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Conserved domains on  [gi|1006542799|ref|WP_061793531|]
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homoserine dehydrogenase [Cytobacillus firmus]

Protein Classification

homoserine dehydrogenase( domain architecture ID 11421468)

homoserine dehydrogenase catalyzes the conversion from L-homoserine and NAD(P)(+) to L-aspartate 4-semialdehyde and NAD(P)H

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-318 2.10e-129

Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis


:

Pssm-ID: 440228 [Multi-domain]  Cd Length: 302  Bit Score: 374.38  E-value: 2.10e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  23 RKHQERLQTILGKEVKVSAILVKNVNKH-SLPDDQVLLTDDFQDIIELPKLDVVIDAIVGREPGYTYLRQAISRGCHVIT 101
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPrGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 102 ANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKI 181
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 182 AQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEySV-REGITDITIEQIRLADSLGLKFKHAASIQKEKDFVRC 260
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELE-DVyVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799 261 TVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:COG0460   240 RVHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIAR 297
 
Name Accession Description Interval E-value
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-318 2.10e-129

Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440228 [Multi-domain]  Cd Length: 302  Bit Score: 374.38  E-value: 2.10e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  23 RKHQERLQTILGKEVKVSAILVKNVNKH-SLPDDQVLLTDDFQDIIELPKLDVVIDAIVGREPGYTYLRQAISRGCHVIT 101
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPrGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 102 ANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKI 181
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 182 AQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEySV-REGITDITIEQIRLADSLGLKFKHAASIQKEKDFVRC 260
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELE-DVyVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799 261 TVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:COG0460   240 RVHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIAR 297
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-318 1.10e-125

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 369.40  E-value: 1.10e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   1 MSAITIGLLGFGTVGKGVYETIRKHQERLQTILGKEVKVSAILVKNVNKH-SLPDDQVLLTDDFQDIIELPKLDVVIDAI 79
Cdd:PRK06349    1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDrGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  80 VGREPGYTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLNANRIERIEGILNG 159
Cdd:PRK06349   81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 160 TSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEYSVREGITDITIEQIRLAD 239
Cdd:PRK06349  161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1006542799 240 SLGLKFKHAASIQKEKDFVRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:PRK06349  241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIAR 319
Homoserine_dh pfam00742
Homoserine dehydrogenase;
136-313 2.48e-76

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 234.57  E-value: 2.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 136 PIIQTIRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGK 215
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 216 APAQEYSVREGITDITIEQIRLADSLGLKFKHAASIQKEKDFVRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISL 295
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1006542799 296 QGPGAGMFPTASAIIEDL 313
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-147 8.22e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 48.31  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  10 GFGTVGKGVYETIRKHqerlqtilgKEVKVSAILVKNVNK--------HSLPDDQVLLTDDFQDIIELPKLDVVIDAIVG 81
Cdd:cd24146     7 GLGAMGRGIARYLLEK---------PGLEIVGAVDRDPAKvgkdlgelGGGAPLGVKVTDDLDAVLAATKPDVVVHATTS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799  82 R-EPGYTYLRQAISRGCHVITANKEMFAYHGS--ELAK----LAKEKNVSL-----GFEATVGggiPIIQTIRQLLNA 147
Cdd:cd24146    78 FlADVAPQIERLLEAGLNVITTCEELFYPWARdpELAEeldaLAKENGVTVlgtgpGDVATAA---IVVNRIPDVIAA 152
 
Name Accession Description Interval E-value
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-318 2.10e-129

Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440228 [Multi-domain]  Cd Length: 302  Bit Score: 374.38  E-value: 2.10e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  23 RKHQERLQTILGKEVKVSAILVKNVNKH-SLPDDQVLLTDDFQDIIELPKLDVVIDAIVGREPGYTYLRQAISRGCHVIT 101
Cdd:COG0460     1 LENAEELARRLGLDLRVVGVAVRDGMKPrGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 102 ANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKI 181
Cdd:COG0460    81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 182 AQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEySV-REGITDITIEQIRLADSLGLKFKHAASIQKEKDFVRC 260
Cdd:COG0460   161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELE-DVyVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEA 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799 261 TVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:COG0460   240 RVHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIAR 297
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-318 1.10e-125

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 369.40  E-value: 1.10e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   1 MSAITIGLLGFGTVGKGVYETIRKHQERLQTILGKEVKVSAILVKNVNKH-SLPDDQVLLTDDFQDIIELPKLDVVIDAI 79
Cdd:PRK06349    1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDrGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  80 VGREPGYTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLNANRIERIEGILNG 159
Cdd:PRK06349   81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 160 TSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEYSVREGITDITIEQIRLAD 239
Cdd:PRK06349  161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1006542799 240 SLGLKFKHAASIQKEKDFVRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:PRK06349  241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIAR 319
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 6-319 2.77e-91

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 278.67  E-value: 2.77e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   6 IGLLGFGTVGKGVYETIRKHQERLQTILGKEVKVSAI-----------------LVKNVNK----HSLPDDQVLLTDDfq 64
Cdd:PRK06270    5 IALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIadssgsaidpdgldlelALKVKEEtgklADYPEGGGEISGL-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  65 DIIELPKLDVVIDA----IVGREPGYTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQT 140
Cdd:PRK06270   83 EVIRSVDADVVVEAtptnIETGEPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPIINL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 141 IRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQE 220
Cdd:PRK06270  163 AKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADLTIK 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 221 YSVREGITDITIEQIRLADSLGLKFKHAASIQKEKDFvrcTVKPVLTGESHPLyRVEGVQNAVSIDADIVGNISLQGPGA 300
Cdd:PRK06270  243 DVEVEGITKITPEAIELAAKEGYRIKLIGEVSREKDL---SVSPRLVPLDHPL-AVSGTLNAATFETDLAGDVTVVGRGA 318

                         330
                  ....*....|....*....
gi 1006542799 301 GMFPTASAIIEDLIHVGKA 319
Cdd:PRK06270  319 GSIETASAILSDLIAIHDR 337
Homoserine_dh pfam00742
Homoserine dehydrogenase;
136-313 2.48e-76

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 234.57  E-value: 2.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 136 PIIQTIRQLLNANRIERIEGILNGTSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGK 215
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 216 APAQEYSVREGITDITIEQIRLADSLGLKFKHAASIQKEKDFVRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISL 295
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 1006542799 296 QGPGAGMFPTASAIIEDL 313
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
 4-314 1.18e-57

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 191.94  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   4 ITIGLLGFGTVGKGVYETIRKHQERLQTILGKEVKV-------------------SAILVK-NVNKHS-LPDDQVLLTDD 62
Cdd:PRK08374    3 VKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVvsitdtsgtiwlpedidlrEAKEVKeNFGKLSnWGNDYEVYNFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  63 FQDIIELPKLDVVIDAIVGREPGYTYLRqAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIR 142
Cdd:PRK08374   83 PEEIVEEIDADIVVDVTNDKNAHEWHLE-ALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIGLLR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 143 QLLNANRIERIEGILNGTSNFILTSMrEENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEYS 222
Cdd:PRK08374  162 ENLLGDTVKRIEAVVNATTTFILTRM-EQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAFPPITFEEVG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 223 VReGITDITIEQIRLADSLGLKFKHAASIQKEkdfvRCTVKPVLTGESHPLYrVEGVQNAVSIDADIVGNISLQGPGAGM 302
Cdd:PRK08374  241 IR-GIKDVTEGEIERAKAKGRNVRLVATVEEG----RISVKPKKLPENSPLA-VEGVENAAVIKTDLLGELVLKGPGAGG 314

                         330
                  ....*....|..
gi 1006542799 303 FPTASAIIEDLI 314
Cdd:PRK08374  315 KETASGVVTDII 326
PRK06813 PRK06813
homoserine dehydrogenase; Validated
 4-321 8.25e-38

homoserine dehydrogenase; Validated


Pssm-ID: 168683 [Multi-domain]  Cd Length: 346  Bit Score: 139.61  E-value: 8.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   4 ITIGLLGFGTVGKGVYETIRKHQERLQTILGKEVKVSAILVKNV---NKHSLPDDQVLLTDDFQDIIE-----LPKL--- 72
Cdd:PRK06813    3 IKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVaihNEDGLSIHHLLRYGGGSCAIEkyiehHPEErat 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  73 -----DVVIDAIVGR----EPGYTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQ 143
Cdd:PRK06813   83 dnisgTVLVESTVTNlkdgNPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIGQF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 144 LLNANRIERIEGILNGTSNFILTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKAPAQEYSV 223
Cdd:PRK06813  163 SLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTDIH 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 224 REGITDITIEQIRLADSLGLKFKHAASIQKEKD-FVRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISLQGPGAGM 302
Cdd:PRK06813  243 IKGIEHVTKQQIRNAKEQNKIIKLIASAYKDNEgNVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGASNP 322

                         330
                  ....*....|....*....
gi 1006542799 303 FPTASAIIEDLIHVGKADF 321
Cdd:PRK06813  323 RGAAAAALKDIINLYRKDL 341
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 4-314 2.95e-33

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 131.82  E-value: 2.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   4 ITIGLLGFGTVGKGVYETIRKHQERL--QTIlgkEVKVSAI-----LVKNVNKHSLPDDQVLLTD-----DFQDIIELPK 71
Cdd:PRK09436  466 LDVFVIGVGGVGGALLEQIKRQQPWLkkKNI---DLRVCGIansrkMLLDEHGIDLDNWREELAEagepfDLDRLIRLVK 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  72 LD-----VVID-----AIVGREPGYtylrqaISRGCHVITANK-----EMFAYHgsELAKLAKEKNVSLGFEATVGGGIP 136
Cdd:PRK09436  543 EYhllnpVIVDctssqAVADQYADF------LAAGFHVVTPNKkantsSYAYYH--QLREAARKSRRKFLYETNVGAGLP 614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 137 IIQTIRQLLNA-NRIERIEGILNGTSNFILTsMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLS-ELVFg 214
Cdd:PRK09436  615 VIETLQNLLNAgDELLKFEGILSGSLSFIFG-KLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILArEAGY- 692

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 215 kapAQEYSvregitDITIEQI----------------RL-------------ADSLGLKFKHAASIQKEKdfvrCTVKPV 265
Cdd:PRK09436  693 ---ELELE------DIEVESVlpeefdasgsvdefmaRLpeldaefaarvakARAEGKVLRYVGQIEDGK----CRVGIA 759

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1006542799 266 LTGESHPLYRVEGVQNAVSIDADIVGNISL--QGPGAGMFPTASAIIEDLI 314
Cdd:PRK09436  760 EVDANHPLYKVKGGENALAFYTRYYQPIPLvlRGYGAGNEVTAAGVFADLL 810
PRK06392 PRK06392
homoserine dehydrogenase; Provisional
 4-318 1.22e-22

homoserine dehydrogenase; Provisional


Pssm-ID: 102354 [Multi-domain]  Cd Length: 326  Bit Score: 97.63  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   4 ITIGLLGFGTVGKGVYETIRKHQERLQTILG-KEVKVSAILVKNVNKHSLP-------------DDQVLLTDDFQDIIEL 69
Cdd:PRK06392    1 IRISIIGLGNVGLNVLRIIKSRNDDRRNNNGiSVVSVSDSKLSYYNERGLDigkiisykekgrlEEIDYEKIKFDEIFEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  70 pKLDVVIDAIVGREPG---YTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNVSLGFEATVGGGIPIIQTIRQLLN 146
Cdd:PRK06392   81 -KPDVIVDVTPASKDGireKNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYSTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 147 ANRIERIEGILNGTSNFILTSMrEENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELVFGKapaqEYSVReg 226
Cdd:PRK06392  160 PSRIKNFRGIVSSTINYVIRQE-ANGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGK----DYTLR-- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 227 itDITIEQIRLADSlglkfkhaASIQKEKDFvrcTVKPVLTGESHPLYRVEGVQN------------AVSIDADIVGNIS 294
Cdd:PRK06392  233 --DVTYDGIENIDR--------SSMDNERLV---TEVAMINGGPHAESRIRSLSRndflgmigplslGYQMETDINGTIN 299

                         330       340
                  ....*....|....*....|....
gi 1006542799 295 LQGPGAGMFPTASAIIEDLIHVGK 318
Cdd:PRK06392  300 VSDNYDGPYETAGAVVNDVMLLSK 323
PLN02700 PLN02700
homoserine dehydrogenase family protein
 89-314 7.19e-17

homoserine dehydrogenase family protein


Pssm-ID: 215377 [Multi-domain]  Cd Length: 377  Bit Score: 81.36  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  89 LRQAISRGCHVITANKEMFAYHGSELAKLAKEkNVSLGFEATVGGGIPIIQTIRQLLNA-NRIERIEGILNGTSNFILTS 167
Cdd:PLN02700  126 LNEAVDLGCCIVLANKKPLTSTLEDYDKLAAH-PRRIRHESTVGAGLPVIASLNRILSSgDPVHRIVGSLSGTLGYVMSE 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 168 MrEENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSELV------------------FG-KAPAQEYSVREGIT 228
Cdd:PLN02700  205 L-EDGKPFSEVVKQAKSLGYTEPDPRDDLGGMDVARKALILARLLgkrinmdsikveslypeeMGpDLMSTDDFLHSGLV 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 229 --DITI-EQIRLADSLGLKFKHAASIQKEkdfvRCTVKPVLTGESHPLYRVEGVQNAVSIDADIVGNISL--QGPGAGMF 303
Cdd:PLN02700  284 elDLPIeERVKEASLKGCVLRYVCVIEGS----SCQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQPLviQGAGAGND 359

                         250
                  ....*....|.
gi 1006542799 304 PTASAIIEDLI 314
Cdd:PLN02700  360 TTAAGVLADIL 370
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 4-241 7.88e-13

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 70.34  E-value: 7.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   4 ITIGLLGFGTVGKGVYETIRKHQERLQTILGKEVKVSAILVknvNKHSLPDDQVL----LTDDFQD----------IIEL 69
Cdd:PRK09466  459 IGLVLFGKGNIGSRWLELFAREQSTLSARTGFEFVLVGVVD---SRRSLLNYDGLdasrALAFFDDeavewdeeslFLWL 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  70 PKLD----VVIDAIVGREPGYTYLRQAiSRGCHVITANKemfaYHGSelAKLAKEKNVSLGFE---------ATVGGGIP 136
Cdd:PRK09466  536 RAHPydelVVLDVTASEQLALQYPDFA-SHGFHVISANK----LAGS--SPSNFYRQIKDAFAktgrhwlynATVGAGLP 608

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799 137 IIQTIRQLLNA-NRIERIEGILNGTSNFiLTSMREENLSFEEALKIAQDKGYAEADPKNDIEGYDAFYKAVVLSelvfgk 215
Cdd:PRK09466  609 INHTVRDLRNSgDSILAISGIFSGTLSW-LFLQFDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILA------ 681

                         250       260
                  ....*....|....*....|....*.
gi 1006542799 216 apaqeysvREGITDITIEQIRLAdSL 241
Cdd:PRK09466  682 --------REAGYEIEPDDVRVE-SL 698
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 10-128 2.21e-11

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 60.40  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  10 GFGTVGKGVYETIRKHQERlqtilgKEVKVSAILVKNVNKHSLPDD--QVLLTDDFQDIIELPKLDVVIDAivgrePGYT 87
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQSE------IPLELVAVADRDLLSKDPLALlpDEPLTLDLDDLIAHPDPDVVVEC-----ASSE 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1006542799  88 YLR----QAISRGCHVITANKEMFAY--HGSELAKLAKEKNVSLGFE 128
Cdd:pfam03447  70 AVAelvlDALKAGKDVVTASKGALADlaLYEELREAAEANGARIYVE 116
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-147 8.22e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 48.31  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  10 GFGTVGKGVYETIRKHqerlqtilgKEVKVSAILVKNVNK--------HSLPDDQVLLTDDFQDIIELPKLDVVIDAIVG 81
Cdd:cd24146     7 GLGAMGRGIARYLLEK---------PGLEIVGAVDRDPAKvgkdlgelGGGAPLGVKVTDDLDAVLAATKPDVVVHATTS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799  82 R-EPGYTYLRQAISRGCHVITANKEMFAYHGS--ELAK----LAKEKNVSL-----GFEATVGggiPIIQTIRQLLNA 147
Cdd:cd24146    78 FlADVAPQIERLLEAGLNVITTCEELFYPWARdpELAEeldaLAKENGVTVlgtgpGDVATAA---IVVNRIPDVIAA 152
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-156 4.45e-06

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 48.00  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   1 MSAITIGLLGFGTVGKGVYETIRKHqerlqtilgKEVKVSAI--LVKNVNKHSLPDDQVLLTDDFQDIIELPKLDVVIDA 78
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAAL---------PGVELVAVadRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799  79 IvgrePGYT---YLRQAISRGCHV-----ITANKEmfayHGSELAKLAKEKNVSLgFEATVGGGIPIIQTIRQLLNANRI 150
Cdd:COG0673    72 T----PNHLhaeLAIAALEAGKHVlcekpLALTLE----EARELVAAAEEAGVVL-MVGFNRRFDPAVRAARELIDSGAI 142


                  ....*.
gi 1006542799 151 ERIEGI 156
Cdd:COG0673   143 GEIRSV 148
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 56-123 2.49e-05

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 46.30  E-value: 2.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006542799  56 QVLLTDDFQDIIELPKLDVVIDAIVGREPGYTYLRQAISRGCHVITANKEMFAYHGSELAKLAKEKNV 123
Cdd:COG4091    84 KTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGV 151
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 6-120 2.37e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 40.65  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006542799   6 IGLLGFGTVGKGVYETIRKHQERLQ-TILGKEVKVSAILVKNVNKHSLpDDQVLLTDDFQDIIE--LPKLDVVIDAIVGR 82
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDVDRiTVADRTLEKAQALAAKLGGVRF-IAVAVDADNYEAVLAalLKEGDLVVNLSPPT 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1006542799  83 EpGYTYLRQAISRGCHVITAnkemfAYHGSELAKLAKE 120
Cdd:pfam03435  80 L-SLDVLKACIETGVHYVDT-----SYLREAVLALHEK 111
 
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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