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Conserved domains on  [gi|499223838|ref|WP_010921378|]
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NADP-dependent malic enzyme [Caulobacter vibrioides]

Protein Classification

NADP-dependent malic enzyme( domain architecture ID 11482649)

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

EC:  1.1.1.40
Gene Ontology:  GO:0004471|GO:0004470|GO:0051287

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
14-758 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


:

Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1293.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  14 FTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAILGLGDLG 93
Cdd:PRK07232   2 QLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  94 ALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDIPVFHDDQ 173
Cdd:PRK07232  82 ALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDDQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 174 HGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAVE 253
Cdd:PRK07232 162 HGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTEGMDEWKAAYAVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 254 TDKRTLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSDYPNQVNNVLGF 333
Cdd:PRK07232 242 TDARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPDAIIATGRSDYPNQVNNVLCF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 334 PYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPDEVAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQAAMDTG 413
Cdd:PRK07232 322 PYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMDSG 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 414 VARKPIADMDAYRAGLAQRLDPTAGFLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMK 493
Cdd:PRK07232 402 VATRPIADMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIK 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 494 LVGLD-PDTAGLEIINARLSDRNPDYVDALYARLQRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQAL 572
Cdd:PRK07232 482 KLGLDlKAGVDFEIVNPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEHL 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 573 EEVLRVVDPAPG-GRIMGMSVVLAKGRTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLR 651
Cdd:PRK07232 562 RPVRQVIGLRPGvHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPS 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 652 SEKVREAVAMLDEMEVDFEYEGEMPPELALDPEKRA-NYPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLL 730
Cdd:PRK07232 642 ARKMREAVELLRERAPDLEVDGEMHGDAALNEEIRKdLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILL 721
                        730       740
                 ....*....|....*....|....*...
gi 499223838 731 GLSKSVQIAPLSASVSKILNMAMMAAYD 758
Cdd:PRK07232 722 GMAKPVHILTPSATVRRIVNMTALAVVD 749
 
Name Accession Description Interval E-value
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
14-758 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1293.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  14 FTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAILGLGDLG 93
Cdd:PRK07232   2 QLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  94 ALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDIPVFHDDQ 173
Cdd:PRK07232  82 ALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDDQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 174 HGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAVE 253
Cdd:PRK07232 162 HGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTEGMDEWKAAYAVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 254 TDKRTLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSDYPNQVNNVLGF 333
Cdd:PRK07232 242 TDARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPDAIIATGRSDYPNQVNNVLCF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 334 PYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPDEVAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQAAMDTG 413
Cdd:PRK07232 322 PYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMDSG 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 414 VARKPIADMDAYRAGLAQRLDPTAGFLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMK 493
Cdd:PRK07232 402 VATRPIADMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIK 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 494 LVGLD-PDTAGLEIINARLSDRNPDYVDALYARLQRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQAL 572
Cdd:PRK07232 482 KLGLDlKAGVDFEIVNPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEHL 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 573 EEVLRVVDPAPG-GRIMGMSVVLAKGRTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLR 651
Cdd:PRK07232 562 RPVRQVIGLRPGvHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPS 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 652 SEKVREAVAMLDEMEVDFEYEGEMPPELALDPEKRA-NYPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLL 730
Cdd:PRK07232 642 ARKMREAVELLRERAPDLEVDGEMHGDAALNEEIRKdLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILL 721
                        730       740
                 ....*....|....*....|....*...
gi 499223838 731 GLSKSVQIAPLSASVSKILNMAMMAAYD 758
Cdd:PRK07232 722 GMAKPVHILTPSATVRRIVNMTALAVVD 749
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
7-433 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: 699.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   7 SDAERKTFTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAI 86
Cdd:COG0281    1 EDMERVETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  87 LGLGDLGALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDI 166
Cdd:COG0281   81 LGLGDIGPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 167 PVFHDDQHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTeGMNQW 246
Cdd:COG0281  161 PVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRT-DLNPY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 247 KSAHAVETDKR----TLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSD 322
Cdd:COG0281  240 KREFARDTNPRglkgTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDGAIVATGRSD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 323 YPNQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDvpdevaaayhgrqlKFGPDYIIPSAFDPRLIWYVP 402
Cdd:COG0281  320 YPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEE--------------ELGPDYIIPSPFDPRVSPAVA 385
                        410       420       430
                 ....*....|....*....|....*....|.
gi 499223838 403 PFVAQAAMDTGVARKPIAdmDAYRAGLAQRL 433
Cdd:COG0281  386 AAVAKAAIESGVARRPID--EDYREALEARM 414
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
173-410 2.41e-116

