NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|763713103|gb|AJQ30936|]
View 

UDP-N-acetylmuramoylalanyl-D-glutamate--L-lysine ligase, partial [Leuconostoc mesenteroides]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK14022 super family cl36326
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
1-156 3.06e-22

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


The actual alignment was detected with superfamily member PRK14022:

Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 91.64  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   1 LDHSDEVIVNAETDHFDTIYTYAKKTHHKVYtysrqmftseesAIHESRFIVVKSEFN-----EMLGSYRLNVPGDFNES 75
Cdd:PRK14022 232 MENSKAVVVNSDMDHFSELLEQVTPQEHDFY------------GIDSENQIMASNAFSfeatgKLAGTYDIQLIGKFNQE 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103  76 NAMAAMMLVSFAGVKHQAMVKGLDEVFIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNK 155
Cdd:PRK14022 300 NAMAAGLACLRLGASLEDIQKGIAQTPVPGRMEVLTQSNGAKVFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGAAGNK 378


                 .
gi 763713103 156 G 156
Cdd:PRK14022 379 G 379
 
Name Accession Description Interval E-value
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
1-156 3.06e-22

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 91.64  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   1 LDHSDEVIVNAETDHFDTIYTYAKKTHHKVYtysrqmftseesAIHESRFIVVKSEFN-----EMLGSYRLNVPGDFNES 75
Cdd:PRK14022 232 MENSKAVVVNSDMDHFSELLEQVTPQEHDFY------------GIDSENQIMASNAFSfeatgKLAGTYDIQLIGKFNQE 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103  76 NAMAAMMLVSFAGVKHQAMVKGLDEVFIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNK 155
Cdd:PRK14022 300 NAMAAGLACLRLGASLEDIQKGIAQTPVPGRMEVLTQSNGAKVFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGAAGNK 378


                 .
gi 763713103 156 G 156
Cdd:PRK14022 379 G 379
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 8-155 1.03e-20

UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440532 [Multi-domain]  Cd Length: 459  Bit Score: 87.06  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   8 IVNAETDHFDTIytyAKKTHHKVYTYSRQ-----MFTSEESAIHESRFiVVKSEFNEMlgSYRLNVPGDFNESNAMAAMM 82
Cdd:COG0769  210 VINADDPYGRRL---AAAAPARVITYGLKadadlRATDIELSADGTRF-TLVTPGGEV--EVRLPLIGRFNVYNALAAIA 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763713103  83 LVSFAGVKHQAMVKGLDEV-FIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNK 155
Cdd:COG0769  284 AALALGIDLEEILAALEKLkGVPGRMERVDGGQGPTVIVDYAHTPDALENVLEALR-PHTKGRLIVVFGCGGDR 356
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 56-155 4.15e-09

UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273435 [Multi-domain]  Cd Length: 464  Bit Score: 53.86  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   56 EFNEMLGSYRLNVPGDFNESNAMAAMMLV-SFAGVKHQAMVKGLDEVF-IPGRMLSLPINGHGVAFVDYAHNFVSMQALL 133
Cdd:TIGR01085 270 ETPAGEGHLHTPLIGRFNVYNLLAALATLlHLGGIDLEDIVAALEKFRgVPGRMELVDGGQKFLVIVDYAHTPDALEKAL 349

                          90       100
                  ....*....|....*....|..
gi 763713103  134 SFAQAqYPNGRVLVVVGSPGNK 155
Cdd:TIGR01085 350 RTLRK-HKDGRLIVVFGCGGDR 370
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 103-156 1.37e-07

Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.


Pssm-ID: 460731 [Multi-domain]  Cd Length: 87  Bit Score: 46.57  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 763713103  103 IPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAqAQYPNGRVLVVVGSPGNKG 156
Cdd:pfam02875   1 VPGRLEVVGENNGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRD 53
 
Name Accession Description Interval E-value
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
1-156 3.06e-22

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 91.64  E-value: 3.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   1 LDHSDEVIVNAETDHFDTIYTYAKKTHHKVYtysrqmftseesAIHESRFIVVKSEFN-----EMLGSYRLNVPGDFNES 75
Cdd:PRK14022 232 MENSKAVVVNSDMDHFSELLEQVTPQEHDFY------------GIDSENQIMASNAFSfeatgKLAGTYDIQLIGKFNQE 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103  76 NAMAAMMLVSFAGVKHQAMVKGLDEVFIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNK 155
Cdd:PRK14022 300 NAMAAGLACLRLGASLEDIQKGIAQTPVPGRMEVLTQSNGAKVFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGAAGNK 378


                 .
gi 763713103 156 G 156
Cdd:PRK14022 379 G 379
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 8-155 1.03e-20

UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440532 [Multi-domain]  Cd Length: 459  Bit Score: 87.06  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   8 IVNAETDHFDTIytyAKKTHHKVYTYSRQ-----MFTSEESAIHESRFiVVKSEFNEMlgSYRLNVPGDFNESNAMAAMM 82
Cdd:COG0769  210 VINADDPYGRRL---AAAAPARVITYGLKadadlRATDIELSADGTRF-TLVTPGGEV--EVRLPLIGRFNVYNALAAIA 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763713103  83 LVSFAGVKHQAMVKGLDEV-FIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNK 155
Cdd:COG0769  284 AALALGIDLEEILAALEKLkGVPGRMERVDGGQGPTVIVDYAHTPDALENVLEALR-PHTKGRLIVVFGCGGDR 356
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 8-156 1.55e-20

UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 86.72  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   8 IVNAETDHFDTIYTYAKkthhkVYTYSRQ----MFTSEESAIHESRFIVVksefnemlGSYRLNVPGDFNESNAMAAMML 83
Cdd:PRK00139 223 VINADDEVGRRLLALPD-----AYAVSMAgadlRATDVEYTDSGQTFTLV--------TEVESPLIGRFNVSNLLAALAA 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763713103  84 VSFAGVKHQAMVKGLDEV-FIPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAQaQYPNGRVLVVVGSPGNKG 156
Cdd:PRK00139 290 LLALGVPLEDALAALAKLqGVPGRMERVDAGQGPLVIVDYAHTPDALEKVLEALR-PHAKGRLICVFGCGGDRD 362
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 7-148 7.43e-11

UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440536 [Multi-domain]  Cd Length: 451  Bit Score: 58.92  E-value: 7.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   7 VIVNAETDHFDTIytyAKKTHHKVYTYSrqmfTSEESAIH---------ESRFIVVKSefNEMLGSYRLNVPGDFNESNA 77
Cdd:COG0773  211 LVLCADDPGLREL---LPRCGRPVITYG----FSEDADYRaeniridggGSTFDVLRR--GEELGEVELNLPGRHNVLNA 281

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763713103  78 MAAMMLVSFAGVKHQAMVKGLDEvFI-PGRMLSLPINGHGVAFV-DYAHNFVSMQALLSFAQAQYPNGRVLVV 148
Cdd:COG0773  282 LAAIAVALELGVDPEAIAEALAS-FKgVKRRFELKGEVGGVTVIdDYAHHPTEIAATLAAAREKYPDRRLVAV 353
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 7-150 1.38e-09

UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440533 [Multi-domain]  Cd Length: 451  Bit Score: 55.11  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   7 VIVNAETDHFDTIytyAKKTHHKVYTYSRQ-----MFTSEESAIHESRFIVVKSEFNEmlgSYRLNVPGDFNESNAMAAM 81
Cdd:COG0770  215 AVLNADDPLLAAL---AERAKARVLTFGLSedadvRAEDIELDEDGTRFTLHTPGGEL---EVTLPLPGRHNVSNALAAA 288

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763713103  82 MLVSFAGVKHQAMVKGLDEV-FIPGRMLSLPInGHGVAFVD--Y-AhNFVSMQALLSFAQAQYPNGRVLVVVG 150
Cdd:COG0770  289 AVALALGLDLEEIAAGLAAFqPVKGRLEVIEG-AGGVTLIDdsYnA-NPDSMKAALDVLAQLPGGGRRIAVLG 359
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 56-155 4.15e-09

UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273435 [Multi-domain]  Cd Length: 464  Bit Score: 53.86  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103   56 EFNEMLGSYRLNVPGDFNESNAMAAMMLV-SFAGVKHQAMVKGLDEVF-IPGRMLSLPINGHGVAFVDYAHNFVSMQALL 133
Cdd:TIGR01085 270 ETPAGEGHLHTPLIGRFNVYNLLAALATLlHLGGIDLEDIVAALEKFRgVPGRMELVDGGQKFLVIVDYAHTPDALEKAL 349

                          90       100
                  ....*....|....*....|..
gi 763713103  134 SFAQAqYPNGRVLVVVGSPGNK 155
Cdd:TIGR01085 350 RTLRK-HKDGRLIVVFGCGGDR 370
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 63-155 6.35e-09

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 53.55  E-value: 6.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103  63 SYRLNVPGDFNESNAMAAMMLVSFAGVKHQAMVKGLDEVF-IPGRMLSLPINGHG---VAFVDYAHN----FVSMQALLS 134
Cdd:PRK11929 298 QLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSpVPGRMERVGPTAGAqgpLVVVDYAHTpdalAKALTALRP 377

                         90       100
                 ....*....|....*....|.
gi 763713103 135 FAQAQypNGRVLVVVGSPGNK 155
Cdd:PRK11929 378 VAQAR--NGRLVCVFGCGGDR 396
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 103-156 1.37e-07

Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.


Pssm-ID: 460731 [Multi-domain]  Cd Length: 87  Bit Score: 46.57  E-value: 1.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 763713103  103 IPGRMLSLPINGHGVAFVDYAHNFVSMQALLSFAqAQYPNGRVLVVVGSPGNKG 156
Cdd:pfam02875   1 VPGRLEVVGENNGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRD 53
Mur_ligase_M pfam08245
Mur ligase middle domain;
7-81 2.09e-05

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 42.68  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103    7 VIVNAETDHFDTIYTYAKKTHHKVYTYSrqmfTSEESAIHESRFIVVKSE-------FNEMLGSYRLNVPGDFNESNAMA 79
Cdd:pfam08245 119 AVINADDPYGAFLIAKLKKAGVRVITYG----IEGEADLRAANIELSSDGtsfdlftVPGGELEIEIPLLGRHNVYNALA 194


                  ..
gi 763713103   80 AM 81
Cdd:pfam08245 195 AI 196
murF PRK10773
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
 66-148 4.93e-04

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed


Pssm-ID: 182718 [Multi-domain]  Cd Length: 453  Bit Score: 39.24  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763713103  66 LNVPGDFNESNAMAAMMLVSFAGVKHQAMVKGLDEV-FIPGRMLSLPINGHGVAFVD-YAHNFVSMQALlsfAQ--AQYP 141
Cdd:PRK10773 276 LPLPGRHNIANALAAAALAMSVGATLDAVKAGLANLkAVPGRLFPIQLAEGQLLLDDsYNANVGSMTAA---AQvlAEMP 352


                 ....*..
gi 763713103 142 NGRVLVV 148
Cdd:PRK10773 353 GYRVMVV 359
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH