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Conserved domains on  [gi|518794103|ref|WP_019951392|]
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NAD-dependent malic enzyme [Kushneria aurantia]

Protein Classification

NAD-dependent malic enzyme( domain architecture ID 11486672)

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
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
7-561 0e+00

oxaloacetate-decarboxylating malate dehydrogenase;


:

Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 998.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   7 RPLYIVHSGPTLLETPLLNKDSAFSLEERIQFNLLGLLPQNIETIEEQADRAYRQYEQQGSDLDRHIYLRSIQDSNETLF 86
Cdd:PRK13529   9 RPLYTPLRGPALLNNPLLNKGTAFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTDLEKHIYLRNLQDRNETLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  87 FRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILGLGDQGIGG 166
Cdd:PRK13529  89 YRLLSDHLEEMMPIIYTPTVGEACERFSHIYRRPRGLFISYDDRDRIEDILQNAPNRDIKLIVVTDGERILGIGDQGIGG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 167 MGIPIGKLSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRWPNAIIQFEDF 246
Cdd:PRK13529 169 MGIPIGKLSLYTACGGIDPARTLPVVLDVGTNNEQLLNDPLYLGWRHPRIRGEEYDEFVDEFVQAVKRRFPNALLQFEDF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 247 AQANAMPLLERYRDEVCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEA 326
Cdd:PRK13529 249 AQKNARRILERYRDEICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSEEEA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 327 RKRVFMVDRYGLLTDDMSNLVNFQRKLVQKRADLADWDTGDGDLALIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNC 406
Cdd:PRK13529 329 RKRFFMVDRQGLLTDDMPDLLDFQKPYARKREELADWDTEGDVISLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHC 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 407 EEPLVMPLSNPTSRVEATPREILEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLM 486
Cdd:PRK13529 409 ERPIIFPLSNPTSRAEATPEDLIAWTDGRALVATGSPFAPVEYNGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLM 488
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518794103 487 SAARALADCSPVAIDGKGAVLPPLADIQQVSRKIAIAVAKRAQQDGVALETDDATIEKAIDDNFWLPRYRHYRRA 561
Cdd:PRK13529 489 AAAHALADCVPLAKPGEGALLPPVEDIREVSRAIAIAVAKAAIEEGLARETSDEDLEQAIEDNMWQPEYRPYRRT 563
 
Name Accession Description Interval E-value
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
7-561 0e+00

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 998.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   7 RPLYIVHSGPTLLETPLLNKDSAFSLEERIQFNLLGLLPQNIETIEEQADRAYRQYEQQGSDLDRHIYLRSIQDSNETLF 86
Cdd:PRK13529   9 RPLYTPLRGPALLNNPLLNKGTAFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTDLEKHIYLRNLQDRNETLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  87 FRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILGLGDQGIGG 166
Cdd:PRK13529  89 YRLLSDHLEEMMPIIYTPTVGEACERFSHIYRRPRGLFISYDDRDRIEDILQNAPNRDIKLIVVTDGERILGIGDQGIGG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 167 MGIPIGKLSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRWPNAIIQFEDF 246
Cdd:PRK13529 169 MGIPIGKLSLYTACGGIDPARTLPVVLDVGTNNEQLLNDPLYLGWRHPRIRGEEYDEFVDEFVQAVKRRFPNALLQFEDF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 247 AQANAMPLLERYRDEVCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEA 326
Cdd:PRK13529 249 AQKNARRILERYRDEICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSEEEA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 327 RKRVFMVDRYGLLTDDMSNLVNFQRKLVQKRADLADWDTGDGDLALIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNC 406
Cdd:PRK13529 329 RKRFFMVDRQGLLTDDMPDLLDFQKPYARKREELADWDTEGDVISLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHC 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 407 EEPLVMPLSNPTSRVEATPREILEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLM 486
Cdd:PRK13529 409 ERPIIFPLSNPTSRAEATPEDLIAWTDGRALVATGSPFAPVEYNGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLM 488
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518794103 487 SAARALADCSPVAIDGKGAVLPPLADIQQVSRKIAIAVAKRAQQDGVALETDDATIEKAIDDNFWLPRYRHYRRA 561
Cdd:PRK13529 489 AAAHALADCVPLAKPGEGALLPPVEDIREVSRAIAIAVAKAAIEEGLARETSDEDLEQAIEDNMWQPEYRPYRRT 563
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
67-550 2.40e-144

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: 422.50  E-value: 2.40e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  67 SDLDRHiylrSIQDSNETLFFRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLfisydhrdhitdilhsaTKDNVK 146
Cdd:COG0281   12 EALEYH----RIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGY-----------------TAKGNL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 147 VVVITDSERILGLGDQgiggm-gipigKLSLYTACGGISpayTMPIVLDvgTNNddllddpmymgwrhervtgddyydfV 225
Cdd:COG0281   71 VAVVTDGTAVLGLGDIgplagmpvmegKAVLFKAFAGID---AFPICLD--TND-------------------------P 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 226 DRCVQGIRKRWPN-AIIQFEDFAQANAMPLLERYRDE--VCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITF---- 298
Cdd:COG0281  121 DEFVEAVKALEPTfGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVIngag 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 299 -----VGagsagagiaeQIILAMqeeGISEaearKRVFMVDRYGLLTDDMSNLVNFQRKLVQKRADladwDTGDGDLAli 373
Cdd:COG0281  201 aagiaIA----------RLLVAA---GLSE----ENIIMVDSKGLLYEGRTDLNPYKREFARDTNP----RGLKGTLA-- 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 374 DVVRNAkpTVLIGVSgQRGLFTEEVIRTMqsnCEEPLVMPLSNPTSrvEATPREILEWTDGkALVSTGspfkpvslgeRK 453
Cdd:COG0281  258 EAIKGA--DVFIGVS-APGAFTEEMVKSM---AKRPIIFALANPTP--EITPEDAKAWGDG-AIVATG----------RS 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 454 IPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLPPLADIqQVSRKIAIAVAKRAQQDGV 533
Cdd:COG0281  319 DYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGPDYIIPSPFDP-RVSPAVAAAVAKAAIESGV 397
                        490
                 ....*....|....*..
gi 518794103 534 ALETDDATIEKAIDDNF 550
Cdd:COG0281  398 ARRPIDEDYREALEARM 414
Malic_M pfam03949
Malic enzyme, NAD binding domain;
269-528 1.32e-132

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 386.55  E-value: 1.32e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMVDRYGLLTDDMSNLVN 348
Cdd:pfam03949   1 IQGTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVREGLSEEEARKRIWMVDRQGLLTDDREDLTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  349 FQRKLVQKRADLADWDtgdGDLALIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVMPLSNPTSRVEATPREI 428
Cdd:pfam03949  81 FQKPFARKRAELKGWG---DGITLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAEATPEDA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  429 LEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:pfam03949 158 YKWTDGRALFATGSPFPPVEYNGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQGRLLP 237
                         250       260
                  ....*....|....*....|
gi 518794103  509 PLADIQQVSRKIAIAVAKRA 528
Cdd:pfam03949 238 PLSDIREVSRKIAVAVAKYA 257
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
269-553 6.49e-118

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: 349.92  E-value: 6.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMVDRYGLLTDDMSNLVN 348
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRKDLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 349 FQRKLVQKRADladWDTGDgdlaLIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVMPLSNPTSRVEATPREI 428
Cdd:cd05312   81 FKKPFARKDEE---KEGKS----LLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 429 LEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:cd05312  154 YKWTDGRALFASGSPFPPVEYNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGRLYP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 518794103 509 PLADIQQVSRKIAIAVAKRAQQDGVA-LETDDATIEKAIDDNFWLP 553
Cdd:cd05312  234 PLSNIREISAQIAVAVAKYAYEEGLAtRYPPPEDLEEYVKSQMWEP 279
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
269-529 6.65e-85

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: 263.51  E-value: 6.65e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEegiseaeaRKRVFMVDRYGLLTDDMSNLVN 348
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVK--------RKNIWLVDSKGLLTKGREDNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   349 -FQRKLVQKRADLADWDtgdgdlaLIDVVRnaKPTVLIGVSGQRGLFTEEVIRTMqsnCEEPLVMPLSNPTSRVEATPRE 427
Cdd:smart00919  73 pYKKPFARKTNERETGT-------LEEAVK--GADVLIGVSGPGGAFTEEMVKSM---AERPIIFALSNPTPEIEPTAAD 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   428 ILEWTDgkALVSTGSPFKPvslgerkipiAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAID--GKGA 505
Cdd:smart00919 141 AYRWTA--AIVATGRSDYP----------NQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADAVPVSEEelGPGY 208
                          250       260
                   ....*....|....*....|....
gi 518794103   506 VLPPLADiQQVSRKIAIAVAKRAQ 529
Cdd:smart00919 209 IIPSPFD-RRVSARVAVAVAKAAI 231
 
Name Accession Description Interval E-value
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
7-561 0e+00

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 998.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   7 RPLYIVHSGPTLLETPLLNKDSAFSLEERIQFNLLGLLPQNIETIEEQADRAYRQYEQQGSDLDRHIYLRSIQDSNETLF 86
Cdd:PRK13529   9 RPLYTPLRGPALLNNPLLNKGTAFTEEEREEFGLEGLLPPAVETLEEQAERAYRQYQSKPTDLEKHIYLRNLQDRNETLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  87 FRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILGLGDQGIGG 166
Cdd:PRK13529  89 YRLLSDHLEEMMPIIYTPTVGEACERFSHIYRRPRGLFISYDDRDRIEDILQNAPNRDIKLIVVTDGERILGIGDQGIGG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 167 MGIPIGKLSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRWPNAIIQFEDF 246
Cdd:PRK13529 169 MGIPIGKLSLYTACGGIDPARTLPVVLDVGTNNEQLLNDPLYLGWRHPRIRGEEYDEFVDEFVQAVKRRFPNALLQFEDF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 247 AQANAMPLLERYRDEVCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEA 326
Cdd:PRK13529 249 AQKNARRILERYRDEICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVREGLSEEEA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 327 RKRVFMVDRYGLLTDDMSNLVNFQRKLVQKRADLADWDTGDGDLALIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNC 406
Cdd:PRK13529 329 RKRFFMVDRQGLLTDDMPDLLDFQKPYARKREELADWDTEGDVISLLEVVRNVKPTVLIGVSGQPGAFTEEIVKEMAAHC 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 407 EEPLVMPLSNPTSRVEATPREILEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLM 486
Cdd:PRK13529 409 ERPIIFPLSNPTSRAEATPEDLIAWTDGRALVATGSPFAPVEYNGKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLM 488
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518794103 487 SAARALADCSPVAIDGKGAVLPPLADIQQVSRKIAIAVAKRAQQDGVALETDDATIEKAIDDNFWLPRYRHYRRA 561
Cdd:PRK13529 489 AAAHALADCVPLAKPGEGALLPPVEDIREVSRAIAIAVAKAAIEEGLARETSDEDLEQAIEDNMWQPEYRPYRRT 563
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
5-559 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 636.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   5 PSRPLYIVHSGPTLLETPLLNKDSAFSLEERIQFNLLGLLPQNIETIEEQADRAYRQYEQQGSDLDRHIYLRSIQDSNET 84
Cdd:PLN03129  32 PVTPWVRVASGYDLLRDPRYNKGLAFTETERDRLGLRGLLPPAVLSQELQVKRFMENLRALESPLAKYRALMDLQERNER 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  85 LFFRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILGLGDQGI 164
Cdd:PLN03129 112 LFYRVLIDNIEELLPIVYTPTVGEACQKYGSLFRRPRGLYISLKDKGRVLSMLKNWPERDVQVIVVTDGERILGLGDLGV 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 165 GGMGIPIGKLSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRW-PNAIIQF 243
Cdd:PLN03129 192 QGMGIPVGKLDLYTAAGGIRPSAVLPVCIDVGTNNEKLLNDPFYIGLRQPRLTGEEYDELVDEFMEAVKQRWgPKVLVQF 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 244 EDFAQANAMPLLERYRDEVCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAM-QEEGIS 322
Cdd:PLN03129 272 EDFANKNAFRLLQRYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMsRQTGIS 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 323 EAEARKRVFMVDRYGLLTDDMSN-LVNFQRKLVQKRADLADwdtgdgdlaLIDVVRNAKPTVLIGVSGQRGLFTEEVIRT 401
Cdd:PLN03129 352 EEEARKRIWLVDSKGLVTKSRKDsLQPFKKPFAHDHEPGAS---------LLEAVKAIKPTVLIGLSGVGGTFTKEVLEA 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 402 MQSNCEEPLVMPLSNPTSRVEATPREILEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRIT 481
Cdd:PLN03129 423 MASLNERPIIFALSNPTSKAECTAEEAYTWTGGRAIFASGSPFDPVEYNGKTFHPGQANNAYIFPGIGLGALLSGAIRVT 502
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518794103 482 DGMLMSAARALADCSPVAIDGKGAVLPPLADIQQVSRKIAIAVAKRAQQDGVALET-DDATIEKAIDDNFWLPRYRHYR 559
Cdd:PLN03129 503 DDMLLAAAEALAAQVTEEELAKGAIYPPFSRIRDISAHVAAAVAAKAYEEGLATRLpRPEDLVEYAESCMYSPVYRPYR 581
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
14-554 0e+00

