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Conserved domains on  [gi|1600164096|gb|TEU15091|]
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MAG: ketol-acid reductoisomerase [Hadesarchaea archaeon]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 1-319 0e+00

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


:

Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 574.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPD 79
Cdd:COG0059     4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  80 EYQAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQ 159
Cdd:COG0059    84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 160 LALAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHG 239
Cdd:COG0059   164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIYEGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 240 IEGMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:COG0059   244 IANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAELRA 323
 
Name Accession Description Interval E-value
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 1-319 0e+00

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 574.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPD 79
Cdd:COG0059     4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  80 EYQAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQ 159
Cdd:COG0059    84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 160 LALAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHG 239
Cdd:COG0059   164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIYEGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 240 IEGMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:COG0059   244 IANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAELRA 323
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 1-319 0e+00

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 572.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPD 79
Cdd:PRK05479    4 VYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMILLPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  80 EYQAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQ 159
Cdd:PRK05479   84 EVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGNAKD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 160 LALAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHG 239
Cdd:PRK05479  164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIYEGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 240 IEGMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:PRK05479  244 IANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAKLRA 323
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 12-325 1.92e-150

ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273093 [Multi-domain]  Cd Length: 314  Bit Score: 424.87  E-value: 1.92e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDP-SYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEYQAGIYKKDI 90
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGGaSWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  91 EQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQLALAMAKGVGL 170
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 171 TRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHGIEGMMRAVSNT 250
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600164096 251 AEYGGRTRGKwVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRKWAGIEK 325
Cdd:TIGR00465 241 AEYGALTRRR-IIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 11-174 1.98e-91

Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.


Pssm-ID: 285265  Cd Length: 165  Bit Score: 269.42  E-value: 1.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  11 PLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEYQAGIYKKD 89
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  90 IEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQLALAMAKGVG 169
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
gi 1600164096 170 LTRIG 174
Cdd:pfam07991 161 GTRAG 165
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
12-110 5.50e-09

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 54.38  E-value: 5.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDP-SYDQAVKDGFEVYDIAEAAKRGDIIHTlipdeyqA----GIY 86
Cdd:smart00997  21 LAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEI-DPiRALEAAMDGFEVMKMEEAAKRADIFVT-------AtgnkDVI 92

                           90       100
                   ....*....|....*....|....*
gi 1600164096   87 KKDIEQHMKRGKALCfshgfNI-HF 110
Cdd:smart00997  93 TREHFRAMKDGAILA-----NAgHF 112
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 14-72 1.50e-07

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 52.46  E-value: 1.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDPSYD-QAVKDGFEVYDIAEAAKRGDI 72
Cdd:cd00401   195 GKVVVVAGYGWVGKGCAMRARGLGARVIVTEV-DPICAlQAAMDGFEVMPMEEAAKIGDI 253
 
Name Accession Description Interval E-value
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 1-319 0e+00

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 574.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPD 79
Cdd:COG0059     4 IYYDKDADLSLLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEEDGFEVMTVAEAAKRADVIMILTPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  80 EYQAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQ 159
Cdd:COG0059    84 EVQAAVYEEEIAPNLKPGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGFGVPALIAVHQDATGKAKD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 160 LALAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHG 239
Cdd:COG0059   164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTALIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIYEGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 240 IEGMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:COG0059   244 IANMRYSISNTAEYGDYTRGPRVITEEVKEEMKKVLDDIQSGEFAKEWILENQAGRPNLNALRAEEAEHPIEKVGAELRA 323
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 1-319 0e+00

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 572.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPD 79
Cdd:PRK05479    4 VYYDKDADLSLIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVGLREGsKSWKKAEADGFEVLTVAEAAKWADVIMILLPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  80 EYQAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQ 159
Cdd:PRK05479   84 EVQAEVYEEEIEPNLKEGAALAFAHGFNIHFGQIVPPADVDVIMVAPKGPGHLVRREYEEGGGVPCLIAVHQDASGNAKD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 160 LALAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHG 239
Cdd:PRK05479  164 LALAYAKGIGGTRAGVIETTFKEETETDLFGEQAVLCGGLTELIKAGFETLVEAGYQPEMAYFECLHELKLIVDLIYEGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 240 IEGMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:PRK05479  244 IANMRYSISNTAEYGDYVSGPRVITEETKKEMKEVLKDIQSGEFAKEWILENKAGRPTFKALRREEAEHPIEKVGAKLRA 323
ilvC TIGR00465
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
 12-325 1.92e-150

ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273093 [Multi-domain]  Cd Length: 314  Bit Score: 424.87  E-value: 1.92e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDP-SYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEYQAGIYKKDI 90
Cdd:TIGR00465   1 LKGKTVAIIGYGSQGHAQALNLRDSGLNVIVGLRKGGaSWKKATEDGFKVGTVEEAIPQADLIMNLLPDEVQHEVYEAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  91 EQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQLALAMAKGVGL 170
Cdd:TIGR00465  81 QPLLKEGKTLGFSHGFNIHFVQIVPPKDVDVVMVAPKGPGTLVREEYKEGFGVPTLIAVEQDPTGEAMAIALAYAKAIGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 171 TRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHGIEGMMRAVSNT 250
Cdd:TIGR00465 161 GRAGVLETTFKEETESDLFGEQAVLCGGLTALIKAGFDTLVEAGYQPELAYFETVHELKLIVDLIYEGGITGMRDRISNT 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600164096 251 AEYGGRTRGKwVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRKWAGIEK 325
Cdd:TIGR00465 241 AEYGALTRRR-IIKEELKPEMQKILKEIQNGEFAKEWALENEAGKPAFNTARKYESEHEIEKVGKELRAMVPAGK 314
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 2-319 9.49e-130

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 373.31  E-value: 9.49e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   2 FYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEY 81
Cdd:PRK13403    4 YYEKDANVELLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVGVRPGKSFEVAKADGFEVMSVSEAVRTAQVVQMLLPDEQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  82 QAGIYKKDIEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQLA 161
Cdd:PRK13403   84 QAHVYKAEVEENLREGQMLLFSHGFNIHFGQINPPSYVDVAMVAPKSPGHLVRRVFQEGNGVPALVAVHQDATGTALHVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 162 LAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHGIE 241
Cdd:PRK13403  164 LAYAKGVGCTRAGVIETTFQEETETDLFGEQAVLCGGVTALVKAGFETLTEGGYRPEIAYFECLHELKLIVDLMYEGGLT 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1600164096 242 GMMRAVSNTAEYGGRTRGKWVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLRK 319
Cdd:PRK13403  244 NMRHSISDTAEFGDYVTGSRIVTDETKKEMKRVLTEIQQGEFAKKWILENQAGRPTYNAMKKAEQNHQLEKVGEELRE 321
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 11-174 1.98e-91

Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.


Pssm-ID: 285265  Cd Length: 165  Bit Score: 269.42  E-value: 1.98e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  11 PLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKD-PSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEYQAGIYKKD 89
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVGLREGsKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDEVQAEVYEEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  90 IEQHMKRGKALCFSHGFNIHFKQILPPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAVAQDASGQAKQLALAMAKGVG 169
Cdd:pfam07991  81 IAPNLKEGAALAFAHGFNIHFGQIKPPKDVDVIMVAPKGPGHLVRREYEEGGGVPALIAVHQDASGKAKDLALAYAKGIG 160


                  ....*
gi 1600164096 170 LTRIG 174
Cdd:pfam07991 161 GTRAG 165
IlvC pfam01450
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ...
 181-318 1.07e-74

Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.


Pssm-ID: 460215 [Multi-domain]  Cd Length: 138  Bit Score: 225.81  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 181 KEEVETDLFGEQAVLVGGVSELMKAGFETLVQAGYQPEIAYFECVNELKLIIDLVYEHGIEGMMRAVSNTAEYGGRTRGK 260
Cdd:pfam01450   1 KEETETDLFGEQAVLCGGVTGLVKAGFETLVEAGYQPEAAYFECLHELKLIVDLIYEGGIAGMRYSISDTAEYGDLTRGP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1600164096 261 WVIDERARETMKKMLAEVQNGKFAKDWAAESQRGIPELKRMREEANEHLVEKVGRDLR 318
Cdd:pfam01450  81 RVIYDATKELMKEILDEIQSGEFAKEWILEYQAGRPELKALRREEAEHPIEKVGKELR 138
PRK05225 PRK05225
ketol-acid reductoisomerase; Validated
 12-312 1.15e-40

ketol-acid reductoisomerase; Validated


Pssm-ID: 235368 [Multi-domain]  Cd Length: 487  Bit Score: 148.18  E-value: 1.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVII----GSI--KDPSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDEYQAGI 85
Cdd:PRK05225   34 LKGKKIVIVGCGAQGLNQGLNMRDSGLDISYalrkEAIaeKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  86 YKKdIEQHMKRGKALCFSHGFNI--HFKQIlpPKDIDVIMIAPKAPGAILRRMYQQGSGTPGLLAV--AQDASGQAKQLA 161
Cdd:PRK05225  114 VRA-VQPLMKQGAALGYSHGFNIveVGEQI--RKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVhpENDPKGEGMAIA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 162 LAMAKGVGLTRIGVVETTFKEEVETDLFGEQAVLVGgvseLMKAG----FETLVQAGYQPE-----IAY-FECVNE-LKl 230
Cdd:PRK05225  191 KAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCG----MLQAGsllcFDKLVAEGTDPAyaeklIQFgWETITEaLK- 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096 231 iidlvyEHGIEGMMRAVSNTAEYggrtrgkwvideRA---RETMKKMLA--------EVQNGKFAK----DWAAESQrgi 295
Cdd:PRK05225  266 ------QGGITLMMDRLSNPAKI------------RAfelSEQLKEIMAplfqkhmdDIISGEFSStmmaDWANDDK--- 324

                         330
                  ....*....|....*..
gi 1600164096 296 pELKRMREEANEHLVEK 312
Cdd:PRK05225  325 -KLLTWREETGKTAFEN 340
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
12-110 5.50e-09

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 54.38  E-value: 5.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDP-SYDQAVKDGFEVYDIAEAAKRGDIIHTlipdeyqA----GIY 86
Cdd:smart00997  21 LAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEI-DPiRALEAAMDGFEVMKMEEAAKRADIFVT-------AtgnkDVI 92

                           90       100
                   ....*....|....*....|....*
gi 1600164096   87 KKDIEQHMKRGKALCfshgfNI-HF 110
Cdd:smart00997  93 TREHFRAMKDGAILA-----NAgHF 112
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 12-75 3.49e-08

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 54.36  E-value: 3.49e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDPSYD-QAVKDGFEVYDIAEAAKRGDIIHT 75
Cdd:PRK05476  210 IAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEV-DPICAlQAAMDGFRVMTMEEAAELGDIFVT 273
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
14-75 1.47e-07

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 50.43  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600164096  14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDP-SYDQAVKDGFEVYDIAEAAKRGDIIHT 75
Cdd:pfam00670  23 GKVAVVCGYGDVGKGCAASLKGQGARVIVTEI-DPiCALQAAMEGFQVVTLEEVVDKADIFVT 84
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 14-72 1.50e-07

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619 [Multi-domain]  Cd Length: 402  Bit Score: 52.46  E-value: 1.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDPSYD-QAVKDGFEVYDIAEAAKRGDI 72
Cdd:cd00401   195 GKVVVVAGYGWVGKGCAMRARGLGARVIVTEV-DPICAlQAAMDGFEVMPMEEAAKIGDI 253
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
14-75 1.76e-07

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 52.16  E-value: 1.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600164096   14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDP-SYDQAVKDGFEVYDIAEAAKRGDIIHT 75
Cdd:smart00996 207 GKVAVVCGYGDVGKGCAQSLRGQGARVIVTEI-DPiCALQAAMDGFEVVTMEEVAPQADIFVT 268
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 12-75 1.31e-06

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 49.65  E-value: 1.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkDP-SYDQAVKDGFEVYDIAEAAKRGDIIHT 75
Cdd:PTZ00075  252 IAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEI-DPiCALQAAMEGYQVVTLEDVVETADIFVT 315
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
14-75 1.40e-06

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 49.28  E-value: 1.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1600164096  14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIkdpsyD-----QAVKDGFEVYDIAEAAKRGDIIHT 75
Cdd:COG0499   209 GKTVVVAGYGWCGKGVAMRARGLGARVIVTEV-----DpicalEAAMDGFRVMPMEEAAKLGDIFVT 270
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 12-100 3.31e-06

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 48.06  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKdgfEVyDIAEAAKRGDIIHTLIP-DEYQAGIYKKDI 90
Cdd:cd12179   136 LMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAYAE---QV-SLETLFKEADILSLHIPlTPETRGMVNKEF 211

                          90
                  ....*....|....*....
gi 1600164096  91 EQHMK---------RGKAL 100
Cdd:cd12179   212 ISSFKkpfyfintaRGKVV 230
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 12-97 3.62e-06

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 47.82  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIgsikdpsYD-----QAVKDGFEVYDIAEAAKRGDII--HT-LIPDEYQA 83
Cdd:cd12183   142 LHGKTVGVIGTGKIGQAFARILKGFGCRVLA-------YDpypnpELAKLGVEYVDLDELLAESDIIslHCpLTPETHHL 214

                          90
                  ....*....|....
gi 1600164096  84 gIYKKDIEQhMKRG 97
Cdd:cd12183   215 -INAETIAK-MKDG 226
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 12-97 8.36e-06

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 45.56  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDII--HT-LIPDEYqaGIYKK 88
Cdd:pfam02826  34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVslHLpLTPETR--HLINA 111


                  ....*....
gi 1600164096  89 DIEQHMKRG 97
Cdd:pfam02826 112 ERLALMKPG 120
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 12-73 1.83e-05

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 45.70  E-value: 1.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKdPSYDQAVKDGFEVYDIAEAAKRGDII 73
Cdd:cd05198   138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRT-RKPEPEEDLGFRVVSLDELLAQSDVV 198
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 12-97 9.95e-05

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 43.46  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDS-GCKVIigsIKDPSYDQAV--KDGFEVYDIAEAAKRGDII--HTLIPDEYQAGIY 86
Cdd:cd12177   145 LSGKTVGIIGYGNIGSRVAEILKEGfNAKVL---AYDPYVSEEVikKKGAKPVSLEELLAESDIIslHAPLTEETYHMIN 221

                          90
                  ....*....|.
gi 1600164096  87 KKDIEQhMKRG 97
Cdd:cd12177   222 EKAFSK-MKKG 231
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 12-101 1.10e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 43.39  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKViIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDIIHTLIP-DEYQAGIYKKDI 90
Cdd:cd12165   135 LRGKTVGILGYGHIGREIARLLKAFGMRV-IGVSRSPKEDEGADFVGTLSDLDEALEQADVVVVALPlTKQTRGLIGAAE 213

                          90
                  ....*....|.
gi 1600164096  91 EQHMKRGKALC 101
Cdd:cd12165   214 LAAMKPGAILV 224
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 2-73 1.10e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 43.30  E-value: 1.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1600164096   2 FYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIigsIKDPSYDQAV--KDGFEVYDIAEAAKRGDII 73
Cdd:cd12171   135 YYNYDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVL---VYDPYVDPEKieADGVKKVSLEELLKRSDVV 205
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 16-100 1.83e-04

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 41.30  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  16 TVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYD-IAEAAKRGDIIHTLIPDEYQAG--IYKKDIEQ 92
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAsPAEFVAGLDVVITMVPAGAAVDavIFGEGLLP 80


                  ....*...
gi 1600164096  93 HMKRGKAL 100
Cdd:pfam03446  81 GLKPGDII 88
PLN02494 PLN02494
adenosylhomocysteinase
 14-98 2.27e-04

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 42.54  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  14 GKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDIIHTLIPDeyqagiykKDI--E 91
Cdd:PLN02494  254 GKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGN--------KDIimV 325


                  ....*..
gi 1600164096  92 QHMKRGK 98
Cdd:PLN02494  326 DHMRKMK 332
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 6-97 4.16e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 41.28  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   6 DADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEvydiaEAAKRGDII--HTLIPDEYQA 83
Cdd:cd12162   139 DYPIIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPLREGYVSLD-----ELLAQSDVIslHCPLTPETRN 213

                          90
                  ....*....|....
gi 1600164096  84 GIYKKDIEQhMKRG 97
Cdd:cd12162   214 LINAEELAK-MKPG 226
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 12-97 9.04e-04

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 40.60  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSyDQAVKDGFEVYDIAEAAKRGDII--HTLIPDEYQAGIYKKD 89
Cdd:cd05303   137 LRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKD-EQAVELGVKTVSLEELLKNSDFIslHVPLTPETKHMINKKE 215


                  ....*...
gi 1600164096  90 IEQhMKRG 97
Cdd:cd05303   216 LEL-MKDG 222
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 12-73 1.00e-03

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 40.18  E-value: 1.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKdPSYDQAVKDGFE-VYDIAEAAKRGDII 73
Cdd:COG0111   138 LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYDPS-PKPEEAADLGVGlVDSLDELLAEADVV 199
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 1-97 1.12e-03

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 40.26  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096   1 MFYDKDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVI----IGSIKDPsYDQAVKDGfevyDIAEAAKRGDIIHTL 76
Cdd:cd12155   122 KKWKMDSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVIgvntSGRDVEY-FDKCYPLE----ELDEVLKEADIVVNV 196

                          90       100
                  ....*....|....*....|..
gi 1600164096  77 IP-DEYQAGIYKKDIEQHMKRG 97
Cdd:cd12155   197 LPlTEETHHLFDEAFFEQMKKG 218
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
17-73 1.31e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 39.38  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1600164096  17 VAIIGYGNQGQAQANNLRDSGCKVIIGSiKDP-SYDQAVKD---GFEVYDIAEAAKRGDII 73
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGS-RDPeKAAALAAElgpGARAGTNAEAAAAADVV 60
ELFV_dehydrog pfam00208
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;
5-70 1.62e-03

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase;


Pssm-ID: 425526 [Multi-domain]  Cd Length: 240  Bit Score: 39.42  E-value: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1600164096   5 KDADLSPLDGKTVAIIGYGNQGQAQANNLRDSGCKVIigSIKDPS---YDqavKDGFEVYDIAEAAKRG 70
Cdd:pfam00208  23 KKLGGDSLEGKRVAIQGFGNVGSYAALKLHELGAKVV--AVSDSSgaiYD---PDGLDIEELLELKEER 86
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 12-101 1.64e-03

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 39.52  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIK--DPSYDqAVKDGFEVYDIAEAAKRGDII--HTLIPDEYQAGIYK 87
Cdd:cd12154   158 VAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINveALEQL-EELGGKNVEELEEALAEADVIvtTTLLPGKRAGILVP 236

                          90
                  ....*....|....
gi 1600164096  88 KDIEQHMKRGKALC 101
Cdd:cd12154   237 EELVEQMKPGSVIV 250
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 12-73 2.40e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 39.01  E-value: 2.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKdPSYDQAVKDGFEVYDIAEAAKRGDII 73
Cdd:cd12172   140 LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPY-PDEEFAKEHGVEFVSLEELLKESDFI 200
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 11-75 4.30e-03

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 38.28  E-value: 4.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  11 PLDGKTVAIIGYGNQGQAQANNLRDSGCKVIIgsikdpsYD--QAVKDGFEVY-DIAEAAKRGDII--HT 75
Cdd:cd12158   112 SLKGKTVGIVGVGNVGSRLARRLEALGMNVLL-------CDppRAEAEGDPGFvSLEELLAEADIItlHV 174
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 12-97 5.41e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 37.94  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDII--H-TLIPDEyqAGIYKK 88
Cdd:cd12175   140 LSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDVVslHvPLTPET--RHLIGA 217


                  ....*....
gi 1600164096  89 DIEQHMKRG 97
Cdd:cd12175   218 EELAAMKPG 226
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
 5-72 5.69e-03

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 38.12  E-value: 5.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600164096   5 KDADLSpLDGKTVAIIGYGNQGQAQANNLRDSGCKVIigSIKDPS---YDqavKDGFEVYDIAE-AAKRGDI 72
Cdd:COG0334   200 KKLGLS-LEGKTVAVQGFGNVGSYAAELLHELGAKVV--AVSDSSggiYD---PDGIDLDALKEhKEERGSV 265
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 16-97 6.35e-03

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 37.90  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  16 TVAIIGYGNQGQAQANNLRDSGCKVIigsIKDPSYDQAVKD-GFEVYDIAEAAKRGDII--HT-LIPDEYqaGIYKKDIE 91
Cdd:cd12186   147 TVGIIGTGRIGSAAAKIFKGFGAKVI---AYDPYPNPELEKfLLYYDSLEDLLKQADIIslHVpLTKENH--HLINAEAF 221


                  ....*.
gi 1600164096  92 QHMKRG 97
Cdd:cd12186   222 AKMKDG 227
PLN02928 PLN02928
oxidoreductase family protein
 12-100 7.80e-03

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 37.74  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVII------------GSIKDPSYDQAVKDGFEVYDIAEAAKRGDIIHTLIP- 78
Cdd:PLN02928  157 LFGKTVFILGYGAIGIELAKRLRPFGVKLLAtrrswtsepedgLLIPNGDVDDLVDEKGGHEDIYEFAGEADIVVLCCTl 236

                          90       100
                  ....*....|....*....|..
gi 1600164096  79 DEYQAGIYKKDIEQHMKRGKAL 100
Cdd:PLN02928  237 TKETAGIVNDEFLSSMKKGALL 258
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 12-73 8.80e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 37.22  E-value: 8.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600164096  12 LDGKTVAIIGYGNQGQAQANNLRDSGCKVIIGSIKDPSYDQAVKDGFEVYDIAEAAKRGDII 73
Cdd:cd12178   142 LAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHRLSEETEKELGATYVDLDELLKESDFV 203
 
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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