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Conserved domains on  [gi|663528508|gb|AIF18545|]
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aspartate-semialdehyde dehydrogenase (asd) [uncultured marine thaumarchaeote KM3_83_D12]

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
 1-356 6.19e-165

aspartate-semialdehyde dehydrogenase; Reviewed


:

Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 464.30  E-value: 6.19e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   1 MKKKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIRdpdsgiikWEVGGEIPEYIKGMTVKKIDEIN 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVR--------WQLDGPIPEEVADMEVVSTDPEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKNRDWKGWVAPLPNCTTT 159
Cdd:PRK08664  74 VDDVDIVFSALPSDVAGEVEEEFAKAgKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 160 GLVITMKPLYEkYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADIRVSC 239
Cdd:PRK08664 154 GLVLALKPLMD-FGIERVHVTTMQAISGAGY-PGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 240 TCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTTIGRL 319
Cdd:PRK08664 232 TCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRL 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 663528508 320 EKEELFDhgLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:PRK08664 312 REDGIFD--IKFVVLGHNTVRGAAGASVLNAELLKKK 346
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-356 6.19e-165

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 464.30  E-value: 6.19e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   1 MKKKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIRdpdsgiikWEVGGEIPEYIKGMTVKKIDEIN 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVR--------WQLDGPIPEEVADMEVVSTDPEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKNRDWKGWVAPLPNCTTT 159
Cdd:PRK08664  74 VDDVDIVFSALPSDVAGEVEEEFAKAgKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 160 GLVITMKPLYEkYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADIRVSC 239
Cdd:PRK08664 154 GLVLALKPLMD-FGIERVHVTTMQAISGAGY-PGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 240 TCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTTIGRL 319
Cdd:PRK08664 232 TCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRL 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 663528508 320 EKEELFDhgLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:PRK08664 312 REDGIFD--IKFVVLGHNTVRGAAGASVLNAELLKKK 346
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 4-355 1.06e-137

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: 395.28  E-value: 1.06e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508    4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIrdpdsgiiKWEVGGEIPEYIKGMTVKKIDEINAAE 83
Cdd:TIGR00978   2 RVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAV--------KWIEPGDMPEYVRDLPIVEPEPVASKD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   84 LDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKnRDWKGWVAPLPNCTTTGLV 162
Cdd:TIGR00978  74 VDIVFSALPSEVAEEVEPKLAEAgKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKE-RGWKGFIVTNPNCTTAGLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  163 ITMKPLYEKYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADIRVSCTCT 242
Cdd:TIGR00978 153 LALKPLIDAFGIKKVHVTTMQAVSGAGY-PGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSATTT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  243 RVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTTIGRLEKE 322
Cdd:TIGR00978 232 RVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLREE 311

                         330       340       350
                  ....*....|....*....|....*....|...
gi 663528508  323 elfDHGLKYMLFSHNKKMGSAKGAVLLAEMLYK 355
Cdd:TIGR00978 312 ---GGSLKYVVLGHNLVRGAAGATLLNAELAYK 341
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 156-337 1.69e-86

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: 258.70  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADI 235
Cdd:cd18130    1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISGAGY-PGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNEDKIEPADF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 236 RVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTT 315
Cdd:cd18130   80 KVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDEPRRPQPRLDRDAGDGMAVT 159

                        170       180
                 ....*....|....*....|..
gi 663528508 316 IGRLEKEELFDhgLKYMLFSHN 337
Cdd:cd18130  160 VGRIRKDDDFD--LKFVLLSHN 179
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 3-356 2.72e-51

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: 173.68  E-value: 2.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEF--VLSLKDHPWFEVTQIAaSERSAGKnyvdairdpdsgiiKWEVGGEipEYikgmTVKKIDEIN 80
Cdd:COG0136    1 YNVAVVGATGAVGRVLleLLEERDFPVGELRLLA-SSRSAGK--------------TVSFGGK--EL----TVEDATDFD 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINdeqSELLeiqkKNRDWKGWVApLPNCTTT 159
Cdd:COG0136   60 FSGVDIALFSAGGSVSKEYAPKAAAAgAVVIDNSSAFRMDPDVPLVVPEVN---PEAL----ADHLPKGIIA-NPNCSTI 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 160 GLVITMKPLYEKYGAKKVMMTSMQAISGGGRSpGV-----------SAMDVTD---------NIIPYIP--------KEE 211
Cdd:COG0136  132 QMLVALKPLHDAAGIKRVVVSTYQAVSGAGAA-AMdelaeqtaallNGEEIEPevfphpiafNLIPQIDvflengytKEE 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 212 GKVRIETRKILGKlkdgkiepADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNkEISVAGLPsAPKDY- 290
Cdd:COG0136  211 MKMVNETRKILGD--------PDIPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAP-GVKVVDDP-AENDYp 280

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663528508 291 ---YAVHEDPtrpqprierqvgdgmtTTIGRLEKEELFDHGLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:COG0136  281 tplDASGTDE----------------VFVGRIRKDLSVPNGLNLWVVADNLRKGAALNAVQIAELLIKE 333
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 166-337 5.44e-36

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: 128.59  E-value: 5.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  166 KPLYEKYGA-KKVMMTSMQAISGGGR--SPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADI-RVSCTC 241
Cdd:pfam02774   2 KPLRDALGGlERVIVDTYQAVSGAGKkaKPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTpKVSATC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  242 TRVPVIDGHTESVFVETEKEVDPknAKETYEQYNKEISVaglpsapkdyyAVHEDPT--RPQPRIERqvGDGMTTTIGRL 319
Cdd:pfam02774  82 VRVPVFRGHSETVTVKLKLKPID--VEEVYEAFYAAPGV-----------FVVVRPEedYPTPRAVR--GGTNFVYVGRV 146

                         170
                  ....*....|....*...
gi 663528508  320 EKEELFDHGLKYMLFSHN 337
Cdd:pfam02774 147 RKDPDGDRGLKLVSVIDN 164
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-133 2.77e-28

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: 106.86  E-value: 2.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508     4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYvdairdpdsgiikWEVGGEIPEYIKGmtVKKIDEINAAE 83
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKV-------------SEAGPHLKGEVVL--ELDPPDFEELA 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 663528508    84 LDLVFSAVESNAARDI---ETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQ 133
Cdd:smart00859  66 VDIVFLALPHGVSKESaplLPRAAAaGAVVIDLSSAFRMDDDVPYGLPEVNPEA 119
 
Name Accession Description Interval E-value
PRK08664 PRK08664
aspartate-semialdehyde dehydrogenase; Reviewed
 1-356 6.19e-165

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236329 [Multi-domain]  Cd Length: 349  Bit Score: 464.30  E-value: 6.19e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   1 MKKKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIRdpdsgiikWEVGGEIPEYIKGMTVKKIDEIN 80
Cdd:PRK08664   2 MKLKVGILGATGMVGQRFVQLLANHPWFEVTALAASERSAGKTYGEAVR--------WQLDGPIPEEVADMEVVSTDPEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKNRDWKGWVAPLPNCTTT 159
Cdd:PRK08664  74 VDDVDIVFSALPSDVAGEVEEEFAKAgKPVFSNASAHRMDPDVPLVIPEVNPEHLELIEVQRKRRGWDGFIVTNPNCSTI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 160 GLVITMKPLYEkYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADIRVSC 239
Cdd:PRK08664 154 GLVLALKPLMD-FGIERVHVTTMQAISGAGY-PGVPSMDIVDNVIPYIGGEEEKIEKETLKILGKFEGGKIVPADFPISA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 240 TCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTTIGRL 319
Cdd:PRK08664 232 TCHRVPVIDGHTEAVFVKFKEDVDPEEIREALESFKGLPQELGLPSAPKKPIILFEEPDRPQPRLDRDAGDGMAVSVGRL 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 663528508 320 EKEELFDhgLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:PRK08664 312 REDGIFD--IKFVVLGHNTVRGAAGASVLNAELLKKK 346
asd_EA TIGR00978
aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms); Two closely related ...
 4-355 1.06e-137

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: 395.28  E-value: 1.06e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508    4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIrdpdsgiiKWEVGGEIPEYIKGMTVKKIDEINAAE 83
Cdd:TIGR00978   2 RVAVLGATGLVGQKFVKLLAKHPYFELAKVVASPRSAGKRYGEAV--------KWIEPGDMPEYVRDLPIVEPEPVASKD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   84 LDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKnRDWKGWVAPLPNCTTTGLV 162
Cdd:TIGR00978  74 VDIVFSALPSEVAEEVEPKLAEAgKPVFSNASNHRMDPDVPLIIPEVNSDHLELLKVQKE-RGWKGFIVTNPNCTTAGLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  163 ITMKPLYEKYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADIRVSCTCT 242
Cdd:TIGR00978 153 LALKPLIDAFGIKKVHVTTMQAVSGAGY-PGVPSMDILDNIIPHIGGEEEKIERETRKILGKLENGKIEPAPFSVSATTT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  243 RVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTTIGRLEKE 322
Cdd:TIGR00978 232 RVPVLDGHTESVHVEFDKKFDIEEIREALKSFRGLPQKLGLPSAPEKPIIVRDEEDRPQPRLDRDAGGGMAVTVGRLREE 311

                         330       340       350
                  ....*....|....*....|....*....|...
gi 663528508  323 elfDHGLKYMLFSHNKKMGSAKGAVLLAEMLYK 355
Cdd:TIGR00978 312 ---GGSLKYVVLGHNLVRGAAGATLLNAELAYK 341
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 156-337 1.69e-86

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: 258.70  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADI 235
Cdd:cd18130    1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISGAGY-PGVPSLDILDNVIPYIGGEEEKIESETKKILGTLNEDKIEPADF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 236 RVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGDGMTTT 315
Cdd:cd18130   80 KVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQVLGPPSAPKPIIVVEDEPRRPQPRLDRDAGDGMAVT 159

                        170       180
                 ....*....|....*....|..
gi 663528508 316 IGRLEKEELFDhgLKYMLFSHN 337
Cdd:cd18130  160 VGRIRKDDDFD--LKFVLLSHN 179
ScASADH_like_N cd02315
N-terminal NAD(P)-binding domain of Saccharomyces cerevisiae aspartate beta-semialdehyde ...
 3-160 7.34e-73

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: 223.52  E-value: 7.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAIRdpdsgiikWEVGGEIPEYIKGMTVKKIDEINAA 82
Cdd:cd02315    1 IKVGVLGATGMVGQRFIQLLANHPWFELAALGASERSAGKKYGDAVR--------WKQDTPIPEEVADMVVKECEPEEFK 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663528508  83 ELDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKNRDWKGWVAPLPNCTTTG 160
Cdd:cd02315   73 DCDIVFSALDSDVAGEIEPAFAKaGIPVFSNASNHRMDPDVPLVIPEVNPDHLDLIEAQRKRRGWKGFIVTNPNNTVRG 151
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 3-356 2.72e-51

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: 173.68  E-value: 2.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEF--VLSLKDHPWFEVTQIAaSERSAGKnyvdairdpdsgiiKWEVGGEipEYikgmTVKKIDEIN 80
Cdd:COG0136    1 YNVAVVGATGAVGRVLleLLEERDFPVGELRLLA-SSRSAGK--------------TVSFGGK--EL----TVEDATDFD 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAKD-VPVISTSSAYRYEDDVPILIPGINdeqSELLeiqkKNRDWKGWVApLPNCTTT 159
Cdd:COG0136   60 FSGVDIALFSAGGSVSKEYAPKAAAAgAVVIDNSSAFRMDPDVPLVVPEVN---PEAL----ADHLPKGIIA-NPNCSTI 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 160 GLVITMKPLYEKYGAKKVMMTSMQAISGGGRSpGV-----------SAMDVTD---------NIIPYIP--------KEE 211
Cdd:COG0136  132 QMLVALKPLHDAAGIKRVVVSTYQAVSGAGAA-AMdelaeqtaallNGEEIEPevfphpiafNLIPQIDvflengytKEE 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 212 GKVRIETRKILGKlkdgkiepADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNkEISVAGLPsAPKDY- 290
Cdd:COG0136  211 MKMVNETRKILGD--------PDIPVSATCVRVPVFRGHSEAVNIEFERPVSLEEARELLAAAP-GVKVVDDP-AENDYp 280

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663528508 291 ---YAVHEDPtrpqprierqvgdgmtTTIGRLEKEELFDHGLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:COG0136  281 tplDASGTDE----------------VFVGRIRKDLSVPNGLNLWVVADNLRKGAALNAVQIAELLIKE 333
PLN02383 PLN02383
aspartate semialdehyde dehydrogenase
 4-353 4.87e-46

aspartate semialdehyde dehydrogenase


Pssm-ID: 178009 [Multi-domain]  Cd Length: 344  Bit Score: 160.32  E-value: 4.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEF--VLSLKDHPWFEVtQIAASERSAGKnyvdairdpdsgiikwEVGGEIPEYikgmTVKKIDEINA 81
Cdd:PLN02383   9 SVAIVGVTGAVGQEFlsVLTDRDFPYSSL-KMLASARSAGK----------------KVTFEGRDY----TVEELTEDSF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  82 AELDLVFSAvesnAARDIETKFA-----KDVPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKnrdwKGWVAPLPNC 156
Cdd:PLN02383  68 DGVDIALFS----AGGSISKKFGpiavdKGAVVVDNSSAFRMEEGVPLVIPEVNPEAMKHIKLGKG----KGALIANPNC 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 157 TTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGrSPGVSAM-----DVTD---------------NIIPYIP-------- 208
Cdd:PLN02383 140 STIICLMAVTPLHRHAKVKRMVVSTYQAASGAG-AAAMEELeqqtrEVLEgkpptcnifaqqyafNLFSHNApmqengyn 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 209 KEEGKVRIETRKILGklkdgkiePADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETyeqynkeisvagLPSAPK 288
Cdd:PLN02383 219 EEEMKLVKETRKIWN--------DDDVKVTATCIRVPVMRAHAESINLQFEKPLDEATAREI------------LASAPG 278

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663528508 289 ----DYYAVHEDPTrPQprierQVGDGMTTTIGRLEKEELFD--HGLKYMLFSHNKKMGSAKGAVLLAEML 353
Cdd:PLN02383 279 vkiiDDRANNRFPT-PL-----DASNKDDVAVGRIRQDISQDgnKGLDIFVCGDQIRKGAALNAVQIAELL 343
PRK14874 PRK14874
aspartate-semialdehyde dehydrogenase; Provisional
 4-353 6.06e-43

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 237845 [Multi-domain]  Cd Length: 334  Bit Score: 151.85  E-value: 6.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEfVLSLKDHPWFEVTQIA--ASERSAGKnyvdairdpdsgiiKWEVGGEIpeyikgMTVKKIDEINA 81
Cdd:PRK14874   3 NVAVVGATGAVGRE-MLNILEERNFPVDKLRllASARSAGK--------------ELSFKGKE------LKVEDLTTFDF 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  82 AELDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQselleiqKKNRDWKGWVAPlPNCTTTG 160
Cdd:PRK14874  62 SGVDIALFSAGGSVSKKYAPKAAAaGAVVIDNSSAFRMDPDVPLVVPEVNPEA-------LAEHRKKGIIAN-PNCSTIQ 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 161 LVITMKPLYEKYGAKKVMMTSMQAISGGG-----------RSPGVSAMDVTD----------NIIPYI--------PKEE 211
Cdd:PRK14874 134 MVVALKPLHDAAGIKRVVVSTYQAVSGAGkagmeelfeqtRAVLNAAVDPVEpkkfpkpiafNVIPHIdvfmddgyTKEE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 212 GKVRIETRKILGklkdgkiEPaDIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETyeqynkeisvagLPSAPkdYY 291
Cdd:PRK14874 214 MKMVNETKKILG-------DP-DLKVSATCVRVPVFTGHSESVNIEFEEPISVEEAREI------------LAEAP--GV 271

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663528508 292 AVHEDPTR---PQPrIErQVGDGmTTTIGRLEKEELFDHGLKYMLFSHNKKMGSAKGAVLLAEML 353
Cdd:PRK14874 272 VLVDDPENggyPTP-LE-AVGKD-ATFVGRIRKDLTVENGLHLWVVSDNLRKGAALNAVQIAELL 333
Semialdhyde_dhC pfam02774
Semialdehyde dehydrogenase, dimerization domain; This Pfam entry contains the following ...
 166-337 5.44e-36

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: 128.59  E-value: 5.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  166 KPLYEKYGA-KKVMMTSMQAISGGGR--SPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPADI-RVSCTC 241
Cdd:pfam02774   2 KPLRDALGGlERVIVDTYQAVSGAGKkaKPGVFGAPIADNLIPYIDGEEHNGTPETREELKMVNETKKILGFTpKVSATC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  242 TRVPVIDGHTESVFVETEKEVDPknAKETYEQYNKEISVaglpsapkdyyAVHEDPT--RPQPRIERqvGDGMTTTIGRL 319
Cdd:pfam02774  82 VRVPVFRGHSETVTVKLKLKPID--VEEVYEAFYAAPGV-----------FVVVRPEedYPTPRAVR--GGTNFVYVGRV 146

                         170
                  ....*....|....*...
gi 663528508  320 EKEELFDHGLKYMLFSHN 337
Cdd:pfam02774 147 RKDPDGDRGLKLVSVIDN 164
ASADH_C_like cd18124
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 156-337 4.82e-35

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: 126.94  E-value: 4.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGR-------------------SPGVSAMDVTDNIIPYIPK------- 209
Cdd:cd18124    1 CTVSLLVMALKPLFAKFLVEWVSVAT*QAVSGAGYenmrellsqmgelmragplPTGVFS*AIADNLIPWIDKvldngqs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 210 -EEGKVRIETRKILGKLKdgkiepADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPk 288
Cdd:cd18124   81 kEEWKIQAEANKILGTLD------SPIPISVTCNRVPVLDGHSQSFTLKLKEDVPLEEVEEVLDAHKPWVKVIPNDYAI- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663528508 289 dyyavhedptRPQPRIERQVGDGMTTTIGRLEKEELFDHGLKYMLFSHN 337
Cdd:cd18124  154 ----------RPQPRLDRKVTGGLSTPVGRIRKDAMDPFDVNAFAVSDN 192
ASADH_C cd18128
C-terminal catalytic domain of aspartate beta-semialdehyde dehydrogenase (ASADH) and similar ...
 156-337 3.23e-34

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: 123.77  E-value: 3.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRspgvsamDVTDNIIPYIP--------KEEGKVRIETRKILGKLKD 227
Cdd:cd18128    1 CTVSLMLMALGGLFQKFLVEWVSVATYQAVSGAG*-------PIAGNLIPWIDvfldngqtKEEWKGQAETNKILGDLDS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 228 gkiepaDIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAglpsapkdyyavhEDPTRPQPRIERQ 307
Cdd:cd18128   74 ------PIPISGTCVRVGVLRCHSQAFTIKLKEDAPIEEVEEAIAAHN*WIKVI-------------PNVDRITPRTPAN 134

                        170       180       190
                 ....*....|....*....|....*....|
gi 663528508 308 VGDGMTTTIGRLEKEELFDHGLKYMLFSHN 337
Cdd:cd18128  135 VTGTLSTPVGRIRKDAMGPFDLQAFTVGDN 164
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 4-133 6.82e-34

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: 121.48  E-value: 6.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508    4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYVDAirdpdsgiikwevgGEIPEYIKGMTVKKIDEINAAE 83
Cdd:pfam01118   1 KVAIVGATGYVGQELLRLLEEHPPVELVVLFASSRSAGKKLAFV--------------HPILEGGKDLVVEDVDPEDFKD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 663528508   84 LDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQ 133
Cdd:pfam01118  67 VDIVFFALPGGVSKEIAPKLAEaGAKVIDLSSDFRMDDDVPYGLPEVNREA 117
ASADH_MCR_N cd24150
N-terminal NAD(P)-binding domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and ...
 4-160 2.21e-29

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: 110.88  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAAsERSAGKNYVDairdpdsgIIKWEVGGEIPEYIKGMTVKKIDEINAAE 83
Cdd:cd24150    3 KAAILGATGLVGIEYVRMLSNHPYIKPAYLAG-KGSVGKPYGE--------VVRWQTVGQVPKEIADMEIKPTDPKLMDD 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663528508  84 LDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQSELLEIQKKNRDWKGWVAPLPNCTTTG 160
Cdd:cd24150   74 VDIIFSPLPQGAAGPVEEQFAKeGFPVISNSPDHRFDPDVPLLVPELNPHTISLIDEQRKRREWKGFIVTTPLNTVRG 151
Semialdhyde_dh smart00859
Semialdehyde dehydrogenase, NAD binding domain; The semialdehyde dehydrogenase family is found ...
 4-133 2.77e-28

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: 106.86  E-value: 2.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508     4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERSAGKNYvdairdpdsgiikWEVGGEIPEYIKGmtVKKIDEINAAE 83
Cdd:smart00859   1 KVAIVGATGYVGQELLRLLAEHPDFELTALAASSRSAGKKV-------------SEAGPHLKGEVVL--ELDPPDFEELA 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 663528508    84 LDLVFSAVESNAARDI---ETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQ 133
Cdd:smart00859  66 VDIVFLALPHGVSKESaplLPRAAAaGAVVIDLSSAFRMDDDVPYGLPEVNPEA 119
ASADH_C_bac_euk_like cd18131
C-terminal catalytic domain of bacterial/eukaryotic aspartate beta-semialdehyde dehydrogenase ...
 156-329 1.25e-27

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: 107.21  E-value: 1.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRSpGV-----------SAMDVTDNIIPY------IP---------- 208
Cdd:cd18131    1 CSTIQMVVALKPLHDAFGLKRVVVSTYQAVSGAGAA-AMeeleeqtrgllNGKEAEPKVFPYqiafnvIPhidvfldngy 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 209 -KEEGKVRIETRKILGKlkdgkiepADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQynkeisVAGLpsap 287
Cdd:cd18131   80 tKEEMKMVNETRKILGD--------PDLRVSATCVRVPVFRGHSESVNIEFEKPISVEEAREALAK------APGV---- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 663528508 288 kdyyAVHEDPTR---PQPrieRQVGDGMTTTIGRLEKEELFDHGL 329
Cdd:cd18131  142 ----VVVDDPANnvyPTP---LDAAGKDDVFVGRIRKDISVPNGL 179
ASADH_C_MCR cd23940
C-terminal catalytic domain of archaeal NADP-dependent malonyl-CoA reductase (MCR) and similar ...
 156-321 2.94e-25

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: 100.59  E-value: 2.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRsPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDGKIEPA-- 233
Cdd:cd23940    2 CTAQGAAIPLGAIFKDYKMDGAFITTIQSLSGAGY-PGIPSLDVVDNILPLGDGYDAKTIKEIFRILSEVKRNVDEPKle 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 234 DIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSAPKDYYAVHEDPTRPQPRIERQVGD--G 311
Cdd:cd23940   81 DVSLAATTHRIATIHGHYEVLYVSFKEETAAEKVKETLENFRGEPQDLKLPTAPSKPIIVMNEDTRPQVYFDRWAGDipG 160

                        170
                 ....*....|
gi 663528508 312 MTTTIGRLEK 321
Cdd:cd23940  161 MSVVVGRLKQ 170
PRK06728 PRK06728
aspartate-semialdehyde dehydrogenase; Provisional
 5-356 5.19e-25

aspartate-semialdehyde dehydrogenase; Provisional


Pssm-ID: 136022 [Multi-domain]  Cd Length: 347  Bit Score: 103.98  E-value: 5.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   5 VAIIGVTGAVGQEFVLSLKDHPWFEVTQIA--ASERSAGKnyvdairdpdsgIIKWEvGGEIpeYIKGMTVKKIDEINAA 82
Cdd:PRK06728   8 VAVVGATGAVGQKIIELLEKETKFNIAEVTllSSKRSAGK------------TVQFK-GREI--IIQEAKINSFEGVDIA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  83 eldlVFSAVESNAARDIETKFAKDVPVISTSSAYRYEDDVPILIPGINDEQSelleiqkknRDWKGWVApLPNCTTTGLV 162
Cdd:PRK06728  73 ----FFSAGGEVSRQFVNQAVSSGAIVIDNTSEYRMAHDVPLVVPEVNAHTL---------KEHKGIIA-VPNCSALQMV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 163 ITMKPLYEKYGAKKVMMTSMQAISGGG-------RSPGVSAM---DVTDNIIP-------------YIPK---------- 209
Cdd:PRK06728 139 TALQPIRKVFGLERIIVSTYQAVSGSGihaiqelKEQAKSILageEVESTILPakkdkkhypiafnVLPQvdiftdndft 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 210 -EEGKVRIETRKILgklkdgkiEPADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETyeqynkeisvagLPSAPK 288
Cdd:PRK06728 219 fEEVKMIQETKKIL--------EDPNLKMAATCVRVPVISGHSESVYIELEKEATVAEIKEV------------LFDAPG 278

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663528508 289 dyYAVHEDPTR---PQPRIERQVGDgmtTTIGRLEKEELFDHGLKYMLFSHNKKMGSAKGAVLLAEMLYKK 356
Cdd:PRK06728 279 --VILQDNPSEqlyPMPLYAEGKID---TFVGRIRKDPDTPNGFHLWIVSDNLLKGAAWNSVQIAETMVEE 344
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 156-337 6.79e-25

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: 99.13  E-value: 6.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGR-SPGVSAMDVTDNIIPYIPKEEGKVRIETRKILGKLKDgkiepaD 234
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPkTKGPILKSEVRAIIPNIPKNETKHAPETGKVLGEIGK------P 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 235 IRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVaglpsapkdyyaVHEDPTRPQPRIERQVGDGMTT 314
Cdd:cd18122   75 IKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQI------------SAEDGLTYAKVSTRSVGGVYGV 142

                        170       180
                 ....*....|....*....|...
gi 663528508 315 TIGRLEKEELFDHGLKYMLFSHN 337
Cdd:cd18122  143 PVGRQREFAFDDNKLKVFSAVDN 165
ASADH_N_like cd24147
N-terminal NAD(P)-binding domain of aspartate beta-semialdehyde dehydrogenase (ASADH), USG-1 ...
 3-133 2.41e-20

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: 85.85  E-value: 2.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPwFEVTQIA--ASERSAGKNYVDAIRDpdsgiikwevggeipeyikgMTVKKIDEIN 80
Cdd:cd24147    1 LRVGVVGATGAVGSEILQLLAEEP-DPLFELRalASEESAGKKAEFAGEA--------------------IMVQEADPID 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQ 133
Cdd:cd24147   60 FLGLDIVFLCAGAGVSAKFAPEAARaGVLVIDNAGALRMDPDVPLVVPEVNAEA 113
PRK08040 PRK08040
putative semialdehyde dehydrogenase; Provisional
 5-353 1.27e-19

putative semialdehyde dehydrogenase; Provisional


Pssm-ID: 181205 [Multi-domain]  Cd Length: 336  Bit Score: 88.60  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   5 VAIIGVTGAVGqEFVLSLKDHPWFEVTQI--AASERSAGKNyvdaIRdpdsgiikweVGGeipeyiKGMTVKKIDEINAA 82
Cdd:PRK08040   7 IALLGATGAVG-EALLELLAERQFPVGELyaLASEESAGET----LR----------FGG------KSVTVQDAAEFDWS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  83 ELDLVFSAVESNA-ARDIETKFAKDVPVISTSSAYRYEDDVPILIPGINDeqSELLEIQKKNrdwkgwVAPLPNCTTTGL 161
Cdd:PRK08040  66 QAQLAFFVAGREAsAAYAEEATNAGCLVIDSSGLFALEPDVPLVVPEVNP--FVLADYRNRN------IIAVADSLTSQL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 162 VITMKPLYEKYGAKKVMMTSMQAISGGGRS-------------------PGVSAMDVTDNIIPYIPKEEGKVRIE----- 217
Cdd:PRK08040 138 LTAIKPLIDQAGLSRLHVTNLLSASAHGKAavdalagqsakllngipieEGFFGRQLAFNMLPLLPDSEGSVREErrlvd 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 218 -TRKILGklKDGkiepadIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYnKEISVaglpSAPKDYyavhed 296
Cdd:PRK08040 218 qVRKILQ--DEG------LPISVSCVQSPVFYGHAQMVHFEALRPLAAEEARDALEQG-EDIVL----SEENDY------ 278

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663528508 297 PTrpqprierQVGDGMTT---TIGRLEKeelfDHGLKYML----FSHNKKMGSAKGAVLLAEML 353
Cdd:PRK08040 279 PT--------QVGDASGNphlSIGCVRN----DYGMPEQLqfwsVADNVRFGGALMAVKTAEKL 330
ASADH_AGPR_N cd02281
N-terminal NAD(P)-binding domain of aspartate-beta-semialdehyde dehydrogenase (ASADH) and ...
 3-146 1.41e-19

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: 83.95  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPW--FEVTQIAASERSAGKNYVDairdpdsgiikwevggeiPEYIKGMTVKKIDEIN 80
Cdd:cd02281    1 KKVGVVGATGYVGGEFLRLLLEHPFplFEIVLLAASSAGAKKKYFH------------------PKLWGRVLVEFTPEEV 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663528508  81 AAELDLVFSAVESNAARDIETKFAK-DVPVISTSSAYRYEDDVPILIPGINDEQSElleiQKKNRDW 146
Cdd:cd02281   63 LEQVDIVFTALPGGVSAKLAPELSEaGVLVIDNASDFRLDKDVPLVVPEVNREHIG----ELKGTKI 125
VcASADH2_like_N cd02316
N-terminal NAD(P)-binding domain of Vibrio cholerae aspartate beta-semialdehyde dehydrogenase ...
 4-130 1.55e-18

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: 80.94  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEFVLSLKDHPwFEVTQI--AASERSAGKnyvdairdpdsgiiKWEVGGEipEYikgmTVKKIDEINA 81
Cdd:cd02316    2 NVAIVGATGAVGQEMLKVLEERN-FPVSELrlLASARSAGK--------------TLEFKGK--EL----TVEELTEDSF 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663528508  82 AELDLVFSAVESNAARdietKFAKDVP-----VISTSSAYRYEDDVPILIPGIN 130
Cdd:cd02316   61 KGVDIALFSAGGSVSK----EFAPIAAeagavVIDNSSAFRMDPDVPLVVPEVN 110
ASADH_USG1_N cd17894
N-terminal NAD(P)-binding domain of USG-1 protein and similar proteins; The family includes ...
 4-155 7.16e-13

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: 65.34  E-value: 7.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEFVLSLKDHPwFEVTQIAA--SERSAGKnyvdairdpdsgiiKWEVGGEIpeyikgMTVKKIDEINA 81
Cdd:cd17894    2 RIAVVGATGLVGKELLELLEERG-FPVGRLRLldSEESAGE--------------LVEFGGEP------LDVQDLDEFDF 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663528508  82 AELDLVFSAVESNAARD-IETKFAKDVPVISTSSAYRYEDDVPILIPGINDEQselLEIQKKnrdwKGWVApLPN 155
Cdd:cd17894   61 SDVDLVFFAGPAEVARAyAPRARAAGCLVIDLSGALRSDPDVPLVVPGVNPEA---LAAAAE----RRVVA-VPN 127
AGPR_1_N cd17895
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), type 1 ...
 3-121 3.13e-11

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: 61.29  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIaASERSAGKNYvdairdpdsgiikWEVGGEIPEYIKGMTVKKIDEINAA 82
Cdd:cd17895    1 IKVGIIGASGYTGAELLRLLLNHPEVEIVAL-TSRSYAGKPV-------------SEVFPHLRGLTDLTFEPDDDEEIAE 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663528508  83 ELDLVFSAVESNAARDIETKF-AKDVPVISTSSAYRYEDD 121
Cdd:cd17895   67 DADVVFLALPHGVSMELAPKLlEAGVKVIDLSADFRLKDP 106
PRK05671 PRK05671
aspartate-semialdehyde dehydrogenase; Reviewed
 5-355 6.34e-10

aspartate-semialdehyde dehydrogenase; Reviewed


Pssm-ID: 168165 [Multi-domain]  Cd Length: 336  Bit Score: 59.74  E-value: 6.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   5 VAIIGVTGAVGQEFV--LSLKDHPWFEVTQIAASErSAGKNyvdairdpdsgiikwevggeIPEYIKGMTVKKIDEINAA 82
Cdd:PRK05671   7 IAVVGATGTVGEALVqiLEERDFPVGTLHLLASSE-SAGHS--------------------VPFAGKNLRVREVDSFDFS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  83 ELDLVFSAVESNAARDI-ETKFAKDVPVISTSSAYRYEDdVPILIPGINDEQSELLEiqkknrdwKGWVAPLPNCTTTGL 161
Cdd:PRK05671  66 QVQLAFFAAGAAVSRSFaEKARAAGCSVIDLSGALPSAQ-APNVVPEVNAERLASLA--------APFLVSSPSASAVAL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 162 VITMKPLYEKYGAKKVMMTSMQAISGGGRSpGVSAM--------------------DVTDNIIPYI--PKEEGKVRIEtR 219
Cdd:PRK05671 137 AVALAPLKGLLDIQRVQVTACLAVSSLGRE-GVSELarqtaellnarpleprffdrQVAFNLLAQVgaPDAQGHTALE-R 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 220 KILGKLKDGKIEPAdIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKetyeqynkeisvAGLPSAP-------KDYya 292
Cdd:PRK05671 215 RLVAELRQLLGLPE-LKISVTCIQVPVFFGDSLSVALQSAAPVDLAAVN------------AALEAAPgielveaGDY-- 279

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663528508 293 vhedPTrpqprierQVGDGM---TTTIGRLEKEELFDHGLKYMLFSHNKKMGSAKGAVLLAEMLYK 355
Cdd:PRK05671 280 ----PT--------PVGDAVgqdVVYVGRVRAGVDDPCQLNLWLTSDNVRKGAALNAVQVAELLIK 333
ArgC COG0002
N-acetyl-gamma-glutamylphosphate reductase [Amino acid transport and metabolism]; ...
 4-274 6.00e-08

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: 53.54  E-value: 6.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIaASERSAGKNYVDAIrdPD-SGIIkwevggeipeyikGMTVKKID-EINA 81
Cdd:COG0002    2 KVGIVGASGYTGGELLRLLLRHPEVEIVAL-TSRSNAGKPVSEVH--PHlRGLT-------------DLVFEPPDpDELA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  82 AELDLVFSAVESNAARDIETKF-AKDVPVISTSSAYRYEDDV------------PILI-------PGINDEqsellEIQK 141
Cdd:COG0002   66 AGCDVVFLALPHGVSMELAPELlEAGVKVIDLSADFRLKDPAvyekwygfehaaPELLgeavyglPELNRE-----EIKG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 142 KNRdwkgwVApLPNCTTTGLVITMKPLYEkygAKKVMMTSMQA-----ISGGGRSPGV--SAMDVTDNIIPY-------I 207
Cdd:COG0002  141 ARL-----IA-NPGCYPTAVLLALAPLLK---AGLIDPDDIIIdaksgVSGAGRKASEgtHFSEVNENFRAYkvgghrhT 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663528508 208 PkeegkvriETRKILGKLKDgkiepADIRVSCTCTRVPVIDG-HTeSVFVETEKEVDPKNAKETYEQY 274
Cdd:COG0002  212 P--------EIEQELSRLAG-----EDVKVSFTPHLVPMVRGiLA-TIYARLKDGVTEEDLRAAYEEF 265
ASADH_C_USG1_like cd18129
C-terminal domain of USG-1 protein and similar proteins; The family includes Escherichia coli ...
 166-273 9.86e-08

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: 51.43  E-value: 9.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 166 KPLYEKYGAKKVMMTSMQAISGGGRsPGV-----------SAMDVTD---------NIIPYIPK--------EEGKVRIE 217
Cdd:cd18129   11 APLHDAAGLERVVVTVLQPVSEAGQ-AGVdelarqtarllNGQPVEPevfprqlafNLLPQVGDfdadglsdEERRIAAE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663528508 218 TRKILGklkdgkiePADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQ 273
Cdd:cd18129   90 LRRLLG--------GPDLPVSVTCVQVPVFYGHSASVHVELAEPVDLEEVRAALAA 137
AGPR_1_actinobacAGPR_like cd24148
N-terminal NAD(P)-binding domain of actinobacterial N-acetyl-gamma-glutamyl-phosphate ...
 4-120 1.64e-06

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: 47.67  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   4 KVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAAsERSAGKNYVDaiRDPdsgiikwevggEIPEYiKGMTVKKIDEINAAE 83
Cdd:cd24148    2 RVAVAGASGYAGGELLRLLLGHPEFEIGALTA-HSNAGQRLGE--LHP-----------HLPPL-ADRVLEPTTPAVLAG 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663528508  84 LDLVFSAVESNAARDIETKFAKDVPVISTSSAYRYED 120
Cdd:cd24148   67 HDVVFLALPHGASAAIAAQLPPDVLVVDCGADHRLED 103
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-191 1.44e-05

