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Conserved domains on  [gi|270265879|ref|NP_001161807|]
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NAD-dependent malic enzyme, mitochondrial isoform 2 precursor [Homo sapiens]

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
28-473 0e+00

NADP-dependent malic enzyme; Provisional


:

Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 721.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  28 LMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESL 107
Cdd:PLN03129  45 LLRDPRYNKGLAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEEL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 108 MPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLY 187
Cdd:PLN03129 125 LPIVYTPTVGEACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLY 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 188 TACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLR 267
Cdd:PLN03129 205 TAAGGIRPSAVLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQ 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 268 KYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVE-NGLSEQEAQKKIWMFDK 346
Cdd:PLN03129 285 RYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDS 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 347 YGLLVKGRKAKIDSYQEPFTHSAPESipDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQA 426
Cdd:PLN03129 365 KGLVTKSRKDSLQPFKKPFAHDHEPG--ASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKA 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 270265879 427 ECTAEEAYTLTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:PLN03129 443 ECTAEEAYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPG 488
 
Name Accession Description Interval E-value
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
28-473 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 721.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  28 LMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESL 107
Cdd:PLN03129  45 LLRDPRYNKGLAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEEL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 108 MPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLY 187
Cdd:PLN03129 125 LPIVYTPTVGEACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLY 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 188 TACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLR 267
Cdd:PLN03129 205 TAAGGIRPSAVLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQ 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 268 KYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVE-NGLSEQEAQKKIWMFDK 346
Cdd:PLN03129 285 RYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDS 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 347 YGLLVKGRKAKIDSYQEPFTHSAPESipDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQA 426
Cdd:PLN03129 365 KGLVTKSRKDSLQPFKKPFAHDHEPG--ASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKA 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 270265879 427 ECTAEEAYTLTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:PLN03129 443 ECTAEEAYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPG 488
malic pfam00390
Malic enzyme, N-terminal domain;
89-270 2.66e-109

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 321.52  E-value: 2.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   89 QERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILG 168
Cdd:pfam00390   1 QGKNEVLFYKLLSTHIEEDLPIVYTPTVGEACQAISEIYRRPRGLYTSIGNLGKIKDILKNWPEEDVRVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  169 LGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGR 248
Cdd:pfam00390  81 LGDLGVAGMPIMEGKLALYTAFAGIDPSRVLPIVLDVGTNNEKLLNDPLYLGLRHKRVRGEEYDEFVDEFVEAVKALFPP 160
                         170       180
                  ....*....|....*....|..
gi 270265879  249 NTLIQFEDFGNHNAFRFLRKYR 270
Cdd:pfam00390 161 FGGIQFEDFGAPNAFEILERYR 182
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
280-473 3.85e-103

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: 309.48  E-value: 3.85e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKaKID 359
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRK-DLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 360 SYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEG 439
Cdd:cd05312   80 PFKKPFARKDEEKEGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDAYKWTDG 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 270265879 440 RCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:cd05312  160 RALFASGSPFPPVEY-NGKTYVPGQGNNAYIFPG 192
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
77-473 2.96e-101

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: 309.25  E-value: 2.96e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  77 SPLEKYiyimGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGlfisisdrghvrsivdnWPENHVK 156
Cdd:COG0281   12 EALEYH----RIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYG-----------------YTAKGNL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 157 AVVVTDGERILGLGDLGVY-GMGIPVGKLCLYTACAGIrpDrCLPVCIDvgTDNIallkdpfymglyqkrdrtqqyddli 235
Cdd:COG0281   71 VAVVTDGTAVLGLGDIGPLaGMPVMEGKAVLFKAFAGI--D-AFPICLD--TNDP------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 236 DEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREK--YCTFNDDIQGTAavalagllaaqkVIS------------KP 301
Cdd:COG0281  121 DEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTA------------IVVlaallnalklvgKK 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 302 ISEHKILFLGAGEAALGIANLIVmSMvenGLSEqeaqKKIWMFDKYGLLVKGRKaKIDSYQEPF-THSAPESIPDTFEDA 380
Cdd:COG0281  189 LEDQKIVINGAGAAGIAIARLLV-AA---GLSE----ENIIMVDSKGLLYEGRT-DLNPYKREFaRDTNPRGLKGTLAEA 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 381 VnilKPSTI-IGVAGAGrLFTPDVIRAMAsinERPVIFALSNPTaqAECTAEEAYTLTEGRcLFASgspfgpvkltdGRV 459
Cdd:COG0281  260 I---KGADVfIGVSAPG-AFTEEMVKSMA---KRPIIFALANPT--PEITPEDAKAWGDGA-IVAT-----------GRS 318
                        410
                 ....*....|....
gi 270265879 460 FTPGQGNNVYIFPG 473
Cdd:COG0281  319 DYPNQVNNVLIFPG 332
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
280-473 4.45e-62