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: 350.56  E-value: 2.41e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   173 QHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAV 252
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREDNLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   253 ETDKR---TLAEAVVGADVLLGLSAK-GAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRK-DAIMGTGRSDYPNQV 327
Cdd:smart00919  81 KTNERetgTLEEAVKGADVLIGVSGPgGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWtAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   328 NNVLGFPYIFRGALDVRARRVNHEMKIACAQALamlaredvpdevAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQ 407
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLAAAEAL------------ADAVPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 499223838   408 AAM 410
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 ...
173-409 2.33e-101

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: 311.51  E-value: 2.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 173 QHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAV 252
Cdd:cd05311    1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGREDDLNPDKNEIAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 253 ETDKR----TLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDaIMGTGRSDYPNQVN 328
Cdd:cd05311   81 ETNPEktggTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD-IVATGRSDFPNQVN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 329 NVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPdevaaayhgrqlkfGPDYIIPSAFDPRLIWYVPPFVAQA 408
Cdd:cd05311  160 NVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVL--------------GEEYIIPTPFDPRVVPRVATAVAKA 225

                 .
gi 499223838 409 A 409
Cdd:cd05311  226 A 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
439-756 2.57e-90

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: 286.13  E-value: 2.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  439 FLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENlvHENMKLVGLDPDTAGLEIINARLSDRNPDY 518
Cdd:pfam01515   1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEI--EIKAKALGLDLDLDGIEIVDPETSPRLEEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  519 VDALYARLQRQGYLKRDVQRlINQDRNSFAASMVTLGEADGMVTGVTRSFDQALEEVLRVVDPAPGGRIM-GMSVVLAKG 597
Cdd:pfam01515  79 ADFYYELRKRKGMTPEIARE-IVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVsSVFIMLLPD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  598 RTIFVADTNVTELPEAEELVEIACEAARAVRRLGF-KPRVAFMSYSTFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMP 676
Cdd:pfam01515 158 GLLFFADCAVNPNPTAEELAEIALMSAKTAKRFGIiEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  677 PELALDPEKRAN-YPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLLGLSKSVQIAPLSASVSKILNMAMMA 755
Cdd:pfam01515 238 FDAALVEEVAAQkAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAIT 317

                  .
gi 499223838  756 A 756
Cdd:pfam01515 318 A 318
 
Name Accession Description Interval E-value
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
14-758 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1293.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  14 FTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAILGLGDLG 93
Cdd:PRK07232   2 QLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  94 ALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDIPVFHDDQ 173
Cdd:PRK07232  82 ALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDDQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 174 HGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAVE 253
Cdd:PRK07232 162 HGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTEGMDEWKAAYAVD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 254 TDKRTLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSDYPNQVNNVLGF 333
Cdd:PRK07232 242 TDARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPDAIIATGRSDYPNQVNNVLCF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 334 PYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPDEVAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQAAMDTG 413
Cdd:PRK07232 322 PYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMDSG 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 414 VARKPIADMDAYRAGLAQRLDPTAGFLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMK 493
Cdd:PRK07232 402 VATRPIADMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIK 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 494 LVGLD-PDTAGLEIINARLSDRNPDYVDALYARLQRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQAL 572
Cdd:PRK07232 482 KLGLDlKAGVDFEIVNPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEHL 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 573 EEVLRVVDPAPG-GRIMGMSVVLAKGRTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLR 651
Cdd:PRK07232 562 RPVRQVIGLRPGvHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPS 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 652 SEKVREAVAMLDEMEVDFEYEGEMPPELALDPEKRA-NYPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLL 730
Cdd:PRK07232 642 ARKMREAVELLRERAPDLEVDGEMHGDAALNEEIRKdLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILL 721
                        730       740
                 ....*....|....*....|....*...
gi 499223838 731 GLSKSVQIAPLSASVSKILNMAMMAAYD 758
Cdd:PRK07232 722 GMAKPVHILTPSATVRRIVNMTALAVVD 749
PRK12862 PRK12862
malic enzyme; Reviewed
5-762 0e+00

