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Conserved domains on  [gi|199019|gb|AAA39488|]
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malic enzyme, partial [Mus musculus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 99-276 1.25e-94

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05312:

Pssm-ID: 473865  Cd Length: 279  Bit Score: 282.13  E-value: 1.25e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    99 VKGRASLTEEKEVFAHEHEE--MKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSAD 176
Cdd:cd05312  72 TKDRKDLTPFKKPFARKDEEkeGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAE 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   177 ECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGR 256
Cdd:cd05312 152 DAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGR 230

                       170       180
                ....*....|....*....|
gi 199019   257 LYPPLNTIRGVSLKIAVKVF 276
Cdd:cd05312 231 LYPPLSNIREISAQIAVAVA 250
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 1-128 1.82e-47

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05312:

Pssm-ID: 473865  Cd Length: 279  Bit Score: 161.18  E-value: 1.82e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:cd05312 150 AEDAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELAR 228

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 199019    81 GRLYPPLNTIRGVSLKIAVKgrASLTEEKEVFAHEHEEMKNLEAIVQK 128
Cdd:cd05312 229 GRLYPPLSNIREISAQIAVA--VAKYAYEEGLATRYPPPEDLEEYVKS 274
 
Name Accession Description Interval E-value
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
 99-276 1.25e-94

NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133454  Cd Length: 279  Bit Score: 282.13  E-value: 1.25e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    99 VKGRASLTEEKEVFAHEHEE--MKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSAD 176
Cdd:cd05312  72 TKDRKDLTPFKKPFARKDEEkeGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAE 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   177 ECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGR 256
Cdd:cd05312 152 DAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGR 230

                       170       180
                ....*....|....*....|
gi 199019   257 LYPPLNTIRGVSLKIAVKVF 276
Cdd:cd05312 231 LYPPLSNIREISAQIAVAVA 250
Malic_M pfam03949
Malic enzyme, NAD binding domain;
99-275 2.31e-85

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 257.89  E-value: 2.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      99 VKGRASLTEEKEVFAHEHEEMK------NLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAE 172
Cdd:pfam03949  72 TDDREDLTDFQKPFARKRAELKgwgdgiTLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     173 CSADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHL 252
Cdd:pfam03949 152 ATPEDAYKWTDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEP 230

                         170       180
                  ....*....|....*....|...
gi 199019     253 QEGRLYPPLNTIRGVSLKIAVKV 275
Cdd:pfam03949 231 GQGRLLPPLSDIREVSRKIAVAV 253
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
 99-275 2.02e-82

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 260.62  E-value: 2.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     99 VKGRA-SLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSADE 177
Cdd:PLN03129 369 TKSRKdSLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKAECTAEE 448

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    178 CYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGRL 257
Cdd:PLN03129 449 AYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAI 527

                        170
                 ....*....|....*...
gi 199019    258 YPPLNTIRGVSLKIAVKV 275
Cdd:PLN03129 528 YPPFSRIRDISAHVAAAV 545
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
 99-275 9.38e-56

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 181.07  E-value: 9.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019       99 VKGRA-SLTEEKEVFAH--EHEEMKNLEAIVQKikPTALIGVAAIGGAFTEQILKDMAafnERPIIFALSSPTSKAECSA 175
Cdd:smart00919  64 TKGREdNLNPYKKPFARktNERETGTLEEAVKG--ADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTA 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      176 DECYKVTKgrAIFASGSPFdpvtlpdgrtlFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQ--QVSDKHLQ 253
Cdd:smart00919 139 ADAYRWTA--AIVATGRSD-----------YPNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEELG 205

                          170       180
                   ....*....|....*....|..
gi 199019      254 EGRLYPPLNTiRGVSLKIAVKV 275
Cdd:smart00919 206 PGYIIPSPFD-RRVSARVAVAV 226
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
 1-128 1.82e-47

NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133454  Cd Length: 279  Bit Score: 161.18  E-value: 1.82e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:cd05312 150 AEDAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELAR 228

