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Conserved domains on  [gi|7546447|pdb|1D3A|A]
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Chain A, Crystal Structure Of The Wild Type Halophilic Malate Dehydrogenase In The Apo Form

Protein Classification

malate dehydrogenase (domain architecture ID 11482142)

malate dehydrogenase catalyzes the oxidation of malate to oxaloacetate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06223 PRK06223
malate dehydrogenase; Reviewed
18-303 1.57e-132

malate dehydrogenase; Reviewed


:

Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 377.93  E-value: 1.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        18 YNIALRDIADeVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQGG--YEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:PRK06223  19 HLLALKELGD-VVLFDI--VEGVPQGKALDIAEAAPVEGFDTKITGTndYEDIAGSDVVVITAGVPRKPGMSRDDLLGIN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:PRK06223  96 AKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIAEELNVSVKDVTAFVLGGH 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       176 GDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:PRK06223 176 GDSMVPLVRYSTVGGIPLEdlLSKEKLDEIVERTRKGGAEIVGllKTGSAYYAPAASIAEMVEAILKDKKRVLPCSAYLE 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
1D3A_A       252 GEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKIS 303
Cdd:PRK06223 256 GEYGVKDVYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVKKLIEALK 307
 
Name Accession Description Interval E-value
PRK06223 PRK06223
malate dehydrogenase; Reviewed
18-303 1.57e-132

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 377.93  E-value: 1.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        18 YNIALRDIADeVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQGG--YEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:PRK06223  19 HLLALKELGD-VVLFDI--VEGVPQGKALDIAEAAPVEGFDTKITGTndYEDIAGSDVVVITAGVPRKPGMSRDDLLGIN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:PRK06223  96 AKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIAEELNVSVKDVTAFVLGGH 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       176 GDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:PRK06223 176 GDSMVPLVRYSTVGGIPLEdlLSKEKLDEIVERTRKGGAEIVGllKTGSAYYAPAASIAEMVEAILKDKKRVLPCSAYLE 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
1D3A_A       252 GEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKIS 303
Cdd:PRK06223 256 GEYGVKDVYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVKKLIEALK 307
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
18-300 3.37e-113

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 328.66  E-value: 3.37e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADeVVFVDIPdkEDDTVGQAADTNHGIA-YDSNTRVRQGG-YEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:cd01339  15 QLLALKELGD-VVLLDIV--EGLPQGKALDISQAAPiLGSDTKVTGTNdYEDIAGSDVVVITAGIPRKPGMSRDDLLGTN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:cd01339  92 AKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEELGVSVKDVQAMVLGGH 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      176 GDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIERK--GATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:cd01339 172 GDTMVPLPRYSTVGGIPLTelITKEEIDEIVERTRNGGAEIVNLLktGSAYYAPAAAIAEMVEAILKDKKRVLPCSAYLE 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1D3A_A      252 GEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD 300
Cdd:cd01339 252 GEYGIKDIFVGVPVVLGKNGVEKIIELDLTDEEKEAFDKSVESVKELID 300
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion];
18-302 6.01e-102

Malate/lactate dehydrogenase [Energy production and conversion];


Pssm-ID: 223117 [Multi-domain]  Cd Length: 313  Bit Score: 300.62  E-value: 6.01e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADEVVFVDIPdkEDDTVGQAADTNHGIAY-DSNTRVR-QGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:COG0039  17 FLLLLQGLGSELVLIDIN--EEKAEGVALDLSHAAAPlGSDVKITgDGDYEDLKGADIVVITAGVPRKPGMTRLDLLEKN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:COG0039  95 AKIVKDIAKAIAKYAPDAIVLVVTNPVDILTYIAMKFSGFPKNRVIGSGTVLDSARFRTFLAEKLGVSPKDVHAYVIGEH 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      176 GDAQVPVFSKVRVDGTD-----PEFSGDEKEQLLGDLQESAMDVIERKGA-TEWGPARGVAHMVEAILHDTGEVLPASVK 249
Cdd:COG0039 175 GDTMVPLWSQATVGGKPleellKEDTEEDLEELIERVRNAGAEIIEAKGAgTYYGPAAALARMVEAILRDEKRVLPVSVY 254
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
1D3A_A      250 LEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKI 302
Cdd:COG0039 255 LDGEYGVEDVYFGVPAVLGKNGVEEILELLLSDDEQEKLDKSAEELKKNIELV 307
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
18-295 2.48e-88

L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme function as as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of malate dehydrogenases. [Energy metabolism, Anaerobic, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273796 [Multi-domain]  Cd Length: 299  Bit Score: 265.60  E-value: 2.48e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         18 YNIALRDIADEVVFVDIpdKEDDTVGQAADTNHGIA-YDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:TIGR01771  13 FALLNQGIADEIVLIDI--NKDKAEGEAMDLQHAASfLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGETRLELVGRNV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHG 176
Cdd:TIGR01771  91 RIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQSVHAYIIGEHG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        177 DAQVPVFSKVRVDG--------TDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASV 248
Cdd:TIGR01771 171 DSEVPVWSSATIGGvplldylkAKGTETDLDLEEIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAILHDENRVLPVSA 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
1D3A_A        249 KLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKL 295
Cdd:TIGR01771 251 YLDGEYGIKDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETL 297
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
18-142 1.39e-44

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 333804 [Multi-domain]  Cd Length: 140  Bit Score: 148.13  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         18 YNIALRDIADEVVFVDIPdkEDDTVGQAADTNHGIAYDS-NTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:pfam00056  17 FLLANQGLADELVLVDIA--KDKLEGVAMDLSHGSTFLPvPGIVGGGDYEDLKDADVVVITAGAPRKPGMTRLDLLNRNA 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1D3A_A         97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIG 142
Cdd:pfam00056  95 KIFKEIGPAVAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 140
 
Name Accession Description Interval E-value
PRK06223 PRK06223
malate dehydrogenase; Reviewed
18-303 1.57e-132

