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Conserved domains on  [gi|1946390195|emb|CAD7359230|]
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3-isopropylmalate dehydrogenase [Staphylococcus schleiferi]

Protein Classification

isocitrate/isopropylmalate dehydrogenase family protein( domain architecture ID 296)

isocitrate/isopropylmalate dehydrogenase family protein such as isocitrate dehydrogenase that in the Krebs cycle catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate and CO2, and isopropylmalate dehydrogenase that in leucine biosynthesis catalyzes the oxidation and decarboxylation of 3-isopropyl-l-malate to 4-methyl-2-oxovalerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Iso_dh super family cl00445
Isocitrate/isopropylmalate dehydrogenase;
1-170 5.99e-92

Isocitrate/isopropylmalate dehydrogenase;


The actual alignment was detected with superfamily member PRK00772:

Pssm-ID: 444908  Cd Length: 358  Bit Score: 271.59  E-value: 5.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   1 MTFNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWE 80
Cdd:PRK00772    1 MTYKIAVLPGDGIGPEVMAEAVKVLDAVAEKFGFDFEFEEALVGGAAIDAHGVPLPEETLEACRAADAVLLGAVGGPKWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  81 N--PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPRYF----NANEAVDT 154
Cdd:PRK00772   81 NlpPDVRPERGLLALRKELGLFANLRPAKLYPGLADASPLKPEIVAGLDILIVRELTGGIYFGEPRGReglgGEERAFDT 160

                         170
                  ....*....|....*.
gi 1946390195 155 LAYSEAEITRIAHYCF 170
Cdd:PRK00772  161 MVYTREEIERIARVAF 176
 
Name Accession Description Interval E-value
PRK00772 PRK00772
3-isopropylmalate dehydrogenase; Provisional
 1-170 5.99e-92

3-isopropylmalate dehydrogenase; Provisional


Pssm-ID: 234832  Cd Length: 358  Bit Score: 271.59  E-value: 5.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   1 MTFNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWE 80
Cdd:PRK00772    1 MTYKIAVLPGDGIGPEVMAEAVKVLDAVAEKFGFDFEFEEALVGGAAIDAHGVPLPEETLEACRAADAVLLGAVGGPKWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  81 N--PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPRYF----NANEAVDT 154
Cdd:PRK00772   81 NlpPDVRPERGLLALRKELGLFANLRPAKLYPGLADASPLKPEIVAGLDILIVRELTGGIYFGEPRGReglgGEERAFDT 160

                         170
                  ....*....|....*.
gi 1946390195 155 LAYSEAEITRIAHYCF 170
Cdd:PRK00772  161 MVYTREEIERIARVAF 176
leuB TIGR00169
3-isopropylmalate dehydrogenase; Several NAD- or NADP-dependent dehydrogenases, including ...
 4-170 3.29e-77

3-isopropylmalate dehydrogenase; Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the dimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates.Among these decarboxylating dehydrogenases of hydroxyacids, overall sequence homology indicates evolutionary history rather than actual substrate or cofactor specifity, which may be toggled experimentally by replacement of just a few amino acids. 3-isopropylmalate dehydrogenase is an NAD-dependent enzyme and should have a sequence resembling HGSAPDI around residue 340. The subtrate binding loop should include a sequence resembling E[KQR]X(0,1)LLXXR around residue 115. Other contacts of importance are known from crystallography but not detailed here.This model will not find all isopropylmalate dehydrogenases; the enzyme from Sulfolobus sp. strain 7 is more similar to mitochondrial NAD-dependent isocitrate dehydrogenases than to other known isopropylmalate dehydrogenases and was omitted to improve the specificity of the model. It scores below the cutoff and below some enzymes known not to be isopropylmalate dehydrogenase. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272939  Cd Length: 346  Bit Score: 233.45  E-value: 3.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   4 NLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWEN-- 81
Cdd:TIGR00169   1 KIAVLPGDGIGPEVMAQALKVLKAVAERFGLKFEFEEHLIGGAAIDATGQPLPEETLKGCKEADAVLLGAVGGPKWDNlp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  82 PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPR-YFNANEAVDTLAYSEA 160
Cdd:TIGR00169  81 RDQRPEQGLLKLRKSLDLFANLRPAKVFPGLEDLSPLKEEIAKGVDFVVVRELTGGIYFGEPKgREGEGEAWDTEVYTVP 160

                         170
                  ....*....|
gi 1946390195 161 EITRIAHYCF 170
Cdd:TIGR00169 161 EIERIARVAF 170
LeuB COG0473
Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid ...
 2-170 5.92e-75

Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid transport and metabolism]; Isocitrate/isopropylmalate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440241  Cd Length: 346  Bit Score: 227.59  E-value: 5.92e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   2 TFNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWEn 81
Cdd:COG0473     1 TYKIAVLPGDGIGPEVVAAALKVLEAAAERFGLDFEFEEADIGGAAYDKTGTPLPDETLEALRKADAILLGAVGGPKWD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  82 PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVdlSPIKREIVNQTDLIIVRELTGGLYFGEPRYFNA----NEAVDTLAY 157
Cdd:COG0473    80 DGVRPESGLLALRKELDLYANLRPAKLYPGLP--SPLKPEIVEGIDLVIVRENTEGLYFGIGGRIGTgtgeEVAIDTRVY 157

                         170
                  ....*....|...
gi 1946390195 158 SEAEITRIAHYCF 170
Cdd:COG0473   158 TRKGIERIARYAF 170
Iso_dh pfam00180
Isocitrate/isopropylmalate dehydrogenase;
4-170 3.87e-67

Isocitrate/isopropylmalate dehydrogenase;


Pssm-ID: 425507  Cd Length: 346  Bit Score: 207.92  E-value: 3.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   4 NLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWENPD 83
Cdd:pfam00180   1 KIAVLPGDGIGPEVMAAALKVLKAALEKAPLEFEFEERDVGGAAIDETGEPLPDETLEACKKADAVLLGAVGGPKWDPAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  84 CRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNqTDLIIVRELTGGLYFGEP--RYFNANE-AVDTLAYSEA 160
Cdd:pfam00180  81 VRPENGLLALRKELGLFANLRPAKVFPPLGDASPLKNEVEG-VDIVIVRELTGGIYFGIEkgIKGSGNEvAVDTKLYSRD 159

                         170
                  ....*....|
gi 1946390195 161 EITRIAHYCF 170
Cdd:pfam00180 160 EIERIARVAF 169
 
Name Accession Description Interval E-value
PRK00772 PRK00772
3-isopropylmalate dehydrogenase; Provisional
 1-170 5.99e-92

3-isopropylmalate dehydrogenase; Provisional


Pssm-ID: 234832  Cd Length: 358  Bit Score: 271.59  E-value: 5.99e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   1 MTFNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWE 80
Cdd:PRK00772    1 MTYKIAVLPGDGIGPEVMAEAVKVLDAVAEKFGFDFEFEEALVGGAAIDAHGVPLPEETLEACRAADAVLLGAVGGPKWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  81 N--PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPRYF----NANEAVDT 154
Cdd:PRK00772   81 NlpPDVRPERGLLALRKELGLFANLRPAKLYPGLADASPLKPEIVAGLDILIVRELTGGIYFGEPRGReglgGEERAFDT 160

                         170
                  ....*....|....*.
gi 1946390195 155 LAYSEAEITRIAHYCF 170
Cdd:PRK00772  161 MVYTREEIERIARVAF 176
leuB TIGR00169
3-isopropylmalate dehydrogenase; Several NAD- or NADP-dependent dehydrogenases, including ...
 4-170 3.29e-77

3-isopropylmalate dehydrogenase; Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the dimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologs. These enzymes dehydrogenate their substates at a H-C-OH site adjacent to a H-C-COOH site; the latter carbon, now adjacent to a carbonyl group, readily decarboxylates.Among these decarboxylating dehydrogenases of hydroxyacids, overall sequence homology indicates evolutionary history rather than actual substrate or cofactor specifity, which may be toggled experimentally by replacement of just a few amino acids. 3-isopropylmalate dehydrogenase is an NAD-dependent enzyme and should have a sequence resembling HGSAPDI around residue 340. The subtrate binding loop should include a sequence resembling E[KQR]X(0,1)LLXXR around residue 115. Other contacts of importance are known from crystallography but not detailed here.This model will not find all isopropylmalate dehydrogenases; the enzyme from Sulfolobus sp. strain 7 is more similar to mitochondrial NAD-dependent isocitrate dehydrogenases than to other known isopropylmalate dehydrogenases and was omitted to improve the specificity of the model. It scores below the cutoff and below some enzymes known not to be isopropylmalate dehydrogenase. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272939  Cd Length: 346  Bit Score: 233.45  E-value: 3.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   4 NLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWEN-- 81
Cdd:TIGR00169   1 KIAVLPGDGIGPEVMAQALKVLKAVAERFGLKFEFEEHLIGGAAIDATGQPLPEETLKGCKEADAVLLGAVGGPKWDNlp 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  82 PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPR-YFNANEAVDTLAYSEA 160
Cdd:TIGR00169  81 RDQRPEQGLLKLRKSLDLFANLRPAKVFPGLEDLSPLKEEIAKGVDFVVVRELTGGIYFGEPKgREGEGEAWDTEVYTVP 160

