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Conserved domains on  [gi|966987707|ref|XP_014970862|]
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NADP-dependent malic enzyme, mitochondrial isoform X3 [Macaca mulatta]

Protein Classification

NAD-dependent malic enzyme( domain architecture ID 11477469)

NAD-dependent malic enzyme 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+

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
1-526 0e+00

NADP-dependent malic enzyme; Provisional


:

Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 839.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   1 MAFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYRVLTSDVEKFMPIVYTPTVG 80
Cdd:PLN03129  55 LAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEELLPIVYTPTVG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  81 LACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQ 160
Cdd:PLN03129 135 EACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLYTAAGGIRPSA 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 161 CLPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNKYCMFN 240
Cdd:PLN03129 215 VLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQRYRTTHLCFN 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 241 DDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEK-EGVPKAEATRKIWMVDSKGLIVKGRSH 319
Cdd:PLN03129 295 DDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDSKGLVTKSRKD 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 320 -LNHEKEMFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTE 398
Cdd:PLN03129 375 sLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKAECTAEEAYTWTG 454
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 399 GRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLST 478
Cdd:PLN03129 455 GRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAIYPPFSR 533
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 966987707 479 IRDVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTPDYDSFT 526
Cdd:PLN03129 534 IRDISAHVAAAVAAKAYEEGLATRLPRPEDLVEYAESCMYSPVYRPYR 581
 
Name Accession Description Interval E-value
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
1-526 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 839.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   1 MAFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYRVLTSDVEKFMPIVYTPTVG 80
Cdd:PLN03129  55 LAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEELLPIVYTPTVG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  81 LACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQ 160
Cdd:PLN03129 135 EACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLYTAAGGIRPSA 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 161 CLPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNKYCMFN 240
Cdd:PLN03129 215 VLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQRYRTTHLCFN 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 241 DDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEK-EGVPKAEATRKIWMVDSKGLIVKGRSH 319
Cdd:PLN03129 295 DDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDSKGLVTKSRKD 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 320 -LNHEKEMFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTE 398
Cdd:PLN03129 375 sLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKAECTAEEAYTWTG 454
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 399 GRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLST 478
Cdd:PLN03129 455 GRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAIYPPFSR 533
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 966987707 479 IRDVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTPDYDSFT 526
Cdd:PLN03129 534 IRDISAHVAAAVAAKAYEEGLATRLPRPEDLVEYAESCMYSPVYRPYR 581
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
243-520 1.01e-153

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: 440.45  E-value: 1.01e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLNH 322
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRKDLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 323 EKEMFAQDHPE--VNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTEGR 400
Cdd:cd05312   81 FKKPFARKDEEkeGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDAYKWTDGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 401 GIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLSTIR 480
Cdd:cd05312  161 ALFASGSPFPPVEY-NGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGRLYPPLSNIR 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 966987707 481 DVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTP 520
Cdd:cd05312  240 EISAQIAVAVAKYAYEEGLATRYPPPEDLEEYVKSQMWEP 279
Malic_M pfam03949
Malic enzyme, NAD binding domain;
243-494 3.82e-143

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 412.74  E-value: 3.82e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLNH 322
Cdd:pfam03949   1 IQGTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVREGLSEEEARKRIWMVDRQGLLTDDREDLTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  323 EKEMFAQDHPEVN------SLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRV 396
Cdd:pfam03949  81 FQKPFARKRAELKgwgdgiTLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAEATPEDAYKW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  397 TEGRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPL 476
Cdd:pfam03949 161 TDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQGRLLPPL 239
                         250
                  ....*....|....*...
gi 966987707  477 STIRDVSLRIAIKVLDYA 494
Cdd:pfam03949 240 SDIREVSRKIAVAVAKYA 257
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
38-517 4.80e-134

