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Conserved domains on  [gi|499905696|ref|WP_011586430|]
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N-acetyl-gamma-glutamyl-phosphate reductase [Cytophaga hutchinsonii]

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

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]; ...
 5-321 2.88e-155

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: 438.35  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFT----GELSNAIDVLFLCVGHGDA 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEppdpDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  81 IKFLQAnPVESHIKIIDLSQDFRIEKDG----------------NDFIYGLPELQRDKIKLAKNIANPGCFATAIQLGLL 144
Cdd:COG0002   81 MELAPE-LLEAGVKVIDLSADFRLKDPAvyekwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 145 PLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEKNIHFIPYRGDFT 223
Cdd:COG0002  160 PLLKAGLIdPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 224 RGIIATMYTPC--SWTIDEAIAKYKAYYASHPFTHVVDEN--IDLKQVVNTNNCLLYLE--KHGDQLMIVSIIDNLLKGA 297
Cdd:COG0002  239 RGILATIYARLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNLVKGA 318

                        330       340
                 ....*....|....*....|....
gi 499905696 298 SGHAVQNMNLMFGLEETVGLRLKA 321
Cdd:COG0002  319 AGQAVQNMNLMFGLPETTGLELVP 342
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-321 2.88e-155

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: 438.35  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFT----GELSNAIDVLFLCVGHGDA 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEppdpDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  81 IKFLQAnPVESHIKIIDLSQDFRIEKDG----------------NDFIYGLPELQRDKIKLAKNIANPGCFATAIQLGLL 144
Cdd:COG0002   81 MELAPE-LLEAGVKVIDLSADFRLKDPAvyekwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 145 PLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEKNIHFIPYRGDFT 223
Cdd:COG0002  160 PLLKAGLIdPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 224 RGIIATMYTPC--SWTIDEAIAKYKAYYASHPFTHVVDEN--IDLKQVVNTNNCLLYLE--KHGDQLMIVSIIDNLLKGA 297
Cdd:COG0002  239 RGILATIYARLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNLVKGA 318

                        330       340
                 ....*....|....*....|....
gi 499905696 298 SGHAVQNMNLMFGLEETVGLRLKA 321
Cdd:COG0002  319 AGQAVQNMNLMFGLPETTGLELVP 342
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 5-318 7.17e-114

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: 333.39  E-value: 7.17e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696    5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSN-AGNPIYKVHTDLIGSTDLVFTG----ELSNAIDVLFLCVGHGD 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLRGLVDLNLEPidveEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   80 AIKFLQANpVESHIKIIDLSQDFRIeKDGND-----------------FIYGLPELQRDKIKLAKNIANPGCFATAIQLG 142
Cdd:TIGR01850  81 SAELAPEL-LAAGVKVIDLSADFRL-KDPELyekwygfehagpellqkAVYGLPELHREEIKGARLIANPGCYPTATLLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  143 LLPLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEKNIHFIPYRGD 221
Cdd:TIGR01850 159 LAPLLKEGLIdPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGG-KVKVSFTPHLVP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  222 FTRGIIATMYTP--CSWTIDEAIAKYKAYYASHPFTHVVDENI--DLKQVVNTNNCLL--YLEKHGDQLMIVSIIDNLLK 295
Cdd:TIGR01850 238 MTRGILATIYAKlkDGLTEEDLRALYEEFYADEPFVRVLPEGGypSTKAVIGSNFCDIgfAVDERTGRVVVVSAIDNLVK 317

                         330       340
                  ....*....|....*....|...
gi 499905696  296 GASGHAVQNMNLMFGLEETVGLR 318
Cdd:TIGR01850 318 GAAGQAVQNMNLMFGFDETTGLP 340
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 133-297 1.91e-68

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: 211.18  E-value: 1.91e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 133 GCFATAIQLGLLPLAAEN-VLTNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEK 211
Cdd:cd23934    1 GCYPTAALLALAPLLKAGlIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGE-DV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 212 NIHFIPYRGDFTRGIIATMYTPCS--WTIDEAIAKYKAYYASHPFTHVVDENI--DLKQVVNTNNCLLYLEKHG--DQLM 285
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKdgVTAEDVRALYEEFYADEPFVRVLPEGQlpSTKAVRGSNFCDIGVAVDGrtGRLI 159

