NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1056502428|ref|WP_067940135|]
View 

MULTISPECIES: NADP-dependent malic enzyme [Sulfitobacter]

Protein Classification

NADP-dependent malic enzyme( domain architecture ID 11486247)

NADP-dependent malic enzyme catalyzes the conversion of (S)-malate to pyruvate and carbon dioxide using NADP as a cofactor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK12862 PRK12862
malic enzyme; Reviewed
1-757 0e+00

malic enzyme; Reviewed


:

Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 1393.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:PRK12862    5 ASAKAELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRGNLVAVVSNGTAVLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:PRK12862   85 LGNIGPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGINLEDIKAPECFYIERELRERMKIPV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKA 240
Cdd:PRK12862  165 FHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLDLLVSLGVKRENIWVTDIKGVVYEGRTELMDPWKA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLRTLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFPNQVN 320
Cdd:PRK12862  245 RYAQKTDARTLAEVIEGADVFLGLSAAGVLKPEMVKKMAPRPLIFALANPTPEILPEEARAVRPDAIIATGRSDYPNQVN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALARATTSAEAAAAYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:PRK12862  325 NVLCFPYIFRGALDVGATTINEEMKIAAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPAVAQA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 401 AMETGVAARPIEDLDAYKRKLDGSVFKSALIMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVI 480
Cdd:PRK12862  405 AMDSGVATRPIEDMDAYREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVI 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 481 ERRIEKAGLNLQLGQNVDLVNPENDPRYRDYWETYHSLMCRRGVSPDIARAIMRTNTTAIGAVMVHRGEADSLICGTFGE 560
Cdd:PRK12862  485 EARIERAGLRLRPGVDFEIVNPEDDPRYRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICGTEGR 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 561 FGWHLNYVNQVLG-RDGFRPHGALSMMILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQSQFGN 639
Cdd:PRK12862  565 YERHLEFVLQVIGkRPGVRVYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGS 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 640 QGEGSGKRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMK-GDGLE 718
Cdd:PRK12862  645 SDSPSARKMREALEILRERAPDLEVDGEMHGDAALDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAaGNGLA 724
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 1056502428 719 VGPILMGMGNRAHIVSPSITARGLLNVGAIAGTPVAHYG 757
Cdd:PRK12862  725 VGPILLGAAKPVHILTPSATVRRIVNMTALAVADANAYR 763
 
Name Accession Description Interval E-value
PRK12862 PRK12862
malic enzyme; Reviewed
1-757 0e+00

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 1393.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:PRK12862    5 ASAKAELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRGNLVAVVSNGTAVLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:PRK12862   85 LGNIGPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGINLEDIKAPECFYIERELRERMKIPV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKA 240
Cdd:PRK12862  165 FHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLDLLVSLGVKRENIWVTDIKGVVYEGRTELMDPWKA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLRTLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFPNQVN 320
Cdd:PRK12862  245 RYAQKTDARTLAEVIEGADVFLGLSAAGVLKPEMVKKMAPRPLIFALANPTPEILPEEARAVRPDAIIATGRSDYPNQVN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALARATTSAEAAAAYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:PRK12862  325 NVLCFPYIFRGALDVGATTINEEMKIAAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPAVAQA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 401 AMETGVAARPIEDLDAYKRKLDGSVFKSALIMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVI 480
Cdd:PRK12862  405 AMDSGVATRPIEDMDAYREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVI 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 481 ERRIEKAGLNLQLGQNVDLVNPENDPRYRDYWETYHSLMCRRGVSPDIARAIMRTNTTAIGAVMVHRGEADSLICGTFGE 560
Cdd:PRK12862  485 EARIERAGLRLRPGVDFEIVNPEDDPRYRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICGTEGR 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 561 FGWHLNYVNQVLG-RDGFRPHGALSMMILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQSQFGN 639
Cdd:PRK12862  565 YERHLEFVLQVIGkRPGVRVYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGS 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 640 QGEGSGKRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMK-GDGLE 718
Cdd:PRK12862  645 SDSPSARKMREALEILRERAPDLEVDGEMHGDAALDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAaGNGLA 724
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 1056502428 719 VGPILMGMGNRAHIVSPSITARGLLNVGAIAGTPVAHYG 757
Cdd:PRK12862  725 VGPILLGAAKPVHILTPSATVRRIVNMTALAVADANAYR 763
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
1-422 0e+00

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: 692.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:COG0281     3 MERVETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAVLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:COG0281    83 LGDIGPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDIPV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTeDMNPSKA 240
Cdd:COG0281   163 FHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRT-DLNPYKR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLR----TLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFP 316
Cdd:COG0281   242 EFARDTNPRglkgTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDGAIVATGRSDYP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 317 NQVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIAALArattsaeaaaayqgEQLTFGAEYLIPKPFDPRLIGVVSSA 396
Cdd:COG0281   322 NQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLV--------------DEEELGPDYIIPSPFDPRVSPAVAAA 387
                         410       420
                  ....*....|....*....|....*.
gi 1056502428 397 VAKAAMETGVAARPIEdlDAYKRKLD 422
Cdd:COG0281   388 VAKAAIESGVARRPID--EDYREALE 411
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
165-402 4.57e-119

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: 357.11  E-value: 4.57e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  165 QHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKAEYAQ 244
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREDNLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  245 KSDLR---TLDDVIDGADLFLGLSGP-GVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAP-DAIIATGRSDFPNQV 319
Cdd:smart00919  81 KTNERetgTLEEAVKGADVLIGVSGPgGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWtAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  320 NNVLCFPFIFRGALDVGATTINDEMKIACIDGIAALarattsaeaaaaYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAK 399
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLAAAEALADA------------VPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 1056502428  400 AAM 402
Cdd:smart00919 229 AAI 231
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
165-401 4.17e-105

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: 321.14  E-value: 4.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 165 QHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKAEYAQ 244
Cdd:cd05311     1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGREDDLNPDKNEIAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 245 KSDLR----TLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDaIIATGRSDFPNQVN 320
Cdd:cd05311    81 ETNPEktggTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD-IVATGRSDFPNQVN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALArattsaeaaaayqgEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:cd05311   160 NVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLA--------------EEEVLGEEYIIPTPFDPRVVPRVATAVAKA 225

                  .
gi 1056502428 401 A 401
Cdd:cd05311   226 A 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
431-749 6.09e-82

Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.


Pssm-ID: 396207 [Multi-domain]  Cd Length: 318  Bit Score: 263.79  E-value: 6.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 431 IMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGrpEVIERRIEKAGLNLQLGQnVDLVNPENDPRYRD 510
Cdd:pfam01515   1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIG--DEIEIKAKALGLDLDLDG-IEIVDPETSPRLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 511 YWETYHSLMCRRGVSPDIARAIMRtNTTAIGAVMVHRGEADSLICGTFGEFGWHLNYVNQVLG-RDGFRPHGALSMMILE 589
Cdd:pfam01515  78 YADFYYELRKRKGMTPEIAREIVR-DPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGtKPGVKTVSSVFIMLLP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 590 DGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFG-IEPKVALCSQSQFGN-QGEGSGKrLRAALQILDAGNHDFVYEGE 667
Cdd:pfam01515 157 DGLLFFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSgKGEDVEK-VREATKIVRERAPDLVVDGE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 668 MNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMKGDGLEVGPILMGMGNRAHIVSPSITARGLLNVGA 747
Cdd:pfam01515 236 LQFDAALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAA 315

                  ..
gi 1056502428 748 IA 749
Cdd:pfam01515 316 IT 317
 
Name Accession Description Interval E-value
PRK12862 PRK12862
malic enzyme; Reviewed
1-757 0e+00

