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Conserved domains on  [gi|311351508|gb|ADP92939|]
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D-alanine-D-alanine ligase, partial [Clostridium perfringens]

Protein Classification

D-alanine--D-alanine ligase( domain architecture ID 1000119)

D-alanine--D-alanine ligase catalyzes the synthesis of D-alanyl-D-alanine, an essential component of bacterial peptidoglycan, and is involved in cell wall formation

EC:  6.3.2.4
Gene Ontology:  GO:0009252|GO:0008716|GO:0046872|GO:0005524
SCOP:  4002041|4003870

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ddl super family cl35154
D-alanine--D-alanine ligase; Reviewed
 1-196 1.54e-95

D-alanine--D-alanine ligase; Reviewed


The actual alignment was detected with superfamily member PRK01372:

Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 279.69  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSvDEIDYEKIENLGYPVFIKPNNGGSSVATT 80
Cdd:PRK01372  72 GTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTR-EEDLLAAIDKLGLPLVVKPAREGSSVGVS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  81 LVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGKMLPVLAIKPKGKFFDIASKYEDGGADEFIV-KLNEDLHK 159
Cdd:PRK01372 151 KVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPaGLPAEIEA 230

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 311351508 160 EVEKMALETYKLLKCDVYARVDMLVKD-NIPYVLEVNT 196
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFMLDEdGKPYLLEVNT 268
 
Name Accession Description Interval E-value
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 1-196 1.54e-95

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 279.69  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSvDEIDYEKIENLGYPVFIKPNNGGSSVATT 80
Cdd:PRK01372  72 GTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTR-EEDLLAAIDKLGLPLVVKPAREGSSVGVS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  81 LVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGKMLPVLAIKPKGKFFDIASKYEDGGADEFIV-KLNEDLHK 159
Cdd:PRK01372 151 KVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPaGLPAEIEA 230

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 311351508 160 EVEKMALETYKLLKCDVYARVDMLVKD-NIPYVLEVNT 196
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFMLDEdGKPYLLEVNT 268
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 1-196 1.82e-83

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 249.25  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIDYEKIE-NLGYPVFIKPNNGGSSVAT 79
Cdd:COG1181   69 GTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEeELGLPLFVKPAREGSSVGV 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  80 TLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGK---MLPVLAIKPKGKFFDIASKYEDGGADEFI-VKLNE 155
Cdd:COG1181  149 SKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGgprALPPIEIVPENGFYDYEAKYTDGGTEYICpARLPE 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311351508 156 DLHKEVEKMALETYKLLKCDVYARVDMLV-KDNIPYVLEVNT 196
Cdd:COG1181  229 ELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 1-196 1.02e-59

D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273498 [Multi-domain]  Cd Length: 315  Bit Score: 189.03  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508    1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMV-----SSVDEIDYEKIENLGYPVFIKPNNGGS 75
Cdd:TIGR01205  79 GTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLtqnraSADELECEQVAEPLGFPVIVKPAREGS 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   76 SVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIID-GKMLPVLAIKPKG-KFFDIASKYEDGGADEFI-VK 152
Cdd:TIGR01205 159 SVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGnEEALPIIEIVPEIeGFYDYEAKYLDGSTEYVIpAP 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 311351508  153 LNEDLHKEVEKMALETYKLLKCDVYARVD-MLVKDNIPYVLEVNT 196
Cdd:TIGR01205 239 LDEELEEKIKELALKAYKALGCRGLARVDfFLDEEGEIYLNEINT 283
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 34-196 3.95e-41

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 137.83  E-value: 3.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   34 ILAFGNVRTARWVMvsSVDEIDYEKIENLGYPVFIKPNNGGSSVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEI 113
Cdd:pfam07478   9 VVPFVTFTRADWKL--NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIEGREI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  114 TCPII---DGKMLPVLAIKPKGKFFDIASKYEDGGADEFI-VKLNEDLHKEVEKMALETYKLLKCDVYARVD-MLVKDNI 188
Cdd:pfam07478  87 ECAVLgneDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVpADLEEEQEEQIQELALKAYKALGCRGLARVDfFLTEDGE 166