                        170
                 ....*....|..
gi 499905696 286 IVSIIDNLLKGA 297
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 4-317 5.34e-68

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 217.39  E-value: 5.34e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   4 KIKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGST--DLVFTGE-LSNAIDVLFLCVGHGDA 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDlpNLVAVKDaDFSDVDAVFCCLPHGTT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  81 IKFLQAnpVESHIKIIDLSQDFRIeKDGNDF-----------------IYGLPELQRDKIKLAKNIANPGCFATAIQLGL 143
Cdd:PLN02968 118 QEIIKA--LPKDLKIVDLSADFRL-RDIAEYeewyghphrapelqkeaVYGLTELQREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 144 LPLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNlQSSLEKNIHFIPYRGDF 222
Cdd:PLN02968 195 VPLVKAGLIePDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLAD-AAGSKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 223 TRGIIATMYTPCS--WTIDEAIAKYKAYYASHPFTHVVDENIDLK--QVVNTNNCLL--YLEKHGDQLMIVSIIDNLLKG 296
Cdd:PLN02968 274 SRGMQSTVYVHYApgVTAEDLHQHLKERYEGEEFVKVLERGAVPHtdHVRGSNYCELnvFADRIPGRAIIISVIDNLVKG 353

                        330       340
                 ....*....|....*....|.
gi 499905696 297 ASGHAVQNMNLMFGLEETVGL 317
Cdd:PLN02968 354 ASGQAVQNLNLMMGLPETTGL 374
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-126 6.21e-33

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: 118.03  E-value: 6.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696     6 KIGIVGGAGYTGGELLRILVNHPNAEIVFVH-SNSNAGNPIYKVHTDLIGSTDLVFTGE--LSNAIDVLFLCVGHGDAIK 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAaSSRSAGKKVSEAGPHLKGEVVLELDPPdfEELAVDIVFLALPHGVSKE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 499905696    83 FLQANP--VESHIKIIDLSQDFRIEkdgNDFIYGLPELQRDKIKLA 126
Cdd:smart00859  81 SAPLLPraAAAGAVVIDLSSAFRMD---DDVPYGLPEVNPEAIKKA 123
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-126 1.61e-31

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: 114.54  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696    6 KIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSN-AGNPIYKVHTDLIGSTDLVF---TGELSNAIDVLFLCVGHGDAI 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVedvDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499905696   82 KFLQANpVESHIKIIDLSQDFRIEkdgNDFIYGLPELQRDKIKLA 126
Cdd:pfam01118  81 EIAPKL-AEAGAKVIDLSSDFRMD---DDVPYGLPEVNREAIKQA 121
 
Name Accession Description Interval E-value
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-321 2.88e-155

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: 438.35  E-value: 2.88e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFT----GELSNAIDVLFLCVGHGDA 80
Cdd:COG0002    1 IKVGIVGASGYTGGELLRLLLRHPEVEIVALTSRSNAGKPVSEVHPHLRGLTDLVFEppdpDELAAGCDVVFLALPHGVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  81 IKFLQAnPVESHIKIIDLSQDFRIEKDG----------------NDFIYGLPELQRDKIKLAKNIANPGCFATAIQLGLL 144
Cdd:COG0002   81 MELAPE-LLEAGVKVIDLSADFRLKDPAvyekwygfehaapellGEAVYGLPELNREEIKGARLIANPGCYPTAVLLALA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 145 PLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEKNIHFIPYRGDFT 223
Cdd:COG0002  160 PLLKAGLIdPDDIIIDAKSGVSGAGRKASEGTHFSEVNENFRAYKVGGHRHTPEIEQELSRLAGE-DVKVSFTPHLVPMV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 224 RGIIATMYTPC--SWTIDEAIAKYKAYYASHPFTHVVDEN--IDLKQVVNTNNCLLYLE--KHGDQLMIVSIIDNLLKGA 297
Cdd:COG0002  239 RGILATIYARLkdGVTEEDLRAAYEEFYADEPFVRVLPEGrlPETKSVRGSNFCDIGVAvdERTGRLVVVSAIDNLVKGA 318