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 1393.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:PRK12862    5 ASAKAELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRGNLVAVVSNGTAVLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:PRK12862   85 LGNIGPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGINLEDIKAPECFYIERELRERMKIPV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKA 240
Cdd:PRK12862  165 FHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLDLLVSLGVKRENIWVTDIKGVVYEGRTELMDPWKA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLRTLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFPNQVN 320
Cdd:PRK12862  245 RYAQKTDARTLAEVIEGADVFLGLSAAGVLKPEMVKKMAPRPLIFALANPTPEILPEEARAVRPDAIIATGRSDYPNQVN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALARATTSAEAAAAYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:PRK12862  325 NVLCFPYIFRGALDVGATTINEEMKIAAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPAVAQA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 401 AMETGVAARPIEDLDAYKRKLDGSVFKSALIMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVI 480
Cdd:PRK12862  405 AMDSGVATRPIEDMDAYREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVI 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 481 ERRIEKAGLNLQLGQNVDLVNPENDPRYRDYWETYHSLMCRRGVSPDIARAIMRTNTTAIGAVMVHRGEADSLICGTFGE 560
Cdd:PRK12862  485 EARIERAGLRLRPGVDFEIVNPEDDPRYRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICGTEGR 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 561 FGWHLNYVNQVLG-RDGFRPHGALSMMILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQSQFGN 639
Cdd:PRK12862  565 YERHLEFVLQVIGkRPGVRVYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGS 644
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 640 QGEGSGKRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMK-GDGLE 718
Cdd:PRK12862  645 SDSPSARKMREALEILRERAPDLEVDGEMHGDAALDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAaGNGLA 724
                         730       740       750
                  ....*....|....*....|....*....|....*....
gi 1056502428 719 VGPILMGMGNRAHIVSPSITARGLLNVGAIAGTPVAHYG 757
Cdd:PRK12862  725 VGPILLGAAKPVHILTPSATVRRIVNMTALAVADANAYR 763
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
7-749 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1257.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   7 LRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLGLGNIGA 86
Cdd:PRK07232    3 LKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNIGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  87 LASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPVFHDDQH 166
Cdd:PRK07232   83 LASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDDQH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 167 GTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKAEYAQKS 246
Cdd:PRK07232  163 GTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTEGMDEWKAAYAVDT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 247 DLRTLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFPNQVNNVLCFP 326
Cdd:PRK07232  243 DARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPDAIIATGRSDYPNQVNNVLCFP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 327 FIFRGALDVGATTINDEMKIACIDGIAALARATTSAEAAAAYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAKAAMETGV 406
Cdd:PRK07232  323 YIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMDSGV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 407 AARPIEDLDAYKRKLDGSVFKSALIMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVIERRIEK 486
Cdd:PRK07232  403 ATRPIADMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIKK 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 487 AGLNLQLGQNVDLVNPENDPRYRDYWETYHSLMCRRGVSPDIARAIMRTNTTAIGAVMVHRGEADSLICGTFGEFGWHLN 566
Cdd:PRK07232  483 LGLDLKAGVDFEIVNPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEHLR 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 567 YVNQVLG-RDGFRPHGALSMMILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQSQFGNQGEGSG 645
Cdd:PRK07232  563 PVRQVIGlRPGVHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPSA 642
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 646 KRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMKGDGLEVGPILMG 725
Cdd:PRK07232  643 RKMREAVELLRERAPDLEVDGEMHGDAALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILLG 722
                         730       740
                  ....*....|....*....|....
gi 1056502428 726 MGNRAHIVSPSITARGLLNVGAIA 749
Cdd:PRK07232  723 MAKPVHILTPSATVRRIVNMTALA 746
PRK12861 PRK12861
malic enzyme; Reviewed
1-748 0e+00

