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Conserved domains on  [gi|612662022|gb|EZS78260|]
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hypothetical protein W490_01543 [Staphylococcus aureus VET0191R]

Protein Classification

homoserine dehydrogenase( domain architecture ID 11482218)

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

EC:  1.1.1.3
Gene Ontology:  GO:0006520|GO:0004412
PubMed:  25945586|3098560|8500624

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-330 0e+00

homoserine dehydrogenase; Provisional


:

Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 553.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   1 MKKLNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHLTEDVNEILNDDSLDIIVEVM 80
Cdd:PRK06349   1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  81 GGIEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNANNISKFMGILNG 160
Cdd:PRK06349  81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 161 TSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKRRGISGVTLTDINVAD 240
Cdd:PRK06349 161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 241 QLGYKIKLIGKGIYENGKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGAGSLATGSAVVSDLLNVALF 320
Cdd:PRK06349 241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                        330
                 ....*....|
gi 612662022 321 FESDLHTLPP 330
Cdd:PRK06349 321 LVRVPHLGFQ 330
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-330 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 553.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   1 MKKLNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHLTEDVNEILNDDSLDIIVEVM 80
Cdd:PRK06349   1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  81 GGIEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNANNISKFMGILNG 160
Cdd:PRK06349  81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 161 TSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKRRGISGVTLTDINVAD 240
Cdd:PRK06349 161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 241 QLGYKIKLIGKGIYENGKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGAGSLATGSAVVSDLLNVALF 320
Cdd:PRK06349 241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                        330
                 ....*....|
gi 612662022 321 FESDLHTLPP 330
Cdd:PRK06349 321 LVRVPHLGFQ 330
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-318 1.85e-146

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: 418.29  E-value: 1.85e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  23 EENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHLTEDVNEILNDDSLDIIVEVMGGIEPTVDWLRTALKNKKHVIT 102
Cdd:COG0460    1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 103 ANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDE 182
Cdd:COG0460   81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 183 AKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKRRGISGVTLTDINVADQLGYKIKLIGKGIYENGKVNAS 262
Cdd:COG0460  161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612662022 263 VEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGAGSLATGSAVVSDLLNVA 318
Cdd:COG0460  241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIA 296
Homoserine_dh pfam00742
Homoserine dehydrogenase;
137-314 3.01e-85

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 258.07  E-value: 3.01e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  137 PIVNAINNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQ 216
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  217 VIKLNDVKRRGISGVTLTDINVADQLGYKIKLIGKGIYENGKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMF 296
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 612662022  297 YGKGAGSLATGSAVVSDL 314
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) ...
 4-142 4.71e-05

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: 43.30  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   4 LNIALLGLGTVGSGVVKIIEEnrqqiqdtlNKDIVIKHILVRDKSK----------KRPLNISqyhLTEDVNEILNDDSL 73
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYLLE---------KPGLEIVGAVDRDPAKvgkdlgelggGAPLGVK---VTDDLDAVLAATKP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  74 DIIV----EVMGGIEPTvdwLRTALKNKKHVITANKDLL---AVHLKL---LEDLAEENGVAL-----KFEASVAggiPI 138
Cdd:cd24146   69 DVVVhattSFLADVAPQ---IERLLEAGLNVITTCEELFypwARDPELaeeLDALAKENGVTVlgtgpGDVATAA---IV 142


                 ....
gi 612662022 139 VNAI 142
Cdd:cd24146  143 VNRI 146
 
Name Accession Description Interval E-value
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-330 0e+00

