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Conserved domains on  [gi|556299649|ref|WP_023292473|]
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MULTISPECIES: oxidoreductase [Enterobacter]

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
 6-345 6.05e-156

putative oxidoreductase; Provisional


The actual alignment was detected with superfamily member PRK11579:

Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 441.46  E-value: 6.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   6 TINIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVKRDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPLATL 85
Cdd:PRK11579   4 KIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  86 ALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEVRVRW 165
Cdd:PRK11579  84 ALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVRQRW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 166 REQNVPGSGLWFDLGPHLIDQTLQLFGLPQSVQGNIATLRDGAEINDWAHVVLNYPEHKVILHASMLVAGGTARFAVHGD 245
Cdd:PRK11579 164 REQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIVHGS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 246 KGSVVKARIDQQEAQLLSGVIPGSEAWGED-SDSMVFF--GADGASQTIPTPKGDQRQYYISVRDALLGKIANPVHPVEA 322
Cdd:PRK11579 244 RGSYVKYGLDPQEERLKNGERLPQEDWGYDmRDGVLTLveGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPASQA 323

                        330       340
                 ....*....|....*....|...
gi 556299649 323 LAVMAVLEAAVTSSETGSTQTLA 345
Cdd:PRK11579 324 IQVMELIELGIESAKHRATLCLA 346
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 6-345 6.05e-156

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 441.46  E-value: 6.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   6 TINIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVKRDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPLATL 85
Cdd:PRK11579   4 KIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  86 ALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEVRVRW 165
Cdd:PRK11579  84 ALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVRQRW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 166 REQNVPGSGLWFDLGPHLIDQTLQLFGLPQSVQGNIATLRDGAEINDWAHVVLNYPEHKVILHASMLVAGGTARFAVHGD 245
Cdd:PRK11579 164 REQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIVHGS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 246 KGSVVKARIDQQEAQLLSGVIPGSEAWGED-SDSMVFF--GADGASQTIPTPKGDQRQYYISVRDALLGKIANPVHPVEA 322
Cdd:PRK11579 244 RGSYVKYGLDPQEERLKNGERLPQEDWGYDmRDGVLTLveGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPASQA 323

                        330       340
                 ....*....|....*....|...
gi 556299649 323 LAVMAVLEAAVTSSETGSTQTLA 345
Cdd:PRK11579 324 IQVMELIELGIESAKHRATLCLA 346
MviM COG0673
Predicted dehydrogenase [General function prediction only];
5-345 8.22e-73

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 227.88  E-value: 8.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   5 RTINIALIGYGFVGKtFHAPLIQSVDGLKLAVVSSRDEEKVKR--DLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPL 82
Cdd:COG0673    2 DKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEAfaEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  83 ATLALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEVR 162
Cdd:COG0673   81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 163 VRWREQ-NVPGSGLWFDLGPHLIDQTLQLFGL-PQSVQGNIAT-LRDGAEINDWAHVVLNYPEH-KVILHASMLVAGG-- 236
Cdd:COG0673  161 ADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRlVPDRVEVDDTAAATLRFANGaVATLEASWVAPGGer 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 237 TARFAVHGDKGSVvkaridqqeaqllsgvipgseawgedsdsmvffgadgasqtiptpkgdqrqyyisVRDALLGKIANP 316
Cdd:COG0673  241 DERLEVYGTKGTL-------------------------------------------------------FVDAIRGGEPPP 265

                        330       340
                 ....*....|....*....|....*....
gi 556299649 317 VHPVEALAVMAVLEAAVTSSETGSTQTLA 345
Cdd:COG0673  266 VSLEDGLRALELAEAAYESARTGRRVELP 294
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 7-124 3.38e-32

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: 116.92  E-value: 3.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649    7 INIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVK--RDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPLAT 84
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEavAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 556299649   85 LALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFH 124
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 6-150 3.02e-28

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: 112.31  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649    6 TINIALIGYGFVGKtFHAPLIQS-VDGLKLAVVSSRDEEKVK---RDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAP 81
Cdd:TIGR04380   1 KLKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAelaEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556299649   82 LATLALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHL 150
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEIL 148
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 7-94 9.72e-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: 45.22  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   7 INIALIGYGFVGKTFhAPLIQSVDGLKLAVVSSRDEEKVKRDL--------PDVEVVTTPEEAIQHPDVDLVVIASPNAT 78
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVGKDLgelgggapLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90
                 ....*....|....*...
gi 556299649  79 HAPLATL--ALNAGKHVV 94
Cdd:cd24146   80 ADVAPQIerLLEAGLNVI 97
 