                  ....*...
gi 311351508  189 PYVLEVNT 196
Cdd:pfam07478 167 IVLNEVNT 174
 
Name Accession Description Interval E-value
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 1-196 1.54e-95

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 279.69  E-value: 1.54e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSvDEIDYEKIENLGYPVFIKPNNGGSSVATT 80
Cdd:PRK01372  72 GTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTR-EEDLLAAIDKLGLPLVVKPAREGSSVGVS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  81 LVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGKMLPVLAIKPKGKFFDIASKYEDGGADEFIV-KLNEDLHK 159
Cdd:PRK01372 151 KVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGGKALPVIEIVPAGEFYDYEAKYLAGGTQYICPaGLPAEIEA 230

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 311351508 160 EVEKMALETYKLLKCDVYARVDMLVKD-NIPYVLEVNT 196
Cdd:PRK01372 231 ELQELALKAYRALGCRGWGRVDFMLDEdGKPYLLEVNT 268
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 1-196 1.82e-83

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 249.25  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIDYEKIE-NLGYPVFIKPNNGGSSVAT 79
Cdd:COG1181   69 GTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEeELGLPLFVKPAREGSSVGV 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  80 TLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGK---MLPVLAIKPKGKFFDIASKYEDGGADEFI-VKLNE 155
Cdd:COG1181  149 SKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGgprALPPIEIVPENGFYDYEAKYTDGGTEYICpARLPE 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311351508 156 DLHKEVEKMALETYKLLKCDVYARVDMLV-KDNIPYVLEVNT 196
Cdd:COG1181  229 ELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
ddl PRK01966
D-alanine--D-alanine ligase;
1-196 7.63e-61

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 192.26  E-value: 7.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMV--SSVDEIDYEKIEN-LGYPVFIKPNNGGSSV 77
Cdd:PRK01966  97 GTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLtrGDWEEASLAEIEAkLGLPVFVKPANLGSSV 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  78 ATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPII--DGKMLPVLAIKPKGKFFDIASKYEDGGADEFI-VKLN 154
Cdd:PRK01966 177 GISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLgnDPKASVPGEIVKPDDFYDYEAKYLDGSAELIIpADLS 256

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 311351508 155 EDLHKEVEKMALETYKLLKCDVYARVDMLV-KDNIPYVLEVNT 196
Cdd:PRK01966 257 EELTEKIRELAIKAFKALGCSGLARVDFFLtEDGEIYLNEINT 299
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 1-196 1.02e-59

D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273498 [Multi-domain]  Cd Length: 315  Bit Score: 189.03  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508    1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMV-----SSVDEIDYEKIENLGYPVFIKPNNGGS 75
Cdd:TIGR01205  79 GTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLtqnraSADELECEQVAEPLGFPVIVKPAREGS 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   76 SVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIID-GKMLPVLAIKPKG-KFFDIASKYEDGGADEFI-VK 152
Cdd:TIGR01205 159 SVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGnEEALPIIEIVPEIeGFYDYEAKYLDGSTEYVIpAP 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 311351508  153 LNEDLHKEVEKMALETYKLLKCDVYARVD-MLVKDNIPYVLEVNT 196
Cdd:TIGR01205 239 LDEELEEKIKELALKAYKALGCRGLARVDfFLDEEGEIYLNEINT 283
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 1-196 2.64e-43

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 146.51  E-value: 2.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAfGNVRTARWVMVSsvdeiDYEKIENLGYPVFIKPNNGGSSVATT 80
Cdd:PRK14571  69 GTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLK-GTVEIPDFVEIK-----EFMKTSPLGYPCVVKPRREGSSIGVF 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  81 LVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDG----KMLPVLAIKPKGKFFDIASKYEDgGADEFIV--KLN 154
Cdd:PRK14571 143 ICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILETekgfEVLPILELRPKRRFYDYVAKYTK-GETEFILpaPLN 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 311351508 155 EDLHKEVEKMALETYKLLKCDVYARVDMLVKDNIPYVLEVNT 196
Cdd:PRK14571 222 PEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEINT 263
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 34-196 3.95e-41