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 199019    81 GRLYPPLNTIRGVSLKIAVKgrASLTEEKEVFAHEHEEMKNLEAIVQK 128
Cdd:cd05312 229 GRLYPPLSNIREISAQIAVA--VAKYAYEEGLATRYPPPEDLEEYVKS 274
Malic_M pfam03949
Malic enzyme, NAD binding domain;
1-100 1.03e-40

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 143.10  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019       1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:pfam03949 154 PEDAYKWTDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQ 232

                          90       100
                  ....*....|....*....|
gi 199019      81 GRLYPPLNTIRGVSLKIAVK 100
Cdd:pfam03949 233 GRLLPPLSDIREVSRKIAVA 252
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
 99-275 3.09e-38

Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440050 [Multi-domain]  Cd Length: 414  Bit Score: 140.15  E-value: 3.09e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    99 VKGRASLTEEKEVFAHEHEEMKN----LEAIVQKikpTALIGVAAiGGAFTEQILKDMAafnERPIIFALSSPTSkaECS 174
Cdd:COG0281 230 YEGRTDLNPYKREFARDTNPRGLkgtlAEAIKGA---DVFIGVSA-PGAFTEEMVKSMA---KRPIIFALANPTP--EIT 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   175 ADECYKVTKGrAIFASGspfdpvtlpdgRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 254
Cdd:COG0281 301 PEDAKAWGDG-AIVATG-----------RSDYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGP 368

                       170       180
                ....*....|....*....|.
gi 199019   255 GRLYPPLNTIRgVSLKIAVKV 275
Cdd:COG0281 369 DYIIPSPFDPR-VSPAVAAAV 388
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
 1-118 6.61e-37

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 139.28  E-value: 6.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:PLN03129 446 AEEAYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAK 524

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 199019     81 GRLYPPLNTIRGVSLKIAVKGRASLTEEKEVFAHEHEE 118
Cdd:PLN03129 525 GAIYPPFSRIRDISAHVAAAVAAKAYEEGLATRLPRPE 562
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
 1-100 4.06e-22

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 92.86  E-value: 4.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019        1 ADECYKVTKgrAIFASGSPFdpvtlpdgrtlFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQ--QVSDKHL 78
Cdd:smart00919 138 AADAYRWTA--AIVATGRSD-----------YPNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEEL 204

                           90       100
                   ....*....|....*....|..
gi 199019       79 QEGRLYPPLNTiRGVSLKIAVK 100
Cdd:smart00919 205 GPGYIIPSPFD-RRVSARVAVA 225
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
 1-99 4.78e-15

Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440050 [Multi-domain]  Cd Length: 414  Bit Score: 75.43  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGrAIFASGspfdpvtlpdgRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:COG0281 301 PEDAKAWGDG-AIVATG-----------RSDYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGP 368

                        90
                ....*....|....*....
gi 199019    81 GRLYPPLNTIRgVSLKIAV 99
Cdd:COG0281 369 DYIIPSPFDPR-VSPAVAA 386
 
Name Accession Description Interval E-value
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
 99-276 1.25e-94

NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133454  Cd Length: 279  Bit Score: 282.13  E-value: 1.25e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    99 VKGRASLTEEKEVFAHEHEE--MKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSAD 176
Cdd:cd05312  72 TKDRKDLTPFKKPFARKDEEkeGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAE 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   177 ECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGR 256
Cdd:cd05312 152 DAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGR 230

                       170       180
                ....*....|....*....|
gi 199019   257 LYPPLNTIRGVSLKIAVKVF 276
Cdd:cd05312 231 LYPPLSNIREISAQIAVAVA 250
Malic_M pfam03949
Malic enzyme, NAD binding domain;
99-275 2.31e-85

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 257.89  E-value: 2.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      99 VKGRASLTEEKEVFAHEHEEMK------NLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAE 172
Cdd:pfam03949  72 TDDREDLTDFQKPFARKRAELKgwgdgiTLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     173 CSADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHL 252
Cdd:pfam03949 152 ATPEDAYKWTDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEP 230

                         170       180
                  ....*....|....*....|...
gi 199019     253 QEGRLYPPLNTIRGVSLKIAVKV 275
Cdd:pfam03949 231 GQGRLLPPLSDIREVSRKIAVAV 253
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
 99-275 2.02e-82

