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Conserved domains on  [gi|496089037|ref|WP_008813544|]
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MULTISPECIES: oxidoreductase [Hafnia]

Protein Classification

oxidoreductase( domain architecture ID 1005443)

oxidoreductase similar to Escherichia coli putative oxidoreductase YdgJ

EC:  1.-.-.-
Gene Ontology:  GO:0016491

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK11579 super family cl32709
putative oxidoreductase; Provisional
 1-345 0e+00

putative oxidoreductase; Provisional


The actual alignment was detected with superfamily member PRK11579:

Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 676.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   1 MADSIRVGLVGYGFAGKTFHAPLIAGTPGLELAAISSSDAHKVLADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  81 AKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVKTLLSEGALGDVVQFESHYDRFRLEVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 161 DRWREKVGAGSGIWFDLGSHLLDQALQLFGKPQSLLADLCAMRPNSQTTDYFHAILYYSDKRIILHGSMVTAAETPRYVI 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 241 HGTKGSYIKHGLDPQEDRLKAGERPPQADWGYDMRDGVLTLVQDDMMAEQSLLTIPGNYPAYYAGIRDAINGDGENPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*
gi 496089037 321 SEAITVMELLELGQESSLQQRALPL 345
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCL 345
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-345 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 676.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   1 MADSIRVGLVGYGFAGKTFHAPLIAGTPGLELAAISSSDAHKVLADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  81 AKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVKTLLSEGALGDVVQFESHYDRFRLEVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 161 DRWREKVGAGSGIWFDLGSHLLDQALQLFGKPQSLLADLCAMRPNSQTTDYFHAILYYSDKRIILHGSMVTAAETPRYVI 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 241 HGTKGSYIKHGLDPQEDRLKAGERPPQADWGYDMRDGVLTLVQDDMMAEQSLLTIPGNYPAYYAGIRDAINGDGENPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*
gi 496089037 321 SEAITVMELLELGQESSLQQRALPL 345
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCL 345
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-346 1.45e-70

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 221.72  E-value: 1.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   2 ADSIRVGLVGYGFAGKtFHAPLIAGTPGLELAAISSSDAHKV--LADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYP 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAeaFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  80 LAKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVKTLLSEGALGDVVQFESHYDRFRLEV 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 160 RDRWR-EKVGAGSGIWFDLGSHLLDQALQLFG-KPQSLLADL-CAMRPNSQTTDYFHAILYYSD-KRIILHGSMVTAAE- 234
Cdd:COG0673  160 PADWRfDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGgRLVPDRVEVDDTAAATLRFANgAVATLEASWVAPGGe 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 235 -TPRYVIHGTKGSYikhgldpqedrlkagerppqadwgydmrdgvltlvqddmmaeqslltipgnypayyagIRDAINGD 313
Cdd:COG0673  240 rDERLEVYGTKGTL----------------------------------------------------------FVDAIRGG 261

                        330       340       350
                 ....*....|....*....|....*....|...
gi 496089037 314 GENPVPASEAITVMELLELGQESSLQQRALPLP 346
Cdd:COG0673  262 EPPPVSLEDGLRALELAEAAYESARTGRRVELP 294
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.25e-39

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: 139.09  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  134 KTLLSEGALGDVVQFESHY-DRFRLEVRD-RWREKVGAGSGIWFDLGSHLLDQALQLFGKPQSLLADLCAMrpnsqttDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHTrDPFRPPQEFkRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYASE-------DT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  212 FHAILYYSDKRII---LHGSMVTAAETPRYVIHGTKGSYIKHGLDpqeDRLKAGERPPQADWGYDMRDGVLTlvQDDMMA 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGID---DGLLSVTVVGEPGWATDDPMVRKG--GDEVPE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 496089037  289 EQSllTIPGNYPAYYAGIRDAINGDGENPVPASEAITVMELLELGQESSLQQRALPL 345
Cdd:pfam02894 149 FLG--SFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 5-148 9.94e-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: 91.13  E-value: 9.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037    5 IRVGLVGYGFAGKtFHAPLIAG-TPGLELAAISSSDAHKV--LAD-WPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAaeLAEkLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496089037   81 AKQALLAGKHVVVDKPFTVNLQEARE-LEMLAKQQKRLLSVFhNRRWDSDFLTVKTLLSEGALGDVVQF 148
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEaLAAVEKAGVKLQIGF-NRRFDPNFRRVKQLVEAGKIGKPEIL 148
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-113 4.19e-06

