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Conserved domains on  [gi|1823258099|ref|WP_166340582|]
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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]; ...
 1-332 3.94e-150

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: 425.64  E-value: 3.94e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYvseGSLDKGKLLSDLYPEHLGLLEYPLQPLTAEAfqdIESNADYVCLC 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHPHLRGLTDLVFEPPDPDE---LAAGCDVVFLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAA 160
Cdd:COG0002    75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 161 LNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHL------GHPVLFTPHL 232
Cdd:COG0002   155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 233 GNFPRGILETIYVQLKPGVTVEQVSAAY-QVLANEPLIRLL-GNKIPSIKGVAKQPFVDIAWQ--QKGEQLIVMSAIDNL 308
Cdd:COG0002   235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLpEGRLPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                         330       340
                  ....*....|....*....|....
gi 1823258099 309 LKGAAGQALQCINLAMGEPHHTGL 332
Cdd:COG0002   315 VKGAAGQAVQNMNLMFGLPETTGL 338
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 1-332 3.94e-150

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: 425.64  E-value: 3.94e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYvseGSLDKGKLLSDLYPEHLGLLEYPLQPLTAEAfqdIESNADYVCLC 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHPHLRGLTDLVFEPPDPDE---LAAGCDVVFLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAA 160
Cdd:COG0002    75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 161 LNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHL------GHPVLFTPHL 232
Cdd:COG0002   155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 233 GNFPRGILETIYVQLKPGVTVEQVSAAY-QVLANEPLIRLL-GNKIPSIKGVAKQPFVDIAWQ--QKGEQLIVMSAIDNL 308
Cdd:COG0002   235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLpEGRLPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                         330       340
                  ....*....|....*....|....
gi 1823258099 309 LKGAAGQALQCINLAMGEPHHTGL 332
Cdd:COG0002   315 VKGAAGQAVQNMNLMFGLPETTGL 338
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 1-332 6.25e-148

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: 420.06  E-value: 6.25e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEHLGLLEYPLQPLTAEafqDIESNADYVCLC 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPIDVE---EILEDADVVFLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAA 160
Cdd:TIGR01850  76 LPHGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTAT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 161 LNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHLG------HPVLFTPHL 232
Cdd:TIGR01850 156 LLALAPLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 233 GNFPRGILETIYVQLKPGVTVEQVSAAYQ-VLANEPLIRLLGNK-IPSIKGVAKQPFVDIAW--QQKGEQLIVMSAIDNL 308
Cdd:TIGR01850 236 VPMTRGILATIYAKLKDGLTEEDLRALYEeFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFavDERTGRVVVVSAIDNL 315

                         330       340
                  ....*....|....*....|....
gi 1823258099 309 LKGAAGQALQCINLAMGEPHHTGL 332
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGL 339
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 154-312 4.60e-80

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: 241.23  E-value: 4.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 154 GCYPTAALNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHLGH------P 225
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSKlagedvE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 226 VLFTPHLGNFPRGILETIYVQLKPGVTVEQVSAAYQ-VLANEPLIRLL-GNKIPSIKGVAKQPFVDIAWQQKGE--QLIV 301
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEeFYADEPFVRVLpEGQLPSTKAVRGSNFCDIGVAVDGRtgRLIV 160

                         170
                  ....*....|.
gi 1823258099 302 MSAIDNLLKGA 312
Cdd:cd23934   161 VSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 3-332 3.52e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 233.57  E-value: 3.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   3 VVIIGASGYSGAELASLVAKHPKLTLQacyVSEGSLDKGKLLSDLYPeHLGLLEYPlqPLTAEAFQDIeSNADYVCLCTD 82
Cdd:PLN02968   41 IFVLGASGYTGAEVRRLLANHPDFEIT---VMTADRKAGQSFGSVFP-HLITQDLP--NLVAVKDADF-SDVDAVFCCLP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  83 HKVSVDLApKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAALN 162
Cdd:PLN02968  114 HGTTQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 163 SLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEVS--LAPYGLFNHRHTPEIEQ------HLGHPVLFTPHLGN 234
Cdd:PLN02968  193 PLVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIEQgladaaGSKVTPSFTPHLMP 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 235 FPRGILETIYVQLKPGVTVEQVsaaYQVL----ANEPLIRLLGnkipsiKGVAKQP---------FVDIAWQQKGEQLIV 301
Cdd:PLN02968  273 MSRGMQSTVYVHYAPGVTAEDL---HQHLkeryEGEEFVKVLE------RGAVPHTdhvrgsnycELNVFADRIPGRAII 343

