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Conserved domains on  [gi|167727384|emb|CAP14172|]
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malate dehydrogenase (oxaloacetate-decarboxylating) [Halobacterium salinarum R1]

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
1-737 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


:

Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1248.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:PRK07232   1 EQLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:PRK07232  81 GALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQ 238
Cdd:PRK07232 161 QHGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTegMDEWKAAYAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 PADsGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVNNV 318
Cdd:PRK07232 241 DTD-ARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPD-AIIATGRSDYPNQVNNV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 319 LGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVADAAM 398
Cdd:PRK07232 319 LCFPYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAM 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 399 ETGVARTEL-DLVDYREELEARLGKSREMMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQG 477
Cdd:PRK07232 399 DSGVATRPIaDMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 478 TVDALSLDFDPDVV-----DPDEGDHSAYADTLYDLRKRKGITRNEAESLVARDPNYLGSTMVEAGDADAFLTGLTHHYP 552
Cdd:PRK07232 479 RIKKLGLDLKAGVDfeivnPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYH 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 553 SALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVD 632
Cdd:PRK07232 559 EHLRPVRQVIGLRPGVHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSD 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 633 NEGTRKPRRAAQQLREdDDIDFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIG 712
Cdd:PRK07232 639 SPSARKMREAVELLRE-RAPDLEVDGEMHGDAALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIG 717
                        730       740
                 ....*....|....*....|....*
gi 167727384 713 PMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK07232 718 PILLGMAKPVHILTPSATVRRIVNM 742
 
Name Accession Description Interval E-value
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
1-737 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1248.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:PRK07232   1 EQLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:PRK07232  81 GALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQ 238
Cdd:PRK07232 161 QHGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTegMDEWKAAYAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 PADsGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVNNV 318
Cdd:PRK07232 241 DTD-ARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPD-AIIATGRSDYPNQVNNV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 319 LGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVADAAM 398
Cdd:PRK07232 319 LCFPYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAM 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 399 ETGVARTEL-DLVDYREELEARLGKSREMMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQG 477
Cdd:PRK07232 399 DSGVATRPIaDMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 478 TVDALSLDFDPDVV-----DPDEGDHSAYADTLYDLRKRKGITRNEAESLVARDPNYLGSTMVEAGDADAFLTGLTHHYP 552
Cdd:PRK07232 479 RIKKLGLDLKAGVDfeivnPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYH 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 553 SALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVD 632
Cdd:PRK07232 559 EHLRPVRQVIGLRPGVHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSD 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 633 NEGTRKPRRAAQQLREdDDIDFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIG 712
Cdd:PRK07232 639 SPSARKMREAVELLRE-RAPDLEVDGEMHGDAALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIG 717
                        730       740
                 ....*....|....*....|....*
gi 167727384 713 PMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK07232 718 PILLGMAKPVHILTPSATVRRIVNM 742
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
1-420 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: 661.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:COG0281    7 ETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAVLGLGDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:COG0281   87 GPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDIPVFHDD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDR-DVNEFKAAFAQ- 238
Cdd:COG0281  167 QHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRtDLNPYKREFARd 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 --PADSGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVN 316
Cdd:COG0281  247 tnPRGLKGTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDG-AIVATGRSDYPNQVN 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 317 NVLGFPFIFRGALDVRATDINEEMKVaaataladlakqdvpdEVVKAYGDQ--PLQFGSEYIIPKPLDPRVLFEVAPAVA 394
Cdd:COG0281  326 NVLIFPGIFRGALDVRATRITDEMKL----------------AAARALADLvdEEELGPDYIIPSPFDPRVSPAVAAAVA 389
                        410       420
                 ....*....|....*....|....*.
gi 167727384 395 DAAMETGVARTELDlVDYREELEARL 420
Cdd:COG0281  390 KAAIESGVARRPID-EDYREALEARM 414
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
161-398 8.65e-110

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: 332.84  E-value: 8.65e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQ 238
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREdnLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   239 PAD--SGGDLADAMAGADVFVGLS-VGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDTVIMATGRSDYPNQV 315
Cdd:smart00919  81 KTNerETGTLEEAVKGADVLIGVSgPGGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWTAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   316 NNVLGFPFIFRGALDVRATDINEEMKVAaataladlakqdVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVAD 395
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLA------------AAEALADAVPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 167727384   396 AAM 398
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 ...
161-397 5.97e-107

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: 325.38  E-value: 5.97e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDR------DVNEFKA 234
Cdd:cd05311    1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGReddlnpDKNEIAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 235 AFAqPADSGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtvIMATGRSDYPNQ 314
Cdd:cd05311   81 ETN-PEKTGGTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD--IVATGRSDFPNQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 315 VNNVLGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPdevvkaygdqplqfGSEYIIPKPLDPRVLFEVAPAVA 394
Cdd:cd05311  158 VNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVL--------------GEEYIIPTPFDPRVVPRVATAVA 223

                 ...
gi 167727384 395 DAA 397
Cdd:cd05311  224 KAA 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
427-737 2.77e-95