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: 395.53  E-value: 4.80e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  38 QQSDLDKYIILmtlqDRNEKLFYRVLTSDVEKFMPIVYTPTVGLACQHYGLTFRRPRGlfitihdkghlatmlnsWPEDN 117
Cdd:COG0281   10 EQEALEYHRIY----DRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYG-----------------YTAKG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 118 IKAVVVTDGERILGLGDLGCY-GMGIPVGKLALYTACGGVNpqqCLPVLLDvgTNNeellrdplyiglkhqrvrgkaydd 196
Cdd:COG0281   69 NLVAVVTDGTAVLGLGDIGPLaGMPVMEGKAVLFKAFAGID---AFPICLD--TND------------------------ 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 197 lLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNK--YCMFNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQG 274
Cdd:COG0281  120 -PDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVING 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 275 AGEAAMGIAHLLVmaleKEGVPKaeatRKIWMVDSKGLIVKGRSHLNHEKEMFAQDHPEVN---SLEEVVRLVkpTAIIG 351
Cdd:COG0281  199 AGAAGIAIARLLV----AAGLSE----ENIIMVDSKGLLYEGRTDLNPYKREFARDTNPRGlkgTLAEAIKGA--DVFIG 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 352 VAAiAGAFTEQILRDMAsfhERPIIFALSNPTSkaECTAEKCYRVTEGRgIFASgspfksvtledGKTFIPGQGNNAYVF 431
Cdd:COG0281  269 VSA-PGAFTEEMVKSMA---KRPIIFALANPTP--EITPEDAKAWGDGA-IVAT-----------GRSDYPNQVNNVLIF 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 432 PGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLSTIRdVSLRIAIKVLDYAYKHNLASyYPEPKDKEA 511
Cdd:COG0281  331 PGIFRGALDVRATRITDEMKLAAARALADLVDEEELGPDYIIPSPFDPR-VSPAVAAAVAKAAIESGVAR-RPIDEDYRE 408

                 ....*.
gi 966987707 512 FVRSLV 517
Cdd:COG0281  409 ALEARM 414
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
243-495 1.03e-101

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: 305.88  E-value: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEgvpkaeatRKIWMVDSKGLIVKGRS-HLN 321
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKR--------KNIWLVDSKGLLTKGREdNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   322 HEKEMFAQ--DHPEVNSLEEVVRlvKPTAIIGVAAIAGAFTEQILRDMAsfhERPIIFALSNPTSKAECTAEKCYRVTEg 399
Cdd:smart00919  73 PYKKPFARktNERETGTLEEAVK--GADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTAADAYRWTA- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   400 rGIFASGSPFKsvtledgktfiPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQ--EVSEQHLSQGRLYPPLS 477
Cdd:smart00919 147 -AIVATGRSDY-----------PNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEELGPGYIIPSPF 214
                          250
                   ....*....|....*...
gi 966987707   478 TiRDVSLRIAIKVLDYAY 495
Cdd:smart00919 215 D-RRVSARVAVAVAKAAI 231
 
Name Accession Description Interval E-value
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
1-526 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 839.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   1 MAFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYRVLTSDVEKFMPIVYTPTVG 80
Cdd:PLN03129  55 LAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEELLPIVYTPTVG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  81 LACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQ 160
Cdd:PLN03129 135 EACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLYTAAGGIRPSA 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 161 CLPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNKYCMFN 240
Cdd:PLN03129 215 VLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQRYRTTHLCFN 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 241 DDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEK-EGVPKAEATRKIWMVDSKGLIVKGRSH 319
Cdd:PLN03129 295 DDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDSKGLVTKSRKD 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 320 -LNHEKEMFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTE 398
Cdd:PLN03129 375 sLQPFKKPFAHDHEPGASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKAECTAEEAYTWTG 454
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 399 GRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLST 478
Cdd:PLN03129 455 GRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALAAQVTEEELAKGAIYPPFSR 533
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 966987707 479 IRDVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTPDYDSFT 526
Cdd:PLN03129 534 IRDISAHVAAAVAAKAYEEGLATRLPRPEDLVEYAESCMYSPVYRPYR 581
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
2-525 0e+00

