIGSHGQTVRHRPGEGF--------TLQIGDGALIAELTGITVVADFRRRDVAAGGQGAPLVPAFHQA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 178 LYSDTSIDRVLLNIGGISNLTYLPQNcaltQSMCS--DIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLS 255
Cdd:PRK09585 153 LFGHPDETRAVLNIGGIANITLLPPG----GGPVIgfDTGPGNALIDAWIQRHGGKPYDKDGAWAASGKVDEALLARLLA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 256 HEFFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIES 335
Cdd:PRK09585 229 HPYFALPPPKSTGRELFNLAWLERQLAGFGLSPEDVQATLTELTAASIARAVRRLPPGPDELLVCGGGARNPTLMERLAA 308
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 498064520 336 HLNNRVLIKDfsQLGINPDAKEAALFALLANETVSG 371
Cdd:PRK09585 309 LLPTEVATTD--ALGIDGDAKEALAFAWLAVRTLRG 342
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
18-377 9.86e-101

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: 303.15  E-value: 9.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520   18 YILGLMSGTSLDGLDIALCKIEGvgKNTQLTVEQFTTieYNSSQKQLLSDHASKSQVNLKTLCQLNAWLGELYASLINNA 97
Cdd:pfam03702   2 RYIGLMSGTSLDGVDAALVDLDD--ARVELLASHFSP--MPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520   98 LAEWQVAADTVDLIASHGQTLYHCPKQAFAdienlnSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPLVQYGDYL 177
Cdd:pfam03702  78 LQKQNLSPEQIRAIGCHGQTVRHEPEGAVP------FTMQLGDANLIAERTGITVVADFRRRDVAAGGQGAPLVPAFHEA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  178 LYSDTSIDRVLLNIGGISNLTYLPQNCALtqsMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLPFLEALLSHE 257
Cdd:pfam03702 152 LFAAPNETRAVLNIGGIANVSVLPPGAPV---LGFDTGPGNMLMDAWIQKHRGEPYDKDGEWAASGKVNPALLAVLLADP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  258 FFDIPLPKSTGQELFNQTFVHHALDGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNVFLMERIESHL 337
Cdd:pfam03702 229 YFALPAPKSTGRELFNLPWLETHLAKHPVAAADVQATLAELTAVTIVDALLQAQPDCERLLVCGGGARNPLLMARLAALL 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 498064520  338 NNrVLIKDFSQLGINPDAKEAALFALLANETVSGDGDALP 377
Cdd:pfam03702 309 PG-VQVASTDAYGLDPDYMEAMAFAWLAARTLNGLPGNLP 347
ASKHA_NBD_LGK cd24051
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
19-384 4.87e-67

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: 217.80  E-value: 4.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  19 ILGLMSGTSLDGLDIALCKIegvgknTQLTVE---QFTTIEYN-----SSQKQLLSDHASKSQVNLKTLCQLNAWLGELY 90
Cdd:cd24051    3 VLGLNSGTSMDGIDCALCHF------TQKTPDapmEFELIEYGevplaQPIKQRVMSMILEDTTSPSELSEVNVILGETF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  91 ASLINNALAEWQVAADTVDLIASHGQTLYHcpkQAFADIENLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGAPL 170
Cdd:cd24051   77 ADAVRQFAAERNVDLSDIDAIASHGQTIWL---LSMPEEGQVKSALTMGEGAIIAARTGITSVTDFRISDQAAGRQGAPL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 171 VQYGDYLLYSDTSIDRVLLNIGGISNLTYLPQNCALTQSMCS--DIGPGNTLVDQYCRH-VLGLP-FDENGEIASSGKIQ 246
Cdd:cd24051  154 IAFFDALLLHHPTKLRACQNIGGIANVCFIPPDNDGRTDEYYdfDTGPGNVFIDAVVRHfTNGEQeYDKDGAMGKRGKVD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 247 LPFLEALLSHEFFDIPLPKSTGQELFNQTFVHHAL---DGKDYNHEDIITTLTEFTAITIANAVNKLSTAE--LELYVSG 321
Cdd:cd24051  234 QELVDDFLKMPYFQLDPPKTTGREVFRDTLAHDLIrraEAKGLSPDDIVATTTRITAQSIVDHYRRYAPSQeiDEIFMCG 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498064520 322 GGIHNVFLMERIESHLNNRVLIKdFSQLGINPDAKEAALFALLANETVSGDGDALP--------FSMGKIS 384
Cdd:cd24051  314 GGAFNPNIVEFIQQSYPGTKIMM-LDEAGVPAGAKEAITFAWQGMEALVGRSIPVPtrvetrqhTVLGKVS 383
ASKHA_NBD_ANMK-like cd24005
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
19-384 4.03e-52

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: 177.60  E-value: 4.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  19 ILGLMSGTSLDGLDIALCKIegvgkntqltVEQFTTIEYNSS----------QKQLLSDHASKSQvnlktLCQLNAWLGE 88
Cdd:cd24005    1 YLGLMSGTSLDGMDIVLIEQ----------GDRTTLLASHYLpmpaglrediLALCVPGPDEIAR-----AAEVEQRWVA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520  89 LYASLINNALAEWQVAADTVDLIASHGQTLYHcpkqafadIENLNSTLQIVDADIIATKTNIITIADFRQKHIAKGYEGA 168
Cdd:cd24005   66 LAAQGVRELLLQQQMSPDEVRAIGSHGQTIRH--------EPARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 169 PLVQYGDYLLYSDTSIDRVLLNIGGISNLTYLPQNcalTQSMCSDIGPGNTLVDQYCRHVLGLPFDENGEIASSGKIQLP 248
Cdd:cd24005  138 PLVPAFHQALFGDDDTSRAVLNIGGFSNVSLLSPG---KPVRGFDCGPGNVLMDAWIHHQRGEHFDRDGAWAASGQVNHA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498064520 249 FLEALLSHEFFDIPLPKSTGQELFNQTFVHHAL-DGKDYNHEDIITTLTEFTAITIANAVNKLSTAELELYVSGGGIHNV 327
Cdd:cd24005  215 LLASLLADEFFAARGPKSTGRERFNLPWLQEHLaRHPALPAADIQATLLELSARSISESLLDAQPDCEEVLVCGGGAFNT 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498064520 328 FLMERI-ESHLNNRVLIKDfsQLGINPDAKEAALFALLANETVSGDGDALP--------FSMGKIS 384
Cdd:cd24005  295 ALMKRLaMLMPEARVASTD--EYGIPPAWMEGMAFAWLAHRFLERLPGNCPdvtgalgpRTLGALY 358
 
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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