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: 298.84  E-value: 2.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  427 MRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDALSLDFDPDVVDPDEGD--HSAYADT 504
Cdd:pfam01515   2 LERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLDGIEIVDPETSprLEEYADF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  505 LYDLRKRKGITRNEAESLVaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRVV 584
Cdd:pfam01515  82 YYELRKRKGMTPEIAREIV-RDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  585 FCADATVNQDPDADVLAEVAQHTADLARRF-NVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDdIDFPVDGEMQAD 663
Cdd:pfam01515 161 FFADCAVNPNPTAEELAEIALMSAKTAKRFgIIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERA-PDLVVDGELQFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167727384  664 TAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNT 313
pta TIGR00651
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ...
441-737 1.46e-73

phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]


Pssm-ID: 273196 [Multi-domain]  Cd Length: 303  Bit Score: 241.19  E-value: 1.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  441 IALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDA--LSLDFDPDVVDPDEGDHSAYADTLYDLRKRKGITRNE 518
Cdd:TIGR00651   1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGcnLDLGHVVIIDPDVSPDRESYAERYVELRKHKGMTEAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  519 AESLVaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDAD 598
Cdd:TIGR00651  81 ARKQL-RDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  599 VLAEVAQHTADLARRF-NVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDdIDFPVDGEMQADTAVVEDILQGSYEF 677
Cdd:TIGR00651 160 QLAEIAIQSANSAKSFgEIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKR-PDLTIDGELQFDAAFVEKVAEKKAPN 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  678 SDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:TIGR00651 239 SPVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNT 298
 
Name Accession Description Interval E-value
PRK07232 PRK07232
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
1-737 0e+00

bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed


Pssm-ID: 235976 [Multi-domain]  Cd Length: 752  Bit Score: 1248.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:PRK07232   1 EQLKQAALDYHRFPRPGKIEVTPTKPLATQRDLSLAYSPGVAAPCLEIAKDPADAYKYTARGNLVAVISNGTAVLGLGNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:PRK07232  81 GALASKPVMEGKGVLFKKFAGIDVFDIEVDEEDPDKFIEAVAALEPTFGGINLEDIKAPECFYIEEKLRERMDIPVFHDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQ 238
Cdd:PRK07232 161 QHGTAIISAAALLNALELVGKKIEDVKIVVSGAGAAAIACLNLLVALGAKKENIIVCDSKGVIYKGRTegMDEWKAAYAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 PADsGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVNNV 318
Cdd:PRK07232 241 DTD-ARTLAEAIEGADVFLGLSAAGVLTPEMVKSMADNPIIFALANPDPEITPEEAKAVRPD-AIIATGRSDYPNQVNNV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 319 LGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVADAAM 398
Cdd:PRK07232 319 LCFPYIFRGALDVGATTINEEMKLAAVRAIAELAREEVSDEVAAAYGGQKLSFGPEYIIPKPFDPRLIVKIAPAVAKAAM 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 399 ETGVARTEL-DLVDYREELEARLGKSREMMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQG 477
Cdd:PRK07232 399 DSGVATRPIaDMDAYREKLEAFVYKTGLVMKPIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEA 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 478 TVDALSLDFDPDVV-----DPDEGDHSAYADTLYDLRKRKGITRNEAESLVARDPNYLGSTMVEAGDADAFLTGLTHHYP 552
Cdd:PRK07232 479 RIKKLGLDLKAGVDfeivnPEDDPRYEEYWQYYYELLQRKGVTPEDARRLVRRDRTVIGAMMVARGDADAMICGLTGRYH 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 553 SALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVD 632
Cdd:PRK07232 559 EHLRPVRQVIGLRPGVHTAAAMNALLLKGGNLFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSD 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 633 NEGTRKPRRAAQQLREdDDIDFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIG 712
Cdd:PRK07232 639 SPSARKMREAVELLRE-RAPDLEVDGEMHGDAALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIG 717
                        730       740
                 ....*....|....*....|....*
gi 167727384 713 PMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK07232 718 PILLGMAKPVHILTPSATVRRIVNM 742
PRK12862 PRK12862
malic enzyme; Reviewed
1-737 0e+00