Name Accession Description Interval E-value
PRK11579 PRK11579
putative oxidoreductase; Provisional
 6-345 6.05e-156

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 441.46  E-value: 6.05e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   6 TINIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVKRDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPLATL 85
Cdd:PRK11579   4 KIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  86 ALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEVRVRW 165
Cdd:PRK11579  84 ALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVAYFESHFDRFRPQVRQRW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 166 REQNVPGSGLWFDLGPHLIDQTLQLFGLPQSVQGNIATLRDGAEINDWAHVVLNYPEHKVILHASMLVAGGTARFAVHGD 245
Cdd:PRK11579 164 REQGGPGSGIWYDLAPHLLDQAIQLFGLPVSITVDLAQLRPGAQSTDYFHAILSYPQRRVVLHGTMLAAAESARYIVHGS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 246 KGSVVKARIDQQEAQLLSGVIPGSEAWGED-SDSMVFF--GADGASQTIPTPKGDQRQYYISVRDALLGKIANPVHPVEA 322
Cdd:PRK11579 244 RGSYVKYGLDPQEERLKNGERLPQEDWGYDmRDGVLTLveGEERVEETLLTLPGNYPAYYAAIRDALNGDGENPVPASQA 323

                        330       340
                 ....*....|....*....|...
gi 556299649 323 LAVMAVLEAAVTSSETGSTQTLA 345
Cdd:PRK11579 324 IQVMELIELGIESAKHRATLCLA 346
MviM COG0673
Predicted dehydrogenase [General function prediction only];
5-345 8.22e-73

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 227.88  E-value: 8.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   5 RTINIALIGYGFVGKtFHAPLIQSVDGLKLAVVSSRDEEKVKR--DLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPL 82
Cdd:COG0673    2 DKLRVGIIGAGGIGR-AHAPALAALPGVELVAVADRDPERAEAfaEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  83 ATLALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEVR 162
Cdd:COG0673   81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 163 VRWREQ-NVPGSGLWFDLGPHLIDQTLQLFGL-PQSVQGNIAT-LRDGAEINDWAHVVLNYPEH-KVILHASMLVAGG-- 236
Cdd:COG0673  161 ADWRFDpELAGGGALLDLGIHDIDLARWLLGSePESVSATGGRlVPDRVEVDDTAAATLRFANGaVATLEASWVAPGGer 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 237 TARFAVHGDKGSVvkaridqqeaqllsgvipgseawgedsdsmvffgadgasqtiptpkgdqrqyyisVRDALLGKIANP 316
Cdd:COG0673  241 DERLEVYGTKGTL-------------------------------------------------------FVDAIRGGEPPP 265

                        330       340
                 ....*....|....*....|....*....
gi 556299649 317 VHPVEALAVMAVLEAAVTSSETGSTQTLA 345
Cdd:COG0673  266 VSLEDGLRALELAEAAYESARTGRRVELP 294
PRK10206 PRK10206
putative oxidoreductase; Provisional
 6-345 5.60e-65

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 209.29  E-value: 5.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   6 TINIALIGYGFVGKTFHAP-LIQSVDGLKLAVV---SSRDEEKVKRdLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAP 81
Cdd:PRK10206   1 VINCAFIGFGKSTTRYHLPyVLNRKDSWHVAHIfrrHAKPEEQAPI-YSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  82 LATLALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHLESHIDRFRPEV 161
Cdd:PRK10206  80 YAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRPVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 162 RVRwreQNVPGSGLWFDLGPHLIDQTLQLFGLPQSVQGNIATLRDGAEINDWAHVVLNYPEHKVILHASMLVAGGTARFA 241
Cdd:PRK10206 160 ETK---PGLPQDGAFYGLGVHTMDQIISLFGRPDHVAYDIRSLRNKANPDDTFEAQLFYGDLKAIVKTSHLVKIDYPKFI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649 242 VHGDKGSVVKARIDQQEAQLLSGVIPGSEAWGEDSD--SMVFFGADGAS--QTIPTPKGDQRQYYISVRDALLGKIANPV 317
Cdd:PRK10206 237 VHGKKGSFIKYGIDQQETSLKANIMPGEPGFAADDSvgVLEYVNDEGVTvrEEMKPEMGDYGRVYDALYQTLTHGAPNYV 316

                        330       340
                 ....*....|....*....|....*...
gi 556299649 318 HPVEALAVMAVLEAAVTSSeTGSTQTLA 345
Cdd:PRK10206 317 KESEVLTNLEILERGFEQA-SPATVTLA 343
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 7-124 3.38e-32