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1823258099 302 MSAIDNLLKGAAGQALQCINLAMGEPHHTGL 332
Cdd:PLN02968  344 ISVIDNLVKGASGQAVQNLNLMMGLPETTGL 374
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 2-147 2.99e-28

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: 106.07  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   2 NVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEHLGLLEYPLQPLTAEAFQDIesnaDYVCLCT 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVDPEDFKDV----DIVFFAL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823258099  82 DHKVSVDLAPKFLAMGKKVFDLSGGFRLAgnedyltyygfahehpallEQAAYGLAEWNSDAISKA 147
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 2-147 1.92e-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: 1.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099    2 NVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEhlgLLEYPLQPLTAEAFQDIEsnADYVCLCT 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPH---LKGEVVLELDPPDFEELA--VDIVFLAL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823258099   82 DHKVS---VDLAPKFLAMGKKVFDLSGGFRLAgnedyltyygfahehpallEQAAYGLAEWNSDAISKA 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]; ...
 1-332 3.94e-150

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: 425.64  E-value: 3.94e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYvseGSLDKGKLLSDLYPEHLGLLEYPLQPLTAEAfqdIESNADYVCLC 80
Cdd:COG0002     1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALT---SRSNAGKPVSEVHPHLRGLTDLVFEPPDPDE---LAAGCDVVFLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAA 160
Cdd:COG0002    75 LPHGVSMELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFEHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 161 LNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHL------GHPVLFTPHL 232
Cdd:COG0002   155 LLALAPLLKAGLIDPDDIIIDAKSGVSGAGRKASEGTHFSEVneNFRAYKVGGHRHTPEIEQELsrlageDVKVSFTPHL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 233 GNFPRGILETIYVQLKPGVTVEQVSAAY-QVLANEPLIRLL-GNKIPSIKGVAKQPFVDIAWQ--QKGEQLIVMSAIDNL 308
Cdd:COG0002   235 VPMVRGILATIYARLKDGVTEEDLRAAYeEFYADEPFVRVLpEGRLPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNL 314

                         330       340
                  ....*....|....*....|....
gi 1823258099 309 LKGAAGQALQCINLAMGEPHHTGL 332
Cdd:COG0002   315 VKGAAGQAVQNMNLMFGLPETTGL 338
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 1-332 6.25e-148

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: 420.06  E-value: 6.25e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEHLGLLEYPLQPLTAEafqDIESNADYVCLC 80
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSRES--AGKPVSEVHPHLRGLVDLNLEPIDVE---EILEDADVVFLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAA 160
Cdd:TIGR01850  76 LPHGVSAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFEHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTAT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 161 LNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHLG------HPVLFTPHL 232
Cdd:TIGR01850 156 LLALAPLLKEGLIDPTSIIVDAKSGVSGAGRKASEANHFPEVneNLRPYKVTGHRHTPEIEQELGrlaggkVKVSFTPHL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 233 GNFPRGILETIYVQLKPGVTVEQVSAAYQ-VLANEPLIRLLGNK-IPSIKGVAKQPFVDIAW--QQKGEQLIVMSAIDNL 308
Cdd:TIGR01850 236 VPMTRGILATIYAKLKDGLTEEDLRALYEeFYADEPFVRVLPEGgYPSTKAVIGSNFCDIGFavDERTGRVVVVSAIDNL 315

                         330       340
                  ....*....|....*....|....
gi 1823258099 309 LKGAAGQALQCINLAMGEPHHTGL 332
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGL 339
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 154-312 4.60e-80

