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Conserved domains on  [gi|658755872|ref|WP_029773582|]
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MULTISPECIES: N-acetyl-gamma-glutamyl-phosphate reductase [unclassified Pseudoalteromonas]

Protein Classification

N-acetyl-gamma-glutamyl-phosphate reductase( domain architecture ID 11414156)

N-acetyl-gamma-glutamyl-phosphate reductase catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde, as part of the L-arginine biosynthesis

CATH:  3.40.50.720
EC:  1.2.1.38
Gene Ontology:  GO:0051287|GO:0070401|GO:0008652|GO:0016620|GO:0003942
PubMed:  17316682
SCOP:  4000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 1-333 3.26e-153

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


:

Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 433.73  E-value: 3.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYvseGSLDKHKLLSDLYPehrNLLDIPLLPLSESAFDDINSSADYICLC 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHP---HLRGLTDLVFEPPDPDELAAGCDVVFLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAA 160
Cdd:COG0002   75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 161 LNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHL------GHKVLFTPHL 232
Cdd:COG0002  155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 233 GNFPRGILETIYVQLKPGVTKENVSDAY-QVLNNEPLIRLLADKV-PSIKSVVKQPYVDIGWQ--QQGSQLIVMAAIDNL 308
Cdd:COG0002  235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLPEGRlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                        330       340
                 ....*....|....*....|....*
gi 658755872 309 LKGAAGQALQCINLSMNLDHTTGLK 333
Cdd:COG0002  315 VKGAAGQAVQNMNLMFGLPETTGLE 339
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 1-333 3.26e-153

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 433.73  E-value: 3.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYvseGSLDKHKLLSDLYPehrNLLDIPLLPLSESAFDDINSSADYICLC 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHP---HLRGLTDLVFEPPDPDELAAGCDVVFLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAA 160
Cdd:COG0002   75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 161 LNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHL------GHKVLFTPHL 232
Cdd:COG0002  155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 233 GNFPRGILETIYVQLKPGVTKENVSDAY-QVLNNEPLIRLLADKV-PSIKSVVKQPYVDIGWQ--QQGSQLIVMAAIDNL 308
Cdd:COG0002  235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLPEGRlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                        330       340
                 ....*....|....*....|....*
gi 658755872 309 LKGAAGQALQCINLSMNLDHTTGLK 333
Cdd:COG0002  315 VKGAAGQAVQNMNLMFGLPETTGLE 339
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 1-333 1.00e-151

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 429.69  E-value: 1.00e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872    1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSLDKHklLSDLYPEHRNLLDiplLPLSESAFDDINSSADYICLC 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRESAGKP--VSEVHPHLRGLVD---LNLEPIDVEEILEDADVVFLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAA 160
Cdd:TIGR01850  76 LPHGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTAT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  161 LNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHLG------HKVLFTPHL 232
Cdd:TIGR01850 156 LLALAPLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  233 GNFPRGILETIYVQLKPGVTKENVSDAYQ-VLNNEPLIRLLADK-VPSIKSVVKQPYVDIGWQQQG--SQLIVMAAIDNL 308
Cdd:TIGR01850 236 VPMTRGILATIYAKLKDGLTEEDLRALYEeFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNL 315

                         330       340
                  ....*....|....*....|....*
gi 658755872  309 LKGAAGQALQCINLSMNLDHTTGLK 333
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGLP 340
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 154-312 5.90e-78

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 235.84  E-value: 5.90e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 154 GCYPTAALNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHLGH------K 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSKlagedvE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 226 VLFTPHLGNFPRGILETIYVQLKPGVTKENVSDAYQ-VLNNEPLIRLL-ADKVPSIKSVVKQPYVDIGWQQQG--SQLIV 301
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEeFYADEPFVRVLpEGQLPSTKAVRGSNFCDIGVAVDGrtGRLIV 160

                        170
                 ....*....|.
gi 658755872 302 MAAIDNLLKGA 312
Cdd:cd23934  161 VSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 3-332 4.71e-73