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 779.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   2 AFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYRVLTSDVEKFMPIVYTPTVGL 81
Cdd:PRK13529  31 AFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTDLEKHIYLRNLQDRNETLFYRLLSDHLEEMMPIIYTPTVGE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  82 ACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQC 161
Cdd:PRK13529 111 ACERFSHIYRRPRGLFISYDDRDRIEDILQNAPNRDIKLIVVTDGERILGIGDQGIGGMGIPIGKLSLYTACGGIDPART 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 162 LPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGiNCLIQFEDFANANAFRLLNKYRNKYCMFND 241
Cdd:PRK13529 191 LPVVLDVGTNNEQLLNDPLYLGWRHPRIRGEEYDEFVDEFVQAVKRRFP-NALLQFEDFAQKNARRILERYRDEICTFND 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 242 DIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLN 321
Cdd:PRK13529 270 DIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSEEEARKRFFMVDRQGLLTDDMPDLL 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 322 HEKEMFAQDHPEVN---------SLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEK 392
Cdd:PRK13529 350 DFQKPYARKREELAdwdtegdviSLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHCERPIIFPLSNPTSRAEATPED 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 393 CYRVTEGRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRL 472
Cdd:PRK13529 430 LIAWTDGRALVATGSPFAPVEY-NGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLMAAAHALADCVPLAKPGEGAL 508
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966987707 473 YPPLSTIRDVSLRIAIKVLDYAYKHNLASyYPEPKDKEAFVRSLVYTPDYDSF 525
Cdd:PRK13529 509 LPPVEDIREVSRAIAIAVAKAAIEEGLAR-ETSDEDLEQAIEDNMWQPEYRPY 560
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
2-520 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 641.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   2 AFTLEERLQLGIHGLIPPCFLSQDVQLLRIMRYYERQQSDLDKYIILMTLQDRNEKLFYRVLTSDVEKFMPIVYTPTVGL 81
Cdd:PTZ00317  33 AFTAEEREHLGIEGLLPPTVETLEQQVERLWTQFNRIETPINKYQFLRNIHDTNETLFYALLLKYLKELLPIIYTPTVGE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  82 ACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILGLGDLGCYGMGIPVGKLALYTACGGVNPQQC 161
Cdd:PTZ00317 113 ACQNYSNLFQRDRGLYLSRAHKGKIREILKNWPYDNVDVIVITDGSRILGLGDLGANGMGISIGKLSLYVAGGGINPSRV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 162 LPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGiNCLIQFEDFANANAFRLLNKYRNKYCMFND 241
Cdd:PTZ00317 193 LPVVLDVGTNNEKLLNDPLYLGLREKRLDDDEYYELLDEFMEAVSSRWP-NAVVQFEDFSNNHCFDLLERYQNKYRCFND 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 242 DIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGR-SHL 320
Cdd:PTZ00317 272 DIQGTGAVIAAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLAAEYGVTREEALKSFYLVDSKGLVTTTRgDKL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 321 NHEKEMFAQ-DHPE----VNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYR 395
Cdd:PTZ00317 352 AKHKVPFARtDISAedssLKTLEDVVRFVKPTALLGLSGVGGVFTEEVVKTMASNVERPIIFPLSNPTSKAECTAEDAYK 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 396 VTEGRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPP 475
Cdd:PTZ00317 432 WTNGRAIVASGSPFPPVTL-NGKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAAASLATLVSEEDLREGKLYPP 510
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 966987707 476 LSTIRDVSLRIAIKVLDYAYKHNLA--SYYPEPKDK-EAFVRSLVYTP 520
Cdd:PTZ00317 511 LEDIREISAHIAVDVIEEAQEMGIAknKDLPDNRDElLALVKDRMWVP 558
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
243-520 1.01e-153

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: 440.45  E-value: 1.01e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLNH 322
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRKDLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 323 EKEMFAQDHPE--VNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTEGR 400
Cdd:cd05312   81 FKKPFARKDEEkeGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDAYKWTDGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 401 GIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLSTIR 480
Cdd:cd05312  161 ALFASGSPFPPVEY-NGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGRLYPPLSNIR 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 966987707 481 DVSLRIAIKVLDYAYKHNLASYYPEPKDKEAFVRSLVYTP 520
Cdd:cd05312  240 EISAQIAVAVAKYAYEEGLATRYPPPEDLEEYVKSQMWEP 279
Malic_M pfam03949
Malic enzyme, NAD binding domain;
243-494 3.82e-143