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 377.93  E-value: 1.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        18 YNIALRDIADeVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQGG--YEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:PRK06223  19 HLLALKELGD-VVLFDI--VEGVPQGKALDIAEAAPVEGFDTKITGTndYEDIAGSDVVVITAGVPRKPGMSRDDLLGIN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:PRK06223  96 AKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIAEELNVSVKDVTAFVLGGH 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       176 GDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:PRK06223 176 GDSMVPLVRYSTVGGIPLEdlLSKEKLDEIVERTRKGGAEIVGllKTGSAYYAPAASIAEMVEAILKDKKRVLPCSAYLE 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
1D3A_A       252 GEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKIS 303
Cdd:PRK06223 256 GEYGVKDVYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVKKLIEALK 307
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
18-300 3.37e-113

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 328.66  E-value: 3.37e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADeVVFVDIPdkEDDTVGQAADTNHGIA-YDSNTRVRQGG-YEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:cd01339  15 QLLALKELGD-VVLLDIV--EGLPQGKALDISQAAPiLGSDTKVTGTNdYEDIAGSDVVVITAGIPRKPGMSRDDLLGTN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:cd01339  92 AKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEELGVSVKDVQAMVLGGH 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      176 GDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIERK--GATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:cd01339 172 GDTMVPLPRYSTVGGIPLTelITKEEIDEIVERTRNGGAEIVNLLktGSAYYAPAAAIAEMVEAILKDKKRVLPCSAYLE 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1D3A_A      252 GEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD 300
Cdd:cd01339 252 GEYGIKDIFVGVPVVLGKNGVEKIIELDLTDEEKEAFDKSVESVKELID 300
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion];
18-302 6.01e-102

Malate/lactate dehydrogenase [Energy production and conversion];


Pssm-ID: 223117 [Multi-domain]  Cd Length: 313  Bit Score: 300.62  E-value: 6.01e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADEVVFVDIPdkEDDTVGQAADTNHGIAY-DSNTRVR-QGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDN 95
Cdd:COG0039  17 FLLLLQGLGSELVLIDIN--EEKAEGVALDLSHAAAPlGSDVKITgDGDYEDLKGADIVVITAGVPRKPGMTRLDLLEKN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       96 APIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:COG0039  95 AKIVKDIAKAIAKYAPDAIVLVVTNPVDILTYIAMKFSGFPKNRVIGSGTVLDSARFRTFLAEKLGVSPKDVHAYVIGEH 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      176 GDAQVPVFSKVRVDGTD-----PEFSGDEKEQLLGDLQESAMDVIERKGA-TEWGPARGVAHMVEAILHDTGEVLPASVK 249
Cdd:COG0039 175 GDTMVPLWSQATVGGKPleellKEDTEEDLEELIERVRNAGAEIIEAKGAgTYYGPAAALARMVEAILRDEKRVLPVSVY 254
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
1D3A_A      250 LEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKI 302
Cdd:COG0039 255 LDGEYGVEDVYFGVPAVLGKNGVEEILELLLSDDEQEKLDKSAEELKKNIELV 307
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
18-301 1.13e-89

L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133427 [Multi-domain]  Cd Length: 306  Bit Score: 269.34  E-value: 1.13e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADEVVFVDIpdKEDDTVGQAADTNHGIAY-DSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:cd05291  17 YSLVNQGIADELVLIDI--NEEKAEGEALDLEDALAFlPSPVKIKAGDYSDCKDADIVVITAGAPQKPGETRLDLLEKNA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHG 176
Cdd:cd05291  95 KIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKLNVDPRSVHAYVLGEHG 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      177 DAQVPVFSKVRVDG-------TDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVK 249
Cdd:cd05291 175 DSQFVAWSTVTVGGkplldllKEGKLSELDLDEIEEDVRKAGYEIINGKGATYYGIATALARIVKAILNDENAILPVSAY 254
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
1D3A_A      250 LEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDK 301
Cdd:cd05291 255 LDGEYGEKDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADIIKENIKK 306
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
18-300 1.35e-89

L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent 2-hydroxycarboxylate dehydrogenases including LDHs, L-2-hydroxyisocaproate dehydrogenases (L-HicDH), and LDH-like malate dehydrogenases (MDH). Dehydrogenases catalyze the conversion of carbonyl compounds to alcohols or amino acids. LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. L-HicDH catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133418 [Multi-domain]  Cd Length: 300  Bit Score: 268.75  E-value: 1.35e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADEVVFVDIpdKEDDTVGQAADTNHGIAYDSN-TRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:cd00300  15 FALIAKGLASELVLVDV--NEEKAKGDALDLSHASAFLATgTIVRGGDYADAADADIVVITAGAPRKPGETRLDLINRNA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHG 176
Cdd:cd00300  93 PILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLDVDPQSVHAYVLGEHG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      177 DAQVPVFSKVRVDGTD----PEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLEG 252
Cdd:cd00300 173 DSQVVAWSTATVGGLPleelAPFTKLDLEAIEEEVRTSGYEIIRLKGATNYGIATAIADIVKSILLDERRVLPVSAVQEG 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
1D3A_A      253 EFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYD 300
Cdd:cd00300 253 QYGIEDVALSVPAVVGREGVVRILEIPLTEDEEAKLQKSAEALKEVLN 300
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
18-295 2.48e-88

L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme function as as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of malate dehydrogenases. [Energy metabolism, Anaerobic, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273796 [Multi-domain]  Cd Length: 299  Bit Score: 265.60  E-value: 2.48e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         18 YNIALRDIADEVVFVDIpdKEDDTVGQAADTNHGIA-YDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:TIGR01771  13 FALLNQGIADEIVLIDI--NKDKAEGEAMDLQHAASfLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGETRLELVGRNV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHG 176
Cdd:TIGR01771  91 RIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQSVHAYIIGEHG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        177 DAQVPVFSKVRVDG--------TDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASV 248
Cdd:TIGR01771 171 DSEVPVWSSATIGGvplldylkAKGTETDLDLEEIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAILHDENRVLPVSA 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
1D3A_A        249 KLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKL 295
Cdd:TIGR01771 251 YLDGEYGIKDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETL 297
ldh PRK00066
L-lactate dehydrogenase; Reviewed
25-302 2.87e-83