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 553.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   1 MKKLNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHLTEDVNEILNDDSLDIIVEVM 80
Cdd:PRK06349   1 MKPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAVRDLEKDRGVDLPGILLTTDPEELVNDPDIDIVVELM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  81 GGIEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNANNISKFMGILNG 160
Cdd:PRK06349  81 GGIEPARELILKALEAGKHVVTANKALLAVHGAELFAAAEEKGVDLYFEAAVAGGIPIIKALREGLAANRITRVMGIVNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 161 TSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKRRGISGVTLTDINVAD 240
Cdd:PRK06349 161 TTNYILTKMTEEGLSFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAFGTRVDFDDVYVEGISKITAEDIAYAK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 241 QLGYKIKLIGKGIYENGKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGAGSLATGSAVVSDLLNVALF 320
Cdd:PRK06349 241 ELGYRIKLLGIAERTEEGIELRVHPTLIPKSHPLANVNGVMNAVFVEGDAVGETMFYGPGAGGLPTASAVVADLVDIARN 320

                        330
                 ....*....|
gi 612662022 321 FESDLHTLPP 330
Cdd:PRK06349 321 LVRVPHLGFQ 330
ThrA COG0460
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ...
 23-318 1.85e-146

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: 418.29  E-value: 1.85e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  23 EENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHLTEDVNEILNDDSLDIIVEVMGGIEPTVDWLRTALKNKKHVIT 102
Cdd:COG0460    1 LENAEELARRLGLDLRVVGVAVRDGMKPRGIDLPRWLLTTDLEELIKDPEIDVVVELTGGSEPARELYLAALEAGKHVVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 103 ANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDE 182
Cdd:COG0460   81 ANKALLAEHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELLAGDRITRIEGILNGTTNYILTKMEEEGLSFSEALKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 183 AKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKRRGISGVTLTDINVADQLGYKIKLIGKGIYENGKVNAS 262
Cdd:COG0460  161 AQELGYAEADPTADVEGIDAARKLAILARLAFGTPVELEDVYVEGITRITAEDIAAAKELGYVIKLLAIAERTGGGVEAR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612662022 263 VEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGAGSLATGSAVVSDLLNVA 318
Cdd:COG0460  241 VHPTLVPADHPLASVNGVDNAVLVETDAYGELMFYGPGAGAEPTASAVLADLLDIA 296
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 2-318 5.78e-89

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 273.28  E-value: 5.78e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   2 KKLNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVIKHI-----------------LVRDKSKKRPL-NISQYHLTED 63
Cdd:PRK06270   1 MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIadssgsaidpdgldlelALKVKEETGKLaDYPEGGGEIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  64 VNEILNDDSLDIIVEVM-----GGiEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPI 138
Cdd:PRK06270  81 GLEVIRSVDADVVVEATptnieTG-EPALSHCRKALERGKHVVTSNKGPLALAYKELKELAKKNGVRFRYEATVGGAMPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 139 VNAINNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVI 218
Cdd:PRK06270 160 INLAKETLAGNDIKSIKGILNGTTNYILTRMEEEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILANSILGADL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 219 KLNDVKRRGISGVTLTDINVADQLGYKIKLIGKGIYENgkvNASVEPTLIDKKHQLaAVEDEYNAIYVIGDAVGDTMFYG 298
Cdd:PRK06270 240 TIKDVEVEGITKITPEAIELAAKEGYRIKLIGEVSREK---DLSVSPRLVPLDHPL-AVSGTLNAATFETDLAGDVTVVG 315

                        330       340
                 ....*....|....*....|
gi 612662022 299 KGAGSLATGSAVVSDLLNVA 318
Cdd:PRK06270 316 RGAGSIETASAILSDLIAIH 335
Homoserine_dh pfam00742
Homoserine dehydrogenase;
137-314 3.01e-85

Homoserine dehydrogenase;


Pssm-ID: 459921 [Multi-domain]  Cd Length: 178  Bit Score: 258.07  E-value: 3.01e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  137 PIVNAINNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQ 216
Cdd:pfam00742   1 PIIRTLRLSLAGDRITRIEGILNGTTNYILTRMEEEGLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  217 VIKLNDVKRRGISGVTLTDINVADQLGYKIKLIGKGIYENGKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMF 296
Cdd:pfam00742  81 DVELEDVEVEGITRLTAEDIAYAKELGKVIKLVASAKRDDGGVEARVGPTLVPKDHPLASVKGVDNAVVIETDRYGELVF 160

                         170
                  ....*....|....*...
gi 612662022  297 YGKGAGSLATGSAVVSDL 314
Cdd:pfam00742 161 YGPGAGALPTASAVLADL 178
PRK08374 PRK08374
homoserine dehydrogenase; Provisional
 2-321 9.32e-46

homoserine dehydrogenase; Provisional


Pssm-ID: 169409 [Multi-domain]  Cd Length: 336  Bit Score: 161.13  E-value: 9.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   2 KKLNIALLGLGTVGSGVVKIIEENRQ-------------QIQDT-----LNKDI-VIKHILVRDKSKKRPLNISQYHLTE 62
Cdd:PRK08374   1 MEVKVSIFGFGNVGRAVAEVLAEKSRvfkerygvelkvvSITDTsgtiwLPEDIdLREAKEVKENFGKLSNWGNDYEVYN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  63 -DVNEILNDDSLDIIVEVMGGIEPTvDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNA 141
Cdd:PRK08374  81 fSPEEIVEEIDADIVVDVTNDKNAH-EWHLEALKEGKSVVTSNKPPIAFHYDELLDLANERNLPYLFEATVMAGTPIIGL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 142 INNGLNANNISKFMGILNGTSNFILSKMtKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFnQVIKLN 221
Cdd:PRK08374 160 LRENLLGDTVKRIEAVVNATTTFILTRM-EQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAF-PPITFE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 222 DVKRRGISGVTLTDINVADQLGYKIKLIGKgiYENGKVnaSVEPTLIDKKHQLaAVEDEYNAIYVIGDAVGDTMFYGKGA 301
Cdd:PRK08374 238 EVGIRGIKDVTEGEIERAKAKGRNVRLVAT--VEEGRI--SVKPKKLPENSPL-AVEGVENAAVIKTDLLGELVLKGPGA 312

                        330       340
                 ....*....|....*....|
gi 612662022 302 GSLATGSAVVSDLLNVALFF 321
Cdd:PRK08374 313 GGKETASGVVTDIIKAALKF 332
PRK06813 PRK06813
homoserine dehydrogenase; Validated
 3-317 9.26e-42

homoserine dehydrogenase; Validated


Pssm-ID: 168683 [Multi-domain]  Cd Length: 346  Bit Score: 150.79  E-value: 9.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   3 KLNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVIKHILVRDKSKKRPLNISQYHL---------TEDVNEILNDD-- 71
Cdd:PRK06813   2 KIKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEDGLSIHHLlrygggscaIEKYIEHHPEEra 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  72 ----SLDIIVE-----VMGGiEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAI 142
Cdd:PRK06813  82 tdniSGTVLVEstvtnLKDG-NPGKQYIKQAIEKKMDIVAISKGALVTNWREINEAAKIANVRIRYSGATAAALPTLDIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 143 NNGLNANNISKFMGILNGTSNFILSKMTKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLND 222
Cdd:PRK06813 161 QFSLAGCHIEKIEGILNGTTNYILTKMNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLTNSLMGTENKLTD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 223 VKRRGISGVTLTDINVADQLGYKIKLIGKGIYEN-GKVNASVEPTLIDKKHQLAAVEDEYNAIYVIGDAVGDTMFYGKGA 301
Cdd:PRK06813 241 IHIKGIEHVTKQQIRNAKEQNKIIKLIASAYKDNeGNVNLNVEPYKIEKNHPLANVNGTEKGITFFTDTMGQVTTIGGAS 320

                        330
                 ....*....|....*.
gi 612662022 302 GSLATGSAVVSDLLNV 317
Cdd:PRK06813 321 NPRGAAAAALKDIINL 336
PRK06392 PRK06392
homoserine dehydrogenase; Provisional
 4-228 4.76e-24

homoserine dehydrogenase; Provisional


Pssm-ID: 102354 [Multi-domain]  Cd Length: 326  Bit Score: 101.87  E-value: 4.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   4 LNIALLGLGTVGSGVVKIIEENRQQIQDTLNKDIVI----KHIL-----------VRDKSKKRPLNISQYHLTEDvnEIL 68
Cdd:PRK06392   1 IRISIIGLGNVGLNVLRIIKSRNDDRRNNNGISVVSvsdsKLSYynergldigkiISYKEKGRLEEIDYEKIKFD--EIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  69 NDDSlDIIVEVMGGIEPTV---DWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNG 145
Cdd:PRK06392  79 EIKP-DVIVDVTPASKDGIrekNLYINAFEHGIDVVTANKSGLANHWHDIMDSASKNRRIIRYEATVAGGVPLFSLRDYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 146 LNANNISKFMGILNGTSNFILSKMTKEQtTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLSFNQVIKLNDVKR 225
Cdd:PRK06392 158 TLPSRIKNFRGIVSSTINYVIRQEANGR-GFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILANHLFGKDYTLRDVTY 236


                 ...
gi 612662022 226 RGI 228
Cdd:PRK06392 237 DGI 239
thrA PRK09436
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
 2-318 5.81e-19

bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional


Pssm-ID: 181856 [Multi-domain]  Cd Length: 819  Bit Score: 89.45  E-value: 5.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   2 KKLNIALLGLGTVGSgvvKIIEENRQQIQDTLNKDIVI---------KHILVRD-----------KSKKRPLNISQYHLT 61
Cdd:PRK09436 464 QVLDVFVIGVGGVGG---ALLEQIKRQQPWLKKKNIDLrvcgiansrKMLLDEHgidldnwreelAEAGEPFDLDRLIRL 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  62 EDVNEILNDdsldIIVEVMGGiEPTVDWLRTALKNKKHVITANK----DLLAVHLKLLEdLAEENGVALKFEASVAGGIP 137
Cdd:PRK09436 541 VKEYHLLNP----VIVDCTSS-QAVADQYADFLAAGFHVVTPNKkantSSYAYYHQLRE-AARKSRRKFLYETNVGAGLP 614

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 138 IVNAINNGLNA-NNISKFMGILNGTSNFILSKMtKEQTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVI----TSYl 212
Cdd:PRK09436 615 VIETLQNLLNAgDELLKFEGILSGSLSFIFGKL-DEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLIlareAGY- 692

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 213 sfnqVIKLNDVKRRGI------SGVTLTD---------------INVADQLGYKIKLIGKgiYENGKVNASVEPtlIDKK 271
Cdd:PRK09436 693 ----ELELEDIEVESVlpeefdASGSVDEfmarlpeldaefaarVAKARAEGKVLRYVGQ--IEDGKCRVGIAE--VDAN 764

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612662022 272 HQLAAVEDEYNAIyvigdavgdtMFY------------GKGAGSLATGSAVVSDLLNVA 318
Cdd:PRK09436 765 HPLYKVKGGENAL----------AFYtryyqpiplvlrGYGAGNEVTAAGVFADLLRTL 813
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 10-129 4.16e-16

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: 73.88  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   10 GLGTVGSGVVKIIEENRQQIqdtlnkDIVIKHILVRDKSKKRPLN-ISQYHLTEDVNEILNDDSLDIIVEVmGGIEPTVD 88
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQSEI------PLELVAVADRDLLSKDPLAlLPDEPLTLDLDDLIAHPDPDVVVEC-ASSEAVAE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 612662022   89 WLRTALKNKKHVITANKDLLA--VHLKLLEDLAEENGVALKFE 129
Cdd:pfam03447  74 LVLDALKAGKDVVTASKGALAdlALYEELREAAEANGARIYVE 116
PLN02700 PLN02700
homoserine dehydrogenase family protein
 100-224 1.65e-13

homoserine dehydrogenase family protein


Pssm-ID: 215377 [Multi-domain]  Cd Length: 377  Bit Score: 71.34  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 100 VITANKDLLAVHLKLLEDLAEENGvALKFEASVAGGIPIVNAINNGLNANN-ISKFMGILNGTSNFILSKMtKEQTTFEE 178
Cdd:PLN02700 136 IVLANKKPLTSTLEDYDKLAAHPR-RIRHESTVGAGLPVIASLNRILSSGDpVHRIVGSLSGTLGYVMSEL-EDGKPFSE 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 612662022 179 ALDEAKRLGFAEADPTDDVEGVDAARKVVITSYLsFNQVIKLNDVK 224
Cdd:PLN02700 214 VVKQAKSLGYTEPDPRDDLGGMDVARKALILARL-LGKRINMDSIK 258
metL PRK09466
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
 99-314 2.12e-10

bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional


Pssm-ID: 236530 [Multi-domain]  Cd Length: 810  Bit Score: 62.63  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  99 HVITANKdlLA-----VHLKLLEDLAEENGVALKFEASVAGGIPIVNAINNGLNA-NNISKFMGILNGTSNFILSKMTKE 172
Cdd:PRK09466 567 HVISANK--LAgsspsNFYRQIKDAFAKTGRHWLYNATVGAGLPINHTVRDLRNSgDSILAISGIFSGTLSWLFLQFDGS 644

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 173 qTTFEEALDEAKRLGFAEADPTDDVEGVDAARKVVITSY-LSFNqvIKLNDVKRRGISGVTLTDINVaDQLGYKIKLIGK 251
Cdd:PRK09466 645 -VPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAReAGYE--IEPDDVRVESLVPAHLEDGSL-DQFFENGDELDE 720

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022 252 GIYE--------------------NGKVNASVEptLIDKKHQLAAVEDEYNaIYVIgdavgDTMFY--------GKGAGS 303
Cdd:PRK09466 721 QMLQrleaaaeqgkvlryvarfdaNGKARVGVE--AVRPDHPLANLLPCDN-VFAI-----ESRWYrdnplvirGPGAGR 792

                        250
                 ....*....|.
gi 612662022 304 LATGSAVVSDL 314
Cdd:PRK09466 793 EVTAGAIQSDL 803
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 57-124 4.25e-05

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 45.52  E-value: 4.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612662022  57 QYHLTEDVNEILNDDSLDIIVEVMGGIEPTVDWLRTALKNKKHVITANKDLLAVHLKLLEDLAEENGV 124
Cdd:COG4091   84 KTVVTDDAELLIAADGIDVVVEATGVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGV 151
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 4-142 4.71e-05

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: 43.30  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   4 LNIALLGLGTVGSGVVKIIEEnrqqiqdtlNKDIVIKHILVRDKSK----------KRPLNISqyhLTEDVNEILNDDSL 73
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYLLE---------KPGLEIVGAVDRDPAKvgkdlgelggGAPLGVK---VTDDLDAVLAATKP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  74 DIIV----EVMGGIEPTvdwLRTALKNKKHVITANKDLL---AVHLKL---LEDLAEENGVAL-----KFEASVAggiPI 138
Cdd:cd24146   69 DVVVhattSFLADVAPQ---IERLLEAGLNVITTCEELFypwARDPELaeeLDALAKENGVTVlgtgpGDVATAA---IV 142


                 ....
gi 612662022 139 VNAI 142
Cdd:cd24146  143 VNRI 146
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-126 3.66e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.14  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022   1 MKKLNIALLGLGTVGSGVVKIIEEnrqqiqdtlNKDIVIKHILVRDKSK----KRPLNISQYhltEDVNEILNDDSLDII 76
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAA---------LPGVELVAVADRDPERaeafAEEYGVRVY---TDYEELLADPDIDAV 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612662022  77 VevmggIePT-----VDWLRTALKNKKHV-----ITANkdllAVHLKLLEDLAEENGVAL 126
Cdd:COG0673   69 V-----I-ATpnhlhAELAIAALEAGKHVlcekpLALT----LEEARELVAAAEEAGVVL 118
 
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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