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 46.36  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   2 KKKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAAsERSAGKNYvdairdpdSGIIKWEVGGEIPEYIkgmtvkKIDEINA 81
Cdd:PLN02968  38 KKRIFVLGASGYTGAEVRRLLANHPDFEITVMTA-DRKAGQSF--------GSVFPHLITQDLPNLV------AVKDADF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508  82 AELDLVFSAVESNAARDIETKFAKDVPVISTSSAYRYEDDV--------PILIPGINDEQSE-LLEIQKKNRDWKGWVAP 152
Cdd:PLN02968 103 SDVDAVFCCLPHGTTQEIIKALPKDLKIVDLSADFRLRDIAeyeewyghPHRAPELQKEAVYgLTELQREEIKSARLVAN 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 663528508 153 lPNCTTTGLVITMKPLYEK--YGAKKVMMTSMQAISGGGRS 191
Cdd:PLN02968 183 -PGCYPTGIQLPLVPLVKAglIEPDNIIIDAKSGVSGAGRG 222
AGPR_N cd02280
N-terminal NAD(P)-binding domain of N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) and ...
 3-120 2.05e-05

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: 44.10  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPWFEVTQIAASERsAGKnyvdairdpdsgiikwEVGGEIPEYIKGMTVKKIDE---I 79
Cdd:cd02280    1 PRVAIIGASGYTGLEIVRLLLGHPYLRVLTLSSRER-AGP----------------KLREYHPSLIISLQIQEFRPcevL 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663528508  80 NAAelDLVFSAVESNAARD-IETKFAKDVPVISTSSAYRYED 120
Cdd:cd02280   64 NSA--DILVLALPHGASAElVAAISNPQVKIIDLSADFRFTD 103
PRK06901 PRK06901
oxidoreductase;
120-356 2.74e-05

oxidoreductase;


Pssm-ID: 235883 [Multi-domain]  Cd Length: 322  Bit Score: 45.49  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 120 DDVPILIPGINDEQseLLEIQKKNrdwkgwVAPLPNCTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGrSPGVSAM-D 198
Cdd:PRK06901 102 ANVPVVVPSVNDEQ--LAELRQRN------IVSLPDPQVSQLALALAPFLQEQPLSQIFVTSLLPASYTD-AETVKKLaG 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 199 VTDNIIPYIPKEEGKVRIE----TRKILG-KLKDGKIEPADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQ 273
Cdd:PRK06901 173 QTARLLNGIPLDEEEQRLAfdvfPANAQNlELQLQKIFPQLENVTFHSIQVPVFYGLAQMVTALSEYELDIESQLAEWQQ 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 274 yNKEIsvaglpsapkDYyavHEDPT-RPQPRIERQVG-DGMTTTIGRLEKEElfdHGLKYMLFSHNKKMGSAKGAVLLAE 351
Cdd:PRK06901 253 -NNLL----------RY---HEEKLiTPVLNGENENGeESVKLHISQLSAVE---NGVQFWSVADEQRFNLAFLAVKLLE 315


                 ....*
gi 663528508 352 MLYKK 356
Cdd:PRK06901 316 LIYQQ 320
AGPR_1_N_LysY cd24151
N-terminal NAD(P)-binding domain of [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate ...
 3-120 2.91e-05

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: 43.80  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPWFEVTQiAASERSAGKnYVDAIRdPDsgiikwevggeipeyIKGMTVKKIDEINAA 82
Cdd:cd24151    1 ITVSIVGASGYTGGELLRLLLGHPEVEVKQ-VTSESLAGK-PVHRVH-PN---------------LRGRTLLKFVPPEEL 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663528508  83 E-LDLVFSAVESNAARDIETKFAKDVP-VISTSSAYRYED 120
Cdd:cd24151   63 EsCDVLFLALPHGESMKRIDRFAELAPrIIDLSADFRLKD 102
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 156-286 6.35e-05

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 42.99  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508 156 CTTTGLVITMKPLYEKYGAKKVMMTSMQAISGGGRS-PGVSAMDVTD------NIIPYIP---KEEGKVrietrkilgkl 225
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTvDGPSGKDWRAsrgavnNIIPNPTgaaKAVGKV----------- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663528508 226 kdgkIEPADIRVSCTCTRVPVIDGHTESVFVETEKEVDPKNAKETYEQYNKEISVAGLPSA 286
Cdd:cd18123   70 ----LPELNGKLTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGKGRLGYTEA 126
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 3-121 1.09e-04

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


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 42.10  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663528508   3 KKVAIIGVTGAVGQEFVLSLKDHPWFEVTqiAASERS-AGKnyvdairdPDSGIIKWEVGGEIPEyikgmTVKKIDEINA 81
Cdd:cd24149    1 KRVGLIGARGYVGRELIRLLNRHPNLELA--HVSSRElAGQ--------KVSGYTKSPIDYLNLS-----VEDIPEEVAA 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663528508  82 AELDLVFSAVESNAARD----IEtKFAKDVPVISTSSAYRYEDD 121
Cdd:cd24149   66 REVDAWVLALPNGVAKPfvdaID-KANPKSVIVDLSADYRFDDA 108
 
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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