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 412.74  E-value: 3.82e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLNH 322
Cdd:pfam03949   1 IQGTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVREGLSEEEARKRIWMVDRQGLLTDDREDLTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  323 EKEMFAQDHPEVN------SLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRV 396
Cdd:pfam03949  81 FQKPFARKRAELKgwgdgiTLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAEATPEDAYKW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  397 TEGRGIFASGSPFKSVTLeDGKTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPL 476
Cdd:pfam03949 161 TDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQGRLLPPL 239
                         250
                  ....*....|....*...
gi 966987707  477 STIRDVSLRIAIKVLDYA 494
Cdd:pfam03949 240 SDIREVSRKIAVAVAKYA 257
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
38-517 4.80e-134

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: 395.53  E-value: 4.80e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  38 QQSDLDKYIILmtlqDRNEKLFYRVLTSDVEKFMPIVYTPTVGLACQHYGLTFRRPRGlfitihdkghlatmlnsWPEDN 117
Cdd:COG0281   10 EQEALEYHRIY----DRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYG-----------------YTAKG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 118 IKAVVVTDGERILGLGDLGCY-GMGIPVGKLALYTACGGVNpqqCLPVLLDvgTNNeellrdplyiglkhqrvrgkaydd 196
Cdd:COG0281   69 NLVAVVTDGTAVLGLGDIGPLaGMPVMEGKAVLFKAFAGID---AFPICLD--TND------------------------ 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 197 lLDEFMQAVTDKFGINCLIQFEDFANANAFRLLNKYRNK--YCMFNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQG 274
Cdd:COG0281  120 -PDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVING 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 275 AGEAAMGIAHLLVmaleKEGVPKaeatRKIWMVDSKGLIVKGRSHLNHEKEMFAQDHPEVN---SLEEVVRLVkpTAIIG 351
Cdd:COG0281  199 AGAAGIAIARLLV----AAGLSE----ENIIMVDSKGLLYEGRTDLNPYKREFARDTNPRGlkgTLAEAIKGA--DVFIG 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 352 VAAiAGAFTEQILRDMAsfhERPIIFALSNPTSkaECTAEKCYRVTEGRgIFASgspfksvtledGKTFIPGQGNNAYVF 431
Cdd:COG0281  269 VSA-PGAFTEEMVKSMA---KRPIIFALANPTP--EITPEDAKAWGDGA-IVAT-----------GRSDYPNQVNNVLIF 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 432 PGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLSTIRdVSLRIAIKVLDYAYKHNLASyYPEPKDKEA 511
Cdd:COG0281  331 PGIFRGALDVRATRITDEMKLAAARALADLVDEEELGPDYIIPSPFDPR-VSPAVAAAVAKAAIESGVAR-RPIDEDYRE 408

                 ....*.
gi 966987707 512 FVRSLV 517
Cdd:COG0281  409 ALEARM 414
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
243-494 6.90e-117

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: 345.74  E-value: 6.90e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEGVPKAEATRKIWMVDSKGLIVKGRSHLNH 322
Cdd:cd00762    1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKEGISKEEACKRIW*VDRKGLLVKNRKETCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 323 EKE---MFAQDHPEVNSLEEVVRLVKPTAIIGVAAIAGAFTEQILRDMASFHERPIIFALSNPTSKAECTAEKCYRVTEG 399
Cdd:cd00762   81 NEYhlaRFANPERESGDLEDAVEAAKPDFLIGVSRVGGAFTPEVIRA*AEINERPVIFALSNPTSKAECTAEEAYTATEG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 400 RGIFASGSPFKSVTLEDGkTFIPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPPLSTI 479
Cdd:cd00762  161 RAIFASGSPFHPVELNGG-TYKPGQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEAIASSVTEESLKPGRLYPPLFDI 239
                        250
                 ....*....|....*
gi 966987707 480 RDVSLRIAIKVLDYA 494
Cdd:cd00762  240 QEVSLNIAVAVAKYA 254
malic pfam00390
Malic enzyme, N-terminal domain;
52-233 3.77e-109

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 323.06  E-value: 3.77e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   52 QDRNEKLFYRVLTSDVEKFMPIVYTPTVGLACQHYGLTFRRPRGLFITIHDKGHLATMLNSWPEDNIKAVVVTDGERILG 131
Cdd:pfam00390   1 QGKNEVLFYKLLSTHIEEDLPIVYTPTVGEACQAISEIYRRPRGLYTSIGNLGKIKDILKNWPEEDVRVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707  132 LGDLGCYGMGIPVGKLALYTACGGVNPQQCLPVLLDVGTNNEELLRDPLYIGLKHQRVRGKAYDDLLDEFMQAVTDKFGI 211
Cdd:pfam00390  81 LGDLGVAGMPIMEGKLALYTAFAGIDPSRVLPIVLDVGTNNEKLLNDPLYLGLRHKRVRGEEYDEFVDEFVEAVKALFPP 160
                         170       180
                  ....*....|....*....|..
gi 966987707  212 NCLIQFEDFANANAFRLLNKYR 233
Cdd:pfam00390 161 FGGIQFEDFGAPNAFEILERYR 182
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
243-495 1.03e-101

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: 305.88  E-value: 1.03e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   243 IQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKEgvpkaeatRKIWMVDSKGLIVKGRS-HLN 321
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKR--------KNIWLVDSKGLLTKGREdNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   322 HEKEMFAQ--DHPEVNSLEEVVRlvKPTAIIGVAAIAGAFTEQILRDMAsfhERPIIFALSNPTSKAECTAEKCYRVTEg 399
Cdd:smart00919  73 PYKKPFARktNERETGTLEEAVK--GADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTAADAYRWTA- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707   400 rGIFASGSPFKsvtledgktfiPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQ--EVSEQHLSQGRLYPPLS 477
Cdd:smart00919 147 -AIVATGRSDY-----------PNQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADavPVSEEELGPGYIIPSPF 214
                          250
                   ....*....|....*...
gi 966987707   478 TiRDVSLRIAIKVLDYAY 495
Cdd:smart00919 215 D-RRVSARVAVAVAKAAI 231
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
244-475 2.44e-27

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: 109.66  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 244 QGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMAlekeGVPKaeatRKIWMVDSKGLIVKGR-----S 318
Cdd:cd05311    2 HGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAA----GAKP----ENIVVVDSKGVIYEGReddlnP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 319 HLNHEKEMFAQDHPEVnSLEEVVRlvKPTAIIGVAAiAGAFTEQILRDMAsfhERPIIFALSNPTSkaECTAEKCYRVte 398
Cdd:cd05311   74 DKNEIAKETNPEKTGG-TLKEALK--GADVFIGVSR-PGVVKKEMIKKMA---KDPIVFALANPVP--EIWPEEAKEA-- 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966987707 399 GRGIFASG-SPFksvtledgktfiPGQGNNAYVFPGVALGVIAGGIRHIPDEIFLLTAEQIAQEVSEQHLSQGRLYPP 475
Cdd:cd05311  143 GADIVATGrSDF------------PNQVNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVLGEEYIIPT 208
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
239-473 4.30e-23

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 103.64  E-value: 4.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 239 FNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVmALekeGVPKAeatrKIWMVDSKGLIVKGRS 318
Cdd:PRK07232 157 FHDDQHGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLV-AL---GAKKE----NIIVCDSKGVIYKGRT 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 319 -HLNHEKEMFAQDhPEVNSLEEVVrlvkPTA--IIGVAAiAGAFTEQILRDMAsfhERPIIFALSNPTskAECTAEKCYR 395
Cdd:PRK07232 229 eGMDEWKAAYAVD-TDARTLAEAI----EGAdvFLGLSA-AGVLTPEMVKSMA---DNPIIFALANPD--PEITPEEAKA 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 396 VtegRG--IFASG-SPFksvtledgktfiPGQGNNA----YVFPGvALGViagGIRHIPDEIFLLTAEQIA----QEVSE 464
Cdd:PRK07232 298 V---RPdaIIATGrSDY------------PNQVNNVlcfpYIFRG-ALDV---GATTINEEMKLAAVRAIAelarEEVSD 358
                        250
                 ....*....|....*..
gi 966987707 465 --------QHLSQGRLY 473
Cdd:PRK07232 359 evaaayggQKLSFGPEY 375
PRK12862 PRK12862
malic enzyme; Reviewed
122-464 4.65e-22

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 100.35  E-value: 4.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 122 VVTDGERILGLGDLGCYGmGIPV--GKLALYTACGGVNpqqclpvLLDVGTNNeellRDPlyiglkhqrvrgkaydDLLD 199
Cdd:PRK12862  75 VVSNGTAVLGLGNIGPLA-SKPVmeGKAVLFKKFAGID-------VFDIELDE----SDP----------------DKLV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 200 EFMQAVTDKFG-INcliqFEDFANANAFRLLNKYRNKycM----FNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQG 274
Cdd:PRK12862 127 EIVAALEPTFGgIN----LEDIKAPECFYIERELRER--MkipvFHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASG 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 275 AGEAAMGIAHLLVmaleKEGVPKAeatrKIWMVDSKGLIVKGRSHL-NHEKEMFAQDhPEVNSLEEVVrlvkPTA--IIG 351
Cdd:PRK12862 201 AGAAALACLDLLV----SLGVKRE----NIWVTDIKGVVYEGRTELmDPWKARYAQK-TDARTLAEVI----EGAdvFLG 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 352 VAAiAGAFTEQILRDMAsfhERPIIFALSNPTskAECTAEKCYRVtegRG--IFASG-SPFksvtledgktfiPGQGNNA 428
Cdd:PRK12862 268 LSA-AGVLKPEMVKKMA---PRPLIFALANPT--PEILPEEARAV---RPdaIIATGrSDY------------PNQVNNV 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 966987707 429 YVFPGV---ALGViagGIRHIPDEIFLLTAEQIA----QEVSE 464
Cdd:PRK12862 327 LCFPYIfrgALDV---GATTINEEMKIAAVRAIAelarEEQSD 366
PRK12861 PRK12861
malic enzyme; Reviewed
122-465 5.47e-17

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 84.56  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 122 VVTDGERILGLGDLGCYGmGIPV--GKLALYTACGGVNpqqclpvLLDVGTNNEellrDPlyiglkhqrvrgkaydDLLD 199
Cdd:PRK12861  71 VITNGTAVLGLGNIGALA-SKPVmeGKAVLFKKFAGID-------VFDIEINET----DP----------------DKLV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 200 EFMQAVTDKFGincLIQFEDFANANAFRLLNKYRN--KYCMFNDDIQGTASVAVAGILAALRITKNKLSNHVFVFQGAGE 277
Cdd:PRK12861 123 DIIAGLEPTFG---GINLEDIKAPECFTVERKLRErmKIPVFHDDQHGTAITVSAAFINGLKVVGKSIKEVKVVTSGAGA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 278 AAMGIAHLLVmaleKEGVPkaeaTRKIWMVDSKGLIVKGRSHL-NHEKEMFAQDhPEVNSLEEVVRlvKPTAIIGVAAiA 356
Cdd:PRK12861 200 AALACLDLLV----DLGLP----VENIWVTDIEGVVYRGRTTLmDPDKERFAQE-TDARTLAEVIG--GADVFLGLSA-G 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966987707 357 GAFTEQILRDMASfheRPIIFALSNPTskAECTAEKCYRVTEgrgifasgspfkSVTLEDGKTFIPGQGNNAYVFPGVAL 436
Cdd:PRK12861 268 GVLKAEMLKAMAA---RPLILALANPT--PEIFPELAHATRD------------DVVIATGRSDYPNQVNNVLCFPYIFR 330
                        330       340
                 ....*....|....*....|....*....
gi 966987707 437 GVIAGGIRHIPDEIFLLTAEQIAQEVSEQ 465
Cdd:PRK12861 331 GALDVGATTITREMEIAAVHAIAGLAEEE 359
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
245-293 1.83e-06

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (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: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 46.22  E-value: 1.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 966987707 245 GTASVAVAGILAALRITKNKLSNHVFVFQGAGEAAMGIAHLLVMALEKE 293
Cdd:cd05191    1 ATAAGAVALLKAAGKVTNKSLKGKTVVVLGAGEVGKGIAKLLADEGGKK 49
 
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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