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Conserved domains on  [gi|1349347909|gb|PPY13013|]
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oxidoreductase [Cronobacter sakazakii]

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: 764.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   1 MNDNVRVGLIGYGYASKTFHAPLIAGTPGMELAVISSSDAGKVHADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPL 80
Cdd:PRK11579    1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  81 AKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVAYFESHFDRFRPQVR 160
Cdd:PRK11579   81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 161 DRWREQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAELRPSAQATDYFHAVLAYPERRVVLHGTMLAAAESARYIV 240
Cdd:PRK11579  161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 241 HGTRGSYVKFGLDPQEESLKSGTRPPQENWGYDMRDGVLTVARGEMLDEQTLLTVPGNYPAYYAAVRSAIRGEGENPVPA 320
Cdd:PRK11579  241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                         330       340
                  ....*....|....*....|....*.
gi 1349347909 321 SQAIVVMELIEAGIESAKRRAAVCLR 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: 764.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   1 MNDNVRVGLIGYGYASKTFHAPLIAGTPGMELAVISSSDAGKVHADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPL 80
Cdd:PRK11579    1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  81 AKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVAYFESHFDRFRPQVR 160
Cdd:PRK11579   81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 161 DRWREQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAELRPSAQATDYFHAVLAYPERRVVLHGTMLAAAESARYIV 240
Cdd:PRK11579  161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 241 HGTRGSYVKFGLDPQEESLKSGTRPPQENWGYDMRDGVLTVARGEMLDEQTLLTVPGNYPAYYAAVRSAIRGEGENPVPA 320
Cdd:PRK11579  241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                         330       340
                  ....*....|....*....|....*.
gi 1349347909 321 SQAIVVMELIEAGIESAKRRAAVCLR 346
Cdd:PRK11579  321 SQAIQVMELIELGIESAKHRATLCLA 346
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-343 6.92e-70

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.18  E-value: 6.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   2 NDNVRVGLIGYGYASKtFHAPLIAGTPGMELAVISSSDAGKVH--ADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFP 79
Cdd:COG0673     1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEafAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  80 LAKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVAYFESHFDRFRPQV 159
Cdd:COG0673    80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 160 RDRWREQ-AGPGSGIWYDLAPHLLDQAVQLFGL-PVSINVDLAELRP-SAQATDYFHAVLAYPE-RRVVLHGTMLAAAE- 234
Cdd:COG0673   160 PADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRLVPdRVEVDDTAAATLRFANgAVATLEASWVAPGGe 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 235 -SARYIVHGTRGSyvkfgldpqeeslksgtrppqenwgydmrdgvltvargemldeqtlltvpgnypayyaAVRSAIRGE 313
Cdd:COG0673   240 rDERLEVYGTKGT----------------------------------------------------------LFVDAIRGG 261

                         330       340       350
                  ....*....|....*....|....*....|
gi 1349347909 314 GENPVPASQAIVVMELIEAGIESAKRRAAV 343
Cdd:COG0673   262 EPPPVSLEDGLRALELAEAAYESARTGRRV 291
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.32e-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: 151.80  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 134 KQIIAEGQIGEVAYFESH-FDRFRPQVRD-RWREQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAelrpsaqATDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEFkRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYA-------SEDT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 212 FHAVLAYPERRVV---LHGTMLAAAESARYIVHGTRGSYVKFGLDPqeeSLKSGTRPPQENWGYDMRDGVLTVARgemlD 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGIDD---GLLSVTVVGEPGWATDDPMVRKGGDE----V 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1349347909 289 EQTLLTVPGNYPAYYAAVRSAIRGEGENPVPASQAIVVMELIEAGIESAKRRAAVCL 345
Cdd:pfam02894 147 PEFLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 5-194 8.19e-23

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: 96.90  E-value: 8.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYGYASKtFHAPLIAG-TPGMELAVISSSDAGKVHA---DWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAElaeKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  81 AKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVayfesHFdrFRPQVR 160
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP-----EI--LRITSR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1349347909 161 DrwreqAGPGS--------GIWYDLAPHLLDQAVQLFGLPVS 194
Cdd:TIGR04380 154 D-----PAPPPvayvkvsgGLFLDMTIHDFDMARFLLGSEVE 190
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-118 5.04e-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: 42.91  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYGYASKTFhAPLIAGTPGMEL-AVISSS------DAGKVHADWP-GMPVVSDPKHLFNDPHLDLIVIPTPNDT 76
Cdd:cd24146     1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIvGAVDRDpakvgkDLGELGGGAPlGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1349347909  77 H--FPLAKAALEAGKHVV-----VDKPFTVTLSQARELETLAKSAGLVL 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: 764.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   1 MNDNVRVGLIGYGYASKTFHAPLIAGTPGMELAVISSSDAGKVHADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPL 80
Cdd:PRK11579    1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  81 AKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVAYFESHFDRFRPQVR 160
Cdd:PRK11579   81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 161 DRWREQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAELRPSAQATDYFHAVLAYPERRVVLHGTMLAAAESARYIV 240
Cdd:PRK11579  161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 241 HGTRGSYVKFGLDPQEESLKSGTRPPQENWGYDMRDGVLTVARGEMLDEQTLLTVPGNYPAYYAAVRSAIRGEGENPVPA 320
Cdd:PRK11579  241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                         330       340
                  ....*....|....*....|....*.
gi 1349347909 321 SQAIVVMELIEAGIESAKRRAAVCLR 346
Cdd:PRK11579  321 SQAIQVMELIELGIESAKHRATLCLA 346
PRK10206 PRK10206
putative oxidoreductase; Provisional
 54-337 1.76e-73

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 230.87  E-value: 1.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  54 SDPKHLFNDPHLDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTL 133
Cdd:PRK10206   54 SDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 134 KQIIAEGQIGEVAYFESHFDRFRPQVRDRwreQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAELRPSAQATDYFH 213
Cdd:PRK10206  134 KKAIESGKLGEIVEVESHFDYYRPVAETK---PGLPQDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFE 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 214 AVLAYPERRVVLHGTMLAAAESARYIVHGTRGSYVKFGLDPQEESLKSGTRPPQENWGYDMRDGVLTV--ARGEMLDEqT 291
Cdd:PRK10206  211 AQLFYGDLKAIVKTSHLVKIDYPKFIVHGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYvnDEGVTVRE-E 289

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1349347909 292 LLTVPGNYPAYYAAVRSAIRGEGENPVPASQAIVVMELIEAGIESA 337
Cdd:PRK10206  290 MKPEMGDYGRVYDALYQTLTHGAPNYVKESEVLTNLEILERGFEQA 335
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-343 6.92e-70

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.18  E-value: 6.92e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   2 NDNVRVGLIGYGYASKtFHAPLIAGTPGMELAVISSSDAGKVH--ADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFP 79
Cdd:COG0673     1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEafAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  80 LAKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVAYFESHFDRFRPQV 159
Cdd:COG0673    80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 160 RDRWREQ-AGPGSGIWYDLAPHLLDQAVQLFGL-PVSINVDLAELRP-SAQATDYFHAVLAYPE-RRVVLHGTMLAAAE- 234
Cdd:COG0673   160 PADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRLVPdRVEVDDTAAATLRFANgAVATLEASWVAPGGe 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 235 -SARYIVHGTRGSyvkfgldpqeeslksgtrppqenwgydmrdgvltvargemldeqtlltvpgnypayyaAVRSAIRGE 313
Cdd:COG0673   240 rDERLEVYGTKGT----------------------------------------------------------LFVDAIRGG 261

                         330       340       350
                  ....*....|....*....|....*....|
gi 1349347909 314 GENPVPASQAIVVMELIEAGIESAKRRAAV 343
Cdd:COG0673   262 EPPPVSLEDGLRALELAEAAYESARTGRRV 291
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.32e-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: 151.80  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 134 KQIIAEGQIGEVAYFESH-FDRFRPQVRD-RWREQAGPGSGIWYDLAPHLLDQAVQLFGLPVSINVDLAelrpsaqATDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEFkRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYA-------SEDT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909 212 FHAVLAYPERRVV---LHGTMLAAAESARYIVHGTRGSYVKFGLDPqeeSLKSGTRPPQENWGYDMRDGVLTVARgemlD 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGIDD---GLLSVTVVGEPGWATDDPMVRKGGDE----V 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1349347909 289 EQTLLTVPGNYPAYYAAVRSAIRGEGENPVPASQAIVVMELIEAGIESAKRRAAVCL 345
Cdd:pfam02894 147 PEFLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 5-122 5.97e-34

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: 121.16  E-value: 5.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYGYASKTFHAPLIAGTPGMELAVISSSDA--GKVHADWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPLAK 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSerAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1349347909  83 AALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFH 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 ...
 5-194 8.19e-23

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: 96.90  E-value: 8.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYGYASKtFHAPLIAG-TPGMELAVISSSDAGKVHA---DWPGMPVVSDPKHLFNDPHLDLIVIPTPNDTHFPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAElaeKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909  81 AKAALEAGKHVVVDKPFTVTLSQARELETLAKSAGLVLSVFHNRRWDSDFLTLKQIIAEGQIGEVayfesHFdrFRPQVR 160
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP-----EI--LRITSR 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1349347909 161 DrwreqAGPGS--------GIWYDLAPHLLDQAVQLFGLPVS 194
Cdd:TIGR04380 154 D-----PAPPPvayvkvsgGLFLDMTIHDFDMARFLLGSEVE 190
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 2-119 6.56e-06

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 47.45  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   2 NDNVRVGLIGYGYASKTFHAPlIAGTPGMELAVISSSDAGKVH-----ADWP-------------------GMPVVS-DP 56
Cdd:COG4091    13 GRPIRVGLIGAGQMGRGLLAQ-IRRMPGMEVVAIADRNPERARaalreAGIPeedirvvdtaaeadaaiaaGKTVVTdDA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1349347909  57 KHLFNDPHLDLIVIPTPNdthfP-----LAKAALEAGKHVV-----VDkpftVTLsqARELETLAKSAGLVLS 119
Cdd:COG4091    92 ELLIAADGIDVVVEATGV----PeagarHALAAIEAGKHVVmvnveAD----VTV--GPLLKRRADEAGVVYT 154
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-118 5.04e-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: 42.91  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYGYASKTFhAPLIAGTPGMEL-AVISSS------DAGKVHADWP-GMPVVSDPKHLFNDPHLDLIVIPTPNDT 76
Cdd:cd24146     1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIvGAVDRDpakvgkDLGELGGGAPlGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1349347909  77 H--FPLAKAALEAGKHVV-----VDKPFTVTLSQARELETLAKSAGLVL 118
Cdd:cd24146    80 AdvAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKENGVTV 128
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-92 4.46e-04

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: 39.43  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   6 RVGLIGY-GYASKTFhAPLIAGTPGMELAVISSSD--AGKVHADWPGMP------VVSDPKhLFNDPHLDLIVIPTPNDT 76
Cdd:pfam01118   1 KVAIVGAtGYVGQEL-LRLLEEHPPVELVVLFASSrsAGKKLAFVHPILeggkdlVVEDVD-PEDFKDVDIVFFALPGGV 78

                          90
                  ....*....|....*.
gi 1349347909  77 HFPLAKAALEAGKHVV 92
Cdd:pfam01118  79 SKEIAPKLAEAGAKVI 94
PRK13302 PRK13302
aspartate dehydrogenase;
6-93 2.08e-03

aspartate dehydrogenase;


Pssm-ID: 237341 [Multi-domain]  Cd Length: 271  Bit Score: 39.45  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   6 RVGLIGYGYASKTFHAPLIAGTPGMELAVISSSDAGKvHADW---PGMPVVSDPKHLFNDpHLDLIVIPTPNDTHFPLAK 82
Cdd:PRK13302    8 RVAIAGLGAIGKAIAQALDRGLPGLTLSAVAVRDPQR-HADFiwgLRRPPPVVPLDQLAT-HADIVVEAAPASVLRAIVE 85

                          90
                  ....*....|.
gi 1349347909  83 AALEAGKHVVV 93
Cdd:PRK13302   86 PVLAAGKKAIV 96
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 5-118 5.69e-03

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 38.52  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1349347909   5 VRVGLIGYG-YASKTF-----HAPLIAGTPGMELAV--ISSSDAGKVHADW-PGMPVVSDPKHLFNDPHLDLIV-----I 70
Cdd:PRK06349    4 LKVGLLGLGtVGSGVVrileeNAEEIAARAGRPIEIkkVAVRDLEKDRGVDlPGILLTTDPEELVNDPDIDIVVelmggI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1349347909  71 PTPNDthfpLAKAALEAGKHVvvdkpftVTLSQA------RELETLAKSAGLVL 118
Cdd:PRK06349   84 EPARE----LILKALEAGKHV-------VTANKAllavhgAELFAAAEEKGVDL 126
 
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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