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 1245.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   5 DMSDAERKTFTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGT 84
Cdd:PRK12862   1 TSSDASAKAELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRGNLVAVVSNGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  85 AILGLGDLGALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELL 164
Cdd:PRK12862  81 AVLGLGNIGPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGINLEDIKAPECFYIERELRERM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 165 DIPVFHDDQHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMN 244
Cdd:PRK12862 161 KIPVFHDDQHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLDLLVSLGVKRENIWVTDIKGVVYEGRTELMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 245 QWKSAHAVETDKRTLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSDYP 324
Cdd:PRK12862 241 PWKARYAQKTDARTLAEVIEGADVFLGLSAAGVLKPEMVKKMAPRPLIFALANPTPEILPEEARAVRPDAIIATGRSDYP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 325 NQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPDEVAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPF 404
Cdd:PRK12862 321 NQVNNVLCFPYIFRGALDVGATTINEEMKIAAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 405 VAQAAMDTGVARKPIADMDAYRAGLAQRLDPTAGFLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGR 484
Cdd:PRK12862 401 VAQAAMDSGVATRPIEDMDAYREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGR 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 485 ENLVHENMKLVGLD-PDTAGLEIINARLSDRNPDYVDALYARLQRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTG 563
Cdd:PRK12862 481 PAVIEARIERAGLRlRPGVDFEIVNPEDDPRYRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICG 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 564 VTRSFDQALEEVLRVVDPAPGGR-IMGMSVVLAKGRTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYS 642
Cdd:PRK12862 561 TEGRYERHLEFVLQVIGKRPGVRvYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHS 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 643 TFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMPPELALDPEKRAN-YPFMRLTDSANILIMPAIHAASISTKLVQSLGG 721
Cdd:PRK12862 641 NFGSSDSPSARKMREALEILRERAPDLEVDGEMHGDAALDEELRDRiFPDSRLEGEANLLVFPNLDAANIAYNLLKTAAG 720
                        730       740       750       760
                 ....*....|....*....|....*....|....*....|..
gi 499223838 722 ATV-IGPVLLGLSKSVQIAPLSASVSKILNMAMMAAYDQPVD 762
Cdd:PRK12862 721 NGLaVGPILLGAAKPVHILTPSATVRRIVNMTALAVADANAY 762
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
7-433 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: 699.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   7 SDAERKTFTDAEALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAI 86
Cdd:COG0281    1 EDMERVETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  87 LGLGDLGALASKPVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDI 166
Cdd:COG0281   81 LGLGDIGPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 167 PVFHDDQHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTeGMNQW 246
Cdd:COG0281  161 PVFHDDQHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRT-DLNPY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 247 KSAHAVETDKR----TLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSD 322
Cdd:COG0281  240 KREFARDTNPRglkgTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDGAIVATGRSD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 323 YPNQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDvpdevaaayhgrqlKFGPDYIIPSAFDPRLIWYVP 402
Cdd:COG0281  320 YPNQVNNVLIFPGIFRGALDVRATRITDEMKLAAARALADLVDEE--------------ELGPDYIIPSPFDPRVSPAVA 385
                        410       420       430
                 ....*....|....*....|....*....|.
gi 499223838 403 PFVAQAAMDTGVARKPIAdmDAYRAGLAQRL 433
Cdd:COG0281  386 AAVAKAAIESGVARRPID--EDYREALEARM 414
PRK12861 PRK12861
malic enzyme; Reviewed
19-758 0e+00