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 600.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  14 SGPTLLETPLLNKDSAFSLEERIQFNLLGLLPQNIETIEEQADRAYRQYEQQGSDLDRHIYLRSIQDSNETLFFRLLEDH 93
Cdd:PTZ00317  18 RGVDVLRNRFLNKGTAFTAEEREHLGIEGLLPPTVETLEQQVERLWTQFNRIETPINKYQFLRNIHDTNETLFYALLLKY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  94 LEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILGLGDQGIGGMGIPIGK 173
Cdd:PTZ00317  98 LKELLPIIYTPTVGEACQNYSNLFQRDRGLYLSRAHKGKIREILKNWPYDNVDVIVITDGSRILGLGDLGANGMGISIGK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 174 LSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRWPNAIIQFEDFAQANAMP 253
Cdd:PTZ00317 178 LSLYVAGGGINPSRVLPVVLDVGTNNEKLLNDPLYLGLREKRLDDDEYYELLDEFMEAVSSRWPNAVVQFEDFSNNHCFD 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 254 LLERYRDEVCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMV 333
Cdd:PTZ00317 258 LLERYQNKYRCFNDDIQGTGAVIAAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLAAEYGVTREEALKSFYLV 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 334 DRYGLLTDDMSNLVNfQRKLVQKRADLADwdtGDGDLA-LIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVM 412
Cdd:PTZ00317 338 DSKGLVTTTRGDKLA-KHKVPFARTDISA---EDSSLKtLEDVVRFVKPTALLGLSGVGGVFTEEVVKTMASNVERPIIF 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 413 PLSNPTSRVEATPREILEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARAL 492
Cdd:PTZ00317 414 PLSNPTSKAECTAEDAYKWTNGRAIVASGSPFPPVTLNGKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAAASL 493
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518794103 493 ADCSPVAIDGKGAVLPPLADIQQVSRKIAIAVAKRAQQDGVA----LETDDATIEKAIDDNFWLPR 554
Cdd:PTZ00317 494 ATLVSEEDLREGKLYPPLEDIREISAHIAVDVIEEAQEMGIAknkdLPDNRDELLALVKDRMWVPK 559
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
67-550 2.40e-144