                         170
                  ....*....|
gi 1946390195 161 EITRIAHYCF 170
Cdd:TIGR00169 161 EIERIARVAF 170
LeuB COG0473
Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid ...
 2-170 5.92e-75

Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid transport and metabolism]; Isocitrate/isopropylmalate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440241  Cd Length: 346  Bit Score: 227.59  E-value: 5.92e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   2 TFNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWEn 81
Cdd:COG0473     1 TYKIAVLPGDGIGPEVVAAALKVLEAAAERFGLDFEFEEADIGGAAYDKTGTPLPDETLEALRKADAILLGAVGGPKWD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  82 PDCRPEHDLLQLRKALNLYANIRPTRVTPYTVdlSPIKREIVNQTDLIIVRELTGGLYFGEPRYFNA----NEAVDTLAY 157
Cdd:COG0473    80 DGVRPESGLLALRKELDLYANLRPAKLYPGLP--SPLKPEIVEGIDLVIVRENTEGLYFGIGGRIGTgtgeEVAIDTRVY 157

                         170
                  ....*....|...
gi 1946390195 158 SEAEITRIAHYCF 170
Cdd:COG0473   158 TRKGIERIARYAF 170
Iso_dh pfam00180
Isocitrate/isopropylmalate dehydrogenase;
4-170 3.87e-67

Isocitrate/isopropylmalate dehydrogenase;


Pssm-ID: 425507  Cd Length: 346  Bit Score: 207.92  E-value: 3.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   4 NLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWENPD 83
Cdd:pfam00180   1 KIAVLPGDGIGPEVMAAALKVLKAALEKAPLEFEFEERDVGGAAIDETGEPLPDETLEACKKADAVLLGAVGGPKWDPAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  84 CRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNqTDLIIVRELTGGLYFGEP--RYFNANE-AVDTLAYSEA 160
Cdd:pfam00180  81 VRPENGLLALRKELGLFANLRPAKVFPPLGDASPLKNEVEG-VDIVIVRELTGGIYFGIEkgIKGSGNEvAVDTKLYSRD 159

                         170
                  ....*....|
gi 1946390195 161 EITRIAHYCF 170
Cdd:pfam00180 160 EIERIARVAF 169
PLN02329 PLN02329
3-isopropylmalate dehydrogenase
 3-170 1.05e-43

3-isopropylmalate dehydrogenase


Pssm-ID: 215188  Cd Length: 409  Bit Score: 149.07  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   3 FNLVALPGDGIGPEIMAGTLEILNELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWENP 82
Cdd:PLN02329   47 YNIALLPGDGIGPEVISVAKNVLQKAGSLEGLEFDFQEMPVGGAALDLVGVPLPEETFTAAKQSDAILLGAIGGYKWDKN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  83 D--CRPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPIKREIVNQTDLIIVRELTGGLYFGEPRYFNANE-----AVDTL 155
Cdd:PLN02329  127 EkhLRPEMALFYLRRDLKVFANLRPATVLPQLVDASTLKKEVAEGVDMMIVRELTGGIYFGEPRGITINEngeevGVSTE 206

                         170
                  ....*....|....*
gi 1946390195 156 AYSEAEITRIAHYCF 170
Cdd:PLN02329  207 IYAAHEIDRIARVAF 221
PRK14025 PRK14025
multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase; Provisional
 5-170 9.20e-26

multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase; Provisional


Pssm-ID: 184462  Cd Length: 330  Bit Score: 100.21  E-value: 9.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   5 LVALPGDGIGPEIMAGTLEILNELATKFNFNchvdTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPkwenpdc 84
Cdd:PRK14025    4 ICVIEGDGIGKEVVPAALHVLEATGLPFEFV----YAEAGDEVFEKTGKALPEETIEAAKEADAVLFGAAGET------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  85 rPEHDLLQLRKALNLYANIRPTRVTPYTVDLSPikreivnQTDLIIVRELTGGLYFGEPRYFNANEAVDTLAYSEAEITR 164
Cdd:PRK14025   73 -AADVIVKLRRILDTYANVRPVKSYKGVKCLYP-------DIDYVIVRENTEGLYKGIEAEIADGVTVATRVITRKASER 144


                  ....*.
gi 1946390195 165 IAHYCF 170
Cdd:PRK14025  145 IFRFAF 150
PRK03437 PRK03437
3-isopropylmalate dehydrogenase; Provisional
 1-141 1.99e-21