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 952.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:PRK12861    1 MKQTETQRQAALDYHEFPTPGKISVVASKPLVTQRDLALAYTPGVASACEEIAADPLNAFRFTSRGNLVGVITNGTAVLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:PRK12861   81 LGNIGALASKPVMEGKAVLFKKFAGIDVFDIEINETDPDKLVDIIAGLEPTFGGINLEDIKAPECFTVERKLRERMKIPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKA 240
Cdd:PRK12861  161 FHDDQHGTAITVSAAFINGLKVVGKSIKEVKVVTSGAGAAALACLDLLVDLGLPVENIWVTDIEGVVYRGRTTLMDPDKE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLRTLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFPNQVN 320
Cdd:PRK12861  241 RFAQETDARTLAEVIGGADVFLGLSAGGVLKAEMLKAMAARPLILALANPTPEIFPELAHATRDDVVIATGRSDYPNQVN 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALARATTSAEAAAAYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:PRK12861  321 NVLCFPYIFRGALDVGATTITREMEIAAVHAIAGLAEEEQNDVVAAAYGAYDVSFGPQYLIPKPFDPRLIVRIAPAVAKA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 401 AMETGVAARPIEDLDAYKRKLDGSVFKSALIMRPVFESARSSPR-----RLVFAEGEDERVLRAAQAIIEETVERPILIG 475
Cdd:PRK12861  401 AMEGGVATRPIADLDAYVEQLQQFVYHSGAFMKPLFAAARQLVRdggkaRIVFTEGEDERVLRAVQVIVDEKLARPILVG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 476 RPEVIERRIEKAGLNLQLGQNVDLVNPENDPRYRDYWETYHSLMCRRGVSPDIARAIMRTNTTAIGAVMVHRGEADSLIC 555
Cdd:PRK12861  481 RPEVLLARIERFGLRLRLGQDVEVTNPEYDERFPQYWTTYWELRCRDGISKEMARVEMRRRLTLIGAMMVRLGDADGMIC 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 556 GTFGEFGWHLNYVNQVLGR-DGFRPHGALSMMILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQ 634
Cdd:PRK12861  561 GTVGEYHNHLRFVDEVIGRkPGASTYAAMNILLLDQRTVALVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSR 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 635 SQFGNQGEGSGKRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMK- 713
Cdd:PRK12861  641 SNFGSGSAASGVKMRRALEIVREQAPDLEADGEMHGDCALDEGLRARLLPMSPLKGAANLLVCPNVDAGNIAYNLLKTEa 720
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 1056502428 714 GDGLEVGPILMGMGNRAHIVSPSITARGLLNVGAI 748
Cdd:PRK12861  721 GSNVAVGPFLLGVNAPVNILTSSATVRRIVNMAAL 755
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
1-422 0e+00

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: 692.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428   1 MSDTPNLRQAALDYHEHPRPGKLEVRATKPLANGRDLARAYSPGVAEACIEIKNDPDTAARYTSRGNLVAVVTNGTAVLG 80
Cdd:COG0281     3 MERVETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAVLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGALASKPVMEGKAVLFKKFANIDCFDIELDQADPEKLAEIVCAMEPSFGAINLEDIKAPDCFVVEKICRERMNIPV 160
Cdd:COG0281    83 LGDIGPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDIPV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 161 FHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTeDMNPSKA 240
Cdd:COG0281   163 FHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRT-DLNPYKR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 241 EYAQKSDLR----TLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDAIIATGRSDFP 316
Cdd:COG0281   242 EFARDTNPRglkgTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDGAIVATGRSDYP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 317 NQVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIAALArattsaeaaaayqgEQLTFGAEYLIPKPFDPRLIGVVSSA 396
Cdd:COG0281   322 NQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLV--------------DEEELGPDYIIPSPFDPRVSPAVAAA 387
                         410       420
                  ....*....|....*....|....*.
gi 1056502428 397 VAKAAMETGVAARPIEdlDAYKRKLD 422
Cdd:COG0281   388 VAKAAIESGVARRPID--EDYREALE 411
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
165-402 4.57e-119

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: 357.11  E-value: 4.57e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  165 QHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKAEYAQ 244
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREDNLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  245 KSDLR---TLDDVIDGADLFLGLSGP-GVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAP-DAIIATGRSDFPNQV 319
Cdd:smart00919  81 KTNERetgTLEEAVKGADVLIGVSGPgGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWtAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  320 NNVLCFPFIFRGALDVGATTINDEMKIACIDGIAALarattsaeaaaaYQGEQLTFGAEYLIPKPFDPRLIGVVSSAVAK 399
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLAAAEALADA------------VPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 1056502428  400 AAM 402
Cdd:smart00919 229 AAI 231
Pta COG0280
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ...
432-749 3.77e-116

Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion];