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: 201.87  E-value: 4.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENglseqeaqKKIWMFDKYGLLVKGRKAKID 359
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKR--------KNIWLVDSKGLLTKGREDNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   360 SYQEPFTHSAPESIPDTFEDAVNilKPSTIIGVAGAGRLFTPDVIRAMAsinERPVIFALSNPTAQAECTAEEAYTLTEg 439
Cdd:smart00919  73 PYKKPFARKTNERETGTLEEAVK--GADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTAADAYRWTA- 146
                          170       180       190
                   ....*....|....*....|....*....|....
gi 270265879   440 rCLFASGSPFGpvkltdgrvftPGQGNNVYIFPG 473
Cdd:smart00919 147 -AIVATGRSDY-----------PNQVNNVLIFPG 168
 
Name Accession Description Interval E-value
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
28-473 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 721.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  28 LMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESL 107
Cdd:PLN03129  45 LLRDPRYNKGLAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNERLFYRVLIDNIEEL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 108 MPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLY 187
Cdd:PLN03129 125 LPIVYTPTVGEACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGVQGMGIPVGKLDLY 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 188 TACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLR 267
Cdd:PLN03129 205 TAAGGIRPSAVLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWGPKVLVQFEDFANKNAFRLLQ 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 268 KYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVE-NGLSEQEAQKKIWMFDK 346
Cdd:PLN03129 285 RYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqTGISEEEARKRIWLVDS 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 347 YGLLVKGRKAKIDSYQEPFTHSAPESipDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQA 426
Cdd:PLN03129 365 KGLVTKSRKDSLQPFKKPFAHDHEPG--ASLLEAVKAIKPTVLIGLSGVGGTFTKEVLEAMASLNERPIIFALSNPTSKA 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 270265879 427 ECTAEEAYTLTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:PLN03129 443 ECTAEEAYTWTGGRAIFASGSPFDPVEY-NGKTFHPGQANNAYIFPG 488
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
15-473 0e+00

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 669.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  15 ACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEK 94
Cdd:PRK13529   7 KKRPLYTPLRGPALLNNPLLNKGTAFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTDLEKHIYLRNLQDRNET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  95 LFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGV 174
Cdd:PRK13529  87 LFYRLLSDHLEEMMPIIYTPTVGEACERFSHIYRRPRGLFISYDDRDRIEDILQNAPNRDIKLIVVTDGERILGIGDQGI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 175 YGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYgRNTLIQF 254
Cdd:PRK13529 167 GGMGIPIGKLSLYTACGGIDPARTLPVVLDVGTNNEQLLNDPLYLGWRHPRIRGEEYDEFVDEFVQAVKRRF-PNALLQF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 255 EDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSE 334
Cdd:PRK13529 246 EDFAQKNARRILERYRDEICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSE 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 335 QEAQKKIWMFDKYGLLVKGRkAKIDSYQEPFTHSAPE-------SIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAM 407
Cdd:PRK13529 326 EEARKRFFMVDRQGLLTDDM-PDLLDFQKPYARKREEladwdteGDVISLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEM 404
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 270265879 408 ASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:PRK13529 405 AAHCERPIIFPLSNPTSRAEATPEDLIAWTDGRALVATGSPFAPVEY-NGKTYPIGQCNNAYIFPG 469
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
19-473 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 564.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  19 LHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYR 98
Cdd:PTZ00317  13 VPSNARGVDVLRNRFLNKGTAFTAEEREHLGIEGLLPPTVETLEQQVERLWTQFNRIETPINKYQFLRNIHDTNETLFYA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  99 ILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMG 178
Cdd:PTZ00317  93 LLLKYLKELLPIIYTPTVGEACQNYSNLFQRDRGLYLSRAHKGKIREILKNWPYDNVDVIVITDGSRILGLGDLGANGMG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 179 IPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYgRNTLIQFEDFG 258
Cdd:PTZ00317 173 ISIGKLSLYVAGGGINPSRVLPVVLDVGTNNEKLLNDPLYLGLREKRLDDDEYYELLDEFMEAVSSRW-PNAVVQFEDFS 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 259 NHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQ 338
Cdd:PTZ00317 252 NNHCFDLLERYQNKYRCFNDDIQGTGAVIAAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLAAEYGVTREEAL 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 339 KKIWMFDKYGLLVKGRKAKIDSYQEPF--THSAPESIP-DTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPV 415
Cdd:PTZ00317 332 KSFYLVDSKGLVTTTRGDKLAKHKVPFarTDISAEDSSlKTLEDVVRFVKPTALLGLSGVGGVFTEEVVKTMASNVERPI 411
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 270265879 416 IFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:PTZ00317 412 IFPLSNPTSKAECTAEDAYKWTNGRAIVASGSPFPPVTL-NGKTIQPSQGNNLYVFPG 468
malic pfam00390
Malic enzyme, N-terminal domain;
89-270 2.66e-109