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 230.87  E-value: 4.71e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   3 VAIIGASGYSGAELASLVAKHPNLTLSgcyVSEGSLDKHKLLSDLYPeHRNLLDIPLLplseSAFDDIN-SSADYICLCT 81
Cdd:PLN02968  41 IFVLGASGYTGAEVRRLLANHPDFEIT---VMTADRKAGQSFGSVFP-HLITQDLPNL----VAVKDADfSDVDAVFCCL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  82 DHKVSVDLApQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAAL 161
Cdd:PLN02968 113 PHGTTQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQ 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 162 NALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEVS--LAPYGLFNHRHGPEIEQ------HLGHKVLFTPHLG 233
Cdd:PLN02968 192 LPLVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIEQgladaaGSKVTPSFTPHLM 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 234 NFPRGILETIYVQLKPGVTKENVSDAYQV-LNNEPLIRLLA-DKVPSIKSVVKQPYVDIGW--QQQGSQLIVMAAIDNLL 309
Cdd:PLN02968 272 PMSRGMQSTVYVHYAPGVTAEDLHQHLKErYEGEEFVKVLErGAVPHTDHVRGSNYCELNVfaDRIPGRAIIISVIDNLV 351

                        330       340
                 ....*....|....*....|...
gi 658755872 310 KGAAGQALQCINLSMNLDHTTGL 332
Cdd:PLN02968 352 KGASGQAVQNLNLMMGLPETTGL 374
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 2-147 4.71e-27

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 102.99  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872    2 NVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSldKHKLLSDLYPEHRNLLDIPLLPLSESAFDDInssaDYICLCT 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVDPEDFKDV----DIVFFAL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658755872   82 DHKVSVDLAPQFLAMGKKVFDLSGGYRLAsnddyvtyygfehqhpellNEAAYGLAEWNSSAIAKA 147
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 2-147 1.66e-25

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 98.77  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872     2 NVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSldKHKLLSDLYPEHRNLLDiplLPLSESAFDDINssADYICLCT 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEVV---LELDPPDFEELA--VDIVFLAL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658755872    82 DHKVS---VDLAPQFLAMGKKVFDLSGGYRLAsnddyvtyygfehqhpellNEAAYGLAEWNSSAIAKA 147
Cdd:smart00859  74 PHGVSkesAPLLPRAAAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 1-333 3.26e-153

N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; N-acetyl-gamma-glutamylphosphate reductase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439773 [Multi-domain]  Cd Length: 345  Bit Score: 433.73  E-value: 3.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYvseGSLDKHKLLSDLYPehrNLLDIPLLPLSESAFDDINSSADYICLC 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHP---HLRGLTDLVFEPPDPDELAAGCDVVFLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAA 160
Cdd:COG0002   75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 161 LNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHL------GHKVLFTPHL 232
Cdd:COG0002  155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 233 GNFPRGILETIYVQLKPGVTKENVSDAY-QVLNNEPLIRLLADKV-PSIKSVVKQPYVDIGWQ--QQGSQLIVMAAIDNL 308
Cdd:COG0002  235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLPEGRlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                        330       340
                 ....*....|....*....|....*
gi 658755872 309 LKGAAGQALQCINLSMNLDHTTGLK 333
Cdd:COG0002  315 VKGAAGQAVQNMNLMFGLPETTGLE 339
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 1-333 1.00e-151

N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273832 [Multi-domain]  Cd Length: 346  Bit Score: 429.69  E-value: 1.00e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872    1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSLDKHklLSDLYPEHRNLLDiplLPLSESAFDDINSSADYICLC 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRESAGKP--VSEVHPHLRGLVD---LNLEPIDVEEILEDADVVFLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAA 160
Cdd:TIGR01850  76 LPHGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTAT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  161 LNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHLG------HKVLFTPHL 232
Cdd:TIGR01850 156 LLALAPLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  233 GNFPRGILETIYVQLKPGVTKENVSDAYQ-VLNNEPLIRLLADK-VPSIKSVVKQPYVDIGWQQQG--SQLIVMAAIDNL 308
Cdd:TIGR01850 236 VPMTRGILATIYAKLKDGLTEEDLRALYEeFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFAVDErtGRVVVVSAIDNL 315

                         330       340
                  ....*....|....*....|....*
gi 658755872  309 LKGAAGQALQCINLSMNLDHTTGLK 333
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGLP 340
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 154-312 5.90e-78

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both, the arginine and lysine, biosynthetic pathways.