malic enzyme; Reviewed


Pssm-ID: 183799 [Multi-domain]  Cd Length: 763  Bit Score: 1029.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:PRK12862   9 AELREAALDYHRFPTPGKIEIAPTKPLANQRDLALAYSPGVAAPCLEIAADPANAARYTSRGNLVAVVSNGTAVLGLGNI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:PRK12862  89 GPLASKPVMEGKAVLFKKFAGIDVFDIELDESDPDKLVEIVAALEPTFGGINLEDIKAPECFYIERELRERMKIPVFHDD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDR--DVNEFKAAFAQ 238
Cdd:PRK12862 169 QHGTAIIVAAALLNGLKLVGKDIEDVKLVASGAGAAALACLDLLVSLGVKRENIWVTDIKGVVYEGRteLMDPWKARYAQ 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 PADsGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVNNV 318
Cdd:PRK12862 249 KTD-ARTLAEVIEGADVFLGLSAAGVLKPEMVKKMAPRPLIFALANPTPEILPEEARAVRPD-AIIATGRSDYPNQVNNV 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 319 LGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVADAAM 398
Cdd:PRK12862 327 LCFPYIFRGALDVGATTINEEMKIAAVRAIAELAREEQSDVVAAAYGGEDLSFGPDYLIPKPFDPRLILKIAPAVAQAAM 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 399 ETGVARTEL-DLVDYREELEARLGKSREMMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQG 477
Cdd:PRK12862 407 DSGVATRPIeDMDAYREQLNQFVYHSGLIMKPVFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVIEA 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 478 TVDALSLDFDPDVVDP---DEGDH--SAYADTLYDLRKRKGITRNEAESLVARDPNYLGSTMVEAGDADAFLTGLTHHYP 552
Cdd:PRK12862 487 RIERAGLRLRPGVDFEivnPEDDPryRDYWDTYHALMGRKGVTPEMARREVRRRTTLIGAMMVKRGEADAMICGTEGRYE 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 553 SALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVD 632
Cdd:PRK12862 567 RHLEFVLQVIGKRPGVRVYAAMSLLILPGRTLFLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGSSD 646
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 633 NEGTRKPRRAAQQLREdDDIDFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGG-ADAI 711
Cdd:PRK12862 647 SPSARKMREALEILRE-RAPDLEVDGEMHGDAALDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAAGnGLAV 725
                        730       740
                 ....*....|....*....|....*.
gi 167727384 712 GPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK12862 726 GPILLGAAKPVHILTPSATVRRIVNM 751
SfcA COG0281
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ...
1-420 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: 661.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   1 MGLDDDALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDI 80
Cdd:COG0281    7 ETLEQEALEYHRIYDRGKILVYPTVPLHTQEDLSLAYTPGVAEACLEIAEDPRLAYGYTAKGNLVAVVTDGTAVLGLGDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  81 GAQAAKPVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDD 160
Cdd:COG0281   87 GPLAGMPVMEGKAVLFKAFAGIDAFPICLDTNDPDEFVEAVKALEPTFGGINLEDIKAPNCFEIEERLREELDIPVFHDD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDR-DVNEFKAAFAQ- 238
Cdd:COG0281  167 QHGTAIVVLAALLNALKLVGKKLEDQKIVINGAGAAGIAIARLLVAAGLSEENIIMVDSKGLLYEGRtDLNPYKREFARd 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 239 --PADSGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVN 316
Cdd:COG0281  247 tnPRGLKGTLAEAIKGADVFIGVSAPGAFTEEMVKSMAKRPIIFALANPTPEITPEDAKAWGDG-AIVATGRSDYPNQVN 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 317 NVLGFPFIFRGALDVRATDINEEMKVaaataladlakqdvpdEVVKAYGDQ--PLQFGSEYIIPKPLDPRVLFEVAPAVA 394
Cdd:COG0281  326 NVLIFPGIFRGALDVRATRITDEMKL----------------AAARALADLvdEEELGPDYIIPSPFDPRVSPAVAAAVA 389
                        410       420
                 ....*....|....*....|....*.
gi 167727384 395 DAAMETGVARTELDlVDYREELEARL 420
Cdd:COG0281  390 KAAIESGVARRPID-EDYREALEARM 414
PRK12861 PRK12861
malic enzyme; Reviewed
7-737 0e+00

malic enzyme; Reviewed


Pssm-ID: 183798 [Multi-domain]  Cd Length: 764  Bit Score: 650.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   7 ALDYHASDPPGKVEISTTKPTNTQRDLSLAYSPGVAAPCRAIADDPTEAFTHTTKGNMVGVVSNGSAVLGLGDIGAQAAK 86
Cdd:PRK12861  11 ALDYHEFPTPGKISVVASKPLVTQRDLALAYTPGVASACEEIAADPLNAFRFTSRGNLVGVITNGTAVLGLGNIGALASK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  87 PVMEGKGVLFKRFADIDVFDIELDQATADELVATVSAMEPTFGGINLEDIKAPECFEVERRLGDAMDVPVFHDDQHGTAI 166
Cdd:PRK12861  91 PVMEGKAVLFKKFAGIDVFDIEINETDPDKLVDIIAGLEPTFGGINLEDIKAPECFTVERKLRERMKIPVFHDDQHGTAI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 167 ISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQPADSgG 244
Cdd:PRK12861 171 TVSAAFINGLKVVGKSIKEVKVVTSGAGAAALACLDLLVDLGLPVENIWVTDIEGVVYRGRTtlMDPDKERFAQETDA-R 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 245 DLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtVIMATGRSDYPNQVNNVLGFPFI 324
Cdd:PRK12861 250 TLAEVIGGADVFLGLSAGGVLKAEMLKAMAARPLILALANPTPEIFPELAHATRDD-VVIATGRSDYPNQVNNVLCFPYI 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 325 FRGALDVRATDINEEMKVAAATALADLAKQDVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVADAAMETGVAR 404
Cdd:PRK12861 329 FRGALDVGATTITREMEIAAVHAIAGLAEEEQNDVVAAAYGAYDVSFGPQYLIPKPFDPRLIVRIAPAVAKAAMEGGVAT 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 405 TEL-DLVDYREELEARLGKSREMMRIVINKAKS-----EQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGT 478
Cdd:PRK12861 409 RPIaDLDAYVEQLQQFVYHSGAFMKPLFAAARQlvrdgGKARIVFTEGEDERVLRAVQVIVDEKLARPILVGRPEVLLAR 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 479 VDALSL---DFDPDVVDPDEGDHS--AYADTLYDLRKRKGITRNEAESLVARDPNYLGSTMVEAGDADAFLTGLTHHYPS 553
Cdd:PRK12861 489 IERFGLrlrLGQDVEVTNPEYDERfpQYWTTYWELRCRDGISKEMARVEMRRRLTLIGAMMVRLGDADGMICGTVGEYHN 568
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 554 ALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVDN 633
Cdd:PRK12861 569 HLRFVDEVIGRKPGASTYAAMNILLLDQRTVALVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSRSNFGSGSA 648
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 634 EGTRKPRRAAQQLREDDDiDFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGAD-AIG 712
Cdd:PRK12861 649 ASGVKMRRALEIVREQAP-DLEADGEMHGDCALDEGLRARLLPMSPLKGAANLLVCPNVDAGNIAYNLLKTEAGSNvAVG 727
                        730       740
                 ....*....|....*....|....*
gi 167727384 713 PMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK12861 728 PFLLGVNAPVNILTSSATVRRIVNM 752
Pta COG0280
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ...
426-737 8.42e-123