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: 116.92  E-value: 3.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649    7 INIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVK--RDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAPLAT 84
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEavAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 556299649   85 LALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFH 124
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 136-344 7.91e-32

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: 118.67  E-value: 7.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  136 KQVIEQGTLGKVKHLESH-IDRFRPEVR-VRWREQNVPGSGLWFDLGPHLIDQTLQLFGLPQSVQGNIATLrdgaeinDW 213
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEfKRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVAVYASE-------DT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649  214 AHVVLNYPEHKVI---LHASMLVAGGTARFAVHGDKGSVvkaRIDQQEAQLLSGVIPGSEAWGEDsDSMVFFGADGASQT 290
Cdd:pfam02894  74 AFATLEFKNGAVGtleTSGGSIVEANGHRISIHGTKGSI---ELDGIDDGLLSVTVVGEPGWATD-DPMVRKGGDEVPEF 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 556299649  291 IPTPKGDQRQYYISVRDALLGKIANPVHPVEALAVMAVLEAAVTSSETGSTQTL 344
Cdd:pfam02894 150 LGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 6-150 3.02e-28

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: 112.31  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649    6 TINIALIGYGFVGKtFHAPLIQS-VDGLKLAVVSSRDEEKVK---RDLPDVEVVTTPEEAIQHPDVDLVVIASPNATHAP 81
Cdd:TIGR04380   1 KLKVGIIGAGRIGK-VHAENLAThVPGARLKAIVDPFADAAAelaEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556299649   82 LATLALNAGKHVVVDKPFTLDMQEARDLIALAEEKQLLLSVFHNRRWDSDFLGIKQVIEQGTLGKVKHL 150
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEIL 148
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 5-94 4.05e-07

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 51.23  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   5 RTINIALIGYGFVGK-TF-----HAPLIQSVDG--LKLAVVSSRDEEKvKR--DLPDVEVVTTPEEAIQHPDVDLVV--I 72
Cdd:PRK06349   2 KPLKVGLLGLGTVGSgVVrileeNAEEIAARAGrpIEIKKVAVRDLEK-DRgvDLPGILLTTDPEELVNDPDIDIVVelM 80

                         90       100
                 ....*....|....*....|..
gi 556299649  73 ASPNATHApLATLALNAGKHVV 94
Cdd:PRK06349  81 GGIEPARE-LILKALEAGKHVV 101
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
 5-94 9.39e-07

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 50.15  E-value: 9.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   5 RTINIALIGYGFVGKTFHAPlIQSVDGLKLAVVSSRDEEKVKR-------DLPDVEVVTTPEEA---------------- 61
Cdd:COG4091   14 RPIRVGLIGAGQMGRGLLAQ-IRRMPGMEVVAIADRNPERARAalreagiPEEDIRVVDTAAEAdaaiaagktvvtddae 92

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556299649  62 --IQHPDVDLVVIA--SPNAThAPLATLALNAGKHVV 94
Cdd:COG4091   93 llIAADGIDVVVEAtgVPEAG-ARHALAAIEAGKHVV 128
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 13-115 1.31e-06

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: 46.53  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   13 GYGFVGKTFHAPLI--QSVDGLKLAVVSSRDEEKV--KRDLPDVEVVTTPEEAIQHPDVDLVV-IASPNATHApLATLAL 87
Cdd:pfam03447   1 GCGAIGSGVLEQLLrqQSEIPLELVAVADRDLLSKdpLALLPDEPLTLDLDDLIAHPDPDVVVeCASSEAVAE-LVLDAL 79

                          90       100
                  ....*....|....*....|....*....
gi 556299649   88 NAGKHVVV-DKPFTLDMQEARDLIALAEE 115
Cdd:pfam03447  80 KAGKDVVTaSKGALADLALYEELREAAEA 108
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 7-94 9.72e-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: 45.22  E-value: 9.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   7 INIALIGYGFVGKTFhAPLIQSVDGLKLAVVSSRDEEKVKRDL--------PDVEVVTTPEEAIQHPDVDLVVIASPNAT 78
Cdd:cd24146    1 IRVVVWGLGAMGRGI-ARYLLEKPGLEIVGAVDRDPAKVGKDLgelgggapLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                         90
                 ....*....|....*...
gi 556299649  79 HAPLATL--ALNAGKHVV 94
Cdd:cd24146   80 ADVAPQIerLLEAGLNVI 97
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 9-94 3.77e-05

