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Conserved domains on  [gi|1861590434|ref|WP_176193342|]
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anhydro-N-acetylmuramic acid kinase, partial [Salmonella enterica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AnmK super family cl22918
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
 2-98 1.31e-44

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.


The actual alignment was detected with superfamily member pfam03702:

Pssm-ID: 473993  Cd Length: 364  Bit Score: 147.53  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPRD 81
Cdd:pfam03702   8 SGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQKQNLSPEQ 87

                          90
                  ....*....|....*..
gi 1861590434  82 IVAIGCHGQTVWHEPTG 98
Cdd:pfam03702  88 IRAIGCHGQTVRHEPEG 104
 
Name Accession Description Interval E-value
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
 2-98 1.31e-44

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: 147.53  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPRD 81
Cdd:pfam03702   8 SGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQKQNLSPEQ 87

                          90
                  ....*....|....*..
gi 1861590434  82 IVAIGCHGQTVWHEPTG 98
Cdd:pfam03702  88 IRAIGCHGQTVRHEPEG 104
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
 2-96 6.07e-42

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 140.26  E-value: 6.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETM--VAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQP 79
Cdd:PRK09585    9 SGTSLDGVDAALVEIDGEGtkVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNALLAEAGLSP 88

                          90
                  ....*....|....*..
gi 1861590434  80 RDIVAIGCHGQTVWHEP 96
Cdd:PRK09585   89 EDIDAIGSHGQTVRHRP 105
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
 2-99 1.49e-40

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: 136.89  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETM----VAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRL 77
Cdd:cd24050     6 SGTSLDGIDAALVEIDGDGtelrVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELLAKSGI 85

                          90       100
                  ....*....|....*....|..
gi 1861590434  78 QPRDIVAIGCHGQTVWHEPTGE 99
Cdd:cd24050    86 SPSDIDAIGSHGQTVWHRPEPE 107
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-96 1.51e-39

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


Pssm-ID: 441944  Cd Length: 363  Bit Score: 134.04  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAID-ETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPR 80
Cdd:COG2377    10 SGTSLDGIDAALVEFDgEGKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAVLALLAKAGLSAE 89

                          90
                  ....*....|....*.
gi 1861590434  81 DIVAIGCHGQTVWHEP 96
Cdd:COG2377    90 DIDAIGSHGQTVRHRP 105
 
Name Accession Description Interval E-value
AnmK pfam03702
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
 2-98 1.31e-44

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: 147.53  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPRD 81
Cdd:pfam03702   8 SGTSLDGVDAALVDLDDARVELLASHFSPMPAGLRQQLLDLCQGGATTLQRLGELDHQLGLLFADAVNALLQKQNLSPEQ 87

                          90
                  ....*....|....*..
gi 1861590434  82 IVAIGCHGQTVWHEPTG 98
Cdd:pfam03702  88 IRAIGCHGQTVRHEPEG 104
anmK PRK09585
anhydro-N-acetylmuramic acid kinase; Reviewed
 2-96 6.07e-42

anhydro-N-acetylmuramic acid kinase; Reviewed


Pssm-ID: 236579  Cd Length: 365  Bit Score: 140.26  E-value: 6.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETM--VAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQP 79
Cdd:PRK09585    9 SGTSLDGVDAALVEIDGEGtkVELLASATVPYPDELRAALLALLQGGADELERLAELDTALGRLFAEAVNALLAEAGLSP 88

                          90
                  ....*....|....*..
gi 1861590434  80 RDIVAIGCHGQTVWHEP 96
Cdd:PRK09585   89 EDIDAIGSHGQTVRHRP 105
ASKHA_NBD_ANMK cd24050
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
 2-99 1.49e-40

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: 136.89  E-value: 1.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAIDETM----VAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRL 77
Cdd:cd24050     6 SGTSLDGIDAALVEIDGDGtelrVKLLAFHSVPYPKDLREKLLELCQPGTDTLDELCRLNFELGELFAEAVLELLAKSGI 85

                          90       100
                  ....*....|....*....|..
gi 1861590434  78 QPRDIVAIGCHGQTVWHEPTGE 99
Cdd:cd24050    86 SPSDIDAIGSHGQTVWHRPEPE 107
AnmK COG2377
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
2-96 1.51e-39

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


Pssm-ID: 441944  Cd Length: 363  Bit Score: 134.04  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAID-ETMVAQQASLTWPIPVHLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQPR 80
Cdd:COG2377    10 SGTSLDGIDAALVEFDgEGKVELLAAETVPYPEELRARLLALCAPASLSLEELAELDRALGRLFAEAVLALLAKAGLSAE 89

                          90
                  ....*....|....*.
gi 1861590434  81 DIVAIGCHGQTVWHEP 96
Cdd:COG2377    90 DIDAIGSHGQTVRHRP 105
ASKHA_NBD_LGK cd24051
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
 2-100 4.44e-14

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: 66.03  E-value: 4.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAI-----DETM---VAQQASLTWPIPvhLKKGILDICQGQPLTLSQLGQLDTQLGRLFAQAVNALLA 73
Cdd:cd24051     8 SGTSMDGIDCALCHFtqktpDAPMefeLIEYGEVPLAQP--IKQRVMSMILEDTTSPSELSEVNVILGETFADAVRQFAA 85

                          90       100
                  ....*....|....*....|....*..
gi 1861590434  74 QQRLQPRDIVAIGCHGQTVWHEPTGES 100
Cdd:cd24051    86 ERNVDLSDIDAIASHGQTIWLLSMPEE 112
ASKHA_NBD_ANMK-like cd24005
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
 2-93 1.89e-07

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: 47.01  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861590434   2 SGTSLDGVDVVLAAID---ETMVAQQASLTWPIPVHLKKGILDicqgQPLTLSQLGQLDTQLGRLFAQAVNALLAQQRLQ 78
Cdd:cd24005     6 SGTSLDGMDIVLIEQGdrtTLLASHYLPMPAGLREDILALCVP----GPDEIARAAEVEQRWVALAAQGVRELLLQQQMS 81

                          90
                  ....*....|....*
gi 1861590434  79 PRDIVAIGCHGQTVW 93
Cdd:cd24005    82 PDEVRAIGSHGQTIR 96
 
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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