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


Pssm-ID: 440049 [Multi-domain]  Cd Length: 320  Bit Score: 370.17  E-value: 8.42e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 426 MMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDA--LSLDFDPDVVDPDEGDHSAYAD 503
Cdd:COG0280    2 FFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEElgLDLSGFEIIDPEDSPRYEEYAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 504 TLYDLRKRKGITRNEAESLVaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRV 583
Cdd:COG0280   82 AYYELRKRKGVTPEEARELV-RDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGLRPGVKRVSHVFLMELPDRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 584 VFCADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREdDDIDFPVDGEMQAD 663
Cdd:COG0280  161 LFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARG-QIPDLEVDGELQFD 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167727384 664 TAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:COG0280  240 AALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNS 313
Malic_M smart00919
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ...
161-398 8.65e-110

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: 332.84  E-value: 8.65e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDRD--VNEFKAAFAQ 238
Cdd:smart00919   1 QQGTAIVVLAGLLNALKITGKKLEDQRIVVNGAGAAGIGIAKLLVAAGVKRKNIWLVDSKGLLTKGREdnLNPYKKPFAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   239 PAD--SGGDLADAMAGADVFVGLS-VGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDTVIMATGRSDYPNQV 315
Cdd:smart00919  81 KTNerETGTLEEAVKGADVLIGVSgPGGAFTEEMVKSMAERPIIFALSNPTPEIEPTAADAYRWTAAIVATGRSDYPNQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   316 NNVLGFPFIFRGALDVRATDINEEMKVAaataladlakqdVPDEVVKAYGDQPLQFGSEYIIPKPLDPRVLFEVAPAVAD 395
Cdd:smart00919 161 NNVLIFPGIFLGALDVRARRITDEMKLA------------AAEALADAVPVSEEELGPGYIIPSPFDRRVSARVAVAVAK 228

                   ...
gi 167727384   396 AAM 398
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 ...
161-397 5.97e-107

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: 325.38  E-value: 5.97e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDREHITMCDSSGVITEDR------DVNEFKA 234
Cdd:cd05311    1 QHGTAIVTLAGLLNALKLVGKKIEEVKIVINGAGAAGIAIARLLLAAGAKPENIVVVDSKGVIYEGReddlnpDKNEIAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 235 AFAqPADSGGDLADAMAGADVFVGLSVGGIVNQAMVRSMADDPIVFAMANPDPEIDYESAKAAREDtvIMATGRSDYPNQ 314
Cdd:cd05311   81 ETN-PEKTGGTLKEALKGADVFIGVSRPGVVKKEMIKKMAKDPIVFALANPVPEIWPEEAKEAGAD--IVATGRSDFPNQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 315 VNNVLGFPFIFRGALDVRATDINEEMKVAAATALADLAKQDVPdevvkaygdqplqfGSEYIIPKPLDPRVLFEVAPAVA 394
Cdd:cd05311  158 VNNVLGFPGIFRGALDVRATKITEEMKLAAAEAIADLAEEEVL--------------GEEYIIPTPFDPRVVPRVATAVA 223

                 ...
gi 167727384 395 DAA 397
Cdd:cd05311  224 KAA 226
PTA_PTB pfam01515
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ...
427-737 2.77e-95

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: 298.84  E-value: 2.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  427 MRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDALSLDFDPDVVDPDEGD--HSAYADT 504
Cdd:pfam01515   2 LERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLDGIEIVDPETSprLEEYADF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  505 LYDLRKRKGITRNEAESLVaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRVV 584
Cdd:pfam01515  82 YYELRKRKGMTPEIAREIV-RDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  585 FCADATVNQDPDADVLAEVAQHTADLARRF-NVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDdIDFPVDGEMQAD 663
Cdd:pfam01515 161 FFADCAVNPNPTAEELAEIALMSAKTAKRFgIIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERA-PDLVVDGELQFD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167727384  664 TAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNT 313
eutD PRK09653
phosphotransacetylase;
425-737 8.56e-81

phosphotransacetylase;