Pssm-ID: 440049 [Multi-domain]  Cd Length: 320  Bit Score: 353.22  E-value: 3.77e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 432 MRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVIERRIEKAGLNLQlgqNVDLVNPENDPRYRDY 511
Cdd:COG0280     3 FRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDLS---GFEIIDPEDSPRYEEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 512 WETYHSLMCRRGVSPDIARAIMRtNTTAIGAVMVHRGEADSLICGTFGEFGWHLNYVNQVLG-RDGFRPHGALSMMILED 590
Cdd:COG0280    80 AEAYYELRKRKGVTPEEARELVR-DAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGlRPGVKRVSHVFLMELPD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 591 GPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSQSQFGNQGEGSGKRLRAALQILDAGNHDFVYEGEMNI 670
Cdd:COG0280   159 RLLFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARGQIPDLEVDGELQF 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056502428 671 DTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMKGDGLEVGPILMGMGNRAHIVSPSITARGLLNVGAIA 749
Cdd:COG0280   239 DAALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALA 317
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
165-401 4.17e-105

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: 321.14  E-value: 4.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 165 QHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKRENVWLCDINGLVYEGRTEDMNPSKAEYAQ 244
Cdd:cd05311     1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGREDDLNPDKNEIAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 245 KSDLR----TLDDVIDGADLFLGLSGPGVLSPEMVAKMAKRPIIFALANPTPEILPDLARAVAPDaIIATGRSDFPNQVN 320
Cdd:cd05311    81 ETNPEktggTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD-IVATGRSDFPNQVN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 321 NVLCFPFIFRGALDVGATTINDEMKIACIDGIAALArattsaeaaaayqgEQLTFGAEYLIPKPFDPRLIGVVSSAVAKA 400
Cdd:cd05311   160 NVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLA--------------EEEVLGEEYIIPTPFDPRVVPRVATAVAKA 225

                  .
gi 1056502428 401 A 401
Cdd:cd05311   226 A 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
431-749 6.09e-82

Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.


Pssm-ID: 396207 [Multi-domain]  Cd Length: 318  Bit Score: 263.79  E-value: 6.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 431 IMRPVFESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGrpEVIERRIEKAGLNLQLGQnVDLVNPENDPRYRD 510
Cdd:pfam01515   1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIG--DEIEIKAKALGLDLDLDG-IEIVDPETSPRLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 511 YWETYHSLMCRRGVSPDIARAIMRtNTTAIGAVMVHRGEADSLICGTFGEFGWHLNYVNQVLG-RDGFRPHGALSMMILE 589
Cdd:pfam01515  78 YADFYYELRKRKGMTPEIAREIVR-DPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGtKPGVKTVSSVFIMLLP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 590 DGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFG-IEPKVALCSQSQFGN-QGEGSGKrLRAALQILDAGNHDFVYEGE 667
Cdd:pfam01515 157 DGLLFFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSgKGEDVEK-VREATKIVRERAPDLVVDGE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 668 MNIDTALDPELRARLLPCNRMEGAANVLVFAHADAASGVRNILKMKGDGLEVGPILMGMGNRAHIVSPSITARGLLNVGA 747
Cdd:pfam01515 236 LQFDAALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAA 315

                  ..
gi 1056502428 748 IA 749
Cdd:pfam01515 316 IT 317
eutD PRK09653
phosphotransacetylase;
437-726 1.19e-39

phosphotransacetylase;


Pssm-ID: 236609 [Multi-domain]  Cd Length: 324  Bit Score: 149.22  E-value: 1.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 437 ESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVIERRIEKAGLNLqlgQNVDLVNPENDPRYRDYWETYH 516
Cdd:PRK09653    9 EKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDL---DGVEIIDPETYPLLEEFAEAFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 517 SLmcRRG-VSPDIARAIMRTNtTAIGAVMVHRGEADSLICGtfgefgwhLNYVNQvlgrDGFRPhgAL------------ 583
Cdd:PRK09653   86 EL--RKGkGTEEDAAELLKDP-NYFGTMLVKLGKADGMVSG--------AIHSTA----DTLRP--ALqiiktkpgvktv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 584 -SMMILE-DGPLFI-ADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPKVALCSqsqFGNQGEGSG---KRLRAALQILDA 657
Cdd:PRK09653  149 sSVFIMVkGDERYIfADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLS---FSTKGSAKGpevDKVQEATEIAKE 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1056502428 658 GNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVFAHADAAsgvrNI-LKMK---GDGLEVGPILMGM 726
Cdd:PRK09653  226 LAPDLKIDGELQFDAAFVPEVAAKKAPGSPVAGKANVFVFPSLEAG----NIgYKIAqrlGGFEAVGPILQGL 294
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
41-347 3.55e-37