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 137.83  E-value: 3.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   34 ILAFGNVRTARWVMvsSVDEIDYEKIENLGYPVFIKPNNGGSSVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEI 113
Cdd:pfam07478   9 VVPFVTFTRADWKL--NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIEGREI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  114 TCPII---DGKMLPVLAIKPKGKFFDIASKYEDGGADEFI-VKLNEDLHKEVEKMALETYKLLKCDVYARVD-MLVKDNI 188
Cdd:pfam07478  87 ECAVLgneDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVpADLEEEQEEQIQELALKAYKALGCRGLARVDfFLTEDGE 166


                  ....*...
gi 311351508  189 PYVLEVNT 196
Cdd:pfam07478 167 IVLNEVNT 174
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 1-196 2.33e-39

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 137.34  E-value: 2.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVmvsSVDEIDYE--------KIENLGYPVFIKPNN 72
Cdd:PRK14572 104 GRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFF---ELEKLKYLnsprktllKLESLGFPQFLKPVE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  73 GGSSVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPII----DGKM----LPVLAIKPKGKFFDIASKYEDG 144
Cdd:PRK14572 181 GGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLeryrGGKRnpiaLPATEIVPGGEFFDFESKYKQG 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311351508 145 GADEFI-VKLNEDLHKEVEKMALETYKLLKCDVYARVDMLVKDNIPYVLEVNT 196
Cdd:PRK14572 261 GSEEITpARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEPHILETNT 313
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
 1-196 2.08e-27

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 104.76  E-value: 2.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRT--ARWVMVSSVDEidyekiENLGYPVFIKPNNGGSSVA 78
Cdd:PRK14569  72 GRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTpmAKFLTDKLVAE------DEISFPVAVKPSSGGSSIA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  79 TTLVESKEAVKDAVLEALKYDtEVMIEEYIKGDEITCPIIDGKMLPVLAIKPKGKFFDIASKYEDGGADEFIVKLNEDLH 158
Cdd:PRK14569 146 TFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDEVYSSVWIEPQNEFYDYESKYSGKSIYHSPSGLCEQKE 224

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 311351508 159 KEVEKMALETYKLLKCDVYARVDMLVKDNIP-YVLEVNT 196
Cdd:PRK14569 225 LEVRQLAKKAYDLLGCSGHARVDFIYDDRGNfYIMEINS 263
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 19-195 1.99e-22

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 91.54  E-value: 1.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  19 PLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVFIKPNNGGSSVATTLVESKEAVKdAVLEALK- 97
Cdd:COG0189   88 PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLR-AFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-SILEALTe 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  98 -YDTEVMIEEYI---KGDEITCPIIDGKmlPVLAIKPKGKFFDIASKYEDGGADEFIvklneDLHKEVEKMALETYKLLK 173
Cdd:COG0189  166 lGSEPVLVQEFIpeeDGRDIRVLVVGGE--PVAAIRRIPAEGEFRTNLARGGRAEPV-----ELTDEERELALRAAPALG 238

                        170       180
                 ....*....|....*....|..
gi 311351508 174 CDvYARVDMLVKDNIPYVLEVN 195
Cdd:COG0189  239 LD-FAGVDLIEDDDGPLVLEVN 259
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 10-196 1.75e-21

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 88.39  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  10 LGIPfsGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVFIKPNNGGSSVATTLVESKEAVK 89
Cdd:COG0439   39 LGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL-AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  90 DAVLEALKY------DTEVMIEEYIKGDEITCPII--DGKMLpVLAI---KPKGKFFdiaskYEDGGadEFIVKLNEDLH 158
Cdd:COG0439  116 AALAEARAEakagspNGEVLVEEFLEGREYSVEGLvrDGEVV-VCSItrkHQKPPYF-----VELGH--EAPSPLPEELR 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 311351508 159 KEVEKMALETYKLLKcdvYAR----VDMLV-KDNIPYVLEVNT 196
Cdd:COG0439  188 AEIGELVARALRALG---YRRgafhTEFLLtPDGEPYLIEINA 227
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 1-196 1.83e-19