Pssm-ID: 467683  Cd Length: 171  Bit Score: 235.84  E-value: 5.90e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 154 GCYPTAALNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHLGH------K 225
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSKlagedvE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 226 VLFTPHLGNFPRGILETIYVQLKPGVTKENVSDAYQ-VLNNEPLIRLL-ADKVPSIKSVVKQPYVDIGWQQQG--SQLIV 301
Cdd:cd23934   81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEeFYADEPFVRVLpEGQLPSTKAVRGSNFCDIGVAVDGrtGRLIV 160

                        170
                 ....*....|.
gi 658755872 302 MAAIDNLLKGA 312
Cdd:cd23934  161 VSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 3-332 4.71e-73

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 230.87  E-value: 4.71e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   3 VAIIGASGYSGAELASLVAKHPNLTLSgcyVSEGSLDKHKLLSDLYPeHRNLLDIPLLplseSAFDDIN-SSADYICLCT 81
Cdd:PLN02968  41 IFVLGASGYTGAEVRRLLANHPDFEIT---VMTADRKAGQSFGSVFP-HLITQDLPNL----VAVKDADfSDVDAVFCCL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  82 DHKVSVDLApQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVAGCYPTAAL 161
Cdd:PLN02968 113 PHGTTQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQ 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 162 NALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEVS--LAPYGLFNHRHGPEIEQ------HLGHKVLFTPHLG 233
Cdd:PLN02968 192 LPLVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIEQgladaaGSKVTPSFTPHLM 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 234 NFPRGILETIYVQLKPGVTKENVSDAYQV-LNNEPLIRLLA-DKVPSIKSVVKQPYVDIGW--QQQGSQLIVMAAIDNLL 309
Cdd:PLN02968 272 PMSRGMQSTVYVHYAPGVTAEDLHQHLKErYEGEEFVKVLErGAVPHTDHVRGSNYCELNVfaDRIPGRAIIISVIDNLV 351

                        330       340
                 ....*....|....*....|...
gi 658755872 310 KGAAGQALQCINLSMNLDHTTGL 332
Cdd:PLN02968 352 KGASGQAVQNLNLMMGLPETTGL 374
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 1-152 5.87e-59

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate; the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 1 AGPR family. Bacterial members of this family tend to be found within Arg biosynthesis operons. The type 1 AGPR family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467521 [Multi-domain]  Cd Length: 170  Bit Score: 187.25  E-value: 5.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSLDKhklLSDLYPEHRNLLDIPLLPLSEsafDDINSSADYICLC 80
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKP---VSEVFPHLRGLTDLTFEPDDD---EEIAEDADVVFLA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658755872  81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAV 152
Cdd:cd17895   75 LPHGVSMELAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFEHAAPELLKEAVYGLPELNREEIKKARLVAN 146
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 155-312 3.84e-44

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways.


Pssm-ID: 467675  Cd Length: 166  Bit Score: 149.19  E-value: 3.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 155 CYPTAALNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEV--SLAPYGLFNHRHGPEIEQHLG--HKVLFTP 230
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVagSLRPYALSGHRHTPEIAQNLGgkHNVHFTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 231 HLGNFPRGILETIYVQLKPGVTKENVSDAY-QVLNNEPLIRLLAD-KVPSIKSVVKQPYVDIGWQ--QQGSQLIVMAAID 306
Cdd:cd18125   81 HVGPWVRGILMTIQCFTQKGWSLRQLHEAYrEAYAGEPFVRVMPQgKGPDPKFVQGTNYADIGVEleEDTGRLVVMSAID 160


                 ....*.
gi 658755872 307 NLLKGA 312
Cdd:cd18125  161 NLVKGA 166
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 154-312 1.06e-41

C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY; EC 1.2.1.103/EC 1.2.1.106) is involved in both, the arginine and lysine, biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor.