3-isopropylmalate dehydrogenase; Provisional


Pssm-ID: 179579  Cd Length: 344  Bit Score: 88.83  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   1 MTFNLVALPGDGIGPEIMAGTLEILNElATKFNFNCHVDTYDIGGcaiDRY---GTPLPNETLHACQNADAILLGAIGGp 77
Cdd:PRK03437    3 KTMKLAVIPGDGIGPEVVAEALKVLDA-VAAGGPGVETTEYDLGA---RRYlrtGETLPDSVLAELRQHDAILLGAIGD- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  78 kwenPDCRP---EHD-LLQLRKALNLYANIRPTRVTPyTVDlSPIKR--EIvnqtDLIIVRELTGGLYFG 141
Cdd:PRK03437   78 ----PSVPSgvlERGlLLKLRFALDHYVNLRPSKLYP-GVT-SPLAGpgDI----DFVVVREGTEGPYTG 137
PRK08997 PRK08997
isocitrate dehydrogenase; Provisional
 1-164 3.72e-17

isocitrate dehydrogenase; Provisional


Pssm-ID: 181606  Cd Length: 334  Bit Score: 77.07  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   1 MTFNLVALPGDGIGPEIMAGTLEILNELATKFNFnchvDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGPKWE 80
Cdd:PRK08997    1 MKQTITVIPGDGIGPSIIDATLKILDKLGCDFEY----EFADAGLTALEKHGELLPQRTLDLIEKNKIALKGPLTTPVGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  81 -----NpdcrpehdlLQLRKALNLYANIRPTRVTPYTvdlspikREIVNQTDLIIVRELTGGLYFGEPRYFNANeavDTL 155
Cdd:PRK08997   77 gftsiN---------VTLRKKFDLYANVRPVLSFPGT-------KARYDNIDIITVRENTEGMYSGEGQTVSED---GET 137


                  ....*....
gi 1946390195 156 AYSEAEITR 164
Cdd:PRK08997  138 AEATSIITR 146
PRK08194 PRK08194
tartrate dehydrogenase; Provisional
 2-139 3.76e-16

tartrate dehydrogenase; Provisional


Pssm-ID: 181281  Cd Length: 352  Bit Score: 74.37  E-value: 3.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   2 TFNLVALPGDGIGPEIMAGTLEILNELA----------TKFNFNChvDTYdiggcaiDRYGTPLPNETLHACQNADAILL 71
Cdd:PRK08194    3 QFKIAVIPGDGVGKEVVPAAVRVLKAVAevhgglkfefTEFPWSC--EYY-------LEHGEMMPEDGLEQLKQFDAIFL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946390195  72 GAIGgpkweNPDCRPEHD-----LLQLRKALNLYANIRPTRVTPYTVdlSPIKREivNQTDLIIVRELTGGLY 139
Cdd:PRK08194   74 GAVG-----NPKLVPDHIslwglLIKIRREFEQVINIRPAKQLRGIK--SPLANP--KDFDLLVVRENSEGEY 137
PRK06451 PRK06451
NADP-dependent isocitrate dehydrogenase;
10-151 2.26e-11

NADP-dependent isocitrate dehydrogenase;


Pssm-ID: 235803  Cd Length: 412  Bit Score: 61.00  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  10 GDGIGPEIMAGTLEILN---ELATKFNFNCHVDTYDIGGCAIDRYGTPLPNETLHACQNADAILLGAIGGP---KWENPD 83
Cdd:PRK06451   31 GDGIGPEITHAAMKVINkavEKAYGSDREIKWVEVLAGDKAEKLTGNRFPKESEELIEKYRVLLKGPLETPigkGWKSIN 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946390195  84 CRpehdllqLRKALNLYANIRPTRVTPYTVdlSPIKREivNQTDLIIVRELTGGLYFGEPRYFNANEA 151
Cdd:PRK06451  111 VA-------IRLMLDLYANIRPVKYIPGIE--SPLKNP--EKIDLIIFRENTDDLYRGIEYPYDSEEA 167
PRK09222 PRK09222
NADP-dependent isocitrate dehydrogenase;
6-141 5.68e-11

NADP-dependent isocitrate dehydrogenase;