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 253.28  E-value: 2.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        25 IADEVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQS 104
Cdd:PRK00066  30 IADELVIIDI--NKEKAEGDAMDLSHAVPFTSPTKIYAGDYSDCKDADLVVITAGAPQKPGETRLDLVEKNLKIFKSIVG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       105 SLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFS 184
Cdd:PRK00066 108 EVMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYMLSEKLDVDPRSVHAYIIGEHGDTEFPVWS 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       185 KVRVDG--------TDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLEGEFGH 256
Cdd:PRK00066 188 HANVAGvpleeyleENEQYDEEDLDEIFENVRDAAYEIIEKKGATYYGIAMALARITKAILNNENAVLPVSAYLEGQYGE 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
1D3A_A       257 EDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSDQYDKI 302
Cdd:PRK00066 268 EDVYIGVPAVVNRNGIREIVELPLNDDEKQKFAHSADVLKEIMDEA 313
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
18-297 3.55e-80

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133428 [Multi-domain]  Cd Length: 308  Bit Score: 245.09  E-value: 3.55e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       18 YNIALRDIADEVVFVDIpDKeDDTVGQAADTNHGIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAP 97
Cdd:cd05292  17 YALLLRGLASEIVLVDI-NK-AKAEGEAMDLAHGTPFVKPVRIYAGDYADCKGADVVVITAGANQKPGETRLDLLKRNVA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       98 IMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGD 177
Cdd:cd05292  95 IFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHLGVDPRSVHAYIIGEHGD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      178 AQVPVFSKVRVDGTD---------PEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASV 248
Cdd:cd05292 175 SEVAVWSSANIGGVPldefcklcgRPFDEEVREEIFEEVRNAAYEIIERKGATYYAIGLALARIVEAILRDENSVLTVSS 254
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1D3A_A      249 KLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSD 297
Cdd:cd05292 255 LLDGQYGIKDVALSLPCIVGRSGVERVLPPPLSEEEEEALRASAEVLKE 303
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
20-297 6.39e-60

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of eukaryotic LDHs. Vertebrate LDHs are non-allosteric. This is in contrast to some bacterial LDHs that are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133429 [Multi-domain]  Cd Length: 312  Bit Score: 193.20  E-value: 6.39e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       20 IALRDIADEVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQGG-YEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPI 98
Cdd:cd05293  22 ILAKGLADELVLVDV--VEDKLKGEAMDLQHGSAFLKNPKIEADKdYSVTANSKVVIVTAGARQNEGESRLDLVQRNVDI 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       99 MEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDA 178
Cdd:cd05293 100 FKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAERLGVAPSSVHGWIIGEHGDS 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      179 QVPVFSKVRVDGT-----DPEFSGDEKEQLLGDLQE----SAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVK 249
Cdd:cd05293 180 SVPVWSGVNVAGVrlqdlNPDIGTDKDPEKWKEVHKqvvdSAYEVIKLKGYTSWAIGLSVADLVDAILRNTGRVHSVSTL 259
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
1D3A_A      250 LEGEFGHEDTAF-GVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSD 297
Cdd:cd05293 260 VKGLHGIEDEVFlSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWE 308
MalateDH_bact TIGR01763
malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the ...
20-293 6.86e-57

malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the citric acid cycle. The critical residues which discriminate malate dehydrogenase from lactate dehydrogenase have been characterized, and have been used to set the cutoffs for this model. Sequences showing [aflimv][ap]R[rk]pgM[st] and [ltv][ilm]gGhgd were kept above trusted, while those in which the capitalized residues in the patterns were found to be Q, E and E were kept below the noise cutoff. Some sequences in the grey zone have been annotated as malate dehydrogenases, but none have been characterized. Phylogenetically, a clade of sequences from eukaryotes such as Toxoplasma and Plasmodium which include a characterized lactate dehydrogenase and show abiguous critical residue patterns appears to be more closely related to these bacterial sequences than other eukaryotic sequences. These are relatively long branch and have been excluded from the model. All other sequences falling below trusted appear to be phylogenetically outside of the clade including the trusted hits. The annotation of Botryococcus braunii as lactate dehydrogenase appears top be in error. This was initially annotated as MDH by Swiss-Prot and then changed. The rationale for either of these annotations is not traceable. [Energy metabolism, TCA cycle]


Pssm-ID: 273792 [Multi-domain]  Cd Length: 305  Bit Score: 185.46  E-value: 6.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         20 IALRDIADeVVFVDIpdKEDDTVGQAADTnhgiaYDS------NTRVR-QGGYEDTAGSDVVVITAGIPRQPGQTRIDLA 92
Cdd:TIGR01763  20 LAEKELAD-LVLLDV--VEGIPQGKALDM-----YEAspvggfDTKVTgTNNYADTANSDIVVITAGLPRKPGMSREDLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         93 GDNAPIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTIL 172
Cdd:TIGR01763  92 SMNAGIVREVTGRIMEHSPNPIIVVVSNPLDAMTYVAWQKSGFPKERVIGQAGVLDSARFRTFIAMELGVSVQDVTACVL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        173 GEHGDAQVPVFSKVRVDGTDPE--FSGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTGEVLPASV 248
Cdd:TIGR01763 172 GGHGDAMVPLVRYSTVAGIPVAdlISAERIAEIVERTRKGGGEIVNllKQGSAYYAPAASVVEMVEAILKDRKRVLPCAA 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
1D3A_A        249 KLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAE 293
Cdd:TIGR01763 252 YLDGQYGIDGIYVGVPVILGKNGVEHIYELKLDQSELALLNKSAK 296
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
28-295 1.24e-54