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 84.50  E-value: 1.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEI-DYEKI-----ENLGYPVFIKPNNGG 74
Cdd:PRK14570 103 GAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKYDYFlDKEGIkkdikEVLGYPVIVKPAVLG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  75 SSVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGDEITCPIIDGKMLPVLA----IKPKGKFFDIASKYEDGGADEFI 150
Cdd:PRK14570 183 SSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKIFTpgeiVVQDFIFYDYDAKYSTIPGNSIV 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 311351508 151 VKLNEDLHK----EVEKMALETYKLLKCDVYARVDMLV--KDNIPYVLEVNT 196
Cdd:PRK14570 263 FNIPAHLDTkhllDIKEYAFLTYKNLELRGMARIDFLIekDTGLIYLNEINT 314
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 16-195 1.07e-18

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 81.85  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  16 GCGPLSS-----AICMDKDMTKRILAFGNVRTARWVMVSSVDEIDYE-KIENLGYPVFIKPNNGGSSVATTLVESKEAVK 89
Cdd:PRK12767  95 GVKVLVSskeviEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlAKGELQFPLFVKPRDGSASIGVFKVNDKEELE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  90 DavleALKYDTEVMIEEYIKGDEITCPII---DGKmlpVLAIKPKGKFFDIAskyedGGADEFIVKLNEDLHKEVEKMAl 166
Cdd:PRK12767 175 F----LLEYVPNLIIQEFIEGQEYTVDVLcdlNGE---VISIVPRKRIEVRA-----GETSKGVTVKDPELFKLAERLA- 241

                        170       180
                 ....*....|....*....|....*....
gi 311351508 167 etyKLLKCDVYARVDMLVKDNIPYVLEVN 195
Cdd:PRK12767 242 ---EALGARGPLNIQCFVTDGEPYLFEIN 267
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
1-195 8.22e-18

bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 80.63  E-value: 8.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   1 GTVQSVLKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVS------SVDEIDYEKIENLGYPVFIKPNNGG 74
Cdd:PRK14573 542 GTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPLTlagwkrEPELCLAHIVEAFSFPMFVKTAHLG 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  75 SSVATTLVESKEAVKDAVLEALKYDTEVMIEEYIKGD---EITCpIIDGKMLPVLAiKP-----KGKFFDIASKYEDGGA 146
Cdd:PRK14573 622 SSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGSreiEVSC-LGDGSSAYVIA-GPherrgSGGFIDYQEKYGLSGK 699

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 311351508 147 D----EFIVKLNEDLHKEVEKMALETYKLLKCDVYARVDMLVKDNIPYVL-EVN 195
Cdd:PRK14573 700 SsaqiVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLsEMN 753
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 21-122 4.22e-14

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 69.80  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  21 SSAI-----CmDKDMTKRILAFGNVRTARWVMVSSVDEIdYEKIENLGYPVFIKPNNG--GSSVATTLvESKEAVKDAVL 93
Cdd:PRK14016 204 TSAIavdiaC-DKELTKRLLAAAGVPVPEGRVVTSAEDA-WEAAEEIGYPVVVKPLDGnhGRGVTVNI-TTREEIEAAYA 280

                         90       100
                 ....*....|....*....|....*....
gi 311351508  94 EALKYDTEVMIEEYIKGDEITCPIIDGKM 122
Cdd:PRK14016 281 VASKESSDVIVERYIPGKDHRLLVVGGKL 309
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 21-195 7.77e-10

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 56.59  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   21 SSAI--CMDKDMTKRILAFGNVRTARWVMVSSVDEIDYeKIENLGYPVFIKPNNGGSSVATTLVESKEAVKdAVLEALKY 98
Cdd:TIGR00768  80 SDAIlnAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALK-LIEEIGFPVVLKPVFGSWGRGVSLARDRQAAE-SLLEHFEQ 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   99 ---DTEVM-IEEYIK---GDEITCPIIDGKMLPVLAIKPKGKFfdiASKYEDGGADEFIvklneDLHKEVEKMALETYKL 171
Cdd:TIGR00768 158 lngPQNLFlVQEYIKkpgGRDIRVFVVGDEVVAAIYRITSGHW---RSNLARGGKAEPC-----SLTEEIEELAIKAAKA 229