                        330       340
                 ....*....|....*....|....
gi 499905696 298 SGHAVQNMNLMFGLEETVGLRLKA 321
Cdd:COG0002  319 AGQAVQNMNLMFGLPETTGLELVP 342
argC TIGR01850
N-acetyl-gamma-glutamyl-phosphate reductase, common form; This model represents the more ...
 5-318 7.17e-114

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: 333.39  E-value: 7.17e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696    5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSN-AGNPIYKVHTDLIGSTDLVFTG----ELSNAIDVLFLCVGHGD 79
Cdd:TIGR01850   1 IKVAIVGASGYTGGELLRLLLNHPEVEITYLVSSREsAGKPVSEVHPHLRGLVDLNLEPidveEILEDADVVFLALPHGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   80 AIKFLQANpVESHIKIIDLSQDFRIeKDGND-----------------FIYGLPELQRDKIKLAKNIANPGCFATAIQLG 142
Cdd:TIGR01850  81 SAELAPEL-LAAGVKVIDLSADFRL-KDPELyekwygfehagpellqkAVYGLPELHREEIKGARLIANPGCYPTATLLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  143 LLPLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEKNIHFIPYRGD 221
Cdd:TIGR01850 159 LAPLLKEGLIdPTSIIVDAKSGVSGAGRKASEANHFPEVNENLRPYKVTGHRHTPEIEQELGRLAGG-KVKVSFTPHLVP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  222 FTRGIIATMYTP--CSWTIDEAIAKYKAYYASHPFTHVVDENI--DLKQVVNTNNCLL--YLEKHGDQLMIVSIIDNLLK 295
Cdd:TIGR01850 238 MTRGILATIYAKlkDGLTEEDLRALYEEFYADEPFVRVLPEGGypSTKAVIGSNFCDIgfAVDERTGRVVVVSAIDNLVK 317

                         330       340
                  ....*....|....*....|...
gi 499905696  296 GASGHAVQNMNLMFGLEETVGLR 318
Cdd:TIGR01850 318 GAAGQAVQNMNLMFGFDETTGLP 340
AGPR_1_C cd23934
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 and ...
 133-297 1.91e-68

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: 211.18  E-value: 1.91e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 133 GCFATAIQLGLLPLAAEN-VLTNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSlEK 211
Cdd:cd23934    1 GCYPTAALLALAPLLKAGlIEPDDIIIDAKSGVSGAGRKASETTHFSEVNENLKAYKVGGHRHTPEIEQELSKLAGE-DV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 212 NIHFIPYRGDFTRGIIATMYTPCS--WTIDEAIAKYKAYYASHPFTHVVDENI--DLKQVVNTNNCLLYLEKHG--DQLM 285
Cdd:cd23934   80 EVSFTPHLVPMTRGILATIYAKLKdgVTAEDVRALYEEFYADEPFVRVLPEGQlpSTKAVRGSNFCDIGVAVDGrtGRLI 159

                        170
                 ....*....|..
gi 499905696 286 IVSIIDNLLKGA 297
Cdd:cd23934  160 VVSAIDNLVKGA 171
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 4-317 5.34e-68

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 217.39  E-value: 5.34e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   4 KIKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGST--DLVFTGE-LSNAIDVLFLCVGHGDA 80
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTADRKAGQSFGSVFPHLITQDlpNLVAVKDaDFSDVDAVFCCLPHGTT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  81 IKFLQAnpVESHIKIIDLSQDFRIeKDGNDF-----------------IYGLPELQRDKIKLAKNIANPGCFATAIQLGL 143
Cdd:PLN02968 118 QEIIKA--LPKDLKIVDLSADFRL-RDIAEYeewyghphrapelqkeaVYGLTELQREEIKSARLVANPGCYPTGIQLPL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 144 LPLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNlQSSLEKNIHFIPYRGDF 222
Cdd:PLN02968 195 VPLVKAGLIePDNIIIDAKSGVSGAGRGAKEANLYTEIAEGIGAYGVTRHRHVPEIEQGLAD-AAGSKVTPSFTPHLMPM 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 223 TRGIIATMYTPCS--WTIDEAIAKYKAYYASHPFTHVVDENIDLK--QVVNTNNCLL--YLEKHGDQLMIVSIIDNLLKG 296
Cdd:PLN02968 274 SRGMQSTVYVHYApgVTAEDLHQHLKERYEGEEFVKVLERGAVPHtdHVRGSNYCELnvFADRIPGRAIIISVIDNLVKG 353