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 260.62  E-value: 2.02e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     99 VKGRA-SLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSADE 177
Cdd:PLN03129 369 TKSRKdSLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKAECTAEE 448

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    178 CYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGRL 257
Cdd:PLN03129 449 AYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAI 527

                        170
                 ....*....|....*...
gi 199019    258 YPPLNTIRGVSLKIAVKV 275
Cdd:PLN03129 528 YPPFSRIRDISAHVAAAV 545
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
 97-275 1.58e-81

NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133442  Cd Length: 254  Bit Score: 247.90  E-value: 1.58e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    97 IAVKGRASLTEEKE---VFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAEC 173
Cdd:cd00762  70 LLVKNRKETCPNEYhlaRFANPERESGDLEDAVEAAKPDFLIGVSRVGGAFTPEVIRA*AEINERPVIFALSNPTSKAEC 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   174 SADECYKVTKGRAIFASGSPFDPVTLPDGrTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQ 253
Cdd:cd00762 150 TAEEAYTATEGRAIFASGSPFHPVELNGG-TYKPGQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEAIASSVTEESLK 228

                       170       180
                ....*....|....*....|..
gi 199019   254 EGRLYPPLNTIRGVSLKIAVKV 275
Cdd:cd00762 229 PGRLYPPLFDIQEVSLNIAVAV 250
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
99-275 2.71e-70

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 228.48  E-value: 2.71e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     99 VKGRASLTEEKEVFAHEHEEMKN---------LEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTS 169
Cdd:PRK13529 342 TDDMPDLLDFQKPYARKREELADwdtegdvisLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHCERPIIFPLSNPTS 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    170 KAECSADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSD 249
Cdd:PRK13529 422 RAEATPEDLIAWTDGRALVATGSPFAPVEY-NGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLMAAAHALADCVPL 500

                        170       180
                 ....*....|....*....|....*.
gi 199019    250 KHLQEGRLYPPLNTIRGVSLKIAVKV 275
Cdd:PRK13529 501 AKPGEGALLPPVEDIREVSRAIAIAV 526
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
 115-275 6.88e-67

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 219.50  E-value: 6.88e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    115 EHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSSPTSKAECSADECYKVTKGRAIFASGSPF 194
Cdd:PTZ00317 366 EDSSLKTLEDVVRFVKPTALLGLSGVGGVFTEEVVKTMASNVERPIIFPLSNPTSKAECTAEDAYKWTNGRAIVASGSPF 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    195 DPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGRLYPPLNTIRGVSLKIAVK 274
Cdd:PTZ00317 446 PPVTL-NGKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAAASLATLVSEEDLREGKLYPPLEDIREISAHIAVD 524


                 .
gi 199019    275 V 275
Cdd:PTZ00317 525 V 525
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
 99-275 9.38e-56

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 181.07  E-value: 9.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019       99 VKGRA-SLTEEKEVFAH--EHEEMKNLEAIVQKikPTALIGVAAIGGAFTEQILKDMAafnERPIIFALSSPTSKAECSA 175
Cdd:smart00919  64 TKGREdNLNPYKKPFARktNERETGTLEEAVKG--ADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTA 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      176 DECYKVTKgrAIFASGSPFdpvtlpdgrtlFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQ--QVSDKHLQ 253
Cdd:smart00919 139 ADAYRWTA--AIVATGRSD-----------YPNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEELG 205

                          170       180
                   ....*....|....*....|..
gi 199019      254 EGRLYPPLNTiRGVSLKIAVKV 275
Cdd:smart00919 206 PGYIIPSPFD-RRVSARVAVAV 226
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
 1-128 1.82e-47

NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists of eukaryotic and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133454  Cd Length: 279  Bit Score: 161.18  E-value: 1.82e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGRAIFASGSPFDPVTlPDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:cd05312 150 AEDAYKWTDGRALFASGSPFPPVE-YNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELAR 228

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 199019    81 GRLYPPLNTIRGVSLKIAVKgrASLTEEKEVFAHEHEEMKNLEAIVQK 128
Cdd:cd05312 229 GRLYPPLSNIREISAQIAVA--VAKYAYEEGLATRYPPPEDLEEYVKS 274
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
 1-100 2.07e-42

NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133442  Cd Length: 254  Bit Score: 147.36  E-value: 2.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGRAIFASGSPFDPVTLPDGrTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:cd00762 151 AEEAYTATEGRAIFASGSPFHPVELNGG-TYKPGQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEAIASSVTEESLKP 229

                        90       100
                ....*....|....*....|
gi 199019    81 GRLYPPLNTIRGVSLKIAVK 100
Cdd:cd00762 230 GRLYPPLFDIQEVSLNIAVA 249
Malic_M pfam03949
Malic enzyme, NAD binding domain;
1-100 1.03e-40

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 143.10  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019       1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:pfam03949 154 PEDAYKWTDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQ 232

                          90       100
                  ....*....|....*....|
gi 199019      81 GRLYPPLNTIRGVSLKIAVK 100
Cdd:pfam03949 233 GRLLPPLSDIREVSRKIAVA 252
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
 99-275 3.09e-38

Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440050 [Multi-domain]  Cd Length: 414  Bit Score: 140.15  E-value: 3.09e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    99 VKGRASLTEEKEVFAHEHEEMKN----LEAIVQKikpTALIGVAAiGGAFTEQILKDMAafnERPIIFALSSPTSkaECS 174
Cdd:COG0281 230 YEGRTDLNPYKREFARDTNPRGLkgtlAEAIKGA---DVFIGVSA-PGAFTEEMVKSMA---KRPIIFALANPTP--EIT 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   175 ADECYKVTKGrAIFASGspfdpvtlpdgRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 254
Cdd:COG0281 301 PEDAKAWGDG-AIVATG-----------RSDYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGP 368

                       170       180
                ....*....|....*....|.
gi 199019   255 GRLYPPLNTIRgVSLKIAVKV 275
Cdd:COG0281 369 DYIIPSPFDPR-VSPAVAAAV 388
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
 1-118 6.61e-37

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 139.28  E-value: 6.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:PLN03129 446 AEEAYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAK 524

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 199019     81 GRLYPPLNTIRGVSLKIAVKGRASLTEEKEVFAHEHEE 118
Cdd:PLN03129 525 GAIYPPFSRIRDISAHVAAAVAAKAYEEGLATRLPRPE 562
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
 1-100 1.68e-33

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 129.75  E-value: 1.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:PTZ00317 426 AEDAYKWTNGRAIVASGSPFPPVTL-NGKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAAASLATLVSEEDLRE 504

                         90       100
                 ....*....|....*....|
gi 199019     81 GRLYPPLNTIRGVSLKIAVK 100
Cdd:PTZ00317 505 GKLYPPLEDIREISAHIAVD 524
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
1-99 5.08e-31

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 122.55  E-value: 5.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019      1 ADECYKVTKGRAIFASGSPFDPVTLpDGRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:PRK13529 427 PEDLIAWTDGRALVATGSPFAPVEY-NGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLMAAAHALADCVPLAKPGE 505

                         90
                 ....*....|....*....
gi 199019     81 GRLYPPLNTIRGVSLKIAV 99
Cdd:PRK13529 506 GALLPPVEDIREVSRAIAI 524
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
 1-100 4.06e-22

Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.


Pssm-ID: 214912  Cd Length: 231  Bit Score: 92.86  E-value: 4.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019        1 ADECYKVTKgrAIFASGSPFdpvtlpdgrtlFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQ--QVSDKHL 78
Cdd:smart00919 138 AADAYRWTA--AIVATGRSD-----------YPNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEEL 204

                           90       100
                   ....*....|....*....|..
gi 199019       79 QEGRLYPPLNTiRGVSLKIAVK 100
Cdd:smart00919 205 GPGYIIPSPFD-RRVSARVAVA 225
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
 1-99 4.78e-15

Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440050 [Multi-domain]  Cd Length: 414  Bit Score: 75.43  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     1 ADECYKVTKGrAIFASGspfdpvtlpdgRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:COG0281 301 PEDAKAWGDG-AIVATG-----------RSDYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGP 368

                        90
                ....*....|....*....
gi 199019    81 GRLYPPLNTIRgVSLKIAV 99
Cdd:COG0281 369 DYIIPSPFDPR-VSPAVAA 386
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
 133-283 6.27e-09

NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133453 [Multi-domain]  Cd Length: 226  Bit Score: 55.35  E-value: 6.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019   133 ALIGVAAiGGAFTEQILKDMaafNERPIIFALSSPTSkaECSADECYKVtkGRAIFASGspfdpvtlpdgRTLFPGQGNN 212
Cdd:cd05311 100 VFIGVSR-PGVVKKEMIKKM---AKDPIVFALANPVP--EIWPEEAKEA--GADIVATG-----------RSDFPNQVNN 160

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199019   213 SYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQEGRLYP-PLNTirgvslkiavKVFPGVALGV 283
Cdd:cd05311 161 VLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVLGEEYIIPtPFDP----------RVVPRVATAV 222
PRK12862 PRK12862
malic enzyme; Reviewed
 100-233 2.17e-06

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 49.12  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    100 KGRASLTEE-KEVFAHEHEEMKNLEAIvqkikPTA--LIGVAAiGGAFTEQILKDMAafnERPIIFALSSPTskAECSAD 176
Cdd:PRK12862 233 EGRTELMDPwKARYAQKTDARTLAEVI-----EGAdvFLGLSA-AGVLKPEMVKKMA---PRPLIFALANPT--PEILPE 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 199019    177 ECYKVtKGRAIFASgspfdpvtlpdGRTLFPGQGNNSYVFPGVALGVVACGLRHIDD 233
Cdd:PRK12862 302 EARAV-RPDAIIAT-----------GRSDYPNQVNNVLCFPYIFRGALDVGATTINE 346
PRK12861 PRK12861
malic enzyme; Reviewed
 97-227 2.49e-04

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 42.95  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019     97 IAVKGRASLTE-EKEVFAHEHEEMKNLEAIVqkiKPTALIGVAAiGGAFTEQILKDMAAfneRPIIFALSSPTSKaecsa 175
Cdd:PRK12861 226 VVYRGRTTLMDpDKERFAQETDARTLAEVIG---GADVFLGLSA-GGVLKAEMLKAMAA---RPLILALANPTPE----- 293

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 199019    176 decykvtkgraIF--ASGSPFDPVTLPDGRTLFPGQGNNSYVFPGVALGVVACG 227
Cdd:PRK12861 294 -----------IFpeLAHATRDDVVIATGRSDYPNQVNNVLCFPYIFRGALDVG 336
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
 100-225 7.19e-04

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 41.23  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    100 KGRA-SLTEEKEVFAHEHEEMKNLEAIVQkikptA--LIGVAAiGGAFTEQILKDMAafnERPIIFALSSPTskAECSAD 176
Cdd:PRK07232 225 KGRTeGMDEWKAAYAVDTDARTLAEAIEG-----AdvFLGLSA-AGVLTPEMVKSMA---DNPIIFALANPD--PEITPE 293

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 199019    177 ECYKVtKGRAIFASgspfdpvtlpdGRTLFPGQGNN----SYVFPGvALGVVA 225
Cdd:PRK07232 294 EAKAV-RPDAIIAT-----------GRSDYPNQVNNvlcfPYIFRG-ALDVGA 333
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
 13-86 1.48e-03

NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133453 [Multi-domain]  Cd Length: 226  Bit Score: 39.56  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199019    13 IFASGSPfDPVTLPD------------GRTLFPGQGNNSYVFPGVALGVVACGLRHIDDKVFLTTREVISQQVSDKHLQE 80
Cdd:cd05311 124 VFALANP-VPEIWPEeakeagadivatGRSDFPNQVNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVLGE 202


                ....*.
gi 199019    81 GRLYPP 86
Cdd:cd05311 203 EYIIPT 208
 
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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