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Conserved domains on  [gi|6226882|sp|P54886|]
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RecName: Full=Delta-1-pyrroline-5-carboxylate synthase; Short=P5CS; AltName: Full=Aldehyde dehydrogenase family 18 member A1; Includes: RecName: Full=Glutamate 5-kinase; Short=GK; AltName: Full=Gamma-glutamyl kinase; Includes: RecName: Full=Gamma-glutamyl phosphate reductase; Short=GPR; AltName: Full=Glutamate-5-semialdehyde dehydrogenase; AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
64-794 0e+00

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


:

Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 1253.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     64 RSELKHAKRIVVKLGSAVVTRGDECgLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHS 143
Cdd:TIGR01092   1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    144 GqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:TIGR01092  80 Q---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNEND 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    224 AVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQ-SVTFGTKSR 302
Cdd:TIGR01092 151 AVSTRAAPYSDSQGI----FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQgEITFGTKSR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    303 VGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE-----MARSGGRML 377
Cdd:TIGR01092 227 LGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdmavAARESSRML 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVLR 456
Cdd:TIGR01092 303 QALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAAM-EDPIGRVLK 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    457 RTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLV 536
Cdd:TIGR01092 382 RTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLV 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    537 NTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALE 616
Cdd:TIGR01092 462 TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAME 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    617 TLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHT 696
Cdd:TIGR01092 541 TLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHT 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    697 DVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfSE 776
Cdd:TIGR01092 621 DCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVS--GD 698
                         730
                  ....*....|....*...
gi 6226882    777 HGsLKYLHENLPIPQRNT 794
Cdd:TIGR01092 699 HG-LVYTHKDLPIPQRNT 715
 
Name Accession Description Interval E-value
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
64-794 0e+00

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 1253.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     64 RSELKHAKRIVVKLGSAVVTRGDECgLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHS 143
Cdd:TIGR01092   1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    144 GqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:TIGR01092  80 Q---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNEND 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    224 AVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQ-SVTFGTKSR 302
Cdd:TIGR01092 151 AVSTRAAPYSDSQGI----FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQgEITFGTKSR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    303 VGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE-----MARSGGRML 377
Cdd:TIGR01092 227 LGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdmavAARESSRML 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVLR 456
Cdd:TIGR01092 303 QALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAAM-EDPIGRVLK 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    457 RTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLV 536
Cdd:TIGR01092 382 RTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLV 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    537 NTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALE 616
Cdd:TIGR01092 462 TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAME 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    617 TLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHT 696
Cdd:TIGR01092 541 TLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHT 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    697 DVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfSE 776
Cdd:TIGR01092 621 DCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVS--GD 698
                         730
                  ....*....|....*...
gi 6226882    777 HGsLKYLHENLPIPQRNT 794
Cdd:TIGR01092 699 HG-LVYTHKDLPIPQRNT 715
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
64-789 0e+00

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 822.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    64 RSELKHAKRIVVKLGSAVVTRGDecG-LALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQaLH 142
Cdd:PLN02418   9 RAFLRDVKRVVIKVGTAVVTRDD--GrLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLVNSSFAD-LQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   143 SGQNQLKEMAipvlearaCAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:PLN02418  86 KPQMELDGKA--------CAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNEN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   223 DAVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYP-GDQQSVTFGTKS 301
Cdd:PLN02418 158 DAVSTRRAPYEDSSGI----FWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKeKHQDEITFGEKS 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   302 RVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFseVKPAG---PTVEQQG-EMA---RSGG 374
Cdd:PLN02418 234 RVGRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF--HQDAHlwaPSKEVGArEMAvaaRESS 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   375 RMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGR 453
Cdd:PLN02418 308 RKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSRLTLKPGKIASLAASIRQLADM-EDPIGR 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   454 VLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAV 533
Cdd:PLN02418 387 VLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKLI 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   534 QLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACN 613
Cdd:PLN02418 467 GLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACN 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   614 ALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGS 693
Cdd:PLN02418 546 AMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGS 623
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   694 SHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSd 773
Cdd:PLN02418 624 AHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQVVD- 702
                        730
                 ....*....|....*.
gi 6226882   774 fSEHGSLkYLHENLPI 789
Cdd:PLN02418 703 -GDKGVV-YTHKDLPL 716
ALDH_F18-19_ProA-GPR cd07079
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ...
364-766 0e+00

Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).