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


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 42.58  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649    9 IALIGYGFVGKTFhAPLIQSVDGLKLAVVSSRDEEK---VKRDLPDVEVVTTPEEAIQHPDV--------DLVVIASPNA 77
Cdd:pfam03435   1 VLIIGAGSVGQGV-APLLARHFDVDRITVADRTLEKaqaLAAKLGGVRFIAVAVDADNYEAVlaallkegDLVVNLSPPT 79

                          90
                  ....*....|....*..
gi 556299649   78 THAPLATLALNAGKHVV 94
Cdd:pfam03435  80 LSLDVLKACIETGVHYV 96
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 5-115 4.57e-05

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 44.86  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   5 RTINIALIGYGFVGKTFhAPLIQ------------------------SV---DGLKLAVVSSRDEEKVK-RDLPDVEVVT 56
Cdd:PRK06270   1 MEMKIALIGFGGVGQGV-AELLAekreylkkrygldlkvvaiadssgSAidpDGLDLELALKVKEETGKlADYPEGGGEI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556299649  57 TPEEAIQHPDVDLVVIASP-NA-THAPLATL---ALNAGKHVVV-DK-PFTLdmqEARDLIALAEE 115
Cdd:PRK06270  80 SGLEVIRSVDADVVVEATPtNIeTGEPALSHcrkALERGKHVVTsNKgPLAL---AYKELKELAKK 142
PRK13302 PRK13302
aspartate dehydrogenase;
1-95 8.73e-05

aspartate dehydrogenase;


Pssm-ID: 237341 [Multi-domain]  Cd Length: 271  Bit Score: 43.69  E-value: 8.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   1 MSTVRTINIALIGYGFVGKTFHAPLIQSVDGLKLAVVSSRDEEKVK---RDLPDVEVVTTPEEAIQHpdVDLVVIASPNA 77
Cdd:PRK13302   1 MSSRPELRVAIAGLGAIGKAIAQALDRGLPGLTLSAVAVRDPQRHAdfiWGLRRPPPVVPLDQLATH--ADIVVEAAPAS 78

                         90
                 ....*....|....*...
gi 556299649  78 THAPLATLALNAGKHVVV 95
Cdd:PRK13302  79 VLRAIVEPVLAAGKKAIV 96
AGPR_N_ARG5_6_like cd24149
N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme ...
 7-96 2.98e-04

N-terminal NAD(P)-binding domain (AGPR region) of fungal bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) and similar proteins; The family includes bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) from fungi, which contains a N-terminal acetylglutamate kinase ( EC 2.7.2.8, also known as N-acetyl-L-glutamate 5-phosphotransferase/NAG kinase/AGK) domain and a C-terminal N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38, also known as AGPR/N-acetyl-glutamate semialdehyde dehydrogenase/NAGSA dehydrogenase) domain. The model corresponds to the AGPR N-terminal NAD(P)-binding domain. AGPR catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. The budding yeast member, Arg5,6, is expressed as a precursor that is then maturated in the mitochondria into acetylglutamate kinase and acetylglutamyl-phosphate reductase. It is involved in the arginine biosynthesis pathway, catalyzing the second and third steps in the pathway.


Pssm-ID: 467525 [Multi-domain]  Cd Length: 154  Bit Score: 40.56  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   7 INIALIG-YGFVGKTFhAPLIQSVDGLKLAVVSSR--------DEEKVKRDLPDVEVVTTPEEAIQHpDVDLVVIASPNA 77
Cdd:cd24149    1 KRVGLIGaRGYVGREL-IRLLNRHPNLELAHVSSRelagqkvsGYTKSPIDYLNLSVEDIPEEVAAR-EVDAWVLALPNG 78

                         90       100
                 ....*....|....*....|.
gi 556299649  78 THAPLATlALNAGKH--VVVD 96
Cdd:cd24149   79 VAKPFVD-AIDKANPksVIVD 98
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 7-94 3.71e-04

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 40.25  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299649   7 INIALIGYGFVGKtFHAPLIQSVDGLKLAVVSSRDEEKVKRDLPDVEVVTTpEEAIQHPD-VDLVVIASPNATHAPLATL 85
Cdd:cd02270    1 IRVAIVGYGNLGR-GVEEAIQANPDMELVGVFRRRDPKSTKELTPVVVVSV-VEHISELDkVDVAILCGGSATDLPEQAP 78


                 ....*....
gi 556299649  86 ALNAGKHVV 94
Cdd:cd02270   79 EFAQGFNTV 87
 
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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