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: 422.50  E-value: 2.40e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  67 SDLDRHiylrSIQDSNETLFFRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLfisydhrdhitdilhsaTKDNVK 146
Cdd:COG0281   12 EALEYH----RIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGY-----------------TAKGNL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 147 VVVITDSERILGLGDQgiggm-gipigKLSLYTACGGISpayTMPIVLDvgTNNddllddpmymgwrhervtgddyydfV 225
Cdd:COG0281   71 VAVVTDGTAVLGLGDIgplagmpvmegKAVLFKAFAGID---AFPICLD--TND-------------------------P 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 226 DRCVQGIRKRWPN-AIIQFEDFAQANAMPLLERYRDE--VCCFNDDIQGTASVALGTLFAACKAKNEKLSEQTITF---- 298
Cdd:COG0281  121 DEFVEAVKALEPTfGGINLEDIKAPNCFEIEERLREEldIPVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVIngag 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 299 -----VGagsagagiaeQIILAMqeeGISEaearKRVFMVDRYGLLTDDMSNLVNFQRKLVQKRADladwDTGDGDLAli 373
Cdd:COG0281  201 aagiaIA----------RLLVAA---GLSE----ENIIMVDSKGLLYEGRTDLNPYKREFARDTNP----RGLKGTLA-- 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 374 DVVRNAkpTVLIGVSgQRGLFTEEVIRTMqsnCEEPLVMPLSNPTSrvEATPREILEWTDGkALVSTGspfkpvslgeRK 453
Cdd:COG0281  258 EAIKGA--DVFIGVS-APGAFTEEMVKSM---AKRPIIFALANPTP--EITPEDAKAWGDG-AIVATG----------RS 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 454 IPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLPPLADIqQVSRKIAIAVAKRAQQDGV 533
Cdd:COG0281  319 DYPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEEELGPDYIIPSPFDP-RVSPAVAAAVAKAAIESGV 397
                        490
                 ....*....|....*..
gi 518794103 534 ALETDDATIEKAIDDNF 550
Cdd:COG0281  398 ARRPIDEDYREALEARM 414
Malic_M pfam03949
Malic enzyme, NAD binding domain;
269-528 1.32e-132

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 386.55  E-value: 1.32e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMVDRYGLLTDDMSNLVN 348
Cdd:pfam03949   1 IQGTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVREGLSEEEARKRIWMVDRQGLLTDDREDLTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  349 FQRKLVQKRADLADWDtgdGDLALIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVMPLSNPTSRVEATPREI 428
Cdd:pfam03949  81 FQKPFARKRAELKGWG---DGITLLEVVRKVKPTVLIGASGVPGAFTEEIVRAMAAHTERPIIFPLSNPTSKAEATPEDA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  429 LEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:pfam03949 158 YKWTDGRALFATGSPFPPVEYNGKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQGRLLP 237
                         250       260
                  ....*....|....*....|
gi 518794103  509 PLADIQQVSRKIAIAVAKRA 528
Cdd:pfam03949 238 PLSDIREVSRKIAVAVAKYA 257
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
269-553 6.49e-118

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: 349.92  E-value: 6.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMVDRYGLLTDDMSNLVN 348
Cdd:cd05312    1 IQGTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVREGLSEEEARKKIWLVDSKGLLTKDRKDLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 349 FQRKLVQKRADladWDTGDgdlaLIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVMPLSNPTSRVEATPREI 428
Cdd:cd05312   81 FKKPFARKDEE---KEGKS----LLEVVKAVKPTVLIGLSGVGGAFTEEVVRAMAKSNERPIIFALSNPTSKAECTAEDA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 429 LEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:cd05312  154 YKWTDGRALFASGSPFPPVEYNGKTYVPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELARGRLYP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 518794103 509 PLADIQQVSRKIAIAVAKRAQQDGVA-LETDDATIEKAIDDNFWLP 553
Cdd:cd05312  234 PLSNIREISAQIAVAVAKYAYEEGLAtRYPPPEDLEEYVKSQMWEP 279
malic pfam00390
Malic enzyme, N-terminal domain;
79-259 3.89e-91