Pssm-ID: 143398  Cd Length: 406  Bit Score: 596.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  364 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 442
Cdd:cd07079   1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  443 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 522
Cdd:cd07079  81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  523 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 599
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  600 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 678
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  679 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 758
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397

                ....*...
gi 6226882  759 TTKWLLRG 766
Cdd:cd07079 398 TYKYIVRG 405
ProA COG0014
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ...
362-772 6.37e-172

Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 439785  Cd Length: 414  Bit Score: 501.46  E-value: 6.37e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  362 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 440
Cdd:COG0014   2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  441 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:COG0014  82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  521 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  598 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 672
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  673 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 752
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
                       410       420
                ....*....|....*....|
gi 6226882  753 GLEGLLTTKWLLRGKDHVVS 772
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
71-329 8.73e-38

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 140.96  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     71 KRIVVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGavafGKQrLRHEILLSQSVRQALHSGQNQLKE 150
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE-------RLKRLADEIAALLEEGRKLVVVHGG----GAF-ADGLLALLGLSPRFARLTDAETLE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    151 maipVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAE 230
Cdd:pfam00696  69 ----VATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    231 pnsdlqgvnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVtfgTKSRVGMGGME 309
Cdd:pfam00696 145 ----------LGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDELLEL---LASGLATGGMK 211
                         250       260
                  ....*....|....*....|.
gi 6226882    310 AKVKAALWALQ-GGTSVVIAN 329
Cdd:pfam00696 212 VKLPAALEAARrGGIPVVIVN 232
 
Name Accession Description Interval E-value
P5CS TIGR01092
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ...
64-794 0e+00

delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130164 [Multi-domain]  Cd Length: 715  Bit Score: 1253.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     64 RSELKHAKRIVVKLGSAVVTRGDECgLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHS 143
Cdd:TIGR01092   1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    144 GqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:TIGR01092  80 Q---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNEND 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    224 AVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQ-SVTFGTKSR 302
Cdd:TIGR01092 151 AVSTRAAPYSDSQGI----FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKHQgEITFGTKSR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    303 VGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE-----MARSGGRML 377
Cdd:TIGR01092 227 LGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdmavAARESSRML 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGRVLR 456
Cdd:TIGR01092 303 QALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAAM-EDPIGRVLK 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    457 RTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLV 536
Cdd:TIGR01092 382 RTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLV 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    537 NTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALE 616
Cdd:TIGR01092 462 TSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAME 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    617 TLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHT 696
Cdd:TIGR01092 541 TLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHT 620
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    697 DVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSdfSE 776
Cdd:TIGR01092 621 DCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVS--GD 698
                         730
                  ....*....|....*...
gi 6226882    777 HGsLKYLHENLPIPQRNT 794
Cdd:TIGR01092 699 HG-LVYTHKDLPIPQRNT 715
PLN02418 PLN02418
delta-1-pyrroline-5-carboxylate synthase
64-789 0e+00

delta-1-pyrroline-5-carboxylate synthase


Pssm-ID: 215230  Cd Length: 718  Bit Score: 822.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    64 RSELKHAKRIVVKLGSAVVTRGDecG-LALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQaLH 142
Cdd:PLN02418   9 RAFLRDVKRVVIKVGTAVVTRDD--GrLALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLVNSSFAD-LQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   143 SGQNQLKEMAipvlearaCAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:PLN02418  86 KPQMELDGKA--------CAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNEN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   223 DAVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYP-GDQQSVTFGTKS 301
Cdd:PLN02418 158 DAVSTRRAPYEDSSGI----FWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKeKHQDEITFGEKS 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   302 RVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFseVKPAG---PTVEQQG-EMA---RSGG 374
Cdd:PLN02418 234 RVGRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF--HQDAHlwaPSKEVGArEMAvaaRESS 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   375 RMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKRLSLSTSKLNSLAIGLRQIAASsQDSVGR 453
Cdd:PLN02418 308 RKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSRLTLKPGKIASLAASIRQLADM-EDPIGR 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   454 VLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAV 533
Cdd:PLN02418 387 VLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKLI 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   534 QLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACN 613
Cdd:PLN02418 467 GLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAACN 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   614 ALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGS 693
Cdd:PLN02418 546 AMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHGS 623
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   694 SHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSd 773
Cdd:PLN02418 624 AHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQVVD- 702
                        730
                 ....*....|....*.
gi 6226882   774 fSEHGSLkYLHENLPI 789
Cdd:PLN02418 703 -GDKGVV-YTHKDLPL 716
ALDH_F18-19_ProA-GPR cd07079
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ...
364-766 0e+00

Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).


Pssm-ID: 143398  Cd Length: 406  Bit Score: 596.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  364 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 442
Cdd:cd07079   1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  443 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 522
Cdd:cd07079  81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  523 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 599
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  600 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 678
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  679 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 758
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397

                ....*...
gi 6226882  759 TTKWLLRG 766
Cdd:cd07079 398 TYKYIVRG 405
AAK_P5CS_ProBA cd04256
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ...
63-354 0e+00

AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.


Pssm-ID: 239789 [Multi-domain]  Cd Length: 284  Bit Score: 543.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   63 HRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALH 142
Cdd:cd04256   1 SRSELKHAKRIVVKLGSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHEILLSSSMRQTLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  143 SgqNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTN 222
Cdd:cd04256  81 S--GQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  223 DAVVPPAEPNSDLQGVnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTKSR 302
Cdd:cd04256 159 DAVSPPPEPDEDLQGV--ISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYPGDQQSITFGTKSR 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6226882  303 VGMGGMEAKVKAALWALQGGTSVVIANGTHpkvsGHVITDIVEGKKVGTFFS 354
Cdd:cd04256 237 VGTGGMEAKVKAALWALQGGTSVVITNGMA----GDVITKILEGKKVGTFFT 284
proA PRK00197
gamma-glutamyl phosphate reductase; Provisional
362-772 2.06e-174

gamma-glutamyl phosphate reductase; Provisional


Pssm-ID: 234685  Cd Length: 417  Bit Score: 507.68  E-value: 2.06e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   362 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 440
Cdd:PRK00197   5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANgLSAAMLDRLLLTEARIEGIAEGL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   441 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:PRK00197  85 RQVAALP-DPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   521 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:PRK00197 164 QEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENAT-VPVIEHGDGICHIYVDESADLDKA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   598 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTF-SPSEVKSLRTEYGDLELCIE 676
Cdd:PRK00197 243 LKIVLNAKTQRPSVCNALETLLVHEAIAEEFL-PKLAEALAEAGVELRGDEAALALLPDvVPATEEDWDTEYLDLILAVK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   677 VVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEG 756
Cdd:PRK00197 322 VVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEE 401
                        410
                 ....*....|....*.
gi 6226882   757 LLTTKWLLRGKDHVVS 772
Cdd:PRK00197 402 LTTYKYIVLGDGQIRA 417
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
368-765 1.95e-172

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 502.14  E-value: 1.95e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  368 EMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASs 447
Cdd:cd07077   1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  448 qdsVGRVLRRTRIAkNLELEQVTVPIGVLLVIFESRPDCL-PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSI 526
Cdd:cd07077  80 ---VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLSgITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  527 HGVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDS 604
Cdd:cd07077 156 HGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  605 KCEYPAACNALETLLIHRDLLrTPLFDQIIDMLRVEQVKIHAGPKFASYLTFsPSEVKSLRTEYGDLELCIEVVDN---V 681
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVL-DPLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVisaV 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  682 QDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARG-PVGLEGLLTT 760
Cdd:cd07077 313 ENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPL 392

                ....*
gi 6226882  761 KWLLR 765
Cdd:cd07077 393 KRLVR 397
ProA COG0014
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ...
362-772 6.37e-172

Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 439785  Cd Length: 414  Bit Score: 501.46  E-value: 6.37e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  362 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 440
Cdd:COG0014   2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  441 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:COG0014  82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  521 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  598 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 672
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  673 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 752
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
                       410       420
                ....*....|....*....|
gi 6226882  753 GLEGLLTTKWLLRGKDHVVS 772
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
proA TIGR00407
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ...
370-761 9.03e-128

gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion protein delta l-pyrroline-5-carboxylate synthetase that includes a gamma-glutamyl phosphate reductase region as described by this model. Alternate name: glutamate-5-semialdehyde dehydrogenase. The prosite motif begins at residue 332 of the seed alignment although not all of the members of the family exactly obey the motif. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 161862  Cd Length: 398  Bit Score: 387.22  E-value: 9.03e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAaSSQ 448
Cdd:TIGR00407   1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENgLADALLDRLLLTEGRLKGIADGVKDVI-ELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    449 DSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHG 528
Cdd:TIGR00407  80 DPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    529 V-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 605
Cdd:TIGR00407 160 LpVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTST-IPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    606 CEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFSPSEV-----KSLRTEYGDLELCIEVVDN 680
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAIAREFL-PVLENQLLEKGVTIHADAYALKLLELGPATEaivckTDFDKEFLSLDLSVKIVES 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    681 VQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTT 760
Cdd:TIGR00407 318 LEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSY 397

                  .
gi 6226882    761 K 761
Cdd:TIGR00407 398 K 398
AAK_G5K_ProB cd04242
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ...
72-353 9.22e-101

AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.


Pssm-ID: 239775 [Multi-domain]  Cd Length: 251  Bit Score: 311.68  E-value: 9.22e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   72 RIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqalhsgqnqLKEM 151
Cdd:cd04242   1 RIVVKVGSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLG-------------------LEKR 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  152 AIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVppaep 231
Cdd:cd04242  61 PKTLPEKQALAAVGQSLLMALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVA----- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  232 nsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQ--QSVTFGTKSRVGMGGM 308
Cdd:cd04242 136 ------TEEIRFGDNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENpDAKLIPEVEEITDeiEAMAGGSGSSVGTGGM 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6226882  309 EAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 353
Cdd:cd04242 210 RTKLKAARIATEAGIPVVIANGRKP----DVLLDILAGEAVGTLF 250
ProB COG0263
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ...
64-353 2.43e-74

Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440033 [Multi-domain]  Cd Length: 371  Bit Score: 246.49  E-value: 2.43e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   64 RSELKHAKRIVVKLGSAVVTRGDEcGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRheillsqsvrqaLHS 143
Cdd:COG0263   1 REALAKARRIVVKIGSSLLTDEGG-GLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLG------------LPK 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  144 GQNQLKEmaipvleARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTND 223
Cdd:COG0263  68 RPKTLPE-------KQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINEND 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  224 AVVppaepnsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDI---FYPGDQQSVTfGT 299
Cdd:COG0263 141 TVA-----------TDEIRFGDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDpDAKLIPEveeITPEIEAMAG-GA 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6226882  300 KSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 353
Cdd:COG0263 209 GSGLGTGGMATKLEAARIATRAGIPTVIASGREP----NVLLRILAGERVGTLF 258
PRK12314 PRK12314
gamma-glutamyl kinase; Provisional
63-357 3.28e-66

gamma-glutamyl kinase; Provisional


Pssm-ID: 183430 [Multi-domain]  Cd Length: 266  Bit Score: 220.88  E-value: 3.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    63 HRSELKHAKRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLR-HEILLSQSVRQAL 141
Cdd:PRK12314   2 MRRQLENAKRIVIKVGSSTLS-YENGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKlDKRPTSLAEKQAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   142 hsgqnqlkemaipvlearacAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNT 221
Cdd:PRK12314  81 --------------------AAVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   222 NDAVVppaepnsdlqgVNVISVK--DNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQ--SVT 296
Cdd:PRK12314 141 NDAVA-----------TDEIDTKfgDNDRLSAIVAKLVKADLLIILSDIDGLYDKNPrINPDAKLRSEVTEITEEilALA 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6226882   297 FGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFFSEVK 357
Cdd:PRK12314 210 GGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP----SDILDFLEGESIGTLFAPKK 266
proB TIGR01027
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ...
71-353 3.06e-60

glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 162163 [Multi-domain]  Cd Length: 363  Bit Score: 207.93  E-value: 3.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     71 KRIVVKLGSAVVTrGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLrheillsqsvrqalhsGQNQL-K 149
Cdd:TIGR01027   1 QRIVVKVGSSSLT-GSSGSLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEAL----------------GLPERpK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    150 EMAipvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVvppa 229
Cdd:TIGR01027  64 TLA----EKQALAAVGQVRLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTV---- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    230 epnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD--QQSVTFGTKSRVGMG 306
Cdd:TIGR01027 136 -------ATEEIKFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNpDAKLIPVVEEITdlLLGVAGDSGSSVGTG 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 6226882    307 GMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGTFF 353
Cdd:TIGR01027 209 GMRTKLQAADLATRAGVPVIIASGSKPE----KIADALEGAPVGTLF 251
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
370-765 2.79e-59

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 205.54  E-value: 2.79e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEeaegrlaapllKRLSLSTSKLNSLAIGLRQIAASSQD 449
Cdd:cd06534   3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-----------KPIEEALGEVARAIDTFRYAAGLADK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  450 SVGrvLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCL--PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSih 527
Cdd:cd06534  72 LGG--PELPSPDPGGEAYVRREPLGVVGVITPWNFPLLlaAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGL-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  528 gVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHMYVDSEASVDKVTRLVRD 603
Cdd:cd06534 148 -PPGVVNVVPGGgdEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  604 SKCEY-PAACNALETLLIHRDLlrtplFDQIIDMLRveQVKIHAGPKFasyltfspsevKSLRTEYGDLELCIEVVDNVQ 682
Cdd:cd06534 226 GAFFNaGQICTAASRLLVHESI-----YDEFVEKLV--TVLVDVDPDM-----------PIAQEEIFGPVLPVIRFKDEE 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  683 DAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYR-FGlgaevGISTSRIHAR-GPVGLEGLLTT 760
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFG-----GVKNSGIGREgGPYGLEEYTRT 362

                ....*
gi 6226882  761 KWLLR 765
Cdd:cd06534 363 KTVVI 367
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
74-353 2.11e-50

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 177.25  E-value: 2.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   74 VVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLsqsvrqalhsgqNQLKEMAI 153
Cdd:cd02115   1 VIKFGGSSVSSEE-------RLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELL------------GYARGLRI 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  154 PVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHD------EQKRRNLNGTLHELLRMNIVPIVNTNDAVVP 227
Cdd:cd02115  62 TDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFASpnqghvGKITKVSTDRLKSLLENGILPILSGFGGTDE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  228 PaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGDQQSVTfgtksrvGMG 306
Cdd:cd02115 142 K--------ETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPrKVPDAKLLSELTYEEAAELA-------YAG 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 6226882  307 GMEAKVKAALWALQGGTSVVIANGTHPKVSghvitDIVEGKKVGTFF 353
Cdd:cd02115 207 AMVLKPKAADPAARAGIPVRIANTENPGAL-----ALFTPDGGGTLI 248
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
71-329 8.73e-38

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 140.96  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882     71 KRIVVKLGSAVVTRGDecglalgRLASIVEQVSVLQNQGREMMLVTSGavafGKQrLRHEILLSQSVRQALHSGQNQLKE 150
Cdd:pfam00696   1 KRVVIKLGGSSLTDKE-------RLKRLADEIAALLEEGRKLVVVHGG----GAF-ADGLLALLGLSPRFARLTDAETLE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    151 maipVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAE 230
Cdd:pfam00696  69 ----VATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPEGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    231 pnsdlqgvnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVtfgTKSRVGMGGME 309
Cdd:pfam00696 145 ----------LGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDELLEL---LASGLATGGMK 211
                         250       260
                  ....*....|....*....|.
gi 6226882    310 AKVKAALWALQ-GGTSVVIAN 329
Cdd:pfam00696 212 VKLPAALEAARrGGIPVVIVN 232
PTZ00489 PTZ00489
glutamate 5-kinase; Provisional
67-332 4.49e-23