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: 45.99  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   5 IRVGLVGYGFAGKTFhAPLIAGTPGLELAAISSSDAHKV--------LADWPGMTVVGEPGQLFSDPSIDLVVIPTPNIT 76
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVgkdlgelgGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496089037  77 H--YPLAKQALLAGKHVV-----VDKPFTVNLQEARELEMLAKQ 113
Cdd:cd24146   80 AdvAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKE 123
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-345 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 676.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   1 MADSIRVGLVGYGFAGKTFHAPLIAGTPGLELAAISSSDAHKVLADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPL 80
Cdd:PRK11579   1 MSDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  81 AKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVKTLLSEGALGDVVQFESHYDRFRLEVR 160
Cdd:PRK11579  81 AKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 161 DRWREKVGAGSGIWFDLGSHLLDQALQLFGKPQSLLADLCAMRPNSQTTDYFHAILYYSDKRIILHGSMVTAAETPRYVI 240
Cdd:PRK11579 161 QRWREQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 241 HGTKGSYIKHGLDPQEDRLKAGERPPQADWGYDMRDGVLTLVQDDMMAEQSLLTIPGNYPAYYAGIRDAINGDGENPVPA 320
Cdd:PRK11579 241 HGSRGSYVKYGLDPQEERLKNGERLPQEDWGYDMRDGVLTLVEGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPA 320

                        330       340
                 ....*....|....*....|....*
gi 496089037 321 SEAITVMELLELGQESSLQQRALPL 345
Cdd:PRK11579 321 SQAIQVMELIELGIESAKHRATLCL 345
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-346 1.45e-70

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 221.72  E-value: 1.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   2 ADSIRVGLVGYGFAGKtFHAPLIAGTPGLELAAISSSDAHKV--LADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYP 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAeaFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  80 LAKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVKTLLSEGALGDVVQFESHYDRFRLEV 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 160 RDRWR-EKVGAGSGIWFDLGSHLLDQALQLFG-KPQSLLADL-CAMRPNSQTTDYFHAILYYSD-KRIILHGSMVTAAE- 234
Cdd:COG0673  160 PADWRfDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGgRLVPDRVEVDDTAAATLRFANgAVATLEASWVAPGGe 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 235 -TPRYVIHGTKGSYikhgldpqedrlkagerppqadwgydmrdgvltlvqddmmaeqslltipgnypayyagIRDAINGD 313
Cdd:COG0673  240 rDERLEVYGTKGTL----------------------------------------------------------FVDAIRGG 261

                        330       340       350
                 ....*....|....*....|....*....|...
gi 496089037 314 GENPVPASEAITVMELLELGQESSLQQRALPLP 346
Cdd:COG0673  262 EPPPVSLEDGLRALELAEAAYESARTGRRVELP 294
PRK10206 PRK10206
putative oxidoreductase; Provisional
 55-335 1.26e-64

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 208.14  E-value: 1.26e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  55 EPGQLFSDPSIDLVVIPTPNITHYPLAKQALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFHNRRWDSDFLTVK 134
Cdd:PRK10206  55 DLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAK 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 135 TLLSEGALGDVVQFESHYDRFRLEVrdrwREKVGAG-SGIWFDLGSHLLDQALQLFGKPQSLLADLCAMRPNSQTTDYFH 213
Cdd:PRK10206 135 KAIESGKLGEIVEVESHFDYYRPVA----ETKPGLPqDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFE 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037 214 AILYYSDKRIILHGSMVTAAETPRYVIHGTKGSYIKHGLDPQEDRLKAGERPPQADWGYDMRDGVLTLVQDD-MMAEQSL 292
Cdd:PRK10206 211 AQLFYGDLKAIVKTSHLVKIDYPKFIVHGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYVNDEgVTVREEM 290

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 496089037 293 LTIPGNYPAYYAGIRDAINGDGENPVPASEAITVMELLELGQE 335
Cdd:PRK10206 291 KPEMGDYGRVYDALYQTLTHGAPNYVKESEVLTNLEILERGFE 333
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-345 1.25e-39

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: 139.09  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  134 KTLLSEGALGDVVQFESHY-DRFRLEVRD-RWREKVGAGSGIWFDLGSHLLDQALQLFGKPQSLLADLCAMrpnsqttDY 211
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHTrDPFRPPQEFkRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYASE-------DT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037  212 FHAILYYSDKRII---LHGSMVTAAETPRYVIHGTKGSYIKHGLDpqeDRLKAGERPPQADWGYDMRDGVLTlvQDDMMA 288
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSIELDGID---DGLLSVTVVGEPGWATDDPMVRKG--GDEVPE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 496089037  289 EQSllTIPGNYPAYYAGIRDAINGDGENPVPASEAITVMELLELGQESSLQQRALPL 345
Cdd:pfam02894 149 FLG--SFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 5-122 2.10e-33