Pssm-ID: 236609 [Multi-domain]  Cd Length: 324  Bit Score: 260.93  E-value: 8.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 425 EMMRIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDALSLDFDPDVVDPDE--GDHSAYA 502
Cdd:PRK09653   2 DLFESLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDLDGVEIIDPEtyPLLEEFA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 503 DTLYDLRKRKGITRNEAESLvaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVY-MLTFQN 581
Cdd:PRK09653  82 EAFVELRKGKGTEEDAAELL--KDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIKTKPGVKTVSSVFiMVKGDE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 582 RVVFcADATVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDDiDFPVDGEMQ 661
Cdd:PRK09653 160 RYIF-ADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKGPEVDKVQEATEIAKELAP-DLKIDGELQ 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167727384 662 ADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:PRK09653 238 FDAAFVPEVAAKKAPGSPVAGKANVFVFPSLEAGNIGYKIAQRLGGFEAVGPILQGLNKPVNDLSRGCSVEDIYNL 313
pta TIGR00651
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ...
441-737 1.46e-73

phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]


Pssm-ID: 273196 [Multi-domain]  Cd Length: 303  Bit Score: 241.19  E-value: 1.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  441 IALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDA--LSLDFDPDVVDPDEGDHSAYADTLYDLRKRKGITRNE 518
Cdd:TIGR00651   1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGcnLDLGHVVIIDPDVSPDRESYAERYVELRKHKGMTEAQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  519 AESLVaRDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADATVNQDPDAD 598
Cdd:TIGR00651  81 ARKQL-RDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  599 VLAEVAQHTADLARRF-NVDPRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDdIDFPVDGEMQADTAVVEDILQGSYEF 677
Cdd:TIGR00651 160 QLAEIAIQSANSAKSFgEIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKR-PDLTIDGELQFDAAFVEKVAEKKAPN 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  678 SDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVNL 737
Cdd:TIGR00651 239 SPVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNT 298
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
431-736 4.13e-60

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 215.40  E-value: 4.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 431 INKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDALSLD-FDPDVVDPDEGDHSAYADTLYDLR 509
Cdd:PRK05632 370 TERARAAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDlPAGIEIIDPSEVRERYVAPLVELR 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 510 KRKGITRNEAESLVArDPNYLGSTMVEAGDADAFLTGLTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQNRVVFCADA 589
Cdd:PRK05632 450 KHKGMTEEVAREQLE-DNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDC 528
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 590 TVNQDPDADVLAEVAQHTADLARRFNVDPRVAVLSYSNFGS---VDNEGTRKPRRAAQQLREDddidFPVDGEMQADTAV 666
Cdd:PRK05632 529 AVNPDPTAEQLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSgsgADVEKVREATRLARERRPD----LLIDGPLQYDAAV 604
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167727384 667 VEDI----LQGSyefsdlDTA--ANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLVGMNKPVHVLQRGDEVKDIVN 736
Cdd:PRK05632 605 DPSVarskAPNS------PVAgrATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVN 674
malic pfam00390
Malic enzyme, N-terminal domain;
16-148 3.54e-40

Malic enzyme, N-terminal domain;


Pssm-ID: 395314 [Multi-domain]  Cd Length: 182  Bit Score: 145.87  E-value: 3.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   16 PGKVEISTTKPTNTQ--RDLSLAYSPGVAAPCRAIADDPTEAF-THTTKGNM----------------VGVVSNGSAVLG 76
Cdd:pfam00390   1 QGKNEVLFYKLLSTHieEDLPIVYTPTVGEACQAISEIYRRPRgLYTSIGNLgkikdilknwpeedvrVIVVTDGERILG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384   77 LGDIGAqAAKPVMEGKGVLFKRFADID---VFDIELDQATA---------------------------DELVATVSAMEP 126
Cdd:pfam00390  81 LGDLGV-AGMPIMEGKLALYTAFAGIDpsrVLPIVLDVGTNnekllndplylglrhkrvrgeeydefvDEFVEAVKALFP 159
                         170       180
                  ....*....|....*....|..
gi 167727384  127 TFGGINLEDIKAPECFEVERRL 148
Cdd:pfam00390 160 PFGGIQFEDFGAPNAFEILERY 181
PLN03129 PLN03129
NADP-dependent malic enzyme; Provisional
65-412 1.06e-28

NADP-dependent malic enzyme; Provisional


Pssm-ID: 215594 [Multi-domain]  Cd Length: 581  Bit Score: 121.56  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  65 VGVVSNGSAVLGLGDIGAQAakpvM---EGKGVLFKRFAD----------IDV-----------FDIELDQATA-----D 115
Cdd:PLN03129 174 VIVVTDGERILGLGDLGVQG----MgipVGKLDLYTAAGGirpsavlpvcIDVgtnnekllndpFYIGLRQPRLtgeeyD 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 116 ELVA-TVSAMEPTFGG---INLEDIKAPECFEVERRLGDamDVPVFHDDQHGTAIISGAALLNAAEIAGKDLSDLDVVFS 191
Cdd:PLN03129 250 ELVDeFMEAVKQRWGPkvlVQFEDFANKNAFRLLQRYRT--THLCFNDDIQGTAAVALAGLLAALRATGGDLADQRILFA 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 192 GAGASAIATAKFYVS-----LGVD----REHITMCDSSGVITEDR--DVNEFKAAFAQPADSGGDLADAMAGA--DVFVG 258
Cdd:PLN03129 328 GAGEAGTGIAELIALamsrqTGISeeeaRKRIWLVDSKGLVTKSRkdSLQPFKKPFAHDHEPGASLLEAVKAIkpTVLIG 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 259 LS-VGGIVNQAMVRSMADD---PIVFAMANP--DPEIDYESAKAAREDTVIMAT----------GRSDYPNQVNNVLGFP 322
Cdd:PLN03129 408 LSgVGGTFTKEVLEAMASLnerPIIFALSNPtsKAECTAEEAYTWTGGRAIFASgspfdpveynGKTFHPGQANNAYIFP 487
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 323 FIFRGALDVRATDINEEMKVAAAtaladlakqdvpdEVVKAY-GDQPLQFGSEY----IIPKpldprVLFEVAPAVADAA 397
Cdd:PLN03129 488 GIGLGALLSGAIRVTDDMLLAAA-------------EALAAQvTEEELAKGAIYppfsRIRD-----ISAHVAAAVAAKA 549
                        410
                 ....*....|....*...
gi 167727384 398 METGVAR---TELDLVDY 412
Cdd:PLN03129 550 YEEGLATrlpRPEDLVEY 567
PTZ00317 PTZ00317
NADP-dependent malic enzyme; Provisional
33-418 6.96e-27