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: 241.23  E-value: 4.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 154 GCYPTAALNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHLGH------P 225
Cdd:cd23934     1 GCYPTAALLALAPLLKAGLIEPDDIIIDAKSGVSGAGRKASETTHFSEVneNLKAYKVGGHRHTPEIEQELSKlagedvE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 226 VLFTPHLGNFPRGILETIYVQLKPGVTVEQVSAAYQ-VLANEPLIRLL-GNKIPSIKGVAKQPFVDIAWQQKGE--QLIV 301
Cdd:cd23934    81 VSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEeFYADEPFVRVLpEGQLPSTKAVRGSNFCDIGVAVDGRtgRLIV 160

                         170
                  ....*....|.
gi 1823258099 302 MSAIDNLLKGA 312
Cdd:cd23934   161 VSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 3-332 3.52e-74

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 233.57  E-value: 3.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   3 VVIIGASGYSGAELASLVAKHPKLTLQacyVSEGSLDKGKLLSDLYPeHLGLLEYPlqPLTAEAFQDIeSNADYVCLCTD 82
Cdd:PLN02968   41 IFVLGASGYTGAEVRRLLANHPDFEIT---VMTADRKAGQSFGSVFP-HLITQDLP--NLVAVKDADF-SDVDAVFCCLP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099  83 HKVSVDLApKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVAGCYPTAALN 162
Cdd:PLN02968  114 HGTTQEII-KALPKDLKIVDLSADFRLRDIAEYEEWYGHPHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 163 SLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEVS--LAPYGLFNHRHTPEIEQ------HLGHPVLFTPHLGN 234
Cdd:PLN02968  193 PLVPLVKAGLIEPDNIIIDAKSGVSGAGRGAKEANLYTEIAegIGAYGVTRHRHVPEIEQgladaaGSKVTPSFTPHLMP 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 235 FPRGILETIYVQLKPGVTVEQVsaaYQVL----ANEPLIRLLGnkipsiKGVAKQP---------FVDIAWQQKGEQLIV 301
Cdd:PLN02968  273 MSRGMQSTVYVHYAPGVTAEDL---HQHLkeryEGEEFVKVLE------RGAVPHTdhvrgsnycELNVFADRIPGRAII 343

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1823258099 302 MSAIDNLLKGAAGQALQCINLAMGEPHHTGL 332
Cdd:PLN02968  344 ISVIDNLVKGASGQAVQNLNLMMGLPETTGL 374
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 1-152 3.10e-57

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: 183.01  E-value: 3.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldkGKLLSDLYPEHLGLLEYPLQPLTAEAfqdIESNADYVCLC 80
Cdd:cd17895     1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYA---GKPVSEVFPHLRGLTDLTFEPDDDEE---IAEDADVVFLA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAV 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 4.65e-45

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: 151.50  E-value: 4.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 155 CYPTAALNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEV--SLAPYGLFNHRHTPEIEQHLG--HPVLFTP 230
Cdd:cd18125     1 CYATAALLALYPLLKAGLLKPTPITVTGVSGTSGAGRAASPASLHPEVagSLRPYALSGHRHTPEIAQNLGgkHNVHFTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 231 HLGNFPRGILETIYVQLKPGVTVEQVSAAY-QVLANEPLIRLLGNKI-PSIKGVAKQPFVDIAWQ--QKGEQLIVMSAID 306
Cdd:cd18125    81 HVGPWVRGILMTIQCFTQKGWSLRQLHEAYrEAYAGEPFVRVMPQGKgPDPKFVQGTNYADIGVEleEDTGRLVVMSAID 160


                  ....*.
gi 1823258099 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 4.15e-38

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: 133.52  E-value: 4.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 154 GCYPTAALNSLKPLKEAGLLADQAIIVNAVSGVTGAGRKASVNTHFCEVSLA--PYGLFNHRHTPEIEQHLGH-----PV 226
Cdd:cd23939     1 GCNATASILALYPLVKAGLLDDERIVVDVKVGSSGAGAEASEASHHPERSGVvrPYKPTGHRHTAEIEQELGLlareiSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 227 LFTPHLGNFPRGILETIYVQLKPGVTVEQVSAAY-QVLANEPLIRLLGNK-----IPSIKGVAKQPFVDIAWQ--QKGEQ 298
Cdd:cd23939    81 SFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYrKAYGNEPFVRIVKDRkgiyrYPDPKLVIGSNFCDIGFEldEDNGR 160

