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Conserved domains on  [gi|490160079|ref|WP_004058744|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Haloferax mediterranei]

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]; ...
 5-343 8.57e-165

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: 463.39  E-value: 8.57e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHL-DLRFTSP---ADLESVDVLFTATPHGVS 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLtDLVFEPPdpdELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  81 MEHIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGLKP 159
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFeHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 160 LFDADILSGDEqVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------SVSFTVHAVDMVR 233
Cdd:COG0002  161 LLKAGLIDPDD-IIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRlagedvKVSFTPHLVPMVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 234 GAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDNMM 313
Cdd:COG0002  240 GILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEG----RLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLV 315

                        330       340       350
                 ....*....|....*....|....*....|
gi 490160079 314 KGSAGQAVHAANIALGLEETAGLDFTGYHP 343
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGLELVPLYP 345
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-343 8.57e-165

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: 463.39  E-value: 8.57e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHL-DLRFTSP---ADLESVDVLFTATPHGVS 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLtDLVFEPPdpdELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  81 MEHIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGLKP 159
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFeHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 160 LFDADILSGDEqVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------SVSFTVHAVDMVR 233
Cdd:COG0002  161 LLKAGLIDPDD-IIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRlagedvKVSFTPHLVPMVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 234 GAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDNMM 313
Cdd:COG0002  240 GILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEG----RLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLV 315

                        330       340       350
                 ....*....|....*....|....*....|
gi 490160079 314 KGSAGQAVHAANIALGLEETAGLDFTGYHP 343
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 5-343 2.07e-145

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: 414.29  E-value: 2.07e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079    5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQ-ATSRSYERKTVGHVHPNLRHL-DLRFTSPAD---LESVDVLFTATPHGV 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYlVSSRESAGKPVSEVHPHLRGLvDLNLEPIDVeeiLEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   80 SMEHIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGLK 158
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFeHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  159 PLFDADILSgDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------SVSFTVHAVDMV 232
Cdd:TIGR01850 161 PLLKEGLID-PTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRlaggkvKVSFTPHLVPMT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  233 RGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDNM 312
Cdd:TIGR01850 240 RGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEG----GYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNL 315

                         330       340       350
                  ....*....|....*....|....*....|.
gi 490160079  313 MKGSAGQAVHAANIALGLEETAGLDFTGYHP 343
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGLPFPPLYP 346
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 147-316 4.49e-97

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: 284.90  E-value: 4.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 147 GCNATATILGLKPLFDADILsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL-----S 221
Cdd:cd23939    1 GCNATASILALYPLVKAGLL-DDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLlareiS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 222 VSFTVHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGGGVYRYPEPKSVAGTNFGEVGFEIDPTNR 301
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKDRKGIYRYPDPKLVIGSNFCDIGFELDEDNG 159

                        170
                 ....*....|....*
gi 490160079 302 RLVVFSAIDNMMKGS 316
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-336 3.90e-69

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 220.85  E-value: 3.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   2 SEQLTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHLDLRF---TSPADLESVDVLFTATPHG 78
Cdd:PLN02968  36 EEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNlvaVKDADFSDVDAVFCCLPHG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  79 VSMEHIDAFQDAaDTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGL 157
Cdd:PLN02968 116 TTQEIIKALPKD-LKIVDLSADFRLRDIAEYEEWYGHpHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 158 KPLFDADILsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYL------GLSVSFTVHAVDM 231
Cdd:PLN02968 195 VPLVKAGLI-EPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLadaagsKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 232 VRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGGgvyrYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDN 311
Cdd:PLN02968 274 SRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGA----VPHTDHVRGSNYCELNVFADRIPGRAIIISVIDN 349

                        330       340
                 ....*....|....*....|....*
gi 490160079 312 MMKGSAGQAVHAANIALGLEETAGL 336
Cdd:PLN02968 350 LVKGASGQAVQNLNLMMGLPETTGL 374
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-137 5.61e-30

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: 110.69  E-value: 5.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079    6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYER-KTVGHVHPNLRHL-DLRF--TSPADLESVDVLFTATPHGVSM 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAgKKLAFVHPILEGGkDLVVedVDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490160079   82 EHIDAFQDAADTVVDLSADFRLSEETQydewydghicpeylekseYALPELNRENL 137
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDDDVP------------------YGLPEVNREAI 118
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-140 2.60e-29