Pssm-ID: 467688  Cd Length: 174  Bit Score: 143.15  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 154 GCYPTAALNALKPLQQAGLLSDEKVIINAVSGVTGAGRKASVGTHFCEVSLA--PYGLFNHRHGPEIEQHLGH-----KV 226
Cdd:cd23939    1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVvrPYKPTGHRHTAEIEQELGLlareiSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 227 LFTPHLGNFPRGILETIYVQLKPGVTKENVSDAY-QVLNNEPLIRLLADK-----VPSIKSVVKQPYVDIGWQ--QQGSQ 298
Cdd:cd23939   81 SFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYrKAYGNEPFVRIVKDRkgiyrYPDPKLVIGSNFCDIGFEldEDNGR 160

                        170
                 ....*....|....
gi 658755872 299 LIVMAAIDNLLKGA 312
Cdd:cd23939  161 LVVFSAIDNLMKGA 174
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 2-147 4.71e-27

Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase


Pssm-ID: 426059 [Multi-domain]  Cd Length: 121  Bit Score: 102.99  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872    2 NVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSldKHKLLSDLYPEHRNLLDIPLLPLSESAFDDInssaDYICLCT 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVDPEDFKDV----DIVFFAL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658755872   82 DHKVSVDLAPQFLAMGKKVFDLSGGYRLAsnddyvtyygfehqhpellNEAAYGLAEWNSSAIAKA 147
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 154-312 4.72e-27

C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. This model corresponds to the AGPR C-terminal catalytic domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467685  Cd Length: 161  Bit Score: 104.25  E-value: 4.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 154 GCYPTAALNALKPLqqAGLLsDEKVIINAVSGVTGAGRKASVGT--HFCEVSLAPYGLFNHRHGPEIEQHLGHKVLFTPH 231
Cdd:cd23936    1 GCYATGAQLALAPL--LDDL-DGPPSVFGVSGYSGAGTKPSPKNdpEVLADNLIPYSLVGHIHEREVSRHLGTPVAFMPH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 232 LGNFPRGILETIYVQLKPGVTKENVSDAYQ-VLNNEPLIRLLADkVPSIKSVVKQPYVDIG---WQQQGSQLIVMAAIDN 307
Cdd:cd23936   78 VAPWFQGITLTISIPLKKSMTADEIRELYQeAYAGEPLIKVTKE-IPLVRDNAGKHGVVVGgftVHPDGKRVVVVATIDN 156


                 ....*
gi 658755872 308 LLKGA 312
Cdd:cd23936  157 LLKGA 161
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 154-312 6.36e-27

C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and similar proteins; N-acetyl-gamma-glutamyl-phosphate reductase (AGPR; EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the NADPH-dependent reduction of N-acetyl-gamma-glutamyl-phosphate phosphate, the third step of arginine biosynthesis. N-acetyl-gamma-glutamyl-phosphate phosphate, the product of the second step catalyzed by acetylglutamate kinase, undergoes reductive dephosphorylation to give N-acetylglutamic semialdehyde, which is converted to ornithine by acetylornithine aminotransferase and acetylornithine deacetylase. AGPR proteins contain an N-terminal Rossmann fold NAD(P)H-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. NADP(+) binds in a cleft between these domains and contacts both. There are two related families of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The model corresponds to type 2 AGPR family.


Pssm-ID: 467684  Cd Length: 178  Bit Score: 104.22  E-value: 6.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 154 GCYPTAALNALKPLQQAGLLS-DEKVIINAVSGVTGAGRKAsVGTHFCEV-----SLAPYGL-FNHRHGPEIEQH--LGH 224
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPaDYPLSIHAVSGYSGGGKKM-IEQYEAAEaadlpPPRPYGLgLEHKHLPEMQKHagLAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 225 KVLFTPHLGNFPRGILETI---YVQLKPGVTKENVSDAY----------QVL---NNEPLIRLLADkvpsikSVVKQPYV 288
Cdd:cd23935   80 PPIFTPAVGNFYQGMLVTVplhLDLLEKGVSAAEVHEALaehyagerfvKVMpldEPDALGFLDPQ------ALNGTNNL 153

                        170       180
                 ....*....|....*....|....*
gi 658755872 289 DIGWQ-QQGSQLIVMAAIDNLLKGA 312
Cdd:cd23935  154 ELFVFgNDKGQALLVARLDNLGKGA 178
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 2-147 1.66e-25

Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. This family is also found in yeast and fungal Arg5,6 protein, which is cleaved into the enzymes N-acety-gamma-glutamyl-phosphate reductase and acetylglutamate kinase. These are also involved in arginine biosynthesis. All proteins in this entry contain a NAD binding region of semialdehyde dehydrogenase.