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 691.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  19 ALAFHRYPTPGKIAIVPTKPMATQRDLSLAYSPGVAVPVHAIAADPDMAYEYTSKGNLVAVISNGTAILGLGDLGALASK 98
Cdd:PRK12861  11 ALDYHEFPTPGKISVVASKPLVTQRDLALAYTPGVASACEEIAADPLNAFRFTSRGNLVGVITNGTAVLGLGNIGALASK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  99 PVMEGKSVLFKRFGDVDSIDIEVTTKDPDEIITVVKNIGVTFGGINLEDIKSPECFRIETELQELLDIPVFHDDQHGTAI 178
Cdd:PRK12861  91 PVMEGKAVLFKKFAGIDVFDIEINETDPDKLVDIIAGLEPTFGGINLEDIKAPECFTVERKLRERMKIPVFHDDQHGTAI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 179 ICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAVETDKRT 258
Cdd:PRK12861 171 TVSAAFINGLKVVGKSIKEVKVVTSGAGAAALACLDLLVDLGLPVENIWVTDIEGVVYRGRTTLMDPDKERFAQETDART 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 259 LAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDAIMGTGRSDYPNQVNNVLGFPYIFR 338
Cdd:PRK12861 251 LAEVIGGADVFLGLSAGGVLKAEMLKAMAARPLILALANPTPEIFPELAHATRDDVVIATGRSDYPNQVNNVLCFPYIFR 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 339 GALDVRARRVNHEMKIACAQALAMLAREDVPDEVAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQAAMDTGVARKP 418
Cdd:PRK12861 331 GALDVGATTITREMEIAAVHAIAGLAEEEQNDVVAAAYGAYDVSFGPQYLIPKPFDPRLIVRIAPAVAKAAMEGGVATRP 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 419 IADMDAYRAGLAQRLDPTAGFLQKI---SGSVLANP--KRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMK 493
Cdd:PRK12861 411 IADLDAYVEQLQQFVYHSGAFMKPLfaaARQLVRDGgkARIVFTEGEDERVLRAVQVIVDEKLARPILVGRPEVLLARIE 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 494 LVGLDPDTA-GLEIINARLSDRNPDYVDALYARLQRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQAL 572
Cdd:PRK12861 491 RFGLRLRLGqDVEVTNPEYDERFPQYWTTYWELRCRDGISKEMARVEMRRRLTLIGAMMVRLGDADGMICGTVGEYHNHL 570
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 573 EEVLRVVDPAPGGRIMG-MSVVLAKGRTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLR 651
Cdd:PRK12861 571 RFVDEVIGRKPGASTYAaMNILLLDQRTVALVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSRSNFGSGSAAS 650
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 652 SEKVREAVAMLDEMEVDFEYEGEMPPELALDPEKRANY-PFMRLTDSANILIMPAIHAASISTKLVQSLGGATV-IGPVL 729
Cdd:PRK12861 651 GVKMRRALEIVREQAPDLEADGEMHGDCALDEGLRARLlPMSPLKGAANLLVCPNVDAGNIAYNLLKTEAGSNVaVGPFL 730
                        730       740
                 ....*....|....*....|....*....
gi 499223838 730 LGLSKSVQIAPLSASVSKILNMAMMAAYD 758
Cdd:PRK12861 731 LGVNAPVNILTSSATVRRIVNMAALTVIE 759
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
173-410 2.41e-116

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: 350.56  E-value: 2.41e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   173 QHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAV 252
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREDNLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   253 ETDKR---TLAEAVVGADVLLGLSAK-GAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRK-DAIMGTGRSDYPNQV 327
Cdd:smart00919  81 KTNERetgTLEEAVKGADVLIGVSGPgGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWtAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   328 NNVLGFPYIFRGALDVRARRVNHEMKIACAQALamlaredvpdevAAAYHGRQLKFGPDYIIPSAFDPRLIWYVPPFVAQ 407
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLAAAEAL------------ADAVPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 499223838   408 AAM 410
Cdd:smart00919 229 AAI 231
Pta COG0280
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ...
439-758 3.07e-109

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


Pssm-ID: 440049 [Multi-domain]  Cd Length: 320  Bit Score: 335.50  E-value: 3.07e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 439 FLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMKLVGLDPDtaGLEIINARLSDRNPDY 518
Cdd:COG0280    2 FFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDLS--GFEIIDPEDSPRYEEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 519 VDALYARLQRQGYLKRDVQRLInQDRNSFAASMVTLGEADGMVTGVTRSFDQALEEVLRVVDPAPGGRIM-GMSVVLAKG 597
Cdd:COG0280   80 AEAYYELRKRKGVTPEEARELV-RDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGLRPGVKRVsHVFLMELPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 598 RTIFVADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMPP 677
Cdd:COG0280  159 RLLFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARGQIPDLEVDGELQF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 678 ELALDPEKRA-NYPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLLGLSKSVQIAPLSASVSKILNMAMMAA 756
Cdd:COG0280  239 DAALSPEAAKrKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALAA 318

                 ..
gi 499223838 757 YD 758
Cdd:COG0280  319 VQ 320
NAD_bind_2_malic_enz cd05311
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ...
173-409 2.33e-101

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: 311.51  E-value: 2.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 173 QHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVRAENCIAVDSKGVLYRGRTEGMNQWKSAHAV 252
Cdd:cd05311    1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGREDDLNPDKNEIAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 253 ETDKR----TLAEAVVGADVLLGLSAKGAFTPEMIASMAPNPVIFAMANPDPEITPEEVKRVRKDaIMGTGRSDYPNQVN 328
Cdd:cd05311   81 ETNPEktggTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD-IVATGRSDFPNQVN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 329 NVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPdevaaayhgrqlkfGPDYIIPSAFDPRLIWYVPPFVAQA 408
Cdd:cd05311  160 NVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVL--------------GEEYIIPTPFDPRVVPRVATAVAKA 225

                 .
gi 499223838 409 A 409
Cdd:cd05311  226 A 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
439-756 2.57e-90

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: 286.13  E-value: 2.57e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  439 FLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENlvHENMKLVGLDPDTAGLEIINARLSDRNPDY 518
Cdd:pfam01515   1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEI--EIKAKALGLDLDLDGIEIVDPETSPRLEEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  519 VDALYARLQRQGYLKRDVQRlINQDRNSFAASMVTLGEADGMVTGVTRSFDQALEEVLRVVDPAPGGRIM-GMSVVLAKG 597
Cdd:pfam01515  79 ADFYYELRKRKGMTPEIARE-IVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVsSVFIMLLPD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  598 RTIFVADTNVTELPEAEELVEIACEAARAVRRLGF-KPRVAFMSYSTFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMP 676
Cdd:pfam01515 158 GLLFFADCAVNPNPTAEELAEIALMSAKTAKRFGIiEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  677 PELALDPEKRAN-YPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLLGLSKSVQIAPLSASVSKILNMAMMA 755
Cdd:pfam01515 238 FDAALVEEVAAQkAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAIT 317

                  .
gi 499223838  756 A 756
Cdd:pfam01515 318 A 318
eutD PRK09653
phosphotransacetylase;
439-756 9.98e-51

phosphotransacetylase;


Pssm-ID: 236609 [Multi-domain]  Cd Length: 324  Bit Score: 180.43  E-value: 9.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 439 FLQKISGSVLANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMKLVGLDPDtaGLEIINARLSDRNPDY 518
Cdd:PRK09653   3 LFESLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDLD--GVEIIDPETYPLLEEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 519 VDALYARlqRQGYLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQALEEVLRVVDPAPGGRIMGMSVVLAKG- 597
Cdd:PRK09653  81 AEAFVEL--RKGKGTEEDAAELLKDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIKTKPGVKTVSSVFIMVKGd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 598 -RTIFvADTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMP 676
Cdd:PRK09653 159 eRYIF-ADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKGPEVDKVQEATEIAKELAPDLKIDGELQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 677 PELALDPEKRA-NYPFMRLTDSANILIMPAIHAASISTKLVQSLGGATVIGPVLLGLSKSVqiAPLS--ASVSKILNMAM 753
Cdd:PRK09653 238 FDAAFVPEVAAkKAPGSPVAGKANVFVFPSLEAGNIGYKIAQRLGGFEAVGPILQGLNKPV--NDLSrgCSVEDIYNLAL 315

                 ...
gi 499223838 754 MAA 756
Cdd:PRK09653 316 ITA 318
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
77-425 6.75e-36

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 143.51  E-value: 6.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  77 VAVISNGTAILGLGDLGALAskpvM---EGKSVLFKRFGDVD-----SIDIEVTT------KDP---------------- 126
Cdd:PLN03129 174 VIVVTDGERILGLGDLGVQG----MgipVGKLDLYTAAGGIRpsavlPVCIDVGTnnekllNDPfyiglrqprltgeeyd 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 127 ---DEIITVVKNigvTFGG---INLEDIKSPECFRIeteLQELLD-IPVFHDDQHGTAIICAAGLINACHITGKKIEDVK 199
Cdd:PLN03129 250 elvDEFMEAVKQ---RWGPkvlVQFEDFANKNAFRL---LQRYRTtHLCFNDDIQGTAAVALAGLLAALRATGGDLADQR 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 200 VVLNGPGAAGIASLELI-----KAMGVRAE----NCIAVDSKGVLYRGRTEGMNQWKS--AHAVEtDKRTLAEAV--VGA 266
Cdd:PLN03129 324 ILFAGAGEAGTGIAELIalamsRQTGISEEearkRIWLVDSKGLVTKSRKDSLQPFKKpfAHDHE-PGASLLEAVkaIKP 402
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 267 DVLLGLSAKG-AFTPEMIASMA---PNPVIFAMANP--DPEITPEEVKRVRK-----------DAIMGTGRSDYPNQVNN 329
Cdd:PLN03129 403 TVLIGLSGVGgTFTKEVLEAMAslnERPIIFALSNPtsKAECTAEEAYTWTGgraifasgspfDPVEYNGKTFHPGQANN 482
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 330 VLGFPYIFRGALDVRARRVNHEMKIACAQALA-MLAREDVpdEVAAAYhgrqlkfgpdyiipsafdprliwyvPPF---- 404
Cdd:PLN03129 483 AYIFPGIGLGALLSGAIRVTDDMLLAAAEALAaQVTEEEL--AKGAIY-------------------------PPFsrir 535
                        410       420       430
                 ....*....|....*....|....*....|..
gi 499223838 405 ---------VAQAAMDTGVARKP--IADMDAY 425
Cdd:PLN03129 536 disahvaaaVAAKAYEEGLATRLprPEDLVEY 567
malic pfam00390
Malic enzyme, N-terminal domain;
28-157 5.29e-34