                         170
                  ....*....|....
gi 1823258099 299 LIVMSAIDNLLKGA 312
Cdd:cd23939   161 LVVFSAIDNLMKGA 174
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 154-312 1.09e-30

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: 113.88  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 154 GCYPTAALNSLKPLKEaglLADQAIIVNAVSGVTGAGRKASV--NTHFCEVSLAPYGLFNHRHTPEIEQHLGHPVLFTPH 231
Cdd:cd23936     1 GCYATGAQLALAPLLD---DLDGPPSVFGVSGYSGAGTKPSPknDPEVLADNLIPYSLVGHIHEREVSRHLGTPVAFMPH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 232 LGNFPRGILETIYVQLKPGVTVEQVSAAYQ-VLANEPLIRLLGNkIPSIKGVAKQPFVDI---AWQQKGEQLIVMSAIDN 307
Cdd:cd23936    78 VAPWFQGITLTISIPLKKSMTADEIRELYQeAYAGEPLIKVTKE-IPLVRDNAGKHGVVVggfTVHPDGKRVVVVATIDN 156


                  ....*
gi 1823258099 308 LLKGA 312
Cdd:cd23936   157 LLKGA 161
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 2-147 2.99e-28

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: 106.07  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   2 NVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEHLGLLEYPLQPLTAEAFQDIesnaDYVCLCT 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRS--AGKKLAFVHPILEGGKDLVVEDVDPEDFKDV----DIVFFAL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823258099  82 DHKVSVDLAPKFLAMGKKVFDLSGGFRLAgnedyltyygfahehpallEQAAYGLAEWNSDAISKA 147
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAKVIDLSSDFRMD-------------------DDVPYGLPEVNREAIKQA 121
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 154-312 2.38e-26

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: 102.68  E-value: 2.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 154 GCYPTAALNSLKPLKEAGLL-ADQAIIVNAVSGVTGAGRKAsVNTHFCEV-----SLAPYGL-FNHRHTPEIEQH--LGH 224
Cdd:cd23935     1 GCYATGAILLLRPLVEAGLLpADYPLSIHAVSGYSGGGKKM-IEQYEAAEaadlpPPRPYGLgLEHKHLPEMQKHagLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 225 PVLFTPHLGNFPRGILETI---YVQLKPGVTVEQVSAAY----------QVL---ANEPLIRLLGNkipsikGVAKQPFV 288
Cdd:cd23935    80 PPIFTPAVGNFYQGMLVTVplhLDLLEKGVSAAEVHEALaehyagerfvKVMpldEPDALGFLDPQ------ALNGTNNL 153

                         170       180
                  ....*....|....*....|....*
gi 1823258099 289 DIAWQ-QKGEQLIVMSAIDNLLKGA 312
Cdd:cd23935   154 ELFVFgNDKGQALLVARLDNLGKGA 178
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 2-147 1.92e-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: 1.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099    2 NVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSldKGKLLSDLYPEhlgLLEYPLQPLTAEAFQDIEsnADYVCLCT 81
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRS--AGKKVSEAGPH---LKGEVVLELDPPDFEELA--VDIVFLAL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823258099   82 DHKVS---VDLAPKFLAMGKKVFDLSGGFRLAgnedyltyygfahehpallEQAAYGLAEWNSDAISKA 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 1.16e-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: 95.42  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQAcyVSEGSLDkGKLLSDLYPehlglleyPLQPLTAEAF---QDIESnADYV 77
Cdd:cd24151     1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQ--VTSESLA-GKPVHRVHP--------NLRGRTLLKFvppEELES-CDVL 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823258099  78 CLCTDHKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEHPALLEQAAYGLAEWNSDAISKADLVAVA 153
Cdd:cd24151    69 FLALPHGESMKRIDRFAELAPRIIDLSADFRLKDPAAYDRWYGGPHPRPELLERFVYGLPELHREELRGARYIAGA 144
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 164-310 1.97e-22