Pssm-ID: 214863 [Multi-domain]  Cd Length: 123  Bit Score: 98.77  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872     2 NVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSldKHKLLSDLYPEHRNLLDiplLPLSESAFDDINssADYICLCT 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPHLKGEVV---LELDPPDFEELA--VDIVFLAL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658755872    82 DHKVS---VDLAPQFLAMGKKVFDLSGGYRLAsnddyvtyygfehqhpellNEAAYGLAEWNSSAIAKA 147
Cdd:smart00859  74 PHGVSkesAPLLPRAAAAGAVVIDLSSAFRMD-------------------DDVPYGLPEVNPEAIKKA 123
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 1-153 6.03e-23

N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase (LysY) and similar proteins; LysY (EC 1.2.1.103/EC 1.2.1.106) is involved in both the arginine and lysine biosynthetic pathways. LysY interacts with LysW. It may form a ternary complex with LysW and LysZ. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LysY is the third enzyme in lysine biosynthesis from AAA. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor. Members in this subfamily belong to the type 1 AGPR family. They contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467527 [Multi-domain]  Cd Length: 170  Bit Score: 93.49  E-value: 6.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSgcYVSEGSLDkHKLLSDLYPEHRNLLDipllpLSESAFDDInSSADYICLC 80
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVK--QVTSESLA-GKPVHRVHPNLRGRTL-----LKFVPPEEL-ESCDVLFLA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658755872  81 TDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQHPELLNEAAYGLAEWNSSAIAKANLVAVA 153
Cdd:cd24151   72 LPHGESMKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIAGA 144
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 164-310 7.35e-20

Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase.


Pssm-ID: 397067 [Multi-domain]  Cd Length: 167  Bit Score: 85.06  E-value: 7.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  164 LKPLQQA-GLLsdEKVIINAVSGVTGAGRKASVGTHF--CEVSLAPY-GLFNHRHGPEIEQHLGHKVLFTPHLGNFP--- 236
Cdd:pfam02774   1 LKPLRDAlGGL--ERVIVDTYQAVSGAGKKAKPGVFGapIADNLIPYiDGEEHNGTPETREELKMVNETKKILGFTPkvs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  237 ---------RGILETIYVQLKPgvTKENVSDAYQVLNNEP---LIRLLADKVPSIKSVV-KQPYVDIGWQQQ----GSQL 299
Cdd:pfam02774  79 atcvrvpvfRGHSETVTVKLKL--KPIDVEEVYEAFYAAPgvfVVVRPEEDYPTPRAVRgGTNFVYVGRVRKdpdgDRGL 156

                         170
                  ....*....|.
gi 658755872  300 IVMAAIDNLLK 310
Cdd:pfam02774 157 KLVSVIDNLRK 167
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 1-152 1.62e-13

N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate reductase (actinobacAGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC). There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. The family includes N-acetyl-gamma-glutamyl-phosphate reductases mainly from actinobacteria. They belong to the type 1 AGPR family. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467524 [Multi-domain]  Cd Length: 164  Bit Score: 67.31  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLsGCYVSEGSLDKHklLSDLYPEHRNLLDIPLLPLSESAFddinSSADYICLC 80
Cdd:cd24148    1 IRVAVAGASGYAGGELLRLLLGHPEFEI-GALTAHSNAGQR--LGELHPHLPPLADRVLEPTTPAVL----AGHDVVFLA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658755872  81 TDHKVSVDLAPQfLAMGKKVFDLSGGYRLASNDDYVTYYGFEHQhpellNEAAYGLAE--WNSSAIAKANLVAV 152
Cdd:cd24148   74 LPHGASAAIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHA-----GGWTYGLPElpGAREALAGARRIAV 141
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 155-308 2.76e-12

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 64.08  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 155 CYPTAALNALKPLQQAGLLsdEKVIINAVSGVTGAGRKASVGTHFCEVSLA--PYGLFNHRHGPEIEQHLGH-----KVL 227
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGI--EEILVVTVQAVSGAGPKTKGPILKSEVRAIipNIPKNETKHAPETGKVLGEigkpiKVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872 228 FTPHLGNFPRGILETIYVQLKPGVTKENVSDAYQVLNNEPLIRL---LADKVPSIKSVVKQPYVDIGWQQQ----GSQLI 300
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAedgLTYAKVSTRSVGGVYGVPVGRQREfafdDNKLK 158


                 ....*...
gi 658755872 301 VMAAIDNL 308
Cdd:cd18122  159 VFSAVDNE 166
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-164 4.22e-12

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar proteins; AGPR (EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, catalyzes the third step in the biosynthesis of arginine from glutamate, the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (EC 2.7.2.8) domain and a C-terminal AGPR domain. There are two related families (type 1 and type 2) of N-acetyl-gamma-glutamyl-phosphate reductase, which differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase, EC 1.2.1.103/EC 1.2.1.106), which is involved in both the arginine and lysine biosynthetic pathways. Members in this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467515 [Multi-domain]  Cd Length: 160  Bit Score: 63.36  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   3 VAIIGASGYSGAELASLVAKHPNLTLSgcYVSEGSLdKHKLLSDLYPEhrnllDIPLLPLSESAFDDINSSADYICLCTD 82
Cdd:cd02280    3 VAIIGASGYTGLEIVRLLLGHPYLRVL--TLSSRER-AGPKLREYHPS-----LIISLQIQEFRPCEVLNSADILVLALP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872  83 HKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTYYGfehqhPELLNEAAYGLAEW-------NSSAIAKANLVAVAGc 155
Cdd:cd02280   75 HGASAELVAAISNPQVKIIDLSADFRFTDPEVYRRHPR-----PDLEGGWVYGLPELdreqriaNATRIANPNLVKGAA- 148


                 ....*....
gi 658755872 156 ypTAALNAL 164
Cdd:cd02280  149 --GAAVQNL 155
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 1-150 9.26e-09

N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR); Aspartate-beta-semialdehyde dehydrogenase (ASADH, EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the second step of the aspartate biosynthetic pathway, an essential enzyme found in bacteria, fungi, and higher plants. ASADH catalyses the formation of L-aspartate-beta-semialdehyde (ASA) by the reductive dephosphorylation of L-beta-aspartyl phosphate (BAP), utilizing the reducing power of NADPH. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. N-acetyl-gamma-glutamyl-phosphate reductase (AGPR, EC 1.2.1.38), also called N-acetyl-glutamate semialdehyde dehydrogenase, or NAGSA dehydrogenase, reversibly catalyses the NADPH-dependent reduction of N-acetyl-gamma-glutamyl phosphate; the third step of arginine biosynthesis. ASADH and AGPR proteins contain an N-terminal Rossmann fold NAD(P)H binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain.


Pssm-ID: 467516 [Multi-domain]  Cd Length: 145  Bit Score: 53.52  E-value: 9.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHP----NLTLSGCYVSEGSLDKHKllsDLYPEHRNLLDIPllplsESAFDDinssADY 76
Cdd:cd02281    1 KKVGVVGATGYVGGEFLRLLLEHPfplfEIVLLAASSAGAKKKYFH---PKLWGRVLVEFTP-----EEVLEQ----VDI 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658755872  77 ICLCTDHKVSVDLAPQFLAMGKKVFDLSGGYRLASNDDYVTyygfehqhPELLNEAAYGLaeWNSSAIAKANLV 150
Cdd:cd02281   69 VFTALPGGVSAKLAPELSEAGVLVIDNASDFRLDKDVPLVV--------PEVNREHIGEL--KGTKIIANPNLV 132
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 2-151 1.77e-06