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 147.08  E-value: 3.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  41 YSPGVAEACIEIKNDPdTAAR--YTS---RGNL-------------VAVVTNGTAVLGLGNIGAlASKPVMEGKAVLFKK 102
Cdd:PTZ00317  106 YTPTVGEACQNYSNLF-QRDRglYLSrahKGKIreilknwpydnvdVIVITDGSRILGLGDLGA-NGMGISIGKLSLYVA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 103 FANID---CFDIELD--------QADPEKLA----------------EIVCAMEPSF--GAINLEDIKAPDCFVVEKICR 153
Cdd:PTZ00317  184 GGGINpsrVLPVVLDvgtnneklLNDPLYLGlrekrldddeyyelldEFMEAVSSRWpnAVVQFEDFSNNHCFDLLERYQ 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 154 ERmnIPVFHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKL----GVKRE----NVWLCDING 225
Cdd:PTZ00317  264 NK--YRCFNDDIQGTGAVIAAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLaaeyGVTREealkSFYLVDSKG 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 226 LVYEGRTEDMNPSKAEYAQK------SDLRTLDDVIDGA--DLFLGLSG-PGVLSPEMVAKMA---KRPIIFALANPTP- 292
Cdd:PTZ00317  342 LVTTTRGDKLAKHKVPFARTdisaedSSLKTLEDVVRFVkpTALLGLSGvGGVFTEEVVKTMAsnvERPIIFPLSNPTSk 421
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056502428 293 -EILPDLA-RAVAPDAIIATGrSDF-----------PNQVNNVLCFPFIFRGALDVGATTINDEMKIA 347
Cdd:PTZ00317  422 aECTAEDAyKWTNGRAIVASG-SPFppvtlngktiqPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIA 488
malic pfam00390
Malic enzyme, N-terminal domain;
20-150 5.38e-36

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 133.93  E-value: 5.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  20 PGKLEVRATKPLAN--GRDLARAYSPGVAEACIEIKNDPDTA-ARYTSRGNL----------------VAVVTNGTAVLG 80
Cdd:pfam00390   1 QGKNEVLFYKLLSThiEEDLPIVYTPTVGEACQAISEIYRRPrGLYTSIGNLgkikdilknwpeedvrVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  81 LGNIGAlASKPVMEGKAVLFKKFANID---CFDIELD---------------------------QADPEKLAEIVCAMEP 130
Cdd:pfam00390  81 LGDLGV-AGMPIMEGKLALYTAFAGIDpsrVLPIVLDvgtnnekllndplylglrhkrvrgeeyDEFVDEFVEAVKALFP 159
                         170       180
                  ....*....|....*....|
gi 1056502428 131 SFGAINLEDIKAPDCFVVEK 150
Cdd:pfam00390 160 PFGGIQFEDFGAPNAFEILE 179
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
41-421 3.33e-35