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: 91.99  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 164 LKPLKEAGLLADqAIIVNAVSGVTGAGRKASVNTHF--CEVSLAPY-GLFNHRHTPEIEQHLGHPVLFTPHLGNFP---- 236
Cdd:pfam02774   1 LKPLRDALGGLE-RVIVDTYQAVSGAGKKAKPGVFGapIADNLIPYiDGEEHNGTPETREELKMVNETKKILGFTPkvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 237 --------RGILETIYVQLKPgvTVEQVSAAYQVLANEP---LIRLLGNKIPSIKGVA-KQPFVDIAWQQK----GEQLI 300
Cdd:pfam02774  80 tcvrvpvfRGHSETVTVKLKL--KPIDVEEVYEAFYAAPgvfVVVRPEEDYPTPRAVRgGTNFVYVGRVRKdpdgDRGLK 157

                         170
                  ....*....|
gi 1823258099 301 VMSAIDNLLK 310
Cdd:pfam02774 158 LVSVIDNLRK 167
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 1-152 6.59e-14

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: 68.47  E-value: 6.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQAcyVSEGSlDKGKLLSDLYPEHLGLLEYPLQPLTAEAFQDiesnADYVCLC 80
Cdd:cd24148     1 IRVAVAGASGYAGGELLRLLLGHPEFEIGA--LTAHS-NAGQRLGELHPHLPPLADRVLEPTTPAVLAG----HDVVFLA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823258099  81 TDHKVSVDLAPKfLAMGKKVFDLSGGFRLAGNEDYLTYYGFAHEhpallEQAAYGLAE--WNSDAISKADLVAV 152
Cdd:cd24148    74 LPHGASAAIAAQ-LPPDVLVVDCGADHRLEDAAAWEKFYGGEHA-----GGWTYGLPElpGAREALAGARRIAV 141
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-153 8.95e-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: 62.59  E-value: 8.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   3 VVIIGASGYSGAELASLVAKHPKLTLQacYVSEGSLdKGKLLSDLYPEHLGLLEYpLQPLTAEAFQdiesNADYVCLCTD 82
Cdd:cd02280     3 VAIIGASGYTGLEIVRLLLGHPYLRVL--TLSSRER-AGPKLREYHPSLIISLQI-QEFRPCEVLN----SADILVLALP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823258099  83 HKVSVDLAPKFLAMGKKVFDLSGGFRLAGNEDYLTYYGfahehPALLEQAAYGLAEWNSDA-ISKADLVAVA 153
Cdd:cd02280    75 HGASAELVAAISNPQVKIIDLSADFRFTDPEVYRRHPR-----PDLEGGWVYGLPELDREQrIANATRIANP 141
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 155-308 5.50e-11

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: 60.23  E-value: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 155 CYPTAALNSLKPLKEAGLLadQAIIVNAVSGVTGAGRKASVNTHFCEVSLA--PYGLFNHRHTPEIEQHLGH-----PVL 227
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGI--EEILVVTVQAVSGAGPKTKGPILKSEVRAIipNIPKNETKHAPETGKVLGEigkpiKVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 228 FTPHLGNFPRGILETIYVQLKPGVTVEQVSAAY-------QVLANEPLIrllgNKIPSIKGVAKQPFVDIAWQQK----G 296
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVaeaveevQISAEDGLT----YAKVSTRSVGGVYGVPVGRQREfafdD 154

                         170
                  ....*....|..
gi 1823258099 297 EQLIVMSAIDNL 308
Cdd:cd18122   155 NKLKVFSAVDNE 166
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 1-111 2.64e-07

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: 49.28  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHP-----KLTLQACYVSEGSLDKGKllsDLYPEHLglleypLQPLTAEAFqdieSNAD 75
Cdd:cd02281     1 KKVGVVGATGYVGGEFLRLLLEHPfplfeIVLLAASSAGAKKKYFHP---KLWGRVL------VEFTPEEVL----EQVD 67

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823258099  76 YVCLCTDHKVSVDLAPKFLAMGKKVFDLSGGFRLAG 111
Cdd:cd02281    68 IVFTALPGGVSAKLAPELSEAGVLVIDNASDFRLDK 103
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 2-70 9.05e-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: 45.18  E-value: 9.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   2 NVVIIGASGYSGAELASLVAKHPKLTLqaCYVSEGSLdKGKLLSDLYP-EHLGLLEYPLQPLTAEAFQDI 70
Cdd:cd24149     2 RVGLIGARGYVGRELIRLLNRHPNLEL--AHVSSREL-AGQKVSGYTKsPIDYLNLSVEDIPEEVAAREV 68
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 307-325 3.25e-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: 43.25  E-value: 3.25e-05
                          10
                  ....*....|....*....
gi 1823258099 307 NLLKGAAGQALQCINLAMG 325
Cdd:cd24149   132 NLLKGAATQALQNLNLALG 150
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 1-109 1.33e-04

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: 41.55  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHP----KLTLQACYVSEGSL--DKGKLLsdlypehlglleyPLQPLTAEAFQDIesna 74
Cdd:cd24147     1 LRVGVVGATGAVGSEILQLLAEEPdplfELRALASEESAGKKaeFAGEAI-------------MVQEADPIDFLGL---- 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1823258099  75 DYVCLCTDHKVSVDLAPKFLAMGKKVFDLSGGFRL 109
Cdd:cd24147    64 DIVFLCAGAGVSAKFAPEAARAGVLVIDNAGALRM 98
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 1-101 2.51e-04

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: 40.94  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSLDK------GKLLSDLYPEHLGllEYPLQPLTAEAFQDIesna 74
Cdd:cd02315     1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKkygdavRWKQDTPIPEEVA--DMVVKECEPEEFKDC---- 74

                          90       100
                  ....*....|....*....|....*..
gi 1823258099  75 DYVCLCTDHKVSVDLAPKFLAMGKKVF 101
Cdd:cd02315    75 DIVFSALDSDVAGEIEPAFAKAGIPVF 101
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 1-108 3.66e-04

N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase 2 (ASADH2) and similar proteins; The family corresponds to a new branch of bacterial ASADH enzymes that has a similar overall fold and domain organization but sharing less sequence homology with the other bacterial ASADHs. The second isoform of ASADH in Vibrio cholerae is one of the prototypes of this family. It also includes ASADHs from Streptococcus pneumoniae, Mycobacterium tuberculosis, Thermus thermophilus, as well as from eukaryotes. 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.


Pssm-ID: 467519 [Multi-domain]  Cd Length: 142  Bit Score: 40.11  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVA--KHP--KLTLQAcyvSEGSldKGKLLSdlypehLGLLEYPLQPLTAEAFQDIesnaDY 76
Cdd:cd02316     1 YNVAIVGATGAVGQEMLKVLEerNFPvsELRLLA---SARS--AGKTLE------FKGKELTVEELTEDSFKGV----DI 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823258099  77 VCLCTDHKVSVDLAPKFLAMGKKVFDLSGGFR 108
Cdd:cd02316    66 ALFSAGGSVSKEFAPIAAEAGAVVIDNSSAFR 97
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 236-325 1.77e-03

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: 38.32  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099 236 PRGILETIYVQLK-PGVTVEQVSAAYQVLANEPLIRLLGNKIpSIKGVAKQPFVDIAWQQKGEQLIvmsAIDNLLKGAAG 314
Cdd:cd02280    74 PHGASAELVAAISnPQVKIIDLSADFRFTDPEVYRRHPRPDL-EGGWVYGLPELDREQRIANATRI---ANPNLVKGAAG 149

                          90
                  ....*....|.
gi 1823258099 315 QALQCINLAMG 325
Cdd:cd02280   150 AAVQNLNLALG 160
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 1-100 3.43e-03

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: 37.15  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823258099   1 MNVVIIGASGYSGAELASLVAKHPKLTLQACYVSEGSLDKGKLLSDLYPEHLGLLEYplqpLTAEAfqdIESNADYVCLC 80
Cdd:cd02274     1 IKVAVAGATGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGGLAGIGTGVIVS----LDLEL---AAADADVVIDF 73

                          90       100
                  ....*....|....*....|
gi 1823258099  81 TDHKVSVDLAPKFLAMGKKV 100
Cdd:cd02274    74 TTPEATLENLEAAAKAGVPL 93
 
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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