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 47.11  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   2 NVAIIGASGYSGAELASLVAKHPNLTLsgCYVSEGSLdKHKLLSDLYPEHRNLLDI-PLLPLSESAFDDInssaDYICLC 80
Cdd:cd24149    2 RVGLIGARGYVGRELIRLLNRHPNLEL--AHVSSREL-AGQKVSGYTKSPIDYLNLsVEDIPEEVAAREV----DAWVLA 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658755872  81 TDHKVSVDLAPQFLAMGKK--VFDLSGGYRlasnddyvtyygFEhqhpellNEAAYGLAEWNSSAIAKANLVA 151
Cdd:cd24149   75 LPNGVAKPFVDAIDKANPKsvIVDLSADYR------------FD-------DAWTYGLPELNRRRIAGAKRIS 128
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 1-109 2.13e-06

N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 protein and similar proteins; The family includes aspartate beta-semialdehyde dehydrogenase (ASADH), NADP-dependent malonyl-CoA reductase (MCR), and USG-1 protein. They contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain and are members of the GAPDH superfamily of proteins. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. NADP-dependent MCR (EC 1.2.1.75) is mainly found in Archaea. It catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA. Sequence comparison suggests that the archaeal MCR gene (mcr) has evolved from the duplication of a common ancestral ASADH gene (asd). The biological function of USG-1 protein and homologs remains unclear. They are homologs to ASADH but lack the conserved active site residues of the ASADH protein C-terminal catalytic domain.


Pssm-ID: 467523 [Multi-domain]  Cd Length: 142  Bit Score: 46.56  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHP----NLTLsgcYVSEGSLDKhklLSDLYPEhrnllDIPLLPLSESAFDDInssaDY 76
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEPdplfELRA---LASEESAGK---KAEFAGE-----AIMVQEADPIDFLGL----DI 65

                         90       100       110
                 ....*....|....*....|....*....|...
gi 658755872  77 ICLCTDHKVSVDLAPQFLAMGKKVFDLSGGYRL 109
Cdd:cd24147   66 VFLCAGAGVSAKFAPEAARAGVLVIDNAGALRM 98
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 1-101 6.60e-05

N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of ASADH enzymes that has a similar overall fold and domain organization but sharing very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain. Family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.


Pssm-ID: 467518  Cd Length: 162  Bit Score: 42.48  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSLDK------HKLLSDLYPEhrNLLDIPLLPLSESAFDDInssa 74
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKkygdavRWKQDTPIPE--EVADMVVKECEPEEFKDC---- 74

                         90       100
                 ....*....|....*....|....*..
gi 658755872  75 DYICLCTDHKVSVDLAPQFLAMGKKVF 101
Cdd:cd02315   75 DIVFSALDSDVAGEIEPAFAKAGIPVF 101
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 307-328 6.77e-05

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 42.48  E-value: 6.77e-05
                         10        20
                 ....*....|....*....|..
gi 658755872 307 NLLKGAAGQALQCINLSMNLDH 328
Cdd:cd24149  132 NLLKGAATQALQNLNLALGLDE 153
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 1-100 1.22e-04

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 41.39  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGSldkHKLLSDLYPehrnLLDIPLLPLSESAFDDINSSADYICLC 80
Cdd:cd02274    1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGS---GLLGGDAGG----LAGIGTGVIVSLDLELAAADADVVIDF 73

                         90       100
                 ....*....|....*....|
gi 658755872  81 TDHKVSVDLAPQFLAMGKKV 100
Cdd:cd02274   74 TTPEATLENLEAAAKAGVPL 93
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 1-37 3.33e-03

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 36.83  E-value: 3.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 658755872    1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGS 37
Cdd:pfam01113   1 IKIAVAGASGRMGRELIKAVLEAPDLELVAAVDRPGS 37
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 1-37 5.75e-03

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 37.79  E-value: 5.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 658755872   1 MNVAIIGASGYSGAELASLVAKHPNLTLSGCYVSEGS 37
Cdd:COG0289    1 IKIAVAGASGRMGRELIRAVLEAPDLELVAAIDRPGS 37
 
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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