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: 109.18  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079     6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQ-ATSRSYERKTVGHVHPNLRHLDLRFTSPADLE--SVDVLFTATPHGVSME 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTAlAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEelAVDIVFLALPHGVSKE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490160079    83 HIDAFQDAAD---TVVDLSADFRLSEEtqydewydghicpeylekSEYALPELNRENLPGA 140
Cdd:smart00859  81 SAPLLPRAAAagaVVIDLSSAFRMDDD------------------VPYGLPEVNPEAIKKA 123
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-343 8.57e-165

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: 463.39  E-value: 8.57e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHL-DLRFTSP---ADLESVDVLFTATPHGVS 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLtDLVFEPPdpdELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  81 MEHIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGLKP 159
Cdd:COG0002   81 MELAPELLEAGVKVIDLSADFRLKDPAVYEKWYGFeHAAPELLGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 160 LFDADILSGDEqVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------SVSFTVHAVDMVR 233
Cdd:COG0002  161 LLKAGLIDPDD-IIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRlagedvKVSFTPHLVPMVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 234 GAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDNMM 313
Cdd:COG0002  240 GILATIYARLKDGVTEEDLRAAYEEFYADEPFVRVLPEG----RLPETKSVRGSNFCDIGVAVDERTGRLVVVSAIDNLV 315

                        330       340       350
                 ....*....|....*....|....*....|
gi 490160079 314 KGSAGQAVHAANIALGLEETAGLDFTGYHP 343
Cdd:COG0002  316 KGAAGQAVQNMNLMFGLPETTGLELVPLYP 345
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 5-343 2.07e-145

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: 414.29  E-value: 2.07e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079    5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQ-ATSRSYERKTVGHVHPNLRHL-DLRFTSPAD---LESVDVLFTATPHGV 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYlVSSRESAGKPVSEVHPHLRGLvDLNLEPIDVeeiLEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   80 SMEHIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGLK 158
Cdd:TIGR01850  81 SAELAPELLAAGVKVIDLSADFRLKDPELYEKWYGFeHAGPELLQKAVYGLPELHREEIKGARLIANPGCYPTATLLALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  159 PLFDADILSgDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------SVSFTVHAVDMV 232
Cdd:TIGR01850 161 PLLKEGLID-PTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRlaggkvKVSFTPHLVPMT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  233 RGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDNM 312
Cdd:TIGR01850 240 RGILATIYAKLKDGLTEEDLRALYEEFYADEPFVRVLPEG----GYPSTKAVIGSNFCDIGFAVDERTGRVVVVSAIDNL 315

                         330       340       350
                  ....*....|....*....|....*....|.
gi 490160079  313 MKGSAGQAVHAANIALGLEETAGLDFTGYHP 343
Cdd:TIGR01850 316 VKGAAGQAVQNMNLMFGFDETTGLPFPPLYP 346
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 147-316 4.49e-97

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: 284.90  E-value: 4.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 147 GCNATATILGLKPLFDADILsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL-----S 221
Cdd:cd23939    1 GCNATASILALYPLVKAGLL-DDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLlareiS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 222 VSFTVHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGGGVYRYPEPKSVAGTNFGEVGFEIDPTNR 301
Cdd:cd23939   80 VSFTAHSVDMVRGILATAHVFLKEGVTEKDLWKAYRKAYGNEPFVRIVKDRKGIYRYPDPKLVIGSNFCDIGFELDEDNG 159

                        170
                 ....*....|....*
gi 490160079 302 RLVVFSAIDNMMKGS 316
Cdd:cd23939  160 RLVVFSAIDNLMKGA 174
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 5-146 1.04e-83

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: 251.04  E-value: 1.04e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHLDLRFTSP-ADLESVDVLFTATPHGVSMEH 83
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTLLKFVPpEELESCDVLFLALPHGESMKR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490160079  84 IDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAG 146
Cdd:cd24151   81 IDRFAELAPRIIDLSADFRLKDPAAYDRWYGGpHPRPELLERFVYGLPELHREELRGARYIAGA 144
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-336 3.90e-69

