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Conserved domains on  [gi|527037667|ref|WP_020884320|]
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MULTISPECIES: oxidoreductase [Enterobacter]

Protein Classification

oxidoreductase( domain architecture ID 11485416)

oxidoreductase similar to Escherichia coli putative oxidoreductase YdgJ

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-346 0e+00

putative oxidoreductase; Provisional


:

Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 767.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   1 MSDSIRVGLIGYGYASKTFHAPLIAGTPGMALAAVSSSDATKVHADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  81 AKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 161 NRWREQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLRPGAQTTDYFHAVLSYPQRRIVLHGTMVAAAESARYIL 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 241 HGTRGSFVKFGLDPQEERLKNGERLPQEDWGYDMRDGVVTRVEGEERVEETLLTIPGNYPAYYAAIRDALNGTGDNPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*.
gi 527037667 321 SQAIQIMELIELGIESAKHRATLCLA 346
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCLA 346
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-346 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 767.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   1 MSDSIRVGLIGYGYASKTFHAPLIAGTPGMALAAVSSSDATKVHADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  81 AKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 161 NRWREQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLRPGAQTTDYFHAVLSYPQRRIVLHGTMVAAAESARYIL 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 241 HGTRGSFVKFGLDPQEERLKNGERLPQEDWGYDMRDGVVTRVEGEERVEETLLTIPGNYPAYYAAIRDALNGTGDNPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*.
gi 527037667 321 SQAIQIMELIELGIESAKHRATLCLA 346
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCLA 346
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-248 1.88e-68

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 216.33  E-value: 1.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   2 SDSIRVGLIGYGYASKtFHAPLIAGTPGMALAAVSSSDATKVH--ADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFP 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEafAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  80 LAKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQV 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 160 RNRWREQ-AGPGSGIWYDLAPHLLDQAVNLFGL-PVSMTVDLAQLRPGAQTT-DYFHAVLSYP-QRRIVLHGTMVAAAE- 234
Cdd:COG0673  160 PADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRLVPDRVEVdDTAAATLRFAnGAVATLEASWVAPGGe 239

                        250
                 ....*....|....*
gi 527037667 235 -SARYILHGTRGSFV 248
Cdd:COG0673  240 rDERLEVYGTKGTLF 254
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.66e-44

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 151.42  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  134 KALLNEGTLGEILFFESH-FDRFRPQVR-NRWREQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLrpgaqttDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEfKRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYASE-------DT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  212 FHAVLSYPQRRIV---LHGTMVAAAESARYILHGTRGSFVKFGLDPqeeRLKNGERLPQEDWGYDMRDGVVTRVEGEErv 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGIDD---GLLSVTVVGEPGWATDDPMVRKGGDEVPE-- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 527037667  289 eeTLLTIPGNYPAYYAAIRDALNGTGDNPVPASQAIQIMELIELGIESAKHRATLCL 345
Cdd:pfam02894 149 --FLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 5-145 1.37e-21

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 93.82  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667    5 IRVGLIGYGYASKtFHAPLIAG-TPGMALAAVSSSDATKVHA---DWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAElaeKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527037667   81 AKAALEAGKHVIVDKPFTVTLSQARE-LDALAKSfGRVLSVFHNRRWDSDFLTVKALLNEGTLGEI 145
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEaLAAVEKA-GVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP 145
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-118 2.05e-04

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: 41.37  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   5 IRVGLIGYGYASKTFhAPLIAGTPGMALAAVSSSDATKVHADW--------PSVPVVSEPKHLFNDPNIDLIVIPTPNDT 76
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVGKDLgelgggapLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 527037667  77 H--FPLAKAALEAGKHVI-----VDKPFTVTLSQARELDALAKSFGRVL 118
Cdd:cd24146   80 AdvAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKENGVTV 128
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-346 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 767.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   1 MSDSIRVGLIGYGYASKTFHAPLIAGTPGMALAAVSSSDATKVHADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  81 AKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 161 NRWREQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLRPGAQTTDYFHAVLSYPQRRIVLHGTMVAAAESARYIL 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 241 HGTRGSFVKFGLDPQEERLKNGERLPQEDWGYDMRDGVVTRVEGEERVEETLLTIPGNYPAYYAAIRDALNGTGDNPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*.
gi 527037667 321 SQAIQIMELIELGIESAKHRATLCLA 346
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCLA 346
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-248 1.88e-68

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 216.33  E-value: 1.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   2 SDSIRVGLIGYGYASKtFHAPLIAGTPGMALAAVSSSDATKVH--ADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFP 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEafAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  80 LAKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQV 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 160 RNRWREQ-AGPGSGIWYDLAPHLLDQAVNLFGL-PVSMTVDLAQLRPGAQTT-DYFHAVLSYP-QRRIVLHGTMVAAAE- 234
Cdd:COG0673  160 PADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRLVPDRVEVdDTAAATLRFAnGAVATLEASWVAPGGe 239

                        250
                 ....*....|....*
gi 527037667 235 -SARYILHGTRGSFV 248
Cdd:COG0673  240 rDERLEVYGTKGTLF 254
PRK10206 PRK10206
putative oxidoreductase; Provisional
 4-346 2.24e-64

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 207.37  E-value: 2.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   4 SIRVGLIGYGYASKTFHAPLI---AGTPGMALAAVSSSDATKVHADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:PRK10206   1 VINCAFIGFGKSTTRYHLPYVlnrKDSWHVAHIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  81 AKAALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFHNRRWDSDFLTVKALLNEGTLGEILFFESHFDRFRPQVR 160
Cdd:PRK10206  81 AKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRPVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 161 NRwreQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLRPGAQTTDYFHAVLSYPQRRIVLHGTMVAAAESARYIL 240
Cdd:PRK10206 161 TK---PGLPQDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFEAQLFYGDLKAIVKTSHLVKIDYPKFIV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667 241 HGTRGSFVKFGLDPQEERLKNGERLPQEDWGYDMRDGVVTRVEGE-ERVEETLLTIPGNYPAYYAAIRDALNGTGDNPVP 319
Cdd:PRK10206 238 HGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYVNDEgVTVREEMKPEMGDYGRVYDALYQTLTHGAPNYVK 317

                        330       340
                 ....*....|....*....|....*..
gi 527037667 320 ASQAIQIMELIELGIESAKhRATLCLA 346
Cdd:PRK10206 318 ESEVLTNLEILERGFEQAS-PATVTLA 343
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.66e-44

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 151.42  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  134 KALLNEGTLGEILFFESH-FDRFRPQVR-NRWREQAGPGSGIWYDLAPHLLDQAVNLFGLPVSMTVDLAQLrpgaqttDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEfKRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYASE-------DT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667  212 FHAVLSYPQRRIV---LHGTMVAAAESARYILHGTRGSFVKFGLDPqeeRLKNGERLPQEDWGYDMRDGVVTRVEGEErv 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGIDD---GLLSVTVVGEPGWATDDPMVRKGGDEVPE-- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 527037667  289 eeTLLTIPGNYPAYYAAIRDALNGTGDNPVPASQAIQIMELIELGIESAKHRATLCL 345
Cdd:pfam02894 149 --FLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 5-122 5.99e-36

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 126.55  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667    5 IRVGLIGYGYASKTFHAPLIAGTPGMALAAVSSSDATKVH--ADWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPLAK 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEavAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 527037667   83 AALEAGKHVIVDKPFTVTLSQARELDALAKSFGRVLSVFH 122
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 5-145 1.37e-21

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 93.82  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667    5 IRVGLIGYGYASKtFHAPLIAG-TPGMALAAVSSSDATKVHA---DWPSVPVVSEPKHLFNDPNIDLIVIPTPNDTHFPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAElaeKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527037667   81 AKAALEAGKHVIVDKPFTVTLSQARE-LDALAKSfGRVLSVFHNRRWDSDFLTVKALLNEGTLGEI 145
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEaLAAVEKA-GVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP 145
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-118 2.05e-04

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: 41.37  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   5 IRVGLIGYGYASKTFhAPLIAGTPGMALAAVSSSDATKVHADW--------PSVPVVSEPKHLFNDPNIDLIVIPTPNDT 76
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVGKDLgelgggapLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 527037667  77 H--FPLAKAALEAGKHVI-----VDKPFTVTLSQARELDALAKSFGRVL 118
Cdd:cd24146   80 AdvAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKENGVTV 128
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 3-92 1.72e-03

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 40.06  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   3 DSIRVGLIGYG-YASKTF-----HAPLIAGTPG--MALAAVSSSDATKVHADW-PSVPVVSEPKHLFNDPNIDLIV---- 69
Cdd:PRK06349   2 KPLKVGLLGLGtVGSGVVrileeNAEEIAARAGrpIEIKKVAVRDLEKDRGVDlPGILLTTDPEELVNDPDIDIVVelmg 81

                         90       100
                 ....*....|....*....|....
gi 527037667  70 -IPTPNDthfpLAKAALEAGKHVI 92
Cdd:PRK06349  82 gIEPARE----LILKALEAGKHVV 101
PRK13302 PRK13302
aspartate dehydrogenase;
2-93 1.86e-03

aspartate dehydrogenase;


Pssm-ID: 237341 [Multi-domain]  Cd Length: 271  Bit Score: 39.45  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   2 SDSIRVGLIGYGYASKTFHAPLIAGTPGMALAAVSSSDATKvHADW--------PSVPVVSEPKHlfndpnIDLIVIPTP 73
Cdd:PRK13302   4 RPELRVAIAGLGAIGKAIAQALDRGLPGLTLSAVAVRDPQR-HADFiwglrrppPVVPLDQLATH------ADIVVEAAP 76

                         90       100
                 ....*....|....*....|
gi 527037667  74 NDTHFPLAKAALEAGKHVIV 93
Cdd:PRK13302  77 ASVLRAIVEPVLAAGKKAIV 96
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 5-92 4.18e-03

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 38.59  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667   5 IRVGLIGYGYASKTFHAPlIAGTPGMALAAVSSSDATKVH-----ADWP--------------------SVPVVSEPKHL 59
Cdd:COG4091   16 IRVGLIGAGQMGRGLLAQ-IRRMPGMEVVAIADRNPERARaalreAGIPeedirvvdtaaeadaaiaagKTVVTDDAELL 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 527037667  60 FNDPNIDLIVIPTPNdthfP-----LAKAALEAGKHVI 92
Cdd:COG4091   95 IAADGIDVVVEATGV----PeagarHALAAIEAGKHVV 128
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-92 9.92e-03

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: 35.58  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037667    6 RVGLIGY-GYASKTFhAPLIAGTPGMALAAVSSS---------DATKVHADWPSVPVvsEPKHLFNDPNIDLIVIPTPND 75
Cdd:pfam01118   1 KVAIVGAtGYVGQEL-LRLLEEHPPVELVVLFASsrsagkklaFVHPILEGGKDLVV--EDVDPEDFKDVDIVFFALPGG 77

                          90
                  ....*....|....*..
gi 527037667   76 THFPLAKAALEAGKHVI 92
Cdd:pfam01118  78 VSKEIAPKLAEAGAKVI 94
 
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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