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of some bacterial LDHs from firmicutes, gammaproteobacteria, and actinobacteria. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133426 [Multi-domain]  Cd Length: 307  Bit Score: 179.45  E-value: 1.24e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       28 EVVFVDipDKEDDTVGQAADTNH--GIAYDSNTRVRQGGYEDTAGSDVVVITAGIPRQPGQT--RIDLAGDNAPIMEDIQ 103
Cdd:cd05290  26 EIVLID--VNEGVAEGEALDFHHatALTYSTNTKIRAGDYDDCADADIIVITAGPSIDPGNTddRLDLAQTNAKIIREIM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      104 SSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVF 183
Cdd:cd05290 104 GNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVADKYGVDPKNVTGYVLGEHGSHAFPVW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      184 SKV-----RVDGTDPEFSGD--EKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLEGEFGH 256
Cdd:cd05290 184 SLVniaglPLDELEALFGKEpiDKDELLEEVVQAAYDVFNRKGWTNAGIAKSASRLIKAILLDERSILPVCTLLSGEYGL 263
                       250       260       270
                ....*....|....*....|....*....|....*....
1D3A_A      257 EDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKL 295
Cdd:cd05290 264 SDVALSLPTVIGAKGIERVLEIPLDEWELEKLHKSAKAI 302
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
19-293 1.82e-54

A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The LDH-like MDH proteins have a lactate dehyhydrogenase-like (LDH-like) structure and malate dehydrogenase (MDH) enzymatic activity. This subgroup is composed of some archaeal LDH-like MDHs that prefer NADP(H) rather than NAD(H) as a cofactor. One member, MJ0490 from Methanococcus jannaschii, has been observed to form dimers and tetramers during crystalization, although it is believed to exist primarilly as a tetramer in solution. In addition to its MDH activity, MJ0490 also possesses fructose-1,6-bisphosphate-activated LDH activity. Members of this subgroup have a higher sequence similarity to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)- binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133430 [Multi-domain]  Cd Length: 309  Bit Score: 179.14  E-value: 1.82e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       19 NIALRDIADEVVFVDIPDKEDDTVGQAADTNHGIA-YDSNTRVRQGG-YEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:cd05294  19 LLAKEDVVKEINLISRPKSLEKLKGLRLDIYDALAaAGIDAEIKISSdLSDVAGSDIVIITAGVPRKEGMSRLDLAKKNA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLN-RHLYEAGdRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEH 175
Cdd:cd05294  99 KIVKKYAKQIAEFAPDTKILVVTNPVDVMTyKALKESG-FDKNRVFGLGTHLDSLRFKVAIAKHFNVHISEVHTRIIGEH 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      176 GDAQVPVFSKVRVDGTD----PEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVKLE 251
Cdd:cd05294 178 GDSMVPLISSTSIGGIPikrfPEYKDFDVEKIVETVKNAGQNIISLKGGSEYGPASAISNLVRTIANDERRILTVSTYLE 257
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
1D3A_A      252 GEF-GHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAE 293
Cdd:cd05294 258 GEIdGIRDVCIGVPVKLGKNGIEEIVPIEMDDDEREAFRKSAE 300
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
18-296 2.06e-52

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 174.11  E-value: 2.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        18 YNIALRDIADeVVFVDIpdKEDDTVGQAADTNHGIA-YDSNTRVR-QGGYEDTAGSDVVVITAGIPRQPGQT-----RID 90
Cdd:PTZ00082  23 YLIVLKNLGD-VVLFDI--VKNIPQGKALDISHSNViAGSNSKVIgTNNYEDIAGSDVVIVTAGLTKRPGKSdkewnRDD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        91 LAGDNAPIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGT 170
Cdd:PTZ00082 100 LLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTYIAEKLGVNPRDVHAS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       171 ILGEHGDAQVPVFSKVRVDGTD-PEF------SGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTG 241
Cdd:PTZ00082 180 VIGAHGDKMVPLPRYVTVGGIPlSEFikkgliTQEEIDEIVERTRNTGKEIVDllGTGSAYFAPAAAAIEMAEAYLKDKK 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
1D3A_A       242 EVLPASVKLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLS 296
Cdd:PTZ00082 260 RVLPCSAYLEGQYGHKDIYMGTPAVIGANGVEKIIELDLTPEEQKKFDESIKEVK 314
PLN02602 PLN02602
lactate dehydrogenase
20-297 9.19e-51

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 170.72  E-value: 9.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        20 IALRDIADEVVFVDIpdKEDDTVGQAADTNHGIAYDSNTRVRQG-GYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPI 98
Cdd:PLN02602  56 ILTQDLADELALVDV--NPDKLRGEMLDLQHAAAFLPRTKILAStDYAVTAGSDLCIVTAGARQIPGESRLNLLQRNVAL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        99 MEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDA 178
Cdd:PLN02602 134 FRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDS 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       179 QVPVFSKVRVDGT---------DPEFSGDEKEQLLGDLQESAMDVIERKGATEWGPARGVAHMVEAILHDTGEVLPASVK 249
Cdd:PLN02602 214 SVALWSSVSVGGVpvlsflekqQIAYEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGYSVASLVRSLLRDQRRIHPVSVL 293
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
1D3A_A       250 LEGEFG-HEDTAF-GVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLSD 297
Cdd:PLN02602 294 AKGFHGiDEGDVFlSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWE 343
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
20-296 2.02e-50

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 169.13  E-value: 2.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        20 IALRDIADeVVFVDIpdKEDDTVGQAADTNHGIAY-DSNTRVR-QGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAP 97
Cdd:PTZ00117  24 ILQKNLGD-VVLYDV--IKGVPQGKALDLKHFSTLvGSNINILgTNNYEDIKDSDVVVITAGVQRKEEMTREDLLTINGK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        98 IMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGD 177
Cdd:PTZ00117 101 IMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRCNLAEKLGVSPGDVSAVVIGGHGD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       178 AQVPVFSKVRVDG-------TDPEFSGDEKEQLLGDLQESAMDVIE--RKGATEWGPARGVAHMVEAILHDTGEVLPASV 248
Cdd:PTZ00117 181 LMVPLPRYCTVNGiplsdfvKKGAITEKEINEIIKKTRNMGGEIVKllKKGSAFFAPAAAIVAMIEAYLKDEKRVLVCSV 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
1D3A_A       249 KLEGEFGHEDTAFGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKLS 296
Cdd:PTZ00117 261 YLNGQYNCKNLFVGVPVVIGGKGIEKVIELELNAEEKELFDKSIESIQ 308
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
24-295 4.70e-47

NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members of this family include ubiquitous enzymes like L-lactate dehydrogenases (LDH), L-2-hydroxyisocaproate dehydrogenases, and some malate dehydrogenases (MDH). LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH/MDH-like proteins are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133419 [Multi-domain]  Cd Length: 263  Bit Score: 158.64  E-value: 4.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       24 DIADEVVFVDIPdkEDDTVGQAADTNHGIAYDSNTRVRQGG--YEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMED 101
Cdd:cd00650  24 LLAIELVLYDID--EEKLKGVAMDLQDAVEPLADIKVSITDdpYEAFKDADVVIITAGVGRKPGMGRLDLLKRNVPIVKE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      102 IQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFgGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQVP 181
Cdd:cd00650 102 IGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGL-GTLDPIRFRRILAEKLGVDPDDVKVYILGEHGGSQVP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      182 VFSKVRvdgtdpefsgdekeqllgdlqesamdvierkgatewgPARGVAHMVEAILHDTGEVLPASVKLEGEFGH-EDTA 260
Cdd:cd00650 181 DWSTVR-------------------------------------IATSIADLIRSLLNDEGEILPVGVRNNGQIGIpDDVV 223
                       250       260       270
                ....*....|....*....|....*....|....*
1D3A_A      261 FGVPVRLGSNGVEEIVEWDLDDYEQDLMADAAEKL 295
Cdd:cd00650 224 VSVPCIVGKNGVEEPIEVGLTDFELEKLQKSADTL 258
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
18-142 1.39e-44

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 333804 [Multi-domain]  Cd Length: 140  Bit Score: 148.13  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         18 YNIALRDIADEVVFVDIPdkEDDTVGQAADTNHGIAYDS-NTRVRQGGYEDTAGSDVVVITAGIPRQPGQTRIDLAGDNA 96
Cdd:pfam00056  17 FLLANQGLADELVLVDIA--KDKLEGVAMDLSHGSTFLPvPGIVGGGDYEDLKDADVVVITAGAPRKPGMTRLDLLNRNA 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1D3A_A         97 PIMEDIQSSLDEHNDDYISLTTSNPVDLLNRHLYEAGDRSREQVIG 142
Cdd:pfam00056  95 KIFKEIGPAVAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 140
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
146-302 2.79e-33

lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes.


Pssm-ID: 280941  Cd Length: 173  Bit Score: 120.15  E-value: 2.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        146 RLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQVPVFSKVRVDG------TDPE--FSGDEKEQLLGDLQESAMDVIER 217
Cdd:pfam02866   2 TLDINRAKTFLAEKAGVDPRVVNVPVIGGHSGTEFPDWSHAKVTIiplesqVKENvkDSEWELEELTPRVQNRGYEIIKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        218 K-GATEWGPARGVAHMVEAILHDTGEVLPASVKLEGEFG-HEDTAFGVPVRLGSNGVEEIVEW-DLDDYEQDLMADAAEK 294
Cdd:pfam02866  82 KaGSATLSMAVAGARFVRSILRGTGGVLSMGVYEDGYYGiPDDIYFSFPVTLGKDGVEKILEIlPLNDFEREKMEKSAAE 161

                  ....*...
1D3A_A        295 LSDQYDKI 302
Cdd:pfam02866 162 LKKEIEKG 169
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
41-301 2.27e-22

malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exidt in eukaryotes. In S. cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of lactate dehydrogenases. [Energy metabolism, TCA cycle]


Pssm-ID: 130833 [Multi-domain]  Cd Length: 312  Bit Score: 94.40  E-value: 2.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         41 TVGQAADTNHgiaydSNTRVRQGGY------EDTA-GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDY 113
Cdd:TIGR01772  36 AAGVAADLSH-----IPTAASVKGFsgeeglENALkGADVVVIPAGVPRKPGMTRDDLFNVNAGIVKDLVAAVAESCPKA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        114 ISLTTSNPVD---------LLNRHLYeagdrSREQVIGFgGRLDSARFRYVLSEEFDAPVQNVEGTILGEH-GDAQVPVF 183
Cdd:TIGR01772 111 MILVITNPVNstvpiaaevLKKKGVY-----DPNKLFGV-TTLDIVRANTFVAELKGKDPMEVNVPVIGGHsGETIIPLI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        184 SKvrvdgTDPEFSGDEKE--QLLGDLQESAMDVIERK----GAT---EWGPARGVAHMVEAILHDTGEVLPASVklEGEF 254
Cdd:TIGR01772 185 SQ-----CPGKVLFTEDQleALIHRIQNAGTEVVKAKagagSATlsmAFAGARFVLSLVRGLKGEEGVVECAYV--ESDG 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
1D3A_A        255 GHEDTAFGVPVRLGSNGVEEI-VEWDLDDYEQDLMADAAEKLSDQYDK 301
Cdd:TIGR01772 258 VTEATFFATPLLLGKNGVEKRlGIGKLSSFEEKMLNGALPELKKNIKK 305
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
20-295 6.86e-21

Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are localized to the glycosome and mitochondria. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133422 [Multi-domain]  Cd Length: 310  Bit Score: 90.24  E-value: 6.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       20 IALRDIADevvfvdipdkeddTVGQAADTNHgIaydsNTRVRQGGYEDT-------AGSDVVVITAGIPRQPGQTRIDLA 92
Cdd:cd01337  29 LALYDIVN-------------TPGVAADLSH-I----NTPAKVTGYLGPeelkkalKGADVVVIPAGVPRKPGMTRDDLF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       93 GDNAPIMEDIQSSLDEHNDDYISLTTSNPV--------DLLNRHlyEAGDRSREqvigFG-GRLDSARFRYVLSEEFDAP 163
Cdd:cd01337  91 NINAGIVRDLATAVAKACPKALILIISNPVnstvpiaaEVLKKA--GVYDPKRL----FGvTTLDVVRANTFVAELLGLD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      164 VQNVEGTILGEH-GDAQVPVFSKVrvdGTDPEFSGDEKEQLLGDLQESAMDVIERKG----AT---EWGPARGVAHMVEA 235
Cdd:cd01337 165 PAKVNVPVIGGHsGVTILPLLSQC---QPPFTFDQEEIEALTHRIQFGGDEVVKAKAgagsATlsmAYAGARFANSLLRG 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1D3A_A      236 ILHDTGEVLPASVKLEGEfghEDTAFGVPVRLGSNGVEEIVEW-DLDDYEQDLMADAAEKL 295
Cdd:cd01337 242 LKGEKGVIECAYVESDVT---EAPFFATPVELGKNGVEKNLGLgKLNDYEKKLLEAALPEL 299
PTZ00325 PTZ00325
malate dehydrogenase; Provisional
43-296 7.86e-17