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 321.52  E-value: 2.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   89 QERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILG 168
Cdd:pfam00390   1 QGKNEVLFYKLLSTHIEEDLPIVYTPTVGEACQAISEIYRRPRGLYTSIGNLGKIKDILKNWPEEDVRVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  169 LGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGR 248
Cdd:pfam00390  81 LGDLGVAGMPIMEGKLALYTAFAGIDPSRVLPIVLDVGTNNEKLLNDPLYLGLRHKRVRGEEYDEFVDEFVEAVKALFPP 160
                         170       180
                  ....*....|....*....|..
gi 270265879  249 NTLIQFEDFGNHNAFRFLRKYR 270
Cdd:pfam00390 161 FGGIQFEDFGAPNAFEILERYR 182
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
280-473 3.85e-103

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: 309.48  E-value: 3.85e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKaKID 359
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRK-DLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 360 SYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEG 439
Cdd:cd05312   80 PFKKPFARKDEEKEGKSLLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDAYKWTDG 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 270265879 440 RCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:cd05312  160 RALFASGSPFPPVEY-NGKTYVPGQGNNAYIFPG 192
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
280-473 2.01e-102

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: 306.45  E-value: 2.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKID 359
Cdd:cd00762    1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKEGISKEEACKRIW*VDRKGLLVKNRKETCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 360 SYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEG 439
Cdd:cd00762   81 NEYHLARFANPERESGDLEDAVEAAKPDFLIGVSRVGGAFTPEVIRA*AEINERPVIFALSNPTSKAECTAEEAYTATEG 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 270265879 440 RCLFASGSPFGPVKLTDGrVFTPGQGNNVYIFPG 473
Cdd:cd00762  161 RAIFASGSPFHPVELNGG-TYKPGQGNNLYIFPG 193
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
77-473 2.96e-101

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: 309.25  E-value: 2.96e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  77 SPLEKYiyimGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGlfisisdrghvrsivdnWPENHVK 156
Cdd:COG0281   12 EALEYH----RIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYG-----------------YTAKGNL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 157 AVVVTDGERILGLGDLGVY-GMGIPVGKLCLYTACAGIrpDrCLPVCIDvgTDNIallkdpfymglyqkrdrtqqyddli 235
Cdd:COG0281   71 VAVVTDGTAVLGLGDIGPLaGMPVMEGKAVLFKAFAGI--D-AFPICLD--TNDP------------------------- 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 236 DEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREK--YCTFNDDIQGTAavalagllaaqkVIS------------KP 301
Cdd:COG0281  121 DEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTA------------IVVlaallnalklvgKK 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 302 ISEHKILFLGAGEAALGIANLIVmSMvenGLSEqeaqKKIWMFDKYGLLVKGRKaKIDSYQEPF-THSAPESIPDTFEDA 380
Cdd:COG0281  189 LEDQKIVINGAGAAGIAIARLLV-AA---GLSE----ENIIMVDSKGLLYEGRT-DLNPYKREFaRDTNPRGLKGTLAEA 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 381 VnilKPSTI-IGVAGAGrLFTPDVIRAMAsinERPVIFALSNPTaqAECTAEEAYTLTEGRcLFASgspfgpvkltdGRV 459
Cdd:COG0281  260 I---KGADVfIGVSAPG-AFTEEMVKSMA---KRPIIFALANPT--PEITPEDAKAWGDGA-IVAT-----------GRS 318
                        410
                 ....*....|....
gi 270265879 460 FTPGQGNNVYIFPG 473
Cdd:COG0281  319 DYPNQVNNVLIFPG 332
Malic_M pfam03949
Malic enzyme, NAD binding domain;
280-473 4.56e-94

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 285.24  E-value: 4.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKaKID 359
Cdd:pfam03949   1 IQGTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVREGLSEEEARKRIWMVDRQGLLTDDRE-DLT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879  360 SYQEPFTHSAPESIPD----TFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYT 435
Cdd:pfam03949  80 DFQKPFARKRAELKGWgdgiTLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAEATPEDAYK 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 270265879  436 LTEGRCLFASGSPFGPVKLtDGRVFTPGQGNNVYIFPG 473
Cdd:pfam03949 160 WTDGRALFATGSPFPPVEY-NGKTYHIGQGNNAYIFPG 196
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
280-473 4.45e-62

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: 201.87  E-value: 4.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   280 IQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENglseqeaqKKIWMFDKYGLLVKGRKAKID 359
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKR--------KNIWLVDSKGLLTKGREDNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879   360 SYQEPFTHSAPESIPDTFEDAVNilKPSTIIGVAGAGRLFTPDVIRAMAsinERPVIFALSNPTAQAECTAEEAYTLTEg 439
Cdd:smart00919  73 PYKKPFARKTNERETGTLEEAVK--GADVLIGVSGPGGAFTEEMVKSMA---ERPIIFALSNPTPEIEPTAADAYRWTA- 146
                          170       180       190
                   ....*....|....*....|....*....|....
gi 270265879   440 rCLFASGSPFGpvkltdgrvftPGQGNNVYIFPG 473
Cdd:smart00919 147 -AIVATGRSDY-----------PNQVNNVLIFPG 168
PRK12862 PRK12862
malic enzyme; Reviewed
159-473 9.57e-20

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 92.64  E-value: 9.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 159 VVTDGERILGLGDLGVYGmGIPV--GKLCLYTACAGIrpDrclpvCIDVGTDNiallKDPfymglyqkrdrtqqyDDLId 236
Cdd:PRK12862  75 VVSNGTAVLGLGNIGPLA-SKPVmeGKAVLFKKFAGI--D-----VFDIELDE----SDP---------------DKLV- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 237 EFMKAITDRYGRntlIQFEDFGNHNAFRFLRKYRE--KYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGE 314
Cdd:PRK12862 127 EIVAALEPTFGG---INLEDIKAPECFYIERELRErmKIPVFHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGA 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 315 AALGIANLIVmSM---VENglseqeaqkkIWMFDKYGLLVKGRKAKIDSYQEPFthsAPESIPDTFEDAV---NILkpst 388
Cdd:PRK12862 204 AALACLDLLV-SLgvkREN----------IWVTDIKGVVYEGRTELMDPWKARY---AQKTDARTLAEVIegaDVF---- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 389 iIGVAGAGrLFTPDVIRAMAsinERPVIFALSNPTaqAECTAEEAYtltEGR--CLFASgspfgpvkltdGRVFTPGQGN 466
Cdd:PRK12862 266 -LGLSAAG-VLKPEMVKKMA---PRPLIFALANPT--PEILPEEAR---AVRpdAIIAT-----------GRSDYPNQVN 324
                        330
                 ....*....|.
gi 270265879 467 NV----YIFPG 473
Cdd:PRK12862 325 NVlcfpYIFRG 335
PRK12861 PRK12861
malic enzyme; Reviewed
108-472 1.06e-17

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 86.10  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 108 MPIVYTPTVGLACSQyghIFRRPKGLFiSISDRGHVRSivdnwpenhvkavVVTDGERILGLGDLGVYGmGIPV--GKLC 185
Cdd:PRK12861  37 LALAYTPGVASACEE---IAADPLNAF-RFTSRGNLVG-------------VITNGTAVLGLGNIGALA-SKPVmeGKAV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 186 LYTACAGIrpdrclpvciDVGTDNIALlKDPfymglyqkrdrtqqyDDLIDeFMKAITDRYGRntlIQFEDFGNHNAFRF 265
Cdd:PRK12861  99 LFKKFAGI----------DVFDIEINE-TDP---------------DKLVD-IIAGLEPTFGG---INLEDIKAPECFTV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 266 LRKYRE--KYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLivmsMVENGLSEQEaqkkIWM 343
Cdd:PRK12861 149 ERKLRErmKIPVFHDDQHGTAITVSAAFINGLKVVGKSIKEVKVVTSGAGAAALACLDL----LVDLGLPVEN----IWV 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 344 FDKYGLLVKGRKAKIDSYQEPFthsAPESIPDTFEDAvnILKPSTIIGVAgAGRLFTPDVIRAMASineRPVIFALSNPT 423
Cdd:PRK12861 221 TDIEGVVYRGRTTLMDPDKERF---AQETDARTLAEV--IGGADVFLGLS-AGGVLKAEMLKAMAA---RPLILALANPT 291
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 270265879 424 aqAECTAEEAYTLTEGrclfasgspfgpVKLTDGRVFTPGQGNNVYIFP 472
Cdd:PRK12861 292 --PEIFPELAHATRDD------------VVIATGRSDYPNQVNNVLCFP 326
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
281-473 3.73e-15

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: 74.61  E-value: 3.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 281 QGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVEnglseqeaQKKIWMFDKYGLLVKGRKAKIDS 360
Cdd:cd05311    2 HGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAK--------PENIVVVDSKGVIYEGREDDLNP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 361 Y-QEPFTHSAPESIPDTFEDAvniLKPSTI-IGVAGAGRLfTPDVIRAMasiNERPVIFALSNPTaqAECTAEEAytlte 438
Cdd:cd05311   74 DkNEIAKETNPEKTGGTLKEA---LKGADVfIGVSRPGVV-KKEMIKKM---AKDPIVFALANPV--PEIWPEEA----- 139
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 270265879 439 grclfasgSPFGPVKLTDGRVFTPGQGNNVYIFPG 473
Cdd:cd05311  140 --------KEAGADIVATGRSDFPNQVNNVLGFPG 166
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
159-473 1.19e-12

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 70.12  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 159 VVTDGERILGLGDLGVYGmGIPV--GKLCLYTACAGIrpDrclpvCIDVGTDNiallKDPfymglyqkrdrtqqyddliD 236
Cdd:PRK07232  67 VISNGTAVLGLGNIGALA-SKPVmeGKGVLFKKFAGI--D-----VFDIEVDE----EDP-------------------D 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 237 EFMKAItdRYGRNTL--IQFEDFGNHNAFRFLRKYRE--KYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGA 312
Cdd:PRK07232 116 KFIEAV--AALEPTFggINLEDIKAPECFYIEEKLRErmDIPVFHDDQHGTAIISAAALLNALELVGKKIEDVKIVVSGA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 313 GEAALGIANLIVmSM---VENglseqeaqkkIWMFDKYGLLVKGRKAKIDSYQEPFthsAPESIPDTFEDAVN---ILkp 386
Cdd:PRK07232 194 GAAAIACLNLLV-ALgakKEN----------IIVCDSKGVIYKGRTEGMDEWKAAY---AVDTDARTLAEAIEgadVF-- 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 387 stiIGVAGAGrLFTPDVIRAMAsinERPVIFALSNPTaqAECTAEEAYtltEGR--CLFASG-SPFgpvkltdgrvftPG 463
Cdd:PRK07232 258 ---LGLSAAG-VLTPEMVKSMA---DNPIIFALANPD--PEITPEEAK---AVRpdAIIATGrSDY------------PN 313
                        330
                 ....*....|....
gi 270265879 464 QGNNV----YIFPG 473
Cdd:PRK07232 314 QVNNVlcfpYIFRG 327
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
295-420 7.91e-08

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: 49.68  E-value: 7.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265879 295 QKVISKPISEHKILFLGAGEAALGIANLIVmsmvenglseQEAQKKIWMFDKygllvkgrkakidsyqepfthsapesip 374
Cdd:cd05191   14 GKVTNKSLKGKTVVVLGAGEVGKGIAKLLA----------DEGGKKVVLCDR---------------------------- 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 270265879 375 dtfedavnilkpSTIIGVAGAGRLFTPdviRAMASINERPVIFALS 420
Cdd:cd05191   56 ------------DILVTATPAGVPVLE---EATAKINEGAVVIDLA 86
 
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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