Pssm-ID: 236416 [Multi-domain]  Cd Length: 482  Bit Score: 59.90  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   6 VAlPGDGIGPEIMAGTLEILNELATKFNfnchVDTYDIGGCAIDRYGTP-LPNETLHACQNADAILLGAI-----GGPKW 79
Cdd:PRK09222    9 VA-YGDGIGPEIMEAVLKILEAAGAPLE----IETIEIGEKVYKKGWTSgISPSAWESIRRTKVLLKAPIttpqgGGYKS 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946390195  80 ENpdcrpehdlLQLRKALNLYANIRPtrvtpyTVDLSPIKREIVNQTDLIIVRELTGGLYFG 141
Cdd:PRK09222   84 LN---------VTLRKTLGLYANVRP------CVSYHPFVETKHPNLDVVIIRENEEDLYAG 130
PLN00118 PLN00118
isocitrate dehydrogenase (NAD+)
 9-141 7.49e-07

isocitrate dehydrogenase (NAD+)


Pssm-ID: 215062  Cd Length: 372  Bit Score: 47.57  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   9 PGDGIGPEIMAGTLEILNELATKFNFNCHVdtydIGGCAIDRYGTPLPNETLhacqnaDAILLGAIG--GPKwENPDCRP 86
Cdd:PLN00118   48 PGDGIGPEIAESVKQVFTAAGVPIEWEEHY----VGTTVDPRTGSFLTWESL------ESVRRNKVGlkGPM-ATPIGKG 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1946390195  87 EHDL-LQLRKALNLYANIRPTrvtpYTVdlsPIKREIVNQTDLIIVRELTGGLYFG 141
Cdd:PLN00118  117 HRSLnLTLRKELGLYANVRPC----YSL---PGYKTRYDDVDLVTIRENTEGEYSG 165
PLN00123 PLN00123
isocitrate dehydrogenase (NAD+)
 8-170 8.30e-06

isocitrate dehydrogenase (NAD+)


Pssm-ID: 215065  Cd Length: 360  Bit Score: 44.47  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195   8 LPGDGIGPEIMAGTLEILNELATKFNFnchvDTYDIGGCAIDrygtpLPNETLHACQNADAILLGAIGGPKWENPDCRPe 87
Cdd:PLN00123   36 IPGDGIGPLVTGAVEQVMEAMHAPVYF----ERYEVHGDMKK-----VPEEVLESIRRNKVCLKGGLATPVGGGVSSLN- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  88 hdlLQLRKALNLYANIrptrVTPYTVDLSPIKREIVnqtDLIIVRELTGGLYFGEpryfnANEAVDTLAYSEAEIT---- 163
Cdd:PLN00123  106 ---VQLRKELDLFASL----VNCFNLPGLPTRHENV---DIVVIRENTEGEYSGL-----EHEVVPGVVESLKVITkfcs 170


                  ....*...
gi 1946390195 164 -RIAHYCF 170
Cdd:PLN00123  171 eRIAKYAF 178
PRK07006 PRK07006
isocitrate dehydrogenase; Reviewed
 10-141 1.05e-04

isocitrate dehydrogenase; Reviewed


Pssm-ID: 180792  Cd Length: 409  Bit Score: 41.59  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  10 GDGIGPEIMAGTLEILNELATK-FNFNCHVDTYDI--GGCAIDRYGTP--LPNETLHACQNadaiLLGAIGGPkWENPDC 84
Cdd:PRK07006   27 GDGIGPDITPAMLKVVDAAVEKaYKGERKISWMEIyaGEKATKVYGEDvwLPEETLDLIRE----YRVAIKGP-LTTPVG 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946390195  85 RPEHDL-LQLRKALNLYANIRPTRV---TPytvdlSPIKREivNQTDLIIVRELTGGLYFG 141
Cdd:PRK07006  102 GGIRSLnVALRQELDLYVCLRPVRYfkgVP-----SPVKRP--EDTDMVIFRENSEDIYAG 155
PRK07362 PRK07362
NADP-dependent isocitrate dehydrogenase;
10-141 7.74e-04

NADP-dependent isocitrate dehydrogenase;


Pssm-ID: 180944  Cd Length: 474  Bit Score: 38.93  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946390195  10 GDGIGPEIMAGTLEILNE-LATKFNFNCHVDTYDI--GGCAIDRYGT--PLPNETLHACQNADAILLGAI-----GGPKW 79
Cdd:PRK07362   36 GDGTGVDIWPATQKVLDAaVAKAYGGERKINWFKVyaGDEACDLYGTyqYLPEDTLEAIREYGVAIKGPLttpigGGIRS 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1946390195  80 ENpdcrpehdlLQLRKALNLYANIRPTRVTPYTVdlSPIKREivNQTDLIIVRELTGGLYFG 141
Cdd:PRK07362  116 LN---------VALRQIFDLYSCVRPCRYYAGTP--SPHKNP--EKLDVIVYRENTEDIYMG 164
 
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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