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 277.61  E-value: 3.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   79 QDSNETLFFRLLEDHLEEMLPIIYTPTVGEACQAFSQIYRSHRGLFISYDHRDHITDILHSATKDNVKVVVITDSERILG 158
Cdd:pfam00390   1 QGKNEVLFYKLLSTHIEEDLPIVYTPTVGEACQAISEIYRRPRGLYTSIGNLGKIKDILKNWPEEDVRVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103  159 LGDQGIGGMGIPIGKLSLYTACGGISPAYTMPIVLDVGTNNDDLLDDPMYMGWRHERVTGDDYYDFVDRCVQGIRKRW-P 237
Cdd:pfam00390  81 LGDLGVAGMPIMEGKLALYTAFAGIDPSRVLPIVLDVGTNNEKLLNDPLYLGLRHKRVRGEEYDEFVDEFVEAVKALFpP 160
                         170       180
                  ....*....|....*....|..
gi 518794103  238 NAIIQFEDFAQANAMPLLERYR 259
Cdd:pfam00390 161 FGGIQFEDFGAPNAFEILERYR 182
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
269-529 6.65e-85

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: 263.51  E-value: 6.65e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEegiseaeaRKRVFMVDRYGLLTDDMSNLVN 348
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVK--------RKNIWLVDSKGLLTKGREDNLN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   349 -FQRKLVQKRADLADWDtgdgdlaLIDVVRnaKPTVLIGVSGQRGLFTEEVIRTMqsnCEEPLVMPLSNPTSRVEATPRE 427
Cdd:smart00919  73 pYKKPFARKTNERETGT-------LEEAVK--GADVLIGVSGPGGAFTEEMVKSM---AERPIIFALSNPTPEIEPTAAD 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103   428 ILEWTDgkALVSTGSPFKPvslgerkipiAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAID--GKGA 505
Cdd:smart00919 141 AYRWTA--AIVATGRSDYP----------NQVNNVLIFPGIFLGALDVRARRITDEMKLAAAEALADAVPVSEEelGPGY 208
                          250       260
                   ....*....|....*....|....
gi 518794103   506 VLPPLADiQQVSRKIAIAVAKRAQ 529
Cdd:smart00919 209 IIPSPFD-RRVSARVAVAVAKAAI 231
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
269-528 2.36e-64

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: 210.92  E-value: 2.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 269 IQGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAMQEEGISEAEARKRVFMVDRYGLLTDDMSNLVN 348
Cdd:cd00762    1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKEGISKEEACKRIW*VDRKGLLVKNRKETCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 349 FQRKLVQKRADLADWDTgdgdlaLIDVVRNAKPTVLIGVSGQRGLFTEEVIRTMQSNCEEPLVMPLSNPTSRVEATPREI 428
Cdd:cd00762   81 NEYHLARFANPERESGD------LEDAVEAAKPDFLIGVSRVGGAFTPEVIRA*AEINERPVIFALSNPTSKAECTAEEA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 429 LEWTDGKALVSTGSPFKPVSLGERKIPIAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:cd00762  155 YTATEGRAIFASGSPFHPVELNGGTYKPGQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEAIASSVTEESLKPGRLYP 234
                        250       260
                 ....*....|....*....|
gi 518794103 509 PLADIQQVSRKIAIAVAKRA 528
Cdd:cd00762  235 PLFDIQEVSLNIAVAVAKYA 254
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
270-528 5.83e-23

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: 97.34  E-value: 5.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 270 QGTASVALGTLFAACKAKNEKLSEQTITFVGAGSAGAGIAEQIILAmqeeGISeaeaRKRVFMVDRYGLLTDDMSNLVNf 349
Cdd:cd05311    2 HGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAA----GAK----PENIVVVDSKGVIYEGREDDLN- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 350 qrKLVQKRADLADWDTGDGDLAliDVVRNAKptVLIGVSGQrGLFTEEVIRTMQsncEEPLVMPLSNPTSrvEATPREIL 429
Cdd:cd05311   73 --PDKNEIAKETNPEKTGGTLK--EALKGAD--VFIGVSRP-GVVKKEMIKKMA---KDPIVFALANPVP--EIWPEEAK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 430 EwtDGKALVSTG-SPFkpvslgerkiPiAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADCSPVAIDGKGAVLP 508
Cdd:cd05311  141 E--AGADIVATGrSDF----------P-NQVNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVLGEEYIIP 207
                        250       260
                 ....*....|....*....|
gi 518794103 509 PLADiQQVSRKIAIAVAKRA 528
Cdd:cd05311  208 TPFD-PRVVPRVATAVAKAA 226
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
327-534 7.87e-10

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 61.65  E-value: 7.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 327 RKRVFMVDRYGLLTDDMSNLVNfQRKLVQKRadladwDTGDGDLAliDVVRNAKptVLIGVSGqRGLFTEEVIRTMQSNc 406
Cdd:PRK07232 211 KENIIVCDSKGVIYKGRTEGMD-EWKAAYAV------DTDARTLA--EAIEGAD--VFLGLSA-AGVLTPEMVKSMADN- 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 407 eePLVMPLSNPTSrvEATPREILEwTDGKALVSTG-SPFkpvslgerkiPiAQCNNA----YIFPGvglgAITVQASRIT 481
Cdd:PRK07232 278 --PIIFALANPDP--EITPEEAKA-VRPDAIIATGrSDY----------P-NQVNNVlcfpYIFRG----ALDVGATTIN 337
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518794103 482 DGMLMSAARALA-----DCSPVAID---------GKGAVLP-PLaDiQQVSRKIAIAVAKRAQQDGVA 534
Cdd:PRK07232 338 EEMKLAAVRAIAelareEVSDEVAAayggqklsfGPEYIIPkPF-D-PRLIVKIAPAVAKAAMDSGVA 403
PRK12862 PRK12862
malic enzyme; Reviewed
372-534 2.12e-08

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 57.21  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 372 LIDVVRNAKptVLIGVSGQrGLFTEEVIRTMQSNceePLVMPLSNPTSrvEATPREILEWTDgKALVSTGSPFKPvslge 451
Cdd:PRK12862 255 LAEVIEGAD--VFLGLSAA-GVLKPEMVKKMAPR---PLIFALANPTP--EILPEEARAVRP-DAIIATGRSDYP----- 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 452 rkipiAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALA-----DCSPV---AIDGKGAVLPPLADI-----QQVSR 518
Cdd:PRK12862 321 -----NQVNNVLCFPYIFRGALDVGATTINEEMKIAAVRAIAelareEQSDVvaaAYGGEDLSFGPDYLIpkpfdPRLIL 395
                        170
                 ....*....|....*.
gi 518794103 519 KIAIAVAKRAQQDGVA 534
Cdd:PRK12862 396 KIAPAVAQAAMDSGVA 411
PRK12861 PRK12861
malic enzyme; Reviewed
372-534 7.91e-06

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 48.73  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 372 LIDVVRNAKptVLIGVSGQrGLFTEEVIRTMQSNceePLVMPLSNPTSrvEATPREILEWTDgKALVSTGSPFKPvslge 451
Cdd:PRK12861 251 LAEVIGGAD--VFLGLSAG-GVLKAEMLKAMAAR---PLILALANPTP--EIFPELAHATRD-DVVIATGRSDYP----- 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518794103 452 rkipiAQCNNAYIFPGVGLGAITVQASRITDGMLMSAARALADC-----SPVAIDGKGA---------VLPPLADIQQVS 517
Cdd:PRK12861 317 -----NQVNNVLCFPYIFRGALDVGATTITREMEIAAVHAIAGLaeeeqNDVVAAAYGAydvsfgpqyLIPKPFDPRLIV 391
                        170
                 ....*....|....*..
gi 518794103 518 RkIAIAVAKRAQQDGVA 534
Cdd:PRK12861 392 R-IAPAVAKAAMEGGVA 407
 
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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