NADP-dependent malic enzyme; Provisional


Pssm-ID: 240357 [Multi-domain]  Cd Length: 559  Bit Score: 115.88  E-value: 6.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  33 LSLAYSPGVAAPCRAIADDPTEA----FTHTTKGNM-------------VGVVSNGSAVLGLGDIGAQAAkPVMEGKGVL 95
Cdd:PTZ00317 102 LPIIYTPTVGEACQNYSNLFQRDrglyLSRAHKGKIreilknwpydnvdVIVITDGSRILGLGDLGANGM-GISIGKLSL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  96 FKRFADID---VFDIELDQAT---------------------------ADELVATVSAMEPTfGGINLEDIKAPECFEVE 145
Cdd:PTZ00317 181 YVAGGGINpsrVLPVVLDVGTnnekllndplylglrekrldddeyyelLDEFMEAVSSRWPN-AVVQFEDFSNNHCFDLL 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 146 RRLGDAmdVPVFHDDQHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSL----GVDREH----ITMC 217
Cdd:PTZ00317 260 ERYQNK--YRCFNDDIQGTGAVIAAGFLNALKLSGVPPEEQRIVFFGAGSAAIGVANNIADLaaeyGVTREEalksFYLV 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 218 DSSGVITEDRD--VNEFKAAFAQ----PADSGG-DLADAMAGA--DVFVGLS-VGGIVNQAMVRSMADD---PIVFAMAN 284
Cdd:PTZ00317 338 DSKGLVTTTRGdkLAKHKVPFARtdisAEDSSLkTLEDVVRFVkpTALLGLSgVGGVFTEEVVKTMASNverPIIFPLSN 417
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 285 P--DPEIDYESAKAAREDTVIMATG----------RSDYPNQVNNVLGFPFIFRGALDVRATDINEEMKVAAATALADLa 352
Cdd:PTZ00317 418 PtsKAECTAEDAYKWTNGRAIVASGspfppvtlngKTIQPSQGNNLYVFPGVGLGCAIAQPSYIPDEMLIAAAASLATL- 496
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167727384 353 kqdVPDEVVKaygdqplqfgSEYIIPkPLDP--RVLFEVAPAVADAAMETGVARTELdLVDYREELEA 418
Cdd:PTZ00317 497 ---VSEEDLR----------EGKLYP-PLEDirEISAHIAVDVIEEAQEMGIAKNKD-LPDNRDELLA 549
NAD_bind_1_malic_enz cd05312
NAD(P) binding domain of malic enzyme (ME), subgroup 1; Malic enzyme (ME), a member of the ...
163-419 1.47e-26

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: 109.95  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 163 GTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAK----FYVSLGVD----REHITMCDSSGVITEDR-DVNEFK 233
Cdd:cd05312    3 GTAAVALAGLLAALRITGKPLSDQRILFLGAGSAGIGIADlivsAMVREGLSeeeaRKKIWLVDSKGLLTKDRkDLTPFK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 234 AAFAQPADSGG--DLADAM--AGADVFVGLS-VGGIVNQAMVRSMA---DDPIVFAMANPDP--EIDYESAKAAREDTVI 303
Cdd:cd05312   83 KPFARKDEEKEgkSLLEVVkaVKPTVLIGLSgVGGAFTEEVVRAMAksnERPIIFALSNPTSkaECTAEDAYKWTDGRAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 304 MATG----------RSDYPNQVNNVLGFPFIFRGALDVRATDINEEMkvaaATALADLAKQDVPDEVVKAygdqplqfGS 373
Cdd:cd05312  163 FASGspfppveyngKTYVPGQGNNAYIFPGIGLGAILSGARHITDEM----FLAAAEALASLVTDEELAR--------GR 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 167727384 374 EYiiPkPLDP--RVLFEVAPAVADAAMETGVARTELDLVDYREELEAR 419
Cdd:cd05312  231 LY--P-PLSNirEISAQIAVAVAKYAYEEGLATRYPPPEDLEEYVKSQ 275
NAD_bind_malic_enz cd00762
NAD(P) binding domain of malic enzyme; Malic enzyme (ME), a member of the amino acid ...
161-340 2.49e-26