malate dehydrogenase; Provisional


Pssm-ID: 240360 [Multi-domain]  Cd Length: 321  Bit Score: 78.94  E-value: 7.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        43 GQAADTNHgiaYDSNTRVRqgGYEDTA-------GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYIS 115
Cdd:PTZ00325  47 GVAADLSH---IDTPAKVT--GYADGElwekalrGADLVLICAGVPRKPGMTRDDLFNTNAPIVRDLVAAVASSAPKAIV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       116 LTTSNPVDLL----NRHLYEAGDRSREQVIGFgGRLDSARFRYVLSEEFDAPVQNVEGTILGEHGDAQ-VPVFSkvrvdG 190
Cdd:PTZ00325 122 GIVSNPVNSTvpiaAETLKKAGVYDPRKLFGV-TTLDVVRARKFVAEALGMNPYDVNVPVVGGHSGVTiVPLLS-----Q 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       191 TDPEFSGDEKEQLLGDLQESAMDVIERKG------------ATEWgpargVAHMVEAILHDTGEVLPASVKLEGEfgHED 258
Cdd:PTZ00325 196 TGLSLPEEQVEQITHRVQVGGDEVVKAKEgagsatlsmayaAAEW-----STSVLKALRGDKGIVECAFVESDMR--PEC 268
                        250       260       270
                 ....*....|....*....|....*....|....*....
1D3A_A       259 TAFGVPVRLGSNGVEEIVEWD-LDDYEQDLMADAAEKLS 296
Cdd:PTZ00325 269 PFFSSPVELGKEGVERVLPIGpLNAYEEELLEAAVPDLK 307
PLN00106 PLN00106
malate dehydrogenase
41-301 1.04e-16

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 78.84  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        41 TVGQAADTNHgiaydSNTRVRQGGYEDTA-------GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDY 113
Cdd:PLN00106  55 TPGVAADVSH-----INTPAQVRGFLGDDqlgdalkGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       114 ISLTTSNPVD----LLNRHLYEAGDRSREQVIGFgGRLDSARFRYVLSEEFDAPVQNVEGTILGEH-GDAQVPVFSKVRV 188
Cdd:PLN00106 130 LVNIISNPVNstvpIAAEVLKKAGVYDPKKLFGV-TTLDVVRANTFVAEKKGLDPADVDVPVVGGHaGITILPLLSQATP 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       189 DGTdpeFSGDEKEQLLGDLQESAMDVIERK---GATEWGPARGVAHMVEAILH----DTGEVLPASVK---LEGEFghed 258
Cdd:PLN00106 209 KVS---FTDEEIEALTKRIQNGGTEVVEAKagaGSATLSMAYAAARFADACLRglngEADVVECSYVQsevTELPF---- 281
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
1D3A_A       259 taFGVPVRLGSNGVEEIVEW-DLDDYEQDLMADAAEKLSDQYDK 301
Cdd:PLN00106 282 --FASKVRLGRNGVEEVLGLgPLSEYEQKGLEALKPELKASIEK 323
PRK05086 PRK05086
malate dehydrogenase; Provisional
41-286 3.84e-14

malate dehydrogenase; Provisional


Pssm-ID: 235340 [Multi-domain]  Cd Length: 312  Bit Score: 71.18  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        41 TVGQAADTNHgIAydsnTRVRQGGY--EDTA----GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYI 114
Cdd:PRK05086  39 TPGVAVDLSH-IP----TAVKIKGFsgEDPTpaleGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVEKVAKTCPKAC 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       115 SLTTSNPVD----LLNRHLYEAG--DRSREqvigFG-GRLDSARFRYVLSEEFDAPVQNVEGTILGEH-GDAQVPVFSKV 186
Cdd:PRK05086 114 IGIITNPVNttvaIAAEVLKKAGvyDKNKL----FGvTTLDVIRSETFVAELKGKQPGEVEVPVIGGHsGVTILPLLSQV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       187 RvdgtDPEFSGDEKEQLLGDLQESAMDVIERKG----AT---EWGPARGVAHMVEAILHDTGEVLPASVKLEGEFGhedT 259
Cdd:PRK05086 190 P----GVSFTEQEVADLTKRIQNAGTEVVEAKAgggsATlsmGQAAARFGLSLVRALQGEQGVVECAYVEGDGKYA---R 262
                        250       260
                 ....*....|....*....|....*...
1D3A_A       260 AFGVPVRLGSNGVEEIVEW-DLDDYEQD 286
Cdd:PRK05086 263 FFAQPVLLGKNGVEERLPIgTLSAFEQN 290
MalateDH-SF1 TIGR01759
malate dehydrogenase; This model represents a family of malate dehydrogenases in bacteria and ...
70-298 4.28e-11

malate dehydrogenase; This model represents a family of malate dehydrogenases in bacteria and eukaryotes which utilize either NAD or NADP depending on the species and context. MDH interconverts malate and oxaloacetate and is a part of the citric acid cycle as well as the C4 cycle in certain photosynthetic organisms.