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 128.53  E-value: 5.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   28 PGKIAIVPTKPMATQ--RDLSLAYSPGVAVPVHAIAADPDMAY-EYTSKGNL----------------VAVISNGTAILG 88
Cdd:pfam00390   1 QGKNEVLFYKLLSTHieEDLPIVYTPTVGEACQAISEIYRRPRgLYTSIGNLgkikdilknwpeedvrVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838   89 LGDLGAlASKPVMEGKSVLFKRFGDVD---SIDIEVTTK---------------------------DPDEIITVVKNIGV 138
Cdd:pfam00390  81 LGDLGV-AGMPIMEGKLALYTAFAGIDpsrVLPIVLDVGtnnekllndplylglrhkrvrgeeydeFVDEFVEAVKALFP 159
                         170
                  ....*....|....*....
gi 499223838  139 TFGGINLEDIKSPECFRIE 157
Cdd:pfam00390 160 PFGGIQFEDFGAPNAFEIL 178
Malic_M pfam03949
Malic enzyme, NAD binding domain;
175-371 2.60e-32

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 126.15  E-value: 2.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  175 GTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVR--------AENCIAVDSKGVLYRGR------- 239
Cdd:pfam03949   3 GTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQIRDAMVReglseeeaRKRIWMVDRQGLLTDDRedltdfq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  240 ------TEGMNQWKsahavetDKRTLAEAV--VGADVLLGLSA-KGAFTPEMIASMA---PNPVIFAMANPDP--EITPE 305
Cdd:pfam03949  83 kpfarkRAELKGWG-------DGITLLEVVrkVKPTVLIGASGvPGAFTEEIVRAMAahtERPIIFPLSNPTSkaEATPE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499223838  306 EVKRVRK-DAIMGTG----------RSDYPNQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDVPDE 371
Cdd:pfam03949 156 DAYKWTDgRALFATGspfppveyngKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEMFLAAAEALASYVDEEEPGQ 232
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
77-368 5.02e-32

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 131.67  E-value: 5.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838  77 VAVISNGTAILGLGDLGAlASKPVMEGKSVLFKRFGDVD-------SIDIEVTTK----DP------------------- 126
Cdd:PTZ00317 151 VIVITDGSRILGLGDLGA-NGMGISIGKLSLYVAGGGINpsrvlpvVLDVGTNNEkllnDPlylglrekrldddeyyell 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 127 DEIITVVK----NIGVTFgginlEDIKSPECFRIETELQELldIPVFHDDQHGTAIICAAGLINACHITGKKIEDVKVVL 202
Cdd:PTZ00317 230 DEFMEAVSsrwpNAVVQF-----EDFSNNHCFDLLERYQNK--YRCFNDDIQGTGAVIAAGFLNALKLSGVPPEEQRIVF 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 203 NGPGAAGIASLELIKAMGVRAENCIA--------VDSKGVLYRGRTEGMNQWKSAHAVE------TDKRTLAEAV--VGA 266
Cdd:PTZ00317 303 FGAGSAAIGVANNIADLAAEYGVTREealksfylVDSKGLVTTTRGDKLAKHKVPFARTdisaedSSLKTLEDVVrfVKP 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 267 DVLLGLSAKG-AFTPEMIASMA---PNPVIFAMANP--DPEITPEEV-KRVRKDAIMGTG----------RSDYPNQVNN 329
Cdd:PTZ00317 383 TALLGLSGVGgVFTEEVVKTMAsnvERPIIFPLSNPtsKAECTAEDAyKWTNGRAIVASGspfppvtlngKTIQPSQGNN 462
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 499223838 330 VLGFPYIFRGALDVRARRVNHEMKIACAQALAMLAREDV 368
Cdd:PTZ00317 463 LYVFPGVGLGCAIAQPSYIPDEMLIAAAASLATLVSEED 501
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
165-421 3.52e-31