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 220.85  E-value: 3.90e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   2 SEQLTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHLDLRF---TSPADLESVDVLFTATPHG 78
Cdd:PLN02968  36 EEKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDLPNlvaVKDADFSDVDAVFCCLPHG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  79 VSMEHIDAFQDAaDTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIAAGGCNATATILGL 157
Cdd:PLN02968 116 TTQEIIKALPKD-LKIVDLSADFRLRDIAEYEEWYGHpHRAPELQKEAVYGLTELQREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 158 KPLFDADILsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYL------GLSVSFTVHAVDM 231
Cdd:PLN02968 195 VPLVKAGLI-EPDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLadaagsKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 232 VRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGGgvyrYPEPKSVAGTNFGEVGFEIDPTNRRLVVFSAIDN 311
Cdd:PLN02968 274 SRGMQSTVYVHYAPGVTAEDLHQHLKERYEGEEFVKVLERGA----VPHTDHVRGSNYCELNVFADRIPGRAIIISVIDN 349

                        330       340
                 ....*....|....*....|....*
gi 490160079 312 MMKGSAGQAVHAANIALGLEETAGL 336
Cdd:PLN02968 350 LVKGASGQAVQNLNLMMGLPETTGL 374
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 147-315 1.85e-56

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: 181.14  E-value: 1.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 147 GCNATATILGLKPLFDADILSGDEqVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL------ 220
Cdd:cd23934    1 GCYPTAALLALAPLLKAGLIEPDD-IIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKlagedv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 221 SVSFTVHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTN 300
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKDGVTAEDVRALYEEFYADEPFVRVLPEG----QLPSTKAVRGSNFCDIGVAVDGRT 155

                        170
                 ....*....|....*
gi 490160079 301 RRLVVFSAIDNMMKG 315
Cdd:cd23934  156 GRLIVVSAIDNLVKG 170
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 7-144 1.65e-54

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: 176.08  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   7 AGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHL-DLRFTSP---ADLESVDVLFTATPHGVSME 82
Cdd:cd17895    3 VGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLtDLTFEPDddeEIAEDADVVFLALPHGVSME 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490160079  83 HIDAFQDAADTVVDLSADFRLSEETQYDEWYDG-HICPEYLEKSEYALPELNRENLPGADLIA 144
Cdd:cd17895   83 LAPKLLEAGVKVIDLSADFRLKDPETYEKWYGFeHAAPELLKEAVYGLPELNREEIKKARLVA 145
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 148-316 3.28e-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: 149.57  E-value: 3.28e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 148 CNATATILGLKPLFDADILSgDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGL--SVSFT 225
Cdd:cd18125    1 CYATAALLALYPLLKAGLLK-PTPITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNLGGkhNVHFT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 226 VHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGGggvyRYPEPKSVAGTNFGEVGFEIDPTNRRLVV 305
Cdd:cd18125   80 PHVGPWVRGILMTIQCFTQKGWSLRQLHEAYREAYAGEPFVRVMPQG----KGPDPKFVQGTNYADIGVELEEDTGRLVV 155

                        170
                 ....*....|.
gi 490160079 306 FSAIDNMMKGS 316
Cdd:cd18125  156 MSAIDNLVKGA 166
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 6-144 4.86e-32

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: 117.67  E-value: 4.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLR--HLDLRFTSPADLESVDVLFTATPHGVSMEH 83
Cdd:cd02280    2 RVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIisLQIQEFRPCEVLNSADILVLALPHGASAEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490160079  84 IDAFQDAADTVVDLSADFRLSEETQYDEWYDGHICPEYLekseYALPELNREN-LPGADLIA 144
Cdd:cd02280   82 VAAISNPQVKIIDLSADFRFTDPEVYRRHPRPDLEGGWV----YGLPELDREQrIANATRIA 139
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-137 5.61e-30

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: 110.69  E-value: 5.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079    6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYER-KTVGHVHPNLRHL-DLRF--TSPADLESVDVLFTATPHGVSM 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAgKKLAFVHPILEGGkDLVVedVDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490160079   82 EHIDAFQDAADTVVDLSADFRLSEETQydewydghicpeylekseYALPELNRENL 137
Cdd:pfam01118  81 EIAPKLAEAGAKVIDLSSDFRMDDDVP------------------YGLPEVNREAI 118
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 6-144 6.77e-30

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: 112.00  E-value: 6.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHL-DLRF--TSPADLESVDVLFTATPHGVSME 82
Cdd:cd24148    2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLaDRVLepTTPAVLAGHDVVFLALPHGASAA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490160079  83 hIDAFQDAADTVVDLSADFRLSEETQYDEWYDGhicpEYLEKSEYALPEL--NRENLPGADLIA 144
Cdd:cd24148   82 -IAAQLPPDVLVVDCGADHRLEDAAAWEKFYGG----EHAGGWTYGLPELpgAREALAGARRIA 140
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-140 2.60e-29

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: 109.18  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079     6 TAGVVGGSGFTGGELLRLLDGHPNFEVAQ-ATSRSYERKTVGHVHPNLRHLDLRFTSPADLE--SVDVLFTATPHGVSME 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTAlAASSRSAGKKVSEAGPHLKGEVVLELDPPDFEelAVDIVFLALPHGVSKE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490160079    83 HIDAFQDAAD---TVVDLSADFRLSEEtqydewydghicpeylekSEYALPELNRENLPGA 140
Cdd:smart00859  81 SAPLLPRAAAagaVVIDLSSAFRMDDD------------------VPYGLPEVNPEAIKKA 123
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 8-144 1.69e-26

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: 102.58  E-value: 1.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   8 GVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRH-LDLRFTSPADLE---SVDVLFTATPHGVSMEH 83
Cdd:cd24149    4 GLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVSGYTKSPIDyLNLSVEDIPEEVaarEVDAWVLALPNGVAKPF 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490160079  84 IDAFQDAA-DTV-VDLSADFRLSeetqyDEWYdghicpeylekseYALPELNRENLPGADLIA 144
Cdd:cd24149   84 VDAIDKANpKSViVDLSADYRFD-----DAWT-------------YGLPELNRRRIAGAKRIS 128
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 147-315 1.43e-20

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: 86.92  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 147 GCNATATILGLKPLfdADILSGDEQVVvdvkvGSSeGGAGASKASSHAE-----RSGIVrPYAPTGHRHEAEIEEYLGLS 221
Cdd:cd23936    1 GCYATGAQLALAPL--LDDLDGPPSVF-----GVS-GYSGAGTKPSPKNdpevlADNLI-PYSLVGHIHEREVSRHLGTP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 222 VSFTVHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFMRTVAGgggvyrYPEPKSVAGTNFGEV-GFEIDPTN 300
Cdd:cd23936   72 VAFMPHVAPWFQGITLTISIPLKKSMTADEIRELYQEAYAGEPLIKVTKE------IPLVRDNAGKHGVVVgGFTVHPDG 145

                        170
                 ....*....|....*
gi 490160079 301 RRLVVFSAIDNMMKG 315
Cdd:cd23936  146 KRVVVVATIDNLLKG 160
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 6-146 1.04e-18

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: 81.64  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   6 TAGVVGGSGFTGGELLRLLDGHPN-FEVAQATSRSYERKTVGHVHPNLRHLDL-RFTSPADLESVDVLFTATPHGVSMEH 83
Cdd:cd02281    2 KVGVVGATGYVGGEFLRLLLEHPFpLFEIVLLAASSAGAKKKYFHPKLWGRVLvEFTPEEVLEQVDIVFTALPGGVSAKL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490160079  84 IDAFQDAADTVVDLSADFRlseetqydewydghicpeYLEKSEYALPELNRENLP---GADLIAAG 146
Cdd:cd02281   82 APELSEAGVLVIDNASDFR------------------LDKDVPLVVPEVNREHIGelkGTKIIANP 129
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 157-314 1.60e-13

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: 67.72  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  157 LKPLFDADIlsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTG-HRHEAEIEEYLGL------------SVS 223
Cdd:pfam02774   1 LKPLRDALG--GLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIDGEeHNGTPETREELKMvnetkkilgftpKVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  224 FTVHAVDMVRGAAATCHVFPDG-PVSKGDMWKAFRGsyGDEPFMRTVAGGGgvyrYPEPKSVAG-TNFGEVG-FEIDP-T 299
Cdd:pfam02774  79 ATCVRVPVFRGHSETVTVKLKLkPIDVEEVYEAFYA--APGVFVVVRPEED----YPTPRAVRGgTNFVYVGrVRKDPdG 152

                         170
                  ....*....|....*
gi 490160079  300 NRRLVVFSAIDNMMK 314
Cdd:pfam02774 153 DRGLKLVSVIDNLRK 167
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 147-316 2.13e-11

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: 61.85  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 147 GCNATATILGLKPLFDADILSGDEQVVVDVKVGSSEGGAGASKASSHAERSGI--VRPYAPT-GHRHEAEIEEYLGLSVS 223
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYPLSIHAVSGYSGGGKKMIEQYEAAEAADLppPRPYGLGlEHKHLPEMQKHAGLARP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 224 --FTVHAVDMVRGAAATCHVFPD---GPVSKGDMWKAFRGSYGDEPFMRTV-AGGGGVYRYPEPKSVAGTNFGEVGFEID 297
Cdd:cd23935   81 piFTPAVGNFYQGMLVTVPLHLDlleKGVSAAEVHEALAEHYAGERFVKVMpLDEPDALGFLDPQALNGTNNLELFVFGN 160

                        170
                 ....*....|....*....
gi 490160079 298 PTNRRLVVfSAIDNMMKGS 316
Cdd:cd23935  161 DKGQALLV-ARLDNLGKGA 178
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 8-174 1.12e-07

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439906 [Multi-domain]  Cd Length: 333  Bit Score: 52.73  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   8 GVVGGSGFTGGELLRLLDGHpNFEVAQ----ATSRSyERKTV---GHVHPnlrhldLRFTSPADLESVDVLFTATPHGVS 80
Cdd:COG0136    4 AVVGATGAVGRVLLELLEER-DFPVGElrllASSRS-AGKTVsfgGKELT------VEDATDFDFSGVDIALFSAGGSVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  81 MEHIDAFQDAADTVVDLSADFRLSEETqydewydghicPeyLekseyALPELNRENLPGAD---LIAAGGCNATATILGL 157
Cdd:COG0136   76 KEYAPKAAAAGAVVIDNSSAFRMDPDV-----------P--L-----VVPEVNPEALADHLpkgIIANPNCSTIQMLVAL 137

                        170
                 ....*....|....*..
gi 490160079 158 KPLFDADILsgdEQVVV 174
Cdd:COG0136  138 KPLHDAAGI---KRVVV 151
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 5-106 1.66e-07

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: 50.03  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGH--PNFE-VAQATSRS----YE-RKTVGHVHPnlrhldlrfTSPADLESVDVLFTATP 76
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEpdPLFElRALASEESagkkAEfAGEAIMVQE---------ADPIDFLGLDIVFLCAG 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 490160079  77 HGVSMEHIDAFQDAADTVVDLSADFRLSEE 106
Cdd:cd24147   72 AGVSAKFAPEAARAGVLVIDNAGALRMDPD 101
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 148-311 1.47e-06

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: 47.51  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 148 CNATATILGLKPLFDADilsGDEQVVVDVKVGSSEGGAGASKASSHAERSGIVRPYAPTGHRHEAEIEEYLGLS-----V 222
Cdd:cd18122    1 CTTTGLIPAAKALNDKF---GIEEILVVTVQAVSGAGPKTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEIgkpikV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079 223 SFTVHAVDMVRGAAATCHVFPDGPVSKGDMWKAFRGSYGDEPFmrtVAGGGGVYRYPEPKSVAGTNFGEVG--FEIDPTN 300
Cdd:cd18122   78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQI---SAEDGLTYAKVSTRSVGGVYGVPVGrqREFAFDD 154

                        170
                 ....*....|.
gi 490160079 301 RRLVVFSAIDN 311
Cdd:cd18122  155 NKLKVFSAVDN 165
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 5-174 2.09e-06

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 49.05  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQ--ATSRS----YER----KTVGHVHPNLRHLDLRFTSPADLESVDVLFTA 74
Cdd:PRK08664   4 LKVGILGATGMVGQRFVQLLANHPWFEVTAlaASERSagktYGEavrwQLDGPIPEEVADMEVVSTDPEAVDDVDIVFSA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  75 TPHGVSMEHIDAFQDAADTVVDLSADFRLSE-------EtqydewydghICPEYLEkseyaLPELNRENLpGAD--LIAA 145
Cdd:PRK08664  84 LPSDVAGEVEEEFAKAGKPVFSNASAHRMDPdvplvipE----------VNPEHLE-----LIEVQRKRR-GWDgfIVTN 147

                        170       180
                 ....*....|....*....|....*....
gi 490160079 146 GGCNATATILGLKPLFDADIlsgdEQVVV 174
Cdd:PRK08664 148 PNCSTIGLVLALKPLMDFGI----ERVHV 172
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 8-106 5.33e-06

N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes Escherichia coli USG-1 protein, Pseudomonas aeruginosa USG-1 homolog proteins and similar proteins. Although their biological function remains unknown, they are homologs to aspartate beta-semialdehyde dehydrogenase (ASADH) which contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like domain. However, USG-1 proteins lack the conserved active site residues of the ASADH protein C-terminal domain.


Pssm-ID: 467520 [Multi-domain]  Cd Length: 144  Bit Score: 45.69  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   8 GVVGGSGFTGGELLRLLDGHPnFEVAQATSRSYERKTVGHVHPNLRHLDLRFTSPADLESVDVLFTATPHGVSMEHIDAF 87
Cdd:cd17894    4 AVVGATGLVGKELLELLEERG-FPVGRLRLLDSEESAGELVEFGGEPLDVQDLDEFDFSDVDLVFFAGPAEVARAYAPRA 82

                         90
                 ....*....|....*....
gi 490160079  88 QDAADTVVDLSADFRLSEE 106
Cdd:cd17894   83 RAAGCLVIDLSGALRSDPD 101
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 5-102 1.07e-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: 45.17  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQ--ATSRSY--------ERKTVGHVHPNLRHLDLRFTSPADLESVDVLFTA 74
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAAlgASERSAgkkygdavRWKQDTPIPEEVADMVVKECEPEEFKDCDIVFSA 80

                         90       100
                 ....*....|....*....|....*...
gi 490160079  75 TPHGVSMEHIDAFQDAADTVVDLSADFR 102
Cdd:cd02315   81 LDSDVAGEIEPAFAKAGIPVFSNASNHR 108
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 5-103 2.23e-05

N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar proteins; Archaeal NADP-dependent MCR (EC 1.2.1.75) 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 malonyl-CoA reductase gene (mcr) has evolved from the duplication of a common ancestral aspartate beta-semialdehyde dehydrogenase (ASADH) gene (asd). MCR contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain.


Pssm-ID: 467526  Cd Length: 163  Bit Score: 44.24  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERK---------TVGHVHPNLRHLDLRFTSPADLESVDVLFTAT 75
Cdd:cd24150    2 LKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKpygevvrwqTVGQVPKEIADMEIKPTDPKLMDDVDIIFSPL 81

                         90       100
                 ....*....|....*....|....*...
gi 490160079  76 PHGVSMEHIDAFQDAADTVVDLSADFRL 103
Cdd:cd24150   82 PQGAAGPVEEQFAKEGFPVISNSPDHRF 109
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 1-187 7.49e-05

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 44.27  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   1 MSEQ-LTAGVVGGSGFTGGELLRLLDGHPNFEVAQATSRSYERKTVGHVHPNLRHLDLRFTSPADLESVDVLFTATPHGV 79
Cdd:PRK06728   1 MSEKgYHVAVVGATGAVGQKIIELLEKETKFNIAEVTLLSSKRSAGKTVQFKGREIIIQEAKINSFEGVDIAFFSAGGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079  80 SMEHIDAFQDAADTVVDLSADFRLSEETqydewydghicpeyleksEYALPELNRENL-PGADLIAAGGCNATATILGLK 158
Cdd:PRK06728  81 SRQFVNQAVSSGAIVIDNTSEYRMAHDV------------------PLVVPEVNAHTLkEHKGIIAVPNCSALQMVTALQ 142

                        170       180
                 ....*....|....*....|....*....
gi 490160079 159 PLFDAdilSGDEQVVVDVKVGSSEGGAGA 187
Cdd:PRK06728 143 PIRKV---FGLERIIVSTYQAVSGSGIHA 168
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 5-107 2.12e-03

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: 37.80  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490160079   5 LTAGVVGGSGFTGGELLRLLDGHpNFEVAQ----ATSRSYERKtvghVHPNLRHLDLRFTSPADLESVDVLFTATPHGVS 80
Cdd:cd02316    1 YNVAIVGATGAVGQEMLKVLEER-NFPVSElrllASARSAGKT----LEFKGKELTVEELTEDSFKGVDIALFSAGGSVS 75

                         90       100
                 ....*....|....*....|....*..
gi 490160079  81 MEHIDAFQDAADTVVDLSADFRLSEET 107
Cdd:cd02316   76 KEFAPIAAEAGAVVIDNSSAFRMDPDV 102
 
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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