Pssm-ID: 130820 [Multi-domain]  Cd Length: 323  Bit Score: 62.35  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         70 GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLD 148
Cdd:TIGR01759  79 DVDAALLVGAFPRKPGMERADLLSKNGKIFKEQGKALNKVaKKDVKVLVVGNPANTNALIASKNAPDIPPKNFSAMTRLD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        149 SARFRYVLSEEFDAPVQNVEG-TILGEHGDAQVPVFSKVRVDGTD-PEFSGDE---KEQLLGDLQESAMDVIERKGATE- 222
Cdd:TIGR01759 159 HNRAKYQLAAKAGVPVSDVKNvIIWGNHSNTQVPDFTHATVDGRPvKEVIKDDkwlEGEFIPTVQQRGAAVIEARGASSa 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        223 WGPARGVAHMVEAILHDT--GEVLPASVKLEGE-FG-HEDTAFGVPVRLGSNGVEEIVE-WDLDDYEQDLMADAAEKLSD 297
Cdd:TIGR01759 239 ASAANAAIDHVRDWVTGTpeGDWVSMGVYSDGNpYGiPEGIIFSFPVTCKGDGEWEIVEgLPLDDFVRGKLDATEDELLE 318

                  .
1D3A_A        298 Q 298
Cdd:TIGR01759 319 E 319
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
72-295 7.77e-11

Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. MDHs belong to the NAD-dependent, lactate dehydrogenase (LDH)-like, 2-hydroxycarboxylate dehydrogenase family, which also includes the GH4 family of glycoside hydrolases. They are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133420 [Multi-domain]  Cd Length: 323  Bit Score: 61.52  E-value: 7.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       72 DVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVD-----LLNrhlyEAGDRSREQVIGFgG 145
Cdd:cd00704  78 DVAILVGAFPRKPGMERADLLRKNAKIFKEQGEALNKVaKPTVKVLVVGNPANtnaliALK----NAPNLPPKNFTAL-T 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      146 RLDSARFRYVLSEEFDAP---VQNVegTILGEHGDAQVPVFSKVRVDGTDPEFSG---DEKEQLLGDL----QESAMDVI 215
Cdd:cd00704 153 RLDHNRAKAQVARKLGVRvsdVKNV--IIWGNHSNTQVPDLSNAVVYGPGGTEWVldlLDEEWLNDEFvktvQKRGAAII 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      216 ERKGATEWG-PARGVAHMVEAILHDT--GEVLPASVKLEGEFG--HEDTAFGVPVRLgSNGVEEIVEWD-LDDYEQDLMA 289
Cdd:cd00704 231 KKRGASSAAsAAKAIADHVKDWLFGTppGEIVSMGVYSPGNPYgiPPGIVFSFPCTC-KGGGWHVVEDLkLNDWLREKLK 309

                ....*.
1D3A_A      290 DAAEKL 295
Cdd:cd00704 310 ATEEEL 315
MDH_euk_cyt TIGR01758
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate ...
70-300 1.29e-09

malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate dehydrogenase from eukaryotes. The enzyme from pig has been studied by X-ray crystallography


Pssm-ID: 130819  Cd Length: 324  Bit Score: 57.93  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         70 GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFGGRLD 148
Cdd:TIGR01758  75 DVDVAILVGAFPRKEGMERRDLLSKNVKIFKEQGRALDKLaKKDCKVLVVGNPANTNALVLSNYAPSIPPKNFSALTRLD 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        149 SARFRYVLSEEFDAPVQNVEGTIL-GEHGDAQVPVFSKVRVDGTDPEFSGDEKEQLLGDLQESAMDVIERKGATEWGpAR 227
Cdd:TIGR01758 155 HNRALAQVAERAGVPVSDVKNVIIwGNHSSTQYPDVNHATVTKGGKQKPVREAIKDDAYLDGEFITTVQQRGAAIIR-AR 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        228 GVAHMVEAI------LHD------TGEVLPASVKLEGEF--GHEDTAFGVPVRLgSNGVEEIVE-WDLDDYEQDLMADAA 292
Cdd:TIGR01758 234 KLSSALSAAkaavdqMHDwvlgtpEGTFVSMGVYSDGSPygVPKGLIFSFPVTC-KNGEWKIVEgLCVDDSSRKKLALTA 312

                  ....*...
1D3A_A        293 EKLSDQYD 300
Cdd:TIGR01758 313 KELEEERD 320
PLN00135 PLN00135
malate dehydrogenase
66-300 1.46e-07

malate dehydrogenase


Pssm-ID: 177744  Cd Length: 309  Bit Score: 51.70  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        66 EDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVDLLNRHLYEAGDRSREQVIGFG 144
Cdd:PLN00135  54 EACKGVNIAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKHaAPDCKVLVVANPANTNALILKEFAPSIPEKNITCL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       145 GRLDSARFRYVLSEEFDAPVQNVEGTIL-GEHGDAQVPVFSKVRVD---GTDP--EFSGDE---KEQLLGDLQESAMDVI 215
Cdd:PLN00135 134 TRLDHNRALGQISERLGVPVSDVKNVIIwGNHSSTQYPDVNHATVKtpsGEKPvrELVADDawlNGEFITTVQQRGAAII 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       216 E-RKGATEWGPARGVAHMVEAILHDT--GEVLPASVKLEGEFG-HEDTAFGVPVRLgSNGVEEIVE-WDLDDYEQDLMAD 290
Cdd:PLN00135 214 KaRKLSSALSAASSACDHIRDWVLGTpeGTWVSMGVYSDGSYGvPPGLIYSFPVTC-EKGEWSIVQgLSIDEFSRKKMDA 292
                        250
                 ....*....|
1D3A_A       291 AAEKLSDQYD 300
Cdd:PLN00135 293 TAKELKEEKE 302
LDH_protist TIGR01756
lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which ...
70-295 6.52e-07

lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which have aparrently evolved from a recent protist malate dehydrogenase ancestor. Lactate dehydrogenase converts the hydroxyl at C-2 of lactate to a carbonyl in the product, pyruvate. The preference of this enzyme for NAD or NADP has not been determined. A critical residue in malate dehydrogenase, arginine-91 (T. vaginalis numbering) has been mutated to a leucine, eliminating the positive charge which complemeted the carboxylate in malate which is absent in lactate. Several other more subtle changes are proposed to make the active site smaller to accomadate the less bulky lactate molecule.


Pssm-ID: 130817  Cd Length: 313  Bit Score: 49.88  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         70 GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYI-SLTTSNPVD------LLNrhlyeAGDRSREQVIG 142
Cdd:TIGR01756  60 DIDCAFLVASVPLKPGEVRADLLTKNTPIFKATGEALSEYAKPTVkVLVIGNPVNtnclvaMLH-----APKLSAENFSS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        143 FgGRLDSARFRYVLSEEFDAPVQNVEGTIL-GEHGDAQVPvfskvrvDGTDPEFSGDEKEQLLGDL-------------- 207
Cdd:TIGR01756 135 L-CMLDHNRAVSRIASKLKVPVDHIYHVVVwGNHAESMVA-------DLTHAEFTKNGKHQKVFDElcrdypepdffevi 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        208 QESAMDVIERKGATEWGPARGVA--HMvEAILHDT--GEVLPASVKLEgefghEDTAFGV--------PVRLGSNGVEEI 275
Cdd:TIGR01756 207 AQRAWKILEMRGFTSAASPVKASlqHM-KAWLFGTrpGEVLSMGIPVP-----EGNPYGIkpgvifsfPCTVDEDGKVHV 280
                         250       260
                  ....*....|....*....|.
1D3A_A        276 VE-WDLDDYEQDLMADAAEKL 295
Cdd:TIGR01756 281 VEnFELNPWLKTKLAQTEKDL 301
MDH_choloroplast_like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
70-288 5.23e-06

Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are bacterial MDHs, and plant MDHs localized to the choloroplasts. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133423 [Multi-domain]  Cd Length: 322  Bit Score: 46.81  E-value: 5.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       70 GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVD----LLNRHlyeAGDRSREQvigFG 144
Cdd:cd01338  78 DADWALLVGAKPRGPGMERADLLKANGKIFTAQGKALNDVaSRDVKVLVVGNPCNtnalIAMKN---APDIPPDN---FT 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A      145 G--RLDSARFRYVLSEEFDAPVQNVEG-TILGEHGDAQVPVFSKVRVDGTDPEFSGDEKEQLLGDL----QESAMDVIER 217
Cdd:cd01338 152 AmtRLDHNRAKSQLAKKAGVPVTDVKNmVIWGNHSPTQYPDFTNATIGGKPAAEVINDRAWLEDEFiptvQKRGAAIIKA 231
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D3A_A      218 KGA-TEWGPARGVAHMVEAILHDT--GEVLPASVKLEGEFG-HEDTAFGVPVRLgSNGVEEIVE-WDLDDYEQDLM 288
Cdd:cd01338 232 RGAsSAASAANAAIDHMRDWVLGTpeGDWFSMAVPSDGSYGiPEGLIFSFPVRS-KGGGYEIVEgLEIDDFAREKI 306
Malate-DH_plant TIGR01757
malate dehydrogenase, NADP-dependent; This model represents the NADP-dependent malate ...
65-283 1.64e-05

malate dehydrogenase, NADP-dependent; This model represents the NADP-dependent malate dehydrogenase found in plants, mosses and green algae and localized to the chloroplast. Malate dehydrogenase converts oxaloacetate into malate, a critical step in the C4 cycle which allows circumvention of the effects of photorespiration. Malate is subsequenctly transported from the chloroplast to the cytoplasm (and then to the bundle sheath cells in C4 plants). The plant and moss enzymes are light regulated via cysteine disulfide bonds. The enzyme from Sorghum has been crystallized.


Pssm-ID: 130818  Cd Length: 387  Bit Score: 45.73  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A         65 YEDTAGSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEHNDDYIS-LTTSNPVD------LLNrhlyeAGDRSR 137
Cdd:TIGR01757 115 YEVFEDADWALLIGAKPRGPGMERADLLDINGQIFADQGKALNAVASKNCKvLVVGNPCNtnaliaMKN-----APNIPR 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        138 EQVIGFgGRLDSARFRYVL---SEEFDAPVQNVegTILGEHGDAQVPVFSKVRVDGTD-PEFSGDEKEqllgdLQESAMD 213
Cdd:TIGR01757 190 KNFHAL-TRLDENRAKCQLalkSGKFYTSVSNV--TIWGNHSTTQVPDFVNAKIGGRPaKEVIKDTKW-----LEEEFTP 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        214 VIERKGAT---EWG------PARGVAHMVEAILHDT--GEVLPASVKLEGE-FG-HEDTAFGVPVRLGSNGVEEIV-EWD 279
Cdd:TIGR01757 262 TVQKRGGAlikKWGrssaasTAVSIADAIKSLVVPTpeGDWFSTGVYTDGNpYGiAEGLVFSMPCRSKGDGDYELAtDVS 341

                  ....
1D3A_A        280 LDDY 283
Cdd:TIGR01757 342 MDDF 345
PRK05442 PRK05442
malate dehydrogenase; Provisional
70-303 2.22e-05

malate dehydrogenase; Provisional


Pssm-ID: 235468  Cd Length: 326  Bit Score: 45.17  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A        70 GSDVVVITAGIPRQPGQTRIDLAGDNAPIMEDIQSSLDEH-NDDYISLTTSNPVD---LLNRHlyEAGDRSREQvigFGG 145
Cdd:PRK05442  80 DADVALLVGARPRGPGMERKDLLEANGAIFTAQGKALNEVaARDVKVLVVGNPANtnaLIAMK--NAPDLPAEN---FTA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       146 --RLDSARFRYVLSEEFDAPVQNVEG-TILGEHGDAQVPVFSKVRVDGTD-PEFSGDE---KEQLLGDLQESAMDVIERK 218
Cdd:PRK05442 155 mtRLDHNRALSQLAAKAGVPVADIKKmTVWGNHSATQYPDFRHATIDGKPaAEVINDQawlEDTFIPTVQKRGAAIIEAR 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D3A_A       219 GATEWGPARGVA--HMVEAILH-DTGEVLPASVKLEGEFG-HEDTAFGVPVRLgSNGVEEIVE-WDLDDYEQDLMADAAE 293
Cdd:PRK05442 235 GASSAASAANAAidHVRDWVLGtPEGDWVSMGVPSDGSYGiPEGLIFGFPVTC-ENGEYEIVQgLEIDDFSREKIDATLA 313
                        250
                 ....*....|
1D3A_A       294 KLSDQYDKIS 303
Cdd:PRK05442 314 ELEEERDAVK 323
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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