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 129.10  E-value: 3.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 165 DIPVFHDDQHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAA--GIASLeLIKAM---GVRAE----NCIAVDSKGVL 235
Cdd:PRK13529 263 EICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSAgcGIADQ-IVAAMvreGLSEEearkRFFMVDRQGLL 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 236 yrgrTEGMN-----QWKSAH--------AVETDKRTLAEAV--VGADVLLGLSAK-GAFTPEMIASMA---PNPVIFAMA 296
Cdd:PRK13529 342 ----TDDMPdlldfQKPYARkreeladwDTEGDVISLLEVVrnVKPTVLIGVSGQpGAFTEEIVKEMAahcERPIIFPLS 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 297 NPDP--EITPEEVKRVRK-DAIMGTG----------RSDYPNQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQALAML 363
Cdd:PRK13529 418 NPTSraEATPEDLIAWTDgRALVATGspfapveyngKTYPIGQCNNAYIFPGLGLGVIASGARRVTDGMLMAAAHALADC 497
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499223838 364 AREDVPDE----------------VAAAyhgrqlkfgpdyiipsafdprliwyvppfVAQAAMDTGVARKPIAD 421
Cdd:PRK13529 498 VPLAKPGEgallppvedirevsraIAIA-----------------------------VAKAAIEEGLARETSDE 542
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
173-398 5.32e-29

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: 116.55  E-value: 5.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 173 QHGTAIICAAGLINACHITGKKIEDVKVVLNGPGAAGIASLELIKAMGVR--------AENCIAVDSKGVLYRGRTEGMN 244
Cdd:cd00762    1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKegiskeeaCKRIW*VDRKGLLVKNRKETCP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 245 QWKSAHAVETDKR---TLAEAV--VGADVLLGLSAKG-AFTPEMI---ASMAPNPVIFAMANPDP--EITPEEVKRVRK- 312
Cdd:cd00762   81 NEYHLARFANPEResgDLEDAVeaAKPDFLIGVSRVGgAFTPEVIra*AEINERPVIFALSNPTSkaECTAEEAYTATEg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 313 DAIMGTGRSD----------YPNQVNNVLGFPYIFRGALDVRARRVNHEMKIACAQAlamLAREDVPDEVAaayhgrqlk 382
Cdd:cd00762  161 RAIFASGSPFhpvelnggtyKPGQGNNLYIFPGVALGVILCRIRHITDDVFLSAAEA---IASSVTEESLK--------- 228
                        250
                 ....*....|....*.
gi 499223838 383 fgPDYIIPSAFDPRLI 398
Cdd:cd00762  229 --PGRLYPPLFDIQEV 242
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
449-736 1.77e-21

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 99.84  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 449 ANPKRIVFAEGEDPSVIRAAYAYQSGGFGKAILCGRENLVHENMKLVGLD-PDtaGLEIINArlSDRNPDYVDALYARLQ 527
Cdd:PRK05632 375 AAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDlPA--GIEIIDP--SEVRERYVAPLVELRK 450
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 528 RQGyLKRDVQRLINQDRNSFAASMVTLGEADGMVTGVTRSFDQALEEVLRVVDPAPGGRIMGmSV--------VLAKGrt 599
Cdd:PRK05632 451 HKG-MTEEVAREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVS-SVffmllpdqVLVYG-- 526
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499223838 600 ifvaDTNVTELPEAEELVEIACEAARAVRRLGFKPRVAFMSYSTFGNPMGLRSEKVREAVAMLDEMEVDFEYEGEMPPEL 679
Cdd:PRK05632 527 ----DCAVNPDPTAEQLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDA 602
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499223838 680 ALDPEKRAnypfMRLTDS-----ANILIMPAIHAASISTKLVQSLGGATVIGPVLLGLSKSV 736
Cdd:PRK05632 603 AVDPSVAR----SKAPNSpvagrATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPV 660
 
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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