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: 120.01  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037    5 IRVGLVGYGFAGKTFHAPLIAGTPGLELAAISSSDAHK--VLADWPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPLAK 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERaeAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496089037   83 QALLAGKHVVVDKPFTVNLQEARELEMLAKQQKRLLSVFH 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 ...
 5-148 9.94e-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: 91.13  E-value: 9.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037    5 IRVGLVGYGFAGKtFHAPLIAG-TPGLELAAISSSDAHKV--LAD-WPGMTVVGEPGQLFSDPSIDLVVIPTPNITHYPL 80
Cdd:TIGR04380   2 LKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAaeLAEkLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496089037   81 AKQALLAGKHVVVDKPFTVNLQEARE-LEMLAKQQKRLLSVFhNRRWDSDFLTVKTLLSEGALGDVVQF 148
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEaLAAVEKAGVKLQIGF-NRRFDPNFRRVKQLVEAGKIGKPEIL 148
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 5-113 4.19e-06

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: 45.99  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   5 IRVGLVGYGFAGKTFhAPLIAGTPGLELAAISSSDAHKV--------LADWPGMTVVGEPGQLFSDPSIDLVVIPTPNIT 76
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVgkdlgelgGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496089037  77 H--YPLAKQALLAGKHVV-----VDKPFTVNLQEARELEMLAKQ 113
Cdd:cd24146   80 AdvAPQIERLLEAGLNVIttceeLFYPWARDPELAEELDALAKE 123
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 5-92 8.20e-05

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 43.98  E-value: 8.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   5 IRVGLVGYGFAGKTFHAPlIAGTPGLELAAISSSDAHKVL-----ADWP-------------------GMTVVGE-PGQL 59
Cdd:COG4091   16 IRVGLIGAGQMGRGLLAQ-IRRMPGMEVVAIADRNPERARaalreAGIPeedirvvdtaaeadaaiaaGKTVVTDdAELL 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496089037  60 FSDPSIDLVVIPT--PNI-THYplAKQALLAGKHVV 92
Cdd:COG4091   95 IAADGIDVVVEATgvPEAgARH--ALAAIEAGKHVV 128
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 2-92 6.80e-04

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 41.21  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   2 ADSIRVGLVGYGFAGK-TF-----HAPLIAGTPG--LELAAISSSDAHKV-LADWPGMTVVGEPGQLFSDPSIDLVV--- 69
Cdd:PRK06349   1 MKPLKVGLLGLGTVGSgVVrileeNAEEIAARAGrpIEIKKVAVRDLEKDrGVDLPGILLTTDPEELVNDPDIDIVVelm 80

                         90       100
                 ....*....|....*....|....*.
gi 496089037  70 --I-PTpnithYPLAKQALLAGKHVV 92
Cdd:PRK06349  81 ggIePA-----RELILKALEAGKHVV 101
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 5-93 2.93e-03

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 37.54  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   5 IRVGLVGY-GFAGKTFhAPLIAGTPGLEL-AAISSSDAHKVLADWPGMTVVGEPGQLFSDPSIDL----VVI--PTPNIT 76
Cdd:cd02274    1 IKVAVAGAtGRMGREL-VKAILEAPDLELvGAVDRPGSGLLGGDAGGLAGIGTGVIVSLDLELAAadadVVIdfTTPEAT 79

                         90
                 ....*....|....*..
gi 496089037  77 hYPLAKQALLAGKHVVV 93
Cdd:cd02274   80 -LENLEAAAKAGVPLVI 95
PRK13302 PRK13302
aspartate dehydrogenase;
5-93 5.20e-03

aspartate dehydrogenase;


Pssm-ID: 237341 [Multi-domain]  Cd Length: 271  Bit Score: 38.30  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037   5 IRVGLVGYGFAGKTFHAPLIAGTPGLELAAISSSDAHK---VLADWPGMTVVGEPGQLFSdpSIDLVVIPTPNITHYPLA 81
Cdd:PRK13302   7 LRVAIAGLGAIGKAIAQALDRGLPGLTLSAVAVRDPQRhadFIWGLRRPPPVVPLDQLAT--HADIVVEAAPASVLRAIV 84

                         90
                 ....*....|..
gi 496089037  82 KQALLAGKHVVV 93
Cdd:PRK13302  85 EPVLAAGKKAIV 96
Semialdhyde_dh pfam01118
Semialdehyde dehydrogenase, NAD binding domain; This Pfam entry contains the following members: ...
 6-92 7.53e-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: 35.96  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496089037    6 RVGLVGY-GFAGKTFhAPLIAGTPGLELAAISSS---------DAHKVLADWPGMTVvgEPGQLFSDPSIDLVVIPTPNI 75
Cdd:pfam01118   1 KVAIVGAtGYVGQEL-LRLLEEHPPVELVVLFASsrsagkklaFVHPILEGGKDLVV--EDVDPEDFKDVDIVFFALPGG 77

                          90
                  ....*....|....*..
gi 496089037   76 THYPLAKQALLAGKHVV 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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