                         170       180
                  ....*....|....*....|....
gi 311351508  172 LKCDvYARVDMLVKDNIPYVLEVN 195
Cdd:TIGR00768 230 LGLD-VAGVDLLESEDGLLVNEVN 252
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
28-126 5.55e-09

bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 54.93  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  28 KDMTKRILAFGNVRTARWVMVSSVDEI--DYEKIENlgYPVFIKP---NNG-GSSVATTlVESKEAVKDAVLEALKYDTE 101
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEAlaDYSLFAD--KAIVVKPkstNFGlGISIFKE-PASLEDYEKALEIAFREDSS 565

                         90       100
                 ....*....|....*....|....*
gi 311351508 102 VMIEEYIKGDEITCPIIDGKMLPVL 126
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVLDGKVEAVL 590
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 27-125 1.41e-08

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).


Pssm-ID: 395851 [Multi-domain]  Cd Length: 194  Bit Score: 52.28  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   27 DKDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVF-IKPN----NGGSSVATTLVESKEAVKDaVLEALKYDTE 101
Cdd:pfam01071   2 SKSFAKDFMKRYGIPTAEYETFTDPEEAK-SYIQEAGFPAIvVKADglaaGKGVIVASSNEEAIKAVDE-ILEQKKFGEA 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 311351508  102 ---VMIEEYIKGDEITC-PIIDGK----MLPV 125
Cdd:pfam01071  80 getVVIEEFLEGEEVSVlAFVDGKtvkpLPPA 111
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 55-196 9.24e-08

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 49.81  E-value: 9.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   55 DYEKIE------NLGYPVFIKPNNGGSSVATTLVESKEAVKdAVLEALKydTEVMIEEYIK---GDEITCPIIDGKMlpV 125
Cdd:pfam08443  26 YPEDAEqfieqiKRQFPVIVKSIYGSQGIGVFLAEDEQKLR-QTLSATN--EQILVQEFIAeanNEDIRCLVVGDQV--V 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311351508  126 LAIKPKGKFFDIASKYEDGGADEfivKLNedLHKEVEKMALETYKLLKCDvYARVDMLVKDNIPYVLEVNT 196
Cdd:pfam08443 101 GALHRQSNEGDFRSNLHRGGVGE---KYQ--LSQEETELAIKAAQAMQLD-VAGVDLLRQKRGLLVCEVNS 165
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
26-112 4.17e-07

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 49.16  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  26 MDKDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVFIKPNNGGSSVA--------TTLVESKEAVKDAVLEALK 97
Cdd:COG3919  116 LDKERFYELAEELGVPVPKTVVLDSADDLD-ALAEDLGFPVVVKPADSVGYDElsfpgkkkVFYVDDREELLALLRRIAA 194

                         90
                 ....*....|....*
gi 311351508  98 YDTEVMIEEYIKGDE 112
Cdd:COG3919  195 AGYELIVQEYIPGDD 209
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 57-195 1.43e-06

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 46.22  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   57 EKIENLGYPVFIKPNNGGSSVATTLVESKEavkdavlEALKYDTEVMIEEYIKGDEITCPII-DGKMLPVLAIKPKGKFF 135
Cdd:pfam02655  25 EELLREEKKYVVKPRDGCGGEGVRKVENGR-------EDEAFIENVLVQEFIEGEPLSVSLLsDGEKALPLSVNRQYIDN 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  136 DIASKYEDGGADEFIVKLNEDLHKEVEKMALetyKLLKCDVYARVDMLVKDNIPYVLEVN 195
Cdd:pfam02655  98 GGSGFVYAGNVTPSRTELKEEIIELAEEVVE---CLPGLRGYVGVDLVLKDNEPYVIEVN 154
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 2-141 1.76e-06

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 47.53  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   2 TVQSVLKTLGIPfsGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVFIKPNNGGSSVATTL 81
Cdd:PRK02186  84 VASEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVAL-DALDGLTYPVVVKPRMGSGSVGVRL 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311351508  82 VESKEAVKDAVLEALKYDT-EVMIEEYIKGDEITCPII-DGKMLPVLAI--KPKGK---FFDIASKY 141
Cdd:PRK02186 161 CASVAEAAAHCAALRRAGTrAALVQAYVEGDEYSVETLtVARGHQVLGItrKHLGPpphFVEIGHDF 227
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
63-195 2.36e-06

30S ribosomal protein S6--L-glutamate ligase;


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 46.82  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  63 GYPVFIKPNNGGSSVATTLVESKEAVkDAVLEALK-YDTEVMIEEYI---KGDEITCPIIDGKMlpVLAIKPKGKFFDIA 138
Cdd:PRK10446 135 GAPLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRgLNAHILVQEYIkeaQGCDIRCLVVGDEV--VAAIERRAKEGDFR 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311351508 139 SKYEDGGadefiVKLNEDLHKEVEKMALETYKLLKCDVyARVDMLVKDNIPYVLEVN 195
Cdd:PRK10446 212 SNLHRGG-----AASVASITPQEREIAIKAARTMALDV-AGVDILRANRGPLVMEVN 262
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 7-195 1.24e-05

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 44.99  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508     7 LKTLGIPFSGCGPLSSAICMDKDMTKRILAFGNVRTARWVMVSSVDEIdYEKIENLGYPVFIKPNN--GGSSVATtlVES 84
Cdd:TIGR01369  649 LEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEA-VEFASEIGYPVLVRPSYvlGGRAMEI--VYN 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508    85 KEAVKDAVLEALKYDTE--VMIEEYIKgdeitcpiiDGKMLPVLAIKPKGKFF--DIASKYEDGG---ADEFIV----KL 153
Cdd:TIGR01369  726 EEELRRYLEEAVAVSPEhpVLIDKYLE---------DAVEVDVDAVSDGEEVLipGIMEHIEEAGvhsGDSTCVlppqTL 796

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 311351508   154 NEDLHKEVEKMALETYKLLKCDVYARVDMLVKDNIPYVLEVN 195
Cdd:TIGR01369  797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVN 838
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 39-110 1.46e-05

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 44.48  E-value: 1.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311351508  39 NVRTARWVMVSSVDEIdYEKIENLGYPVFIKPNN--GGSSVAttLVESKEAVKDAVLEALKY--DTEVMIEEYIKG 110
Cdd:COG0458  126 GIPQPKSGTATSVEEA-LAIAEEIGYPVIVRPSYvlGGRGMG--IVYNEEELEEYLERALKVspDHPVLIDESLLG 198
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
23-114 1.46e-05

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 44.36  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  23 AICMDKDMTKRiLAFG--NVRTARWVMVSSVDEIdYEKIENLGYPVFIKP---NNG-GSSVattlVESKEAVKDAVLEAL 96
Cdd:PRK09288 109 RLTMNREGIRR-LAAEelGLPTSPYRFADSLEEL-RAAVEEIGYPCVVKPvmsSSGkGQSV----VRSPEDIEKAWEYAQ 182

                         90       100
                 ....*....|....*....|...
gi 311351508  97 KY----DTEVMIEEYIKGD-EIT 114
Cdd:PRK09288 183 EGgrggAGRVIVEEFIDFDyEIT 205
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 28-121 1.77e-05

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 44.23  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  28 KDMTKRILAFGNVRTARWVMVSSVDE-IDYekIENLGYPVFIKPnNG-----GSSVATTLVESKEAVKDaVLEALKY--- 98
Cdd:COG0151  103 KAFAKEFMARYGIPTAAYRVFTDLEEaLAY--LEEQGAPIVVKA-DGlaagkGVVVAETLEEALAAVDD-MLADGKFgda 178

                         90       100
                 ....*....|....*....|....
gi 311351508  99 DTEVMIEEYIKGDEITC-PIIDGK 121
Cdd:COG0151  179 GARVVIEEFLEGEEASLfALTDGK 202
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 27-110 8.95e-05

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 41.52  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   27 DKDMTKRILAFGNVRTARW--VMVSSVDEIdYEKIENLGYPVFIKPNNG----GSSVATTLVESKEAVKDAVLEALKY-- 98
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEA-LAAAKEIGYPVIIKAAFGggglGMGIARNEEELAELFALALAEAPAAfg 79

                          90
                  ....*....|..
gi 311351508   99 DTEVMIEEYIKG 110
Cdd:pfam02786  80 NPQVLVEKSLKG 91
PRK07206 PRK07206
hypothetical protein; Provisional
 9-112 6.25e-04

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 39.63  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   9 TLGIPFSGCGPLSSAICMDKDMTKrILAFGNVRTARWVMVSSVDEIDYEKIEN--LGYPVFIKPNNGGSSVATTLVESKE 86
Cdd:PRK07206  91 ILTPQYSNDPALSSARRNKAEMIN-ALAEAGLPAARQINTADWEEAEAWLRENglIDRPVVIKPLESAGSDGVFICPAKG 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 311351508  87 AVKDAVLEAL----KYDT---EVMIEEYIKGDE 112
Cdd:PRK07206 170 DWKHAFNAILgkanKLGLvneTVLVQEYLIGTE 202
carB PRK05294
carbamoyl-phosphate synthase large subunit;
28-110 9.41e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 39.31  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508   28 KDMTKRIlafgNVRTARWVMVSSVDEIdYEKIENLGYPVFIKP--NNGGSsvATTLVESKEAVKDAVLEALKYD--TEVM 103
Cdd:PRK05294  133 KEAMKKI----GLPVPRSGIAHSMEEA-LEVAEEIGYPVIIRPsfTLGGT--GGGIAYNEEELEEIVERGLDLSpvTEVL 205


                  ....*..
gi 311351508  104 IEEYIKG 110
Cdd:PRK05294  206 IEESLLG 212
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
48-108 9.92e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 39.20  E-value: 9.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311351508  48 VSSVDEIdYEKIENLGYPVFIKPNNGGSSVATTLVESKEAVKDAVLEALKY------DTEVMIEEYI 108
Cdd:PRK08654 138 IEDIEEA-KEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIaqsafgDSTVFIEKYL 203
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 62-115 1.50e-03

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 37.65  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311351508   62 LGYPVFIKPNNGGSSVATTLVESKEAVKDAVLEALK--------YDTEVM------IEEYIKGDEITC 115
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREeieqwkemYPEAVVdggsflVEEYIEGEEFAV 68
PurT COG0027
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ...
 40-114 1.60e-03

Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439798 [Multi-domain]  Cd Length: 393  Bit Score: 38.57  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  40 VRTARWVMVSSVDEIdYEKIENLGYPVFIKP---NNG-GSSVattlVESKEAVKDAVLEALKY----DTEVMIEEYIKGD 111
Cdd:COG0027  127 LPTSPYRFADSLEEL-RAAVEEIGYPCVVKPvmsSSGkGQSV----VRSPADIEAAWEYAQEGgrggAGRVIVEGFVDFD 201


                 ....
gi 311351508 112 -EIT 114
Cdd:COG0027  202 yEIT 205
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 27-110 2.38e-03

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 38.06  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508    27 DKDMTKRILAFGNVRTARWVMVSSVDEiDYEKIENLGYPVFIKP----NNGGSSVATTLVESKEAVKDAVleALKYDTEV 102
Cdd:TIGR01369  127 DRELFREAMKEIGEPVPESEIAHSVEE-ALAAAKEIGYPVIVRPaftlGGTGGGIAYNREELKEIAERAL--SASPINQV 203


                   ....*...
gi 311351508   103 MIEEYIKG 110
Cdd:TIGR01369  204 LVEKSLAG 211
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 11-120 5.32e-03

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 37.03  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311351508  11 GIP-FsgcGPLSSAICMD--KDMTKRILAFGNVRTARWVMVSSVDEIDyEKIENLGYPVFIKPNN----GGSSVATTLVE 83
Cdd:PLN02257  86 GIPtF---GPSAEAAALEgsKNFMKDLCDKYKIPTAKYETFTDPAAAK-KYIKEQGAPIVVKADGlaagKGVVVAMTLEE 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 311351508  84 SKEAVKDAVLEAL--KYDTEVMIEEYIKGDEIT-CPIIDG 120
Cdd:PLN02257 162 AYEAVDSMLVKGAfgSAGSEVVVEEFLDGEEASfFALVDG 201
 
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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