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 141.59  E-value: 3.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  41 YSPGVAEACIE------------------------IKNDPDTAARytsrgnlVAVVTNGTAVLGLGNIGALAskpvM--- 93
Cdd:PLN03129  129 YTPTVGEACQKygslfrrprglyislkdkgrvlsmLKNWPERDVQ-------VIVVTDGERILGLGDLGVQG----Mgip 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  94 EGKAVLFKKFANID---CFDIELD--------QADP----------------EKLAEIVCAMEPSFGA---INLEDIKAP 143
Cdd:PLN03129  198 VGKLDLYTAAGGIRpsaVLPVCIDvgtnneklLNDPfyiglrqprltgeeydELVDEFMEAVKQRWGPkvlVQFEDFANK 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 144 DCFVVEKicRERMNIPVFHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVK--------- 214
Cdd:PLN03129  278 NAFRLLQ--RYRTTHLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFAGAGEAGTGIAELIALAMSRqtgiseeea 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 215 RENVWLCDINGLVYEGRTEDMNPSKAEYAQK-SDLRTLDDVIDGA--DLFLGLSG-PGVLSPEMVAKMAK---RPIIFAL 287
Cdd:PLN03129  356 RKRIWLVDSKGLVTKSRKDSLQPFKKPFAHDhEPGASLLEAVKAIkpTVLIGLSGvGGTFTKEVLEAMASlneRPIIFAL 435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 288 ANPT--PEILPDLA-RAVAPDAIIATGrSDF-----------PNQVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIA 353
Cdd:PLN03129  436 SNPTskAECTAEEAyTWTGGRAIFASG-SPFdpveyngktfhPGQANNAYIFPGIGLGALLSGAIRVTDDMLLAAAEALA 514
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056502428 354 ALARAttsaeaaaayqgEQLTFGAEYliPkPFDP-RLIGV-VSSAVAKAAMETGVAARP--IEDLDAYKRKL 421
Cdd:PLN03129  515 AQVTE------------EELAKGAIY--P-PFSRiRDISAhVAAAVAAKAYEEGLATRLprPEDLVEYAESC 571
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
413-697 1.15e-34

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 141.06  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 413 DLDAYKRKLDGSVFKSALIMRPVF-----ESARSSPRRLVFAEGEDERVLRAAQAIIEETVERPILIGRPEVIERRIEKA 487
Cdd:PRK05632  342 DTDELLERLTATSERSRRLSPPAFryqltERARAAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQ 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 488 GlnLQLGQNVDLVNPenDPRYRDYWETYHSLMCRRGVSPDIARAIMrTNTTAIGAVMVHRGEADSLICG----Tfgefgw 563
Cdd:PRK05632  422 G--VDLPAGIEIIDP--SEVRERYVAPLVELRKHKGMTEEVAREQL-EDNVYFGTMMLALGEVDGLVSGavhtT------ 490
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 564 hlnyVNQVlgrdgfRPhgALSM---------------MILEDGPLFIADTQVNLHPTPEQIAEIAIGAARHVRRFGIEPK 628
Cdd:PRK05632  491 ----ANTI------RP--ALQLiktapgsslvssvffMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSADSAAAFGIEPR 558
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 629 VALCSQSQfGNQGEGSG-KRLRAALQILDAGNHDFVYEGEMNIDTALDPELRARLLPCNRMEGAANVLVF 697
Cdd:PRK05632  559 VAMLSYST-GTSGSGADvEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPVAGRATVFIF 627
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
41-416 5.43e-33

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 134.49  E-value: 5.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428  41 YSPGVAEAC----------------IEIKNDPDTAARYTSRGNL-VAVVTNGTAVLGLGNIGALAskpvME---GKAVLF 100
Cdd:PRK13529  104 YTPTVGEACerfshiyrrprglfisYDDRDRIEDILQNAPNRDIkLIVVTDGERILGIGDQGIGG----MGipiGKLSLY 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 101 KKFANID---CFDIELD--------QADP----------------EKLAEIVCAMEPSF-GA-INLEDIKAPDCFVVEKi 151
Cdd:PRK13529  180 TACGGIDparTLPVVLDvgtnneqlLNDPlylgwrhprirgeeydEFVDEFVQAVKRRFpNAlLQFEDFAQKNARRILE- 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 152 cRERMNIPVFHDDQHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVK--------RENVWLCDI 223
Cdd:PRK13529  259 -RYRDEICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAGCGIADQIVAAMVReglseeeaRKRFFMVDR 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 224 NGLVYEGRTeDMNPSKAEYAQK----------SDLRTLDDVIDGA--DLFLGLSG-PGVLSPEMVAKMAK---RPIIFAL 287
Cdd:PRK13529  338 QGLLTDDMP-DLLDFQKPYARKreeladwdteGDVISLLEVVRNVkpTVLIGVSGqPGAFTEEIVKEMAAhceRPIIFPL 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 288 ANPTpeilpDLARAVAPD--------AIIATGrSDFPN-----------QVNNVLCFPFIFRGALDVGATTINDEMKIAC 348
Cdd:PRK13529  417 SNPT-----SRAEATPEDliawtdgrALVATG-SPFAPveyngktypigQCNNAYIFPGLGLGVIASGARRVTDGMLMAA 490
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056502428 349 IDGIAALARAttsaeaaaayqgEQLTFGAEYlipkpfdPRL--IGVVS----SAVAKAAMETGVAARP-IEDLDA 416
Cdd:PRK13529  491 AHALADCVPL------------AKPGEGALL-------PPVedIREVSraiaIAVAKAAIEEGLARETsDEDLEQ 546
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
167-417 1.45e-32