                        330       340
                 ....*....|....*....|.
gi 499905696 297 ASGHAVQNMNLMFGLEETVGL 317
Cdd:PLN02968 354 ASGQAVQNLNLMMGLPETTGL 374
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 5-132 9.15e-47

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: 155.66  E-value: 9.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFTG----ELSNAIDVLFLCVGHGDA 80
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSRSYAGKPVSEVFPHLRGLTDLTFEPdddeEIAEDADVVFLALPHGVS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499905696  81 IKFLQANpVESHIKIIDLSQDFRIEKDG----------------NDFIYGLPELQRDKIKLAKNIANP 132
Cdd:cd17895   81 MELAPKL-LEAGVKVIDLSADFRLKDPEtyekwygfehaapellKEAVYGLPELNREEIKKARLVANP 147
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 5-130 1.92e-34

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: 123.54  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFTG--ELSNAiDVLFLCVGHGDAIK 82
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVTSESLAGKPVHRVHPNLRGRTLLKFVPpeELESC-DVLFLALPHGESMK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499905696  83 ----FLQANPveshiKIIDLSQDFRIEK--------DG--------NDFIYGLPELQRDKIKLAKNIA 130
Cdd:cd24151   80 ridrFAELAP-----RIIDLSADFRLKDpaaydrwyGGphprpellERFVYGLPELHREELRGARYIA 142
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 6-126 6.21e-33

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: 118.03  E-value: 6.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696     6 KIGIVGGAGYTGGELLRILVNHPNAEIVFVH-SNSNAGNPIYKVHTDLIGSTDLVFTGE--LSNAIDVLFLCVGHGDAIK 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAaSSRSAGKKVSEAGPHLKGEVVLELDPPdfEELAVDIVFLALPHGVSKE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 499905696    83 FLQANP--VESHIKIIDLSQDFRIEkdgNDFIYGLPELQRDKIKLA 126
Cdd:smart00859  81 SAPLLPraAAAGAVVIDLSSAFRMD---DDVPYGLPEVNPEAIKKA 123
AGPR_1_C_LysY cd23939
C-terminal catalytic domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase ...
 133-297 4.43e-32

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: 117.72  E-value: 4.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 133 GCFATAIQLGLLPLAAENVL-TNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTNLQSSLek 211
Cdd:cd23939    1 GCNATASILALYPLVKAGLLdDERIVVDVKVGSSGAGAEASEASHHPERSGVVRPYKPTGHRHTAEIEQELGLLAREI-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 212 NIHFIPYRGDFTRGIIATMYTpcswTIDEAIAK------YKAYYASHPFTHVVDENI------DLKQVVNTNNCLLYLEK 279
Cdd:cd23939   79 SVSFTAHSVDMVRGILATAHV----FLKEGVTEkdlwkaYRKAYGNEPFVRIVKDRKgiyrypDPKLVIGSNFCDIGFEL 154

                        170       180
                 ....*....|....*....|
gi 499905696 280 HGD--QLMIVSIIDNLLKGA 297
Cdd:cd23939  155 DEDngRLVVFSAIDNLMKGA 174
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 5-133 8.36e-32

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: 116.06  E-value: 8.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPI--Y--KVHTDLIGSTDLVFTGELSNAIDVLFLCVGHGDA 80
Cdd:cd24149    1 KRVGLIGARGYVGRELIRLLNRHPNLELAHVSSRELAGQKVsgYtkSPIDYLNLSVEDIPEEVAAREVDAWVLALPNGVA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499905696  81 IKFLQA-NPVESHIKIIDLSQDFRIEkdgNDFIYGLPELQRDKIKLAKNIANPG 133
Cdd:cd24149   81 KPFVDAiDKANPKSVIVDLSADYRFD---DAWTYGLPELNRRRIAGAKRISNPG 131
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-126 1.61e-31

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: 114.54  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696    6 KIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSN-AGNPIYKVHTDLIGSTDLVF---TGELSNAIDVLFLCVGHGDAI 81
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRsAGKKLAFVHPILEGGKDLVVedvDPEDFKDVDIVFFALPGGVSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499905696   82 KFLQANpVESHIKIIDLSQDFRIEkdgNDFIYGLPELQRDKIKLA 126
Cdd:pfam01118  81 EIAPKL-AEAGAKVIDLSSDFRMD---DDVPYGLPEVNREAIKQA 121
AGPR_C cd18125
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and similar ...
 134-297 2.74e-31

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: 115.29  E-value: 2.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 134 CFATAIQLGLLPLAAENVLTND-VHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLtnlqsSLEKN 212
Cdd:cd18125    1 CYATAALLALYPLLKAGLLKPTpITVTGVSGTSGAGRAASPASLHPEVAGSLRPYALSGHRHTPEIAQNL-----GGKHN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 213 IHFIPYRGDFTRGIIATMYTPC--SWTIDEAIAKYKAYYASHPFTHVVDENI--DLKQVVNTNNCLL--YLEKHGDQLMI 286
Cdd:cd18125   76 VHFTPHVGPWVRGILMTIQCFTqkGWSLRQLHEAYREAYAGEPFVRVMPQGKgpDPKFVQGTNYADIgvELEEDTGRLVV 155

                        170
                 ....*....|.
gi 499905696 287 VSIIDNLLKGA 297
Cdd:cd18125  156 MSAIDNLVKGA 166
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 5-143 8.29e-28

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: 106.22  E-value: 8.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLVF---TGELSNAIDVLFLCVGHGDAI 81
Cdd:cd24148    1 IRVAVAGASGYAGGELLRLLLGHPEFEIGALTAHSNAGQRLGELHPHLPPLADRVLeptTPAVLAGHDVVFLALPHGASA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  82 KFLQANPveSHIKIIDLSQDFRIE--KDGNDFI---------YGLPEL--QRDKIKLAKNIANP----GCFATAIQ---- 140
Cdd:cd24148   81 AIAAQLP--PDVLVVDCGADHRLEdaAAWEKFYggehaggwtYGLPELpgAREALAGARRIAVPnlgkGTAGQAVQsanl 158


                 ....
gi 499905696 141 -LGL 143
Cdd:cd24148  159 aLGL 162
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 5-132 5.71e-24

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: 95.71  E-value: 5.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPNAEIVFVHSNSNAGNPIYKVHTDLIGSTDLV-FTG-ELSNAIDVLFLCVGHGDAIK 82
Cdd:cd02280    1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRERAGPKLREYHPSLIISLQIQeFRPcEVLNSADILVLALPHGASAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499905696  83 FLQA--NPvesHIKIIDLSQDFRIEKDGN-----------DFIYGLPELQRD-KIKLAKNIANP 132
Cdd:cd02280   81 LVAAisNP---QVKIIDLSADFRFTDPEVyrrhprpdlegGWVYGLPELDREqRIANATRIANP 141
AGPR_C_ARG5_6_like cd23936
C-terminal catalytic domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ...
 133-297 2.96e-23

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: 93.85  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 133 GCFATAIQLGLLPLAaeNVLTNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYKALNHQHLKEIRQSLTnlqssleKN 212
Cdd:cd23936    1 GCYATGAQLALAPLL--DDLDGPPSVFGVSGYSGAGTKPSPKNDPEVLADNLIPYSLVGHIHEREVSRHLG-------TP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 213 IHFIPYRGDFTRGIIATMYTPC--SWTIDEAIAKYKAYYASHPFTHVVDENIDLKQVVNTNNCLL---YLEKHGDQLMIV 287
Cdd:cd23936   72 VAFMPHVAPWFQGITLTISIPLkkSMTADEIRELYQEAYAGEPLIKVTKEIPLVRDNAGKHGVVVggfTVHPDGKRVVVV 151

                        170
                 ....*....|
gi 499905696 288 SIIDNLLKGA 297
Cdd:cd23936  152 ATIDNLLKGA 161
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 5-132 3.33e-21

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: 87.80  E-value: 3.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNHPN-AEIVFVHSNSNAGNPIYKVHTDLIGSTDLVFT--GELSNAiDVLFLCVGHGDAI 81
Cdd:cd02281    1 KKVGVVGATGYVGGEFLRLLLEHPFpLFEIVLLAASSAGAKKKYFHPKLWGRVLVEFTpeEVLEQV-DIVFTALPGGVSA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499905696  82 KFLQAnPVESHIKIIDLSQDFRIEKdgnDFIYGLPELQRDKIKLAKN---IANP 132
Cdd:cd02281   80 KLAPE-LSEAGVLVIDNASDFRLDK---DVPLVVPEVNREHIGELKGtkiIANP 129
AGPR_2_C cd23935
C-terminal catalytic domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 and ...
 133-297 9.71e-20

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: 84.96  E-value: 9.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 133 GCFATAIQLGLLPLAAENVLTNDVHVS--GITGSTGAGQSLSQTSHFSWRNNNMS--VYK-ALNHQHLKEIRQsltnlQS 207
Cdd:cd23935    1 GCYATGAILLLRPLVEAGLLPADYPLSihAVSGYSGGGKKMIEQYEAAEAADLPPprPYGlGLEHKHLPEMQK-----HA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696 208 SLEKNIHFIPYRGDFTRGIIATMY-----TPCSWTIDEAIAKYKAYYASHPFTHVVD-------ENIDLKQVVNTNNCLL 275
Cdd:cd23935   76 GLARPPIFTPAVGNFYQGMLVTVPlhldlLEKGVSAAEVHEALAEHYAGERFVKVMPldepdalGFLDPQALNGTNNLEL 155

                        170       180
                 ....*....|....*....|...
gi 499905696 276 YLEKHGD-QLMIVSIIDNLLKGA 297
Cdd:cd23935  156 FVFGNDKgQALLVARLDNLGKGA 178
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 143-295 2.00e-10

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: 58.86  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  143 LLPLAAENVLTNDVHVSGITGSTGAGQSLSQTSHFSWRNNNMSVYK-ALNHQHLKEIRQSLtNLQSSLEKNIHFIPY--- 218
Cdd:pfam02774   1 LKPLRDALGGLERVIVDTYQAVSGAGKKAKPGVFGAPIADNLIPYIdGEEHNGTPETREEL-KMVNETKKILGFTPKvsa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  219 ---RGDFTRGIIATMYTPCSWTIDEAIAKYKAYYASH-PFTHVVDENIDLKQ---VVNTNNCLL----YLEKHGDQLMIV 287
Cdd:pfam02774  80 tcvRVPVFRGHSETVTVKLKLKPIDVEEVYEAFYAAPgVFVVVRPEEDYPTPravRGGTNFVYVgrvrKDPDGDRGLKLV 159


                  ....*...
gi 499905696  288 SIIDNLLK 295
Cdd:pfam02774 160 SVIDNLRK 167
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 6-133 1.36e-09

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 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 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 55.30  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   6 KIGIVGGAGYTGgelLRI---LVNHPNAEIVFVHSNSNagnpiykvhtdligsTDLVFTGELSNAIDVLFLCVgHGDAIK 82
Cdd:cd17896    2 KVFIDGEAGTTG---LQIrerLAGRSDIELLSIPEDKR---------------KDPAARAELLNAADIAILCL-PDDAAR 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499905696  83 ---FLQANPvesHIKIIDLSQDFRIEKDgndFIYGLPEL---QRDKIKLAKNIANPG 133
Cdd:cd17896   63 eavALVTNP---RTRIIDASTAHRTAPG---WAYGFPELspeQREKIATSKRVANPG 113
AGPR_2_N cd17896
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 ...
 287-310 3.99e-05

N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 2 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 2 AGPR family.


Pssm-ID: 467522 [Multi-domain]  Cd Length: 132  Bit Score: 42.59  E-value: 3.99e-05
                         10        20
                 ....*....|....*....|....
gi 499905696 287 VSIIDNLLKGASGHAVQNMNLMFG 310
Cdd:cd17896  109 VANPGNLGKGASGAAVQNMNLMLG 132
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 6-132 7.91e-05

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: 42.04  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   6 KIGIVGGAGYTGGELLRILV--NHPNAEIVFVHSNSNAGNPI------YKVhTDLigsTDLVFTGelsnaIDVLFLCVGh 77
Cdd:cd02316    2 NVAIVGATGAVGQEMLKVLEerNFPVSELRLLASARSAGKTLefkgkeLTV-EEL---TEDSFKG-----VDIALFSAG- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499905696  78 GD-----AIKFLQANPVeshikIIDLSQDFRIEKDgndfiYGL--PELQRDKIKLAKN-IANP 132
Cdd:cd02316   72 GSvskefAPIAAEAGAV-----VIDNSSAFRMDPD-----VPLvvPEVNPEALKNHKGiIANP 124
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 4-170 1.39e-04

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 42.84  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   4 KIKIGIVGGAGYTGGELLRIL--VNHPNAEIVFVHSNSNAGNPI------YKVhTDLigsTDLVFTGelsnaIDVLFLCV 75
Cdd:PRK14874   1 GYNVAVVGATGAVGREMLNILeeRNFPVDKLRLLASARSAGKELsfkgkeLKV-EDL---TTFDFSG-----VDIALFSA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  76 GhGD-----AIKFLQANPVeshikIIDLSQDFRIEKDgndfiYGL--PELQRDKIKLAKN---IANPGCfaTAIQLG--L 143
Cdd:PRK14874  72 G-GSvskkyAPKAAAAGAV-----VIDNSSAFRMDPD-----VPLvvPEVNPEALAEHRKkgiIANPNC--STIQMVvaL 138

                        170       180
                 ....*....|....*....|....*..
gi 499905696 144 LPLAAENVLTNdVHVSGITGSTGAGQS 170
Cdd:PRK14874 139 KPLHDAAGIKR-VVVSTYQAVSGAGKA 164
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 5-107 1.81e-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: 41.17  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILVNH--PNAEIVFVHSNSNAGNPiYKVHTDLIGSTDlVFTGELSNaIDVLFLCVGHGDAIK 82
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEpdPLFELRALASEESAGKK-AEFAGEAIMVQE-ADPIDFLG-LDIVFLCAGAGVSAK 77

                         90       100
                 ....*....|....*....|....*
gi 499905696  83 FLQAnPVESHIKIIDLSQDFRIEKD 107
Cdd:cd24147   78 FAPE-AARAGVLVIDNAGALRMDPD 101
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 5-147 3.25e-04

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: 41.94  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   5 IKIGIVGGAGYTGGELLRILV--NHPNAEIVFVHSNSNAGNPI------YKVHtDLigsTDLVFTGelsnaIDVLFLCVG 76
Cdd:COG0136    1 YNVAVVGATGAVGRVLLELLEerDFPVGELRLLASSRSAGKTVsfggkeLTVE-DA---TDFDFSG-----VDIALFSAG 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499905696  77 hGD-----AIKFLQANPVeshikIIDLSQDFRIEKDgndfiygLPELQRDKIKLAKN---IANPGCfaTAIQLgLLPLA 147
Cdd:COG0136   72 -GSvskeyAPKAAAAGAV-----VIDNSSAFRMDPDvp---lvVPEVNPEALADHLPkgiIANPNC--STIQM-LVALK 138
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 7-162 1.15e-03

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 39.31  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696   7 IGIVGGAGYTGGELLRILVNHPNAEIVFVHS----NSNAGNPIYKVHTDLIGSTDLVFTgelSNAIDVLFLCVG-HGDAI 81
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNtkrlSKEDQEPVAVVEGDLRDLDSLSDA---VQGVDVVIHLAGaPRDTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499905696  82 KFLQANPvESHIKIIDLSQDFRIEK---------DGNDFIYGLPE----LQRDKIKLAKNIANPGCFATAIQ----LGLL 144
Cdd:cd05226   78 DFCEVDV-EGTRNVLEAAKEAGVKHfifisslgaYGDLHEETEPSpsspYLAVKAKTEAVLREASLPYTIVRpgviYGDL 156

                        170
                 ....*....|....*...
gi 499905696 145 PLAAENVLTNDVHVSGIT 162
Cdd:cd05226  157 ARAIANAVVTPGKKNETF 174
 
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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