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: 108.84  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 161 QHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKFYVSLGVDR--------EHITMCDSSGVITEDR----D 228
Cdd:cd00762    1 IQGTASVAVAGLLAALKVTKKKISEHKVLFNGAGAAALGIANLIV*L*VKEgiskeeacKRIW*VDRKGLLVKNRketcP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 229 VNEFKAAFAQPADSGGDLADAM--AGADVFVGLS-VGGIVNQAMVRSMA---DDPIVFAMANPDP--EIDYESAKAARED 300
Cdd:cd00762   81 NEYHLARFANPERESGDLEDAVeaAKPDFLIGVSrVGGAFTPEVIRA*AeinERPVIFALSNPTSkaECTAEEAYTATEG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 167727384 301 TVIMATGRSD----------YPNQVNNVLGFPFIFRGALDVRATDINEEM 340
Cdd:cd00762  161 RAIFASGSPFhpvelnggtyKPGQGNNLYIFPGVALGVILCRIRHITDDV 210
PRK13529 PRK13529
oxaloacetate-decarboxylating malate dehydrogenase;
67-427 2.62e-24

oxaloacetate-decarboxylating malate dehydrogenase;


Pssm-ID: 237414 [Multi-domain]  Cd Length: 563  Bit Score: 107.91  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  67 VVSNGSAVLGLGDIGAQA-AKPVmeGKGVLFKRFADID---VFDIELDQATA-----------------------DELVA 119
Cdd:PRK13529 151 VVTDGERILGIGDQGIGGmGIPI--GKLSLYTACGGIDparTLPVVLDVGTNneqllndplylgwrhprirgeeyDEFVD 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 120 T-VSAMEPTFGG--INLEDIKAPECFEVERRLGDamDVPVFHDDQHGTAIISGAALLNAAEIAGKDLSDLDVVFSGAGAS 196
Cdd:PRK13529 229 EfVQAVKRRFPNalLQFEDFAQKNARRILERYRD--EICTFNDDIQGTGAVTLAGLLAALKITGEPLSDQRIVFLGAGSA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 197 AIATAKFYVSLGVD--------REHITMCDSSGVITEDR-DVNEFKAAFAQPADS---------GGDLADAM--AGADVF 256
Cdd:PRK13529 307 GCGIADQIVAAMVReglseeeaRKRFFMVDRQGLLTDDMpDLLDFQKPYARKREEladwdtegdVISLLEVVrnVKPTVL 386
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 257 VGLS-VGGIVNQAMVRSMA---DDPIVFAMANPDpeidyESAKAAREDT-------VIMATG----------RSDYPNQV 315
Cdd:PRK13529 387 IGVSgQPGAFTEEIVKEMAahcERPIIFPLSNPT-----SRAEATPEDLiawtdgrALVATGspfapveyngKTYPIGQC 461
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 316 NNVLGFPFIFRGALDVRATDINEEMKVaaataladlakqdvpdEVVKAYGDQ--PLQFGSEYIIPkPLDP--RVLFEVAP 391
Cdd:PRK13529 462 NNAYIFPGLGLGVIASGARRVTDGMLM----------------AAAHALADCvpLAKPGEGALLP-PVEDirEVSRAIAI 524
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 167727384 392 AVADAAMETGVARTELDlvdyrEELEARLgksREMM 427
Cdd:PRK13529 525 AVAKAAIEEGLARETSD-----EDLEQAI---EDNM 552
Malic_M pfam03949
Malic enzyme, NAD binding domain;
163-340 7.89e-24

Malic enzyme, NAD binding domain;


Pssm-ID: 427608 [Multi-domain]  Cd Length: 257  Bit Score: 101.50  E-value: 7.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  163 GTAIISGAALLNAAEIAGKDLSDLDVVFSGAGASAIATAKF----YVSLGVDRE----HITMCDSSGVITEDR-DVNEFK 233
Cdd:pfam03949   3 GTAAVALAGLLAALKITGKPLSEQRIVFFGAGSAGIGIADQirdaMVREGLSEEearkRIWMVDRQGLLTDDReDLTDFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384  234 AAFAQPADS------GGDLADAM--AGADVFVGLS-VGGIVNQAMVRSMA---DDPIVFAMANPDP--EIDYESAKAARE 299
Cdd:pfam03949  83 KPFARKRAElkgwgdGITLLEVVrkVKPTVLIGASgVPGAFTEEIVRAMAahtERPIIFPLSNPTSkaEATPEDAYKWTD 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167727384  300 DTVIMATG----------RSDYPNQVNNVLGFPFIFRGALDVRATDINEEM 340
Cdd:pfam03949 163 GRALFATGspfppveyngKTYHIGQGNNAYIFPGLGLGAIVSRARRITDEM 213
PRK05805 PRK05805
phosphate butyryltransferase; Validated
426-729 1.78e-08

phosphate butyryltransferase; Validated


Pssm-ID: 180267  Cd Length: 301  Bit Score: 56.64  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 426 MMRI---VINKAKS-EQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQgtvdalsldfdpdvvdpdegdhsAY 501
Cdd:PRK05805   1 MIKSfdeILSKAKEqPPKTISVAVAQDEPVLEAVKEAKELGIANAILVGDKEKIK-----------------------EI 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 502 AdtlydlrkrKGITRNEAESLVARDPNYLGST-----MVEAGDADAFLTGLTHhYPSALKPPL-QVVG--TAPDTDYVAg 573
Cdd:PRK05805  58 A---------KEIDMDLEDFEIIDEKDNRKAAlkaveLVSSGKADMVMKGLVD-TANFLRAVLnKEIGlrTGKTMSHVA- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 574 VYMLTFQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVD-PRVAVLsysnfGSVDNEGTRKPR----RAAQQLRE 648
Cdd:PRK05805 127 VFEVPKYDRLLFLTDAAFNIAPDLKEKIDIINNAVTVAHAIGIEnPKVAPI-----CAVEVVNPKMPAtldaALLSKMSD 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 649 DDDI-DFPVDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGAdAIGPMLVGMNKPVHVLQR 727
Cdd:PRK05805 202 RGQIkGCIVDGPLALDNALSEEAAKHKGIDGPVAGNADILLVPNIEAGNVMYKTLTYFADC-KNGGLLVGTSAPVVLTSR 280

                 ..
gi 167727384 728 GD 729
Cdd:PRK05805 281 AD 282
PRK07742 PRK07742
phosphate butyryltransferase; Validated
428-729 1.43e-07

phosphate butyryltransferase; Validated


Pssm-ID: 236086  Cd Length: 299  Bit Score: 53.94  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 428 RIVINKAKSEQQRIALGEGGDEKMIRAAHQMHEAGIADPVLLGDRDTIQgtvdalsldfdpdvvdpdegdhsayadtlyD 507
Cdd:PRK07742   5 HLIDQAAGQPKKTVAVAVAEDEEVIEAVAKAIELQLARFRLYGNQEKIM------------------------------G 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 508 LRKRKGITRNEAESLVARDPN----YLGSTMVEAGDADAFLTGlthHYPSA--LKPPLQV---VGTAPDTDYVAgVYMLT 578
Cdd:PRK07742  55 MLQEHGLQTSEHIEIIHAQSSaeaaELAVKAVRNGEADVLMKG---NVPTAniLKAVLNKewgLRKGSVLSHVA-VFEVP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 579 FQNRVVFCADATVNQDPDADVLAEVAQHTADLARRFNVD-PRVAVLSYSNFGSVDNEGTRKPRRAAQQLREDDDIDFPVD 657
Cdd:PRK07742 131 NYDRLIFVTDAAMNIAPDLEQKAAIIQNAVEVARAIGIDlPKVAPLAAVEVVNPAMQATIDAAALTQMNRRGQIKNCVVD 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167727384 658 GEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADaIGPMLVGMNKPVHVLQRGD 729
Cdd:PRK07742 211 GPLALDNAVSQIAAEHKGIVSDVAGKADILLVPTIEAGNVLYKSLVYFADAK-VGAMIAGAKAPIVLTSRAD 281
PRK11890 PRK11890
phosphate acetyltransferase; Provisional
585-731 2.83e-05

phosphate acetyltransferase; Provisional


Pssm-ID: 183361  Cd Length: 312  Bit Score: 46.91  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 585 FCADATVNQDPDADVLAEVAQHTADLARRFNVD-PRVAVLSysnfgSVDNEGTRKPR--------RAAQQLREDDDIdfp 655
Cdd:PRK11890 143 IITDAAVNIAPTLEDKADIVQNAIDLAHALGFDePRVAILS-----AVETVNPKIPStldaaalcKMADRGQITGAI--- 214
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167727384 656 VDGEMQADTAVVEDILQGSYEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGPMLvGMNKPVHVLQRGDEV 731
Cdd:PRK11890 215 LDGPLAFDNAISPEAARIKGIVSPVAGDADILVVPDLEAGNMLAKQLTFLAGADAAGIVL-GARVPIILTSRADSV 289
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
448-732 5.68e-04

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 42.94  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 448 DEKMIRAAHQMHEAGIADPVLLGDRDTIQGTVDALSLDFDPDVVDPDEGDHSAyadtlydlrkrkgitrneAESLVArdp 527
Cdd:PRK08190 186 DAESLRGALEAAEAGLIEPVLVGPEAKIRAAAEEAGLDLSGVRIVDVPHSHAA------------------AARAVA--- 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 528 nylgstMVEAGDADAFLTGlTHHYPSALKPPLQVVGTAPDTDYVAGVYMLTFQN--RVVFCADATVNQDPDADVLAEVAQ 605
Cdd:PRK08190 245 ------LARAGEVEALMKG-SLHTDELLSAVVARDSGLRTERRISHVFAMDVPTypRPLLITDAAINIAPTLEDKRDIVQ 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167727384 606 HTADLARRFNVD-PRVAVLSysnfgSVDNEGTRKPRR--AAQ--------QLRedDDIdfpVDGEMQADTAVVEDILQGS 674
Cdd:PRK08190 318 NAIDLAHALGVEePKVAILS-----AVETVNPKMPSTldAAAlckmadrgQIT--GGI---VDGPLAFDNAISAEAARTK 387
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167727384 675 YEFSDLDTAANVLIFPNLEAGNIGYKLLQRLGGADAIGpMLVGMNKPVHVLQRGDEVK 732
Cdd:PRK08190 388 GIVSPVAGQADILVVPDLEAGNMLAKQLTYLAGADAAG-IVLGARVPIILTSRADSLR 444
 
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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