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: 127.28  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 167 GTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVK--------RENVWLCDINGLVYEGRtEDMNPS 238
Cdd:cd05312     3 GTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADLIVSAMVReglseeeaRKKIWLVDSKGLLTKDR-KDLTPF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 239 KAEYAQK---SDLRTLDDVID--GADLFLGLSG-PGVLSPEMVAKMAK---RPIIFALANPTpeilpDLARAVAPDA--- 306
Cdd:cd05312    82 KKPFARKdeeKEGKSLLEVVKavKPTVLIGLSGvGGAFTEEVVRAMAKsneRPIIFALSNPT-----SKAECTAEDAykw 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 307 -----IIATGrSDF-----------PNQVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIAALARATTSAeaaaayQG 370
Cdd:cd05312   157 tdgraLFASG-SPFppveyngktyvPGQGNNAYIFPGIGLGAILSGARHITDEMFLAAAEALASLVTDEELA------RG 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1056502428 371 EqltfgaeyLIPKPFDPRLIGV-VSSAVAKAAMETGVAAR--PIEDLDAY 417
Cdd:cd05312   230 R--------LYPPLSNIREISAqIAVAVAKYAYEEGLATRypPPEDLEEY 271
Malic_M pfam03949
Malic enzyme, NAD binding domain;
167-355 9.91e-31

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 121.53  E-value: 9.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 167 GTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVK--------RENVWLCDINGLVYEGRtEDMNPS 238
Cdd:pfam03949   3 GTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVReglseeeaRKRIWMVDRQGLLTDDR-EDLTDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 239 KAEYAQK-------SDLRTLDDVIDGA--DLFLGLSG-PGVLSPEMVAKMAK---RPIIFALANPTPeilpdLARAVAPD 305
Cdd:pfam03949  82 QKPFARKraelkgwGDGITLLEVVRKVkpTVLIGASGvPGAFTEEIVRAMAAhteRPIIFPLSNPTS-----KAEATPED 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056502428 306 --------AIIATGrSDF-----------PNQVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIAAL 355
Cdd:pfam03949 157 aykwtdgrALFATG-SPFppveyngktyhIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASY 224
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
165-353 1.97e-30

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: 120.40  E-value: 1.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 165 QHGTAIVVGAAAKNALHVAGKKFEDIKIVSTGGGAAGIACLNMLLKLGVKR--------ENVWLCDINGLVYEGRTEdMN 236
Cdd:cd00762     1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKEgiskeeacKRIW*VDRKGLLVKNRKE-TC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 237 PSKAEYAQ----KSDLRTLDDVID--GADLFLGLSGPG-VLSPEMVAKMA---KRPIIFALANPTP--EILPDLAR-AVA 303
Cdd:cd00762    80 PNEYHLARfanpERESGDLEDAVEaaKPDFLIGVSRVGgAFTPEVIRA*AeinERPVIFALSNPTSkaECTAEEAYtATE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056502428 304 PDAIIATGRSDFPN----------QVNNVLCFPFIFRGALDVGATTINDEMKIACIDGIA 353
Cdd:cd00762   160 GRAIFASGSPFHPVelnggtykpgQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEAIA 219
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH