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Conserved domains on  [gi|19076052|ref|NP_588552|]
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aspartate semialdehyde dehydrogenase [Schizosaccharomyces pombe]

Protein Classification

aspartate-semialdehyde dehydrogenase family protein( domain architecture ID 11483416)

aspartate-semialdehyde dehydrogenase family protein such as aspartate-semialdehyde dehydrogenase and malonyl-CoA reductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 5-355 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


:

Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 522.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:PRK08664   5 KVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDDVDIVFSAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRqENKLDRGCIITNSNCSTAAVVVPLKALQ 164
Cdd:PRK08664  85 PSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQR-KRRGWDGFIVTNPNCSTIGLVLALKPLM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  165 DaFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTIsgYELTDNVVSAQCNRVPVI 244
Cdd:PRK08664 164 D-FG-IERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGK--IVPADFPISATCHRVPVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  245 DGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNENGYAVSVGRIRSDSI 324
Cdd:PRK08664 240 DGHTEAVFVKFKE-DVDPEEIREALESFKGLPQELGLPSAPKKPIILFEE--PDRPQPRLDRDAGDGMAVSVGRLREDGI 316

                        330       340       350
                 ....*....|....*....|....*....|.
gi 19076052  325 FDIKFVSLVHNTVLGAAGAGILNAEVAVKKG 355
Cdd:PRK08664 317 FDIKFVVLGHNTVRGAAGASVLNAELLKKKG 347
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 5-355 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 522.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:PRK08664   5 KVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDDVDIVFSAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRqENKLDRGCIITNSNCSTAAVVVPLKALQ 164
Cdd:PRK08664  85 PSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQR-KRRGWDGFIVTNPNCSTIGLVLALKPLM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  165 DaFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTIsgYELTDNVVSAQCNRVPVI 244
Cdd:PRK08664 164 D-FG-IERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGK--IVPADFPISATCHRVPVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  245 DGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNENGYAVSVGRIRSDSI 324
Cdd:PRK08664 240 DGHTEAVFVKFKE-DVDPEEIREALESFKGLPQELGLPSAPKKPIILFEE--PDRPQPRLDRDAGDGMAVSVGRLREDGI 316

                        330       340       350
                 ....*....|....*....|....*....|.
gi 19076052  325 FDIKFVSLVHNTVLGAAGAGILNAEVAVKKG 355
Cdd:PRK08664 317 FDIKFVVLGHNTVRGAAGASVLNAELLKKKG 347
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 5-353 8.45e-140

aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273376 [Multi-domain]  Cd Length: 341  Bit Score: 400.29  E-value: 8.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052     5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:TIGR00978   2 RVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVKWIEPGDMPEYVRDLPIVEPEPVASKDVDIVFSAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQenKLDRGCIITNSNCSTAAVVVPLKALQ 164
Cdd:TIGR00978  82 PSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKE--RGWKGFIVTNPNCTTAGLTLALKPLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   165 DAFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNStiSGYELTDNVVSAQCNRVPVI 244
Cdd:TIGR00978 160 DAFG-IKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLEN--GKIEPAPFSVSATTTRVPVL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   245 DGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNENGYAVSVGRIRSDSI 324
Cdd:TIGR00978 237 DGHTESVHVEFDK-KFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDE--EDRPQPRLDRDAGGGMAVTVGRLREEGG 313

                         330       340
                  ....*....|....*....|....*....
gi 19076052   325 fDIKFVSLVHNTVLGAAGAGILNAEVAVK 353
Cdd:TIGR00978 314 -SLKYVVLGHNLVRGAAGATLLNAELAYK 341
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 151-336 1.46e-98

C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. This 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: 467680 [Multi-domain]  Cd Length: 180  Bit Score: 289.52  E-value: 1.46e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNStiSGYELT 230
Cdd:cd18130   1 CSTAGLALPLKPLHDFFG-IEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNE--DKIEPA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 231 DNVVSAQCNRVPVIDGHLMCISVKFAKTsPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNEN 310
Cdd:cd18130  78 DFKVSATCNRVPVIDGHTESVSVKFKER-PDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDE--PRRPQPRLDRDAGD 154

                       170       180
                ....*....|....*....|....*.
gi 19076052 311 GYAVSVGRIRSDSIFDIKFVSLVHNT 336
Cdd:cd18130 155 GMAVTVGRIRKDDDFDLKFVLLSHNT 180
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 160-337 3.71e-55

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: 178.28  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   160 LKALQDAFGPIAQTNVVSMQAISGAGY---PGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTISGYELTDNvVSA 236
Cdd:pfam02774   1 LKPLRDALGGLERVIVDTYQAVSGAGKkakPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTPK-VSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   237 QCNRVPVIDGHLMCISVKFaktSPTPDQVREVLANYvsepqklgcYSAPKQAIYVFDdsTPDRPQPRLDRNneNGYAVSV 316
Cdd:pfam02774  80 TCVRVPVFRGHSETVTVKL---KLKPIDVEEVYEAF---------YAAPGVFVVVRP--EEDYPTPRAVRG--GTNFVYV 143

                         170       180
                  ....*....|....*....|...
gi 19076052   317 GRIRSDSIFD--IKFVSLVHNTV 337
Cdd:pfam02774 144 GRVRKDPDGDrgLKLVSVIDNLR 166
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 4-326 1.82e-50

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: 171.37  E-value: 1.82e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHpEFKIA--VLGASARSAGKPYAVAtkwKQSIAmpkeisqmsVKACDPKEFSECDIVF 81
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELLEER-DFPVGelRLLASSRSAGKTVSFG---GKELT---------VEDATDFDFSGVDIAL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  82 SGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDvikyqrqeNKLDRGcIITNSNCSTAAVVVPLK 161
Cdd:COG0136  68 FSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALA--------DHLPKG-IIANPNCSTIQMLVALK 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 162 ALQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD---------------NIVPFIGG--------EEEKIEWET 213
Cdd:COG0136 139 PLHDAAG-IKRVVVSTYQAVSGAGAAAMDELaeqtaALLNgeeiepevfphpiafNLIPQIDVflengytkEEMKMVNET 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 214 RKILGsvnstisgyelTDNV-VSAQCNRVPVIDGHLMCISVKFAKtsP-TPDQVREVLANyvsepqklgcysAPkQAIYV 291
Cdd:COG0136 218 RKILG-----------DPDIpVSATCVRVPVFRGHSEAVNIEFER--PvSLEEARELLAA------------AP-GVKVV 271

                       330       340       350
                ....*....|....*....|....*....|....*
gi 19076052 292 FDDSTPDRPQPrldRNNENGYAVSVGRIRSDSIFD 326
Cdd:COG0136 272 DDPAENDYPTP---LDASGTDEVFVGRIRKDLSVP 303
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 5-129 2.39e-32

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: 117.26  E-value: 2.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052      5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAvatkwkqsiAMPKEISQMSVKACDPKEFSE--CDIVFS 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVS---------EAGPHLKGEVVLELDPPDFEElaVDIVFL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 19076052     83 GLDADFAGEI---EKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLD 129
Cdd:smart00859  72 ALPHGVSKESaplLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIK 121
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 5-355 0e+00

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 522.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:PRK08664   5 KVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVRWQLDGPIPEEVADMEVVSTDPEAVDDVDIVFSAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRqENKLDRGCIITNSNCSTAAVVVPLKALQ 164
Cdd:PRK08664  85 PSDVAGEVEEEFAKAGKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQR-KRRGWDGFIVTNPNCSTIGLVLALKPLM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  165 DaFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTIsgYELTDNVVSAQCNRVPVI 244
Cdd:PRK08664 164 D-FG-IERVHVTTMQAISGAGYPGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGK--IVPADFPISATCHRVPVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  245 DGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNENGYAVSVGRIRSDSI 324
Cdd:PRK08664 240 DGHTEAVFVKFKE-DVDPEEIREALESFKGLPQELGLPSAPKKPIILFEE--PDRPQPRLDRDAGDGMAVSVGRLREDGI 316

                        330       340       350
                 ....*....|....*....|....*....|.
gi 19076052  325 FDIKFVSLVHNTVLGAAGAGILNAEVAVKKG 355
Cdd:PRK08664 317 FDIKFVVLGHNTVRGAAGASVLNAELLKKKG 347
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 5-353 8.45e-140

aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related families of aspartate-semialdehyde dehydrogenase are found. They differ by a deep split in phylogenetic and percent identity trees and in gap patterns. Separate models are built for the two types in order to exclude the USG-1 protein, found in several species, which is specifically related to the Bacillus subtilis type of aspartate-semialdehyde dehydrogenase. Members of this type are found primarily in organisms that lack peptidoglycan. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273376 [Multi-domain]  Cd Length: 341  Bit Score: 400.29  E-value: 8.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052     5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:TIGR00978   2 RVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAVKWIEPGDMPEYVRDLPIVEPEPVASKDVDIVFSAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQenKLDRGCIITNSNCSTAAVVVPLKALQ 164
Cdd:TIGR00978  82 PSEVAEEVEPKLAEAGKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKE--RGWKGFIVTNPNCTTAGLTLALKPLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   165 DAFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNStiSGYELTDNVVSAQCNRVPVI 244
Cdd:TIGR00978 160 DAFG-IKKVHVTTMQAVSGAGYPGVPSMDILDNIIPHIGGEEEKIERETRKILGKLEN--GKIEPAPFSVSATTTRVPVL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   245 DGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNENGYAVSVGRIRSDSI 324
Cdd:TIGR00978 237 DGHTESVHVEFDK-KFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDE--EDRPQPRLDRDAGGGMAVTVGRLREEGG 313

                         330       340
                  ....*....|....*....|....*....
gi 19076052   325 fDIKFVSLVHNTVLGAAGAGILNAEVAVK 353
Cdd:TIGR00978 314 -SLKYVVLGHNLVRGAAGATLLNAELAYK 341
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 151-336 1.46e-98

C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins. This 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: 467680 [Multi-domain]  Cd Length: 180  Bit Score: 289.52  E-value: 1.46e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFGpIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNStiSGYELT 230
Cdd:cd18130   1 CSTAGLALPLKPLHDFFG-IEAVIVTTMQAISGAGYPGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNE--DKIEPA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 231 DNVVSAQCNRVPVIDGHLMCISVKFAKTsPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVFDDstPDRPQPRLDRNNEN 310
Cdd:cd18130  78 DFKVSATCNRVPVIDGHTESVSVKFKER-PDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDE--PRRPQPRLDRDAGD 154

                       170       180
                ....*....|....*....|....*.
gi 19076052 311 GYAVSVGRIRSDSIFDIKFVSLVHNT 336
Cdd:cd18130 155 GMAVTVGRIRKDDDFDLKFVLLSHNT 180
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 4-151 6.82e-86

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: 256.65  E-value: 6.82e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSG 83
Cdd:cd02315   1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAVRWKQDTPIPEEVADMVVKECEPEEFKDCDIVFSA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19076052  84 LDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQENKlDRGCIITNSNC 151
Cdd:cd02315  81 LDSDVAGEIEPAFAKAGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRG-WKGFIVTNPNN 147
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 160-337 3.71e-55

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: 178.28  E-value: 3.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   160 LKALQDAFGPIAQTNVVSMQAISGAGY---PGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTISGYELTDNvVSA 236
Cdd:pfam02774   1 LKPLRDALGGLERVIVDTYQAVSGAGKkakPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTPK-VSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   237 QCNRVPVIDGHLMCISVKFaktSPTPDQVREVLANYvsepqklgcYSAPKQAIYVFDdsTPDRPQPRLDRNneNGYAVSV 316
Cdd:pfam02774  80 TCVRVPVFRGHSETVTVKL---KLKPIDVEEVYEAF---------YAAPGVFVVVRP--EEDYPTPRAVRG--GTNFVYV 143

                         170       180
                  ....*....|....*....|...
gi 19076052   317 GRIRSDSIFD--IKFVSLVHNTV 337
Cdd:pfam02774 144 GRVRKDPDGDrgLKLVSVIDNLR 166
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 4-326 1.82e-50

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: 171.37  E-value: 1.82e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHpEFKIA--VLGASARSAGKPYAVAtkwKQSIAmpkeisqmsVKACDPKEFSECDIVF 81
Cdd:COG0136   1 YNVAVVGATGAVGRVLLELLEER-DFPVGelRLLASSRSAGKTVSFG---GKELT---------VEDATDFDFSGVDIAL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  82 SGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDvikyqrqeNKLDRGcIITNSNCSTAAVVVPLK 161
Cdd:COG0136  68 FSAGGSVSKEYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALA--------DHLPKG-IIANPNCSTIQMLVALK 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 162 ALQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD---------------NIVPFIGG--------EEEKIEWET 213
Cdd:COG0136 139 PLHDAAG-IKRVVVSTYQAVSGAGAAAMDELaeqtaALLNgeeiepevfphpiafNLIPQIDVflengytkEEMKMVNET 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 214 RKILGsvnstisgyelTDNV-VSAQCNRVPVIDGHLMCISVKFAKtsP-TPDQVREVLANyvsepqklgcysAPkQAIYV 291
Cdd:COG0136 218 RKILG-----------DPDIpVSATCVRVPVFRGHSEAVNIEFER--PvSLEEARELLAA------------AP-GVKVV 271

                       330       340       350
                ....*....|....*....|....*....|....*
gi 19076052 292 FDDSTPDRPQPrldRNNENGYAVSVGRIRSDSIFD 326
Cdd:COG0136 272 DDPAENDYPTP---LDASGTDEVFVGRIRKDLSVP 303
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 5-131 5.36e-43

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: 144.97  E-value: 5.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052     5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAVATKwkqsiaMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAFVHP------ILEGGKDLVVEDVDPEDFKDVDIVFFAL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19076052    85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVI 131
Cdd:pfam01118  75 PGGVSKEIAPKLAEAGAKVIDLSSDFRMDDDVPYGLPEVNREAIKQA 121
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 5-322 4.47e-42

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 149.54  E-value: 4.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    5 KVGILGATGTVGQRFITLL--SDHPEFKIAVLgASARSAGKPYavatKWKQsiampKEISqmsVKACDPKEFSECDIVFS 82
Cdd:PRK14874   3 NVAVVGATGAVGREMLNILeeRNFPVDKLRLL-ASARSAGKEL----SFKG-----KELK---VEDLTTFDFSGVDIALF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   83 GLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKyqrqenklDRGcIITNSNCSTAAVVVPLKA 162
Cdd:PRK14874  70 SAGGSVSKKYAPKAAAAGAVVIDNSSAFRMDPDVPLVVPEVNPEALAEHR--------KKG-IIANPNCSTIQMVVALKP 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  163 LQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD-----------------NIVPFIG--------GEEEKIEWE 212
Cdd:PRK14874 141 LHDAAG-IKRVVVSTYQAVSGAGKAGMEELfeqtrAVLNaavdpvepkkfpkpiafNVIPHIDvfmddgytKEEMKMVNE 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  213 TRKILGsvnstisgyeLTDNVVSAQCNRVPVIDGHLMCISVKFAKTSpTPDQVREVLANyvsepqklgcysAPkqAIYVF 292
Cdd:PRK14874 220 TKKILG----------DPDLKVSATCVRVPVFTGHSESVNIEFEEPI-SVEEAREILAE------------AP--GVVLV 274

                        330       340       350
                 ....*....|....*....|....*....|.
gi 19076052  293 DDSTPDR-PQPrLDRNNENgyAVSVGRIRSD 322
Cdd:PRK14874 275 DDPENGGyPTP-LEAVGKD--ATFVGRIRKD 302
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 151-336 7.12e-40

C-terminal catalytic 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. These proteins 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: 467674 [Multi-domain]  Cd Length: 193  Bit Score: 139.65  E-value: 7.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFgPIAQTNVVSMQAISGAGY--------------------PGVSSLDILDNIVPFIG------- 203
Cdd:cd18124   1 CTVSLLVMALKPLFAKF-LVEWVSVAT*QAVSGAGYenmrellsqmgelmragplpTGVFS*AIADNLIPWIDkvldngq 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 204 -GEEEKIEWETRKILGSVNSTISgyeltdnvVSAQCNRVPVIDGHLMCISVKFAKtSPTPDQVREVLANYVSEPQKLGCY 282
Cdd:cd18124  80 sKEEWKIQAEANKILGTLDSPIP--------ISVTCNRVPVLDGHSQSFTLKLKE-DVPLEEVEEVLDAHKPWVKVIPND 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19076052 283 SAPkqaiyvfddstpdRPQPRLDRNNENGYAVSVGRIRSDS--IFDIKFVSLVHNT 336
Cdd:cd18124 151 YAI-------------RPQPRLDRKVTGGLSTPVGRIRKDAmdPFDVNAFAVSDNT 193
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
 151-336 2.76e-38

C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; Aspartate beta-semialdehyde dehydrogenase (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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467678 [Multi-domain]  Cd Length: 165  Bit Score: 134.55  E-value: 2.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFGpIAQTNVVSMQAISGAGYPgvssldILDNIVPFI--------GGEEEKIEWETRKILGSVNS 222
Cdd:cd18128   1 CTVSLMLMALGGLFQKFL-VEWVSVATYQAVSGAG*P------IAGNLIPWIdvfldngqTKEEWKGQAETNKILGDLDS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 223 TISgyeltdnvVSAQCNRVPVIDGHLMCISVKFaKTSPTPDQVREVLANYvsepqklgcysapKQAIYVFDDStpDRPQP 302
Cdd:cd18128  74 PIP--------ISGTCVRVGVLRCHSQAFTIKL-KEDAPIEEVEEAIAAH-------------N*WIKVIPNV--DRITP 129

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19076052 303 RLDRNNENGYAVSVGRIRSD--SIFDIKFVSLVHNT 336
Cdd:cd18128 130 RTPANVTGTLSTPVGRIRKDamGPFDLQAFTVGDNL 165
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 5-326 3.02e-37

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 136.82  E-value: 3.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    5 KVGILGATGTVGQRFITLLS--DHPEFKIAVLgASARSAGKpyAVATKWKQsiampkeisqMSVKACDPKEFSECDIVFS 82
Cdd:PLN02383   9 SVAIVGVTGAVGQEFLSVLTdrDFPYSSLKML-ASARSAGK--KVTFEGRD----------YTVEELTEDSFDGVDIALF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   83 GLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQenkldRGCIITNSNCSTAAVVVPLKA 162
Cdd:PLN02383  76 SAGGSISKKFGPIAVDKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKG-----KGALIANPNCSTIICLMAVTP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  163 LQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD---------------NIVPFIGG--------EEEKIEWETR 214
Cdd:PLN02383 151 LHRHAK-VKRMVVSTYQAASGAGAAAMEELeqqtrEVLEgkpptcnifaqqyafNLFSHNAPmqengyneEEMKLVKETR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  215 KILGsvnstisgyelTDNV-VSAQCNRVPVIDGHLMCISVKFAKtsptP---DQVREVLAnyvsepqklgcySAPkqAIY 290
Cdd:PLN02383 230 KIWN-----------DDDVkVTATCIRVPVMRAHAESINLQFEK----PldeATAREILA------------SAP--GVK 280

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 19076052  291 VFDDSTPDR-PQPrLDRNNEngYAVSVGRIRSDSIFD 326
Cdd:PLN02383 281 IIDDRANNRfPTP-LDASNK--DDVAVGRIRQDISQD 314
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 5-129 2.39e-32

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: 117.26  E-value: 2.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052      5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASARSAGKPYAvatkwkqsiAMPKEISQMSVKACDPKEFSE--CDIVFS 82
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKVS---------EAGPHLKGEVVLELDPPDFEElaVDIVFL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 19076052     83 GLDADFAGEI---EKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLD 129
Cdd:smart00859  72 ALPHGVSKESaplLPRAAAAGAVVIDLSSAFRMDDDVPYGLPEVNPEAIK 121
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 4-150 3.99e-31

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: 115.15  E-value: 3.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDH--PEFKIAVLGASARSAGKPYAvatkwkqsiaMPKEISQMSVKACDPKEFSECDIVF 81
Cdd:cd02281   1 KKVGVVGATGYVGGEFLRLLLEHpfPLFEIVLLAASSAGAKKKYF----------HPKLWGRVLVEFTPEEVLEQVDIVF 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19076052  82 SGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRqenkldrgcIITNSN 150
Cdd:cd02281  71 TALPGGVSAKLAPELSEAGVLVIDNASDFRLDKDVPLVVPEVNREHIGELKGTK---------IIANPN 130
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 5-147 6.69e-30

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: 112.42  E-value: 6.69e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   5 KVGILGATGTVGQRFITLLSDHPEFKIAVLgASARSAGKPYAVATKWKQSIAMPKEISQMSVKACDPKEFSECDIVFSGL 84
Cdd:cd24150   3 KAAILGATGLVGIEYVRMLSNHPYIKPAYL-AGKGSVGKPYGEVVRWQTVGQVPKEIADMEIKPTDPKLMDDVDIIFSPL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19076052  85 DADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQRQENKLdRGCIIT 147
Cdd:cd24150  82 PQGAAGPVEEQFAKEGFPVISNSPDHRFDPDVPLLVPELNPHTISLIDEQRKRREW-KGFIVT 143
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 4-155 4.90e-29

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: 109.35  E-value: 4.90e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDH--PEFKIaVLGASARSAGKPYAVAtkwkqsiampkeISQMSVKACDPKEFSECDIVF 81
Cdd:cd24147   1 LRVGVVGATGAVGSEILQLLAEEpdPLFEL-RALASEESAGKKAEFA------------GEAIMVQEADPIDFLGLDIVF 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19076052  82 SGLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLdvikyqrqenKLDRGC-IITNSNCSTAA 155
Cdd:cd24147  68 LCAGAGVSAKFAPEAARAGVLVIDNAGALRMDPDVPLVVPEVNAEAI----------GLGEGTpLLVIPNLLRGA 132
ASADH_C_MCR cd23940
C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar ...
 151-336 5.37e-27

C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar proteins; Archaeal NADP-dependent malonyl-CoA reductase (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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467689 [Multi-domain]  Cd Length: 185  Bit Score: 105.22  E-value: 5.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFgPIAQTNVVSMQAISGAGYPGVSSLDILDNIVPFIGGEEEKIEWETRKILGSVNSTISGYELT 230
Cdd:cd23940   2 CTAQGAAIPLGAIFKDY-KMDGAFITTIQSLSGAGYPGIPSLDVVDNILPLGDGYDAKTIKEIFRILSEVKRNVDEPKLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 231 DNVVSAQCNRVPVIDGHLMCISVKFaKTSPTPDQVREVLANYVSEPQKLGCYSAPKQAIYVfddSTPD-RPQPRLDR--N 307
Cdd:cd23940  81 DVSLAATTHRIATIHGHYEVLYVSF-KEETAAEKVKETLENFRGEPQDLKLPTAPSKPIIV---MNEDtRPQVYFDRwaG 156

                       170       180
                ....*....|....*....|....*....
gi 19076052 308 NENGYAVSVGRIRSDSIFDIKFVSLVHNT 336
Cdd:cd23940 157 DIPGMSVVVGRLKQVNKRMIRLVSLIHNT 185
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 151-336 2.50e-26

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: 102.98  E-value: 2.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFGPIaQTNVVSMQAISGAGYPGVSSLDI--LDNIVPFIGGEEEKIEWETRKILGSVNSTISgye 228
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIE-EILVVTVQAVSGAGPKTKGPILKseVRAIIPNIPKNETKHAPETGKVLGEIGKPIK--- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 229 ltdnvVSAQCNRVPVIDGHLMCISVKFAKTsPTPDQVREVLANYVSEPQKLGCYSAPkqaiyvfddstpdrPQPRLDRNN 308
Cdd:cd18122  77 -----VDGIAVRVPATLGHLVTVTVKLEKT-ATLEQIAEAVAEAVEEVQISAEDGLT--------------YAKVSTRSV 136

                       170       180       190
                ....*....|....*....|....*....|
gi 19076052 309 ENGYAVSVGRIRSD--SIFDIKFVSLVHNT 336
Cdd:cd18122 137 GGVYGVPVGRQREFafDDNKLKVFSAVDNE 166
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 151-322 9.24e-22

C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of bacterial aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share 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 and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467681  Cd Length: 188  Bit Score: 91.04  E-value: 9.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 151 CSTAAVVVPLKALQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD---------------NIVPFIGG------ 204
Cdd:cd18131   1 CSTIQMVVALKPLHDAFG-LKRVVVSTYQAVSGAGAAAMEELeeqtrGLLNgkeaepkvfpyqiafNVIPHIDVfldngy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 205 --EEEKIEWETRKILGsvnstisgyeLTDNVVSAQCNRVPVIDGHLMCISVKFAKtSPTPDQVREVLANyvsepqklgcy 282
Cdd:cd18131  80 tkEEMKMVNETRKILG----------DPDLRVSATCVRVPVFRGHSESVNIEFEK-PISVEEAREALAK----------- 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19076052 283 sAPkqAIYVFDDSTPDR-PQPrldRNNENGYAVSVGRIRSD 322
Cdd:cd18131 138 -AP--GVVVVDDPANNVyPTP---LDAAGKDDVFVGRIRKD 172
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 6-357 5.48e-21

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 92.42  E-value: 5.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    6 VGILGATGTVGQRFITLLSDHPEFKIA--VLGASARSAGKpyAVATKWKQSIAMPKEISQmsvkacdpkefsecdivFSG 83
Cdd:PRK06728   8 VAVVGATGAVGQKIIELLEKETKFNIAevTLLSSKRSAGK--TVQFKGREIIIQEAKINS-----------------FEG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   84 LDADF---AGEIEKSFRD----ANLVIVSNAKNYRREPTVPLVVPTVNTDHLdvikyqrQENKldrgCIITNSNCSTAAV 156
Cdd:PRK06728  69 VDIAFfsaGGEVSRQFVNqavsSGAIVIDNTSEYRMAHDVPLVVPEVNAHTL-------KEHK----GIIAVPNCSALQM 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  157 VVPLKALQDAFGpIAQTNVVSMQAISGAGYPGVSSL---------------DILD------------NIVPFIG------ 203
Cdd:PRK06728 138 VTALQPIRKVFG-LERIIVSTYQAVSGSGIHAIQELkeqaksilageevesTILPakkdkkhypiafNVLPQVDiftdnd 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  204 --GEEEKIEWETRKILGSVNSTIsgyeltdnvvSAQCNRVPVIDGHLMCISVKFAKTSpTPDQVREVLANyvsEPQKLgC 281
Cdd:PRK06728 217 ftFEEVKMIQETKKILEDPNLKM----------AATCVRVPVISGHSESVYIELEKEA-TVAEIKEVLFD---APGVI-L 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  282 YSAPKQAIYvfddstpdrPQPRLDRNNENGYavsVGRIRSD----SIFDIKFVSlvHNTVLGAAGAGILNAEVAVKKGLM 357
Cdd:PRK06728 282 QDNPSEQLY---------PMPLYAEGKIDTF---VGRIRKDpdtpNGFHLWIVS--DNLLKGAAWNSVQIAETMVEEGII 347
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 5-129 1.42e-17

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: 78.25  E-value: 1.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   5 KVGILGATGTVGQRFITLL--SDHPEFKIAVLgASARSAGKPyaVATKWKQSIampkeisqmsVKACDPKEFSECDIVFS 82
Cdd:cd02316   2 NVAIVGATGAVGQEMLKVLeeRNFPVSELRLL-ASARSAGKT--LEFKGKELT----------VEELTEDSFKGVDIALF 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19076052  83 GLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLD 129
Cdd:cd02316  69 SAGGSVSKEFAPIAAEAGAVVIDNSSAFRMDPDVPLVVPEVNPEALK 115
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
 152-323 1.44e-12

C-terminal 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 its biological function remains unknown, it is found to be homologous 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: 467679  Cd Length: 186  Bit Score: 65.29  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 152 STAAVVVPLKALQDAFGpIAQTNVVSMQAISGAGYPGVSSL---------------DILD-----NIVPFIG-------- 203
Cdd:cd18129   2 AAIALARVLAPLHDAAG-LERVVVTVLQPVSEAGQAGVDELarqtarllngqpvepEVFPrqlafNLLPQVGdfdadgls 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052 204 GEEEKIEWETRKILGSvnstisgyelTDNVVSAQCNRVPVIDGHLMCISVKFAKtSPTPDQVREVLANYvsepqklgcys 283
Cdd:cd18129  81 DEERRIAAELRRLLGG----------PDLPVSVTCVQVPVFYGHSASVHVELAE-PVDLEEVRAALAAA----------- 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19076052 284 apkQAIYVFDDstPDRPQPRLDRNNENGyaVSVGRIRSDS 323
Cdd:cd18129 139 ---PGLELADD--AEAPPYPVDAAGSDD--VLVGRVRQDP 171
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
 6-349 8.37e-11

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 62.41  E-value: 8.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    6 VGILGATGTVGQRFITLLSDHpEFKIAVLG--ASARSAGKPYAVATKwkqsiampkeisqmSVKACDPKEF--SECDIVF 81
Cdd:PRK08040   7 IALLGATGAVGEALLELLAER-QFPVGELYalASEESAGETLRFGGK--------------SVTVQDAAEFdwSQAQLAF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   82 --SGLDADfAGEIEKSFRDANLVIVSNAKnYRREPTVPLVVPTVNTdhlDVIKYQRQENkldrgcIITNSNCSTAAVVVP 159
Cdd:PRK08040  72 fvAGREAS-AAYAEEATNAGCLVIDSSGL-FALEPDVPLVVPEVNP---FVLADYRNRN------IIAVADSLTSQLLTA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  160 LKALQDAFGpIAQTNVVSMQAISGAGYPGVSSL-----DILD---------------NIVPFIGGEEEKIEwETRKILGS 219
Cdd:PRK08040 141 IKPLIDQAG-LSRLHVTNLLSASAHGKAAVDALagqsaKLLNgipieegffgrqlafNMLPLLPDSEGSVR-EERRLVDQ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052  220 VNSTISGYELTdnvVSAQCNRVPVIDGHLMciSVKFAKTSP-TPDQVREVLANYvsepqklgcysapkQAIYVFDDStpD 298
Cdd:PRK08040 219 VRKILQDEGLP---ISVSCVQSPVFYGHAQ--MVHFEALRPlAAEEARDALEQG--------------EDIVLSEEN--D 277

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19076052  299 RPQPRLDRNNENgyAVSVGRIRSDSIFD--IKFVSLVHNTVLGAAGAGILNAE 349
Cdd:PRK08040 278 YPTQVGDASGNP--HLSIGCVRNDYGMPeqLQFWSVADNVRFGGALMAVKTAE 328
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 4-104 5.65e-10

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: 57.82  E-value: 5.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHPEFKIAVLGASaRSAGKPYAvatkwkqSIAmP--KEISQMSVKACDPKE-FSECDIV 80
Cdd:cd17895   1 IKVGIIGASGYTGAELLRLLLNHPEVEIVALTSR-SYAGKPVS-------EVF-PhlRGLTDLTFEPDDDEEiAEDADVV 71

                        90       100
                ....*....|....*....|....
gi 19076052  81 FSGLDADFAGEIEKSFRDANLVIV 104
Cdd:cd17895  72 FLALPHGVSMELAPKLLEAGVKVI 95
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 5-104 1.86e-09

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: 58.16  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASaRSAGKPYavatkwkqSIAMP--KEISQMSVKACDPKE-FSECDIVF 81
Cdd:COG0002   2 KVGIVGASGYTGGELLRLLLRHPEVEIVALTSR-SNAGKPV--------SEVHPhlRGLTDLVFEPPDPDElAAGCDVVF 72

                        90       100
                ....*....|....*....|...
gi 19076052  82 SGLDADFAGEIEKSFRDANLVIV 104
Cdd:COG0002  73 LALPHGVSMELAPELLEAGVKVI 95
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 5-135 3.37e-09

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: 54.93  E-value: 3.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   5 KVGILGATGTVGQRFITLLSDHPeFKIA--VLGASARSAGKPYAVATKwkqsiampkeisQMSVKACDPKEFSECDIVFS 82
Cdd:cd17894   2 RIAVVGATGLVGKELLELLEERG-FPVGrlRLLDSEESAGELVEFGGE------------PLDVQDLDEFDFSDVDLVFF 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19076052  83 GLDADFAGEIEKSFRDANLVIVSNAKNYRREPTVPLVVPTVNTDHLDVIKYQR 135
Cdd:cd17894  69 AGPAEVARAYAPRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEALAAAAERR 121
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-185 1.01e-08

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 56.37  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    2 AIKKVGILGATGTVGQRFITLLSDHPEFKIAVLGASaRSAGKPYAVATKWKQSIAMPKEIsqmsvkACDPKEFSECDIVF 81
Cdd:PLN02968  37 EKKRIFVLGASGYTGAEVRRLLANHPDFEITVMTAD-RKAGQSFGSVFPHLITQDLPNLV------AVKDADFSDVDAVF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   82 SGLDADFAGEIEKSFRDANLVI-------VSNAKNYRREPTVPLVVPTVNTDHL-DVIKYQRQENKLDRgcIITNSNCST 153
Cdd:PLN02968 110 CCLPHGTTQEIIKALPKDLKIVdlsadfrLRDIAEYEEWYGHPHRAPELQKEAVyGLTELQREEIKSAR--LVANPGCYP 187

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19076052  154 AAVVVPLKALQDAfGPIAQTNVV--SMQAISGAG 185
Cdd:PLN02968 188 TGIQLPLVPLVKA-GLIEPDNIIidAKSGVSGAG 220
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 4-104 3.46e-08

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: 52.11  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHPEFKIAVlgASARS-AGKPYAVATKwkqsiampKEISQMSVKACDPKEFS---ECDI 79
Cdd:cd24149   1 KRVGLIGARGYVGRELIRLLNRHPNLELAH--VSSRElAGQKVSGYTK--------SPIDYLNLSVEDIPEEVaarEVDA 70

                        90       100
                ....*....|....*....|....*....
gi 19076052  80 VF----SGLDADFAGEIEKSFRDAnlVIV 104
Cdd:cd24149  71 WVlalpNGVAKPFVDAIDKANPKS--VIV 97
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 4-112 4.62e-07

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: 49.20  E-value: 4.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHPEFKIAVLGaSARSAGKPYavatkwkqSIAMPKEISQMSVKACDPKEFSECDIVFSG 83
Cdd:cd24151   1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQVT-SESLAGKPV--------HRVHPNLRGRTLLKFVPPEELESCDVLFLA 71

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19076052  84 L-DADFAGEIEKSFRDANLVI-------VSNAKNYRR 112
Cdd:cd24151  72 LpHGESMKRIDRFAELAPRIIdlsadfrLKDPAAYDR 108
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 4-91 5.52e-06

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: 46.02  E-value: 5.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   4 KKVGILGATGTVGQRFITLLSDHPEFKIAVLgASARSAGKPyavatkwKQSIAMPKEISQMSVKACDPKEFSECDIVFSG 83
Cdd:cd02280   1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTL-SSRERAGPK-------LREYHPSLIISLQIQEFRPCEVLNSADILVLA 72


                ....*...
gi 19076052  84 LDADFAGE 91
Cdd:cd02280  73 LPHGASAE 80
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 6-192 1.11e-05

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 46.64  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052    6 VGILGATGTVGQRFITLLsDHPEFKIAVLG--ASARSAGKpyavatkwkqsiAMPKEISQMSVKACDPKEFSECDIVFsg 83
Cdd:PRK05671   7 IAVVGATGTVGEALVQIL-EERDFPVGTLHllASSESAGH------------SVPFAGKNLRVREVDSFDFSQVQLAF-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   84 ldadFAG--EIEKSFRD------ANLVIVSNAKNYRReptVPLVVPTVNTDHLDvikyqrqenKLDRGCIITNSNCSTAA 155
Cdd:PRK05671  72 ----FAAgaAVSRSFAEkaraagCSVIDLSGALPSAQ---APNVVPEVNAERLA---------SLAAPFLVSSPSASAVA 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19076052  156 VVV---PLKALQDafgpIAQTNVVSMQAISGAGYPGVSSL 192
Cdd:PRK05671 136 LAValaPLKGLLD----IQRVQVTACLAVSSLGREGVSEL 171
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 5-103 1.31e-05

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: 44.97  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19076052   5 KVGILGATGTVGQRFITLLSDHPEFKIAVLGASArSAGKPYAVatkwkqsiAMPK--EISQMSVKACDPKEFSECDIVFS 82
Cdd:cd24148   2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTAHS-NAGQRLGE--------LHPHlpPLADRVLEPTTPAVLAGHDVVFL 72

                        90       100
                ....*....|....*....|.
gi 19076052  83 GLDADFAGEIEKSFRDANLVI 103
Cdd:cd24148  73 ALPHGASAAIAAQLPPDVLVV 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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