glutamate 5-kinase; Provisional


Pssm-ID: 240438 [Multi-domain]  Cd Length: 264  Bit Score: 99.70  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    67 LKHAKRIVVKLGSAVVTRGDEcgLALGRLASIVEQVSVLQNQgREMMLVTSGAVAFGKQrlrheillsqsvrqalhsgQN 146
Cdd:PTZ00489   5 LKSVKRIVVKVGSSILVDNQE--IAAHRIEALCRFIADLQTK-YEVILVTSGAVAAGYT-------------------KK 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   147 QLKEMAIPvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVv 226
Cdd:PTZ00489  63 EMDKSYVP--NKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDAT- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   227 ppaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSPPGSDDAKLIDIFYPGDQQSVTFGT--KSRV 303
Cdd:PTZ00489 140 ----------ALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTDAKIRSVVHELSPDDLVAEAtpNNRF 209
                        250       260
                 ....*....|....*....|....*....
gi 6226882   304 GMGGMEAKVKAALWALQGGTSVVIANGTH 332
Cdd:PTZ00489 210 ATGGIVTKLQAAQFLLERGGKMYLSSGFH 238
AAK_FomA-like cd04241
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ...
72-351 3.72e-12

AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239774 [Multi-domain]  Cd Length: 252  Bit Score: 67.29  E-value: 3.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   72 RIVVKLGSAVVTRGDECGLA-LGRLASIVEQVSvlQNQGREMMLVtSGAVAFG----KQRLRHEILLSQS------VRQA 140
Cdd:cd04241   1 MIILKLGGSVITDKDRPETIrEENLERIARELA--EAIDEKLVLV-HGGGSFGhpkaKEYGLPDGDGSFSaegvaeTHEA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  141 LHSgqnqlkemaipvLEARACAAAGQSGLMAlyeamftqYSICAAQILVTNldfhdeqKRRNLNG---TLHELLRMNIVP 217
Cdd:cd04241  78 MLE------------LNSIVVDALLEAGVPA--------VSVPPSSFFVTE-------NGRIVSFdleVIKELLDRGFVP 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  218 IVNtNDAVVppaepnSDLQGVNVISvkdNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGsdDAKLIDIFYPGDQQSVTF 297
Cdd:cd04241 131 VLH-GDVVL------DEGGGITILS---GDDIVVELAKALKPERVIFLTDVDGVYDKPPP--DAKLIPEIDVGSLEDILA 198
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6226882  298 GTKSRVG--MGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGT 351
Cdd:cd04241 199 ALGSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPE----NLYRALLGNFIGT 250
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
207-351 3.41e-10

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 61.37  E-value: 3.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDI 286
Cdd:cd04238 131 LETLLEAGYIP-------VIAPIAVDEDGETYNV----NADTAAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISE 194
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226882  287 FYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgHVITDIVEGKK-VGT 351
Cdd:cd04238 195 LTPKEaEELIEDGVIS----GGMIPKVEAALEALEGGvRKVHIIDGRVP----HSLLLELFTDEgIGT 254
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
207-330 2.03e-09

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 59.14  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   207 LHELLRMNIVPIVNtndavvPPAEpnsDLQG--VNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLI 284
Cdd:PRK14058 142 LKLLLKAGYLPVVA------PPAL---SEEGepLNV----DGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGSLI 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6226882   285 DIFYPGDqqsvtFGTKSRVGMGGMEAKVKAALWALQGG-TSVVIANG 330
Cdd:PRK14058 207 ERITPEE-----AEELSKAAGGGMKKKVLMAAEAVEGGvGRVIIADA 248
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
207-330 9.47e-08

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 54.43  E-value: 9.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDI 286
Cdd:cd04250 151 LETLLEAGYIP-------VIAPVGVGEDGETYNI----NADTAAGAIAAALKAEKLILLTDVAGVLDDPN--DPGSLISE 217
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6226882  287 FYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGGT-SVVIANG 330
Cdd:cd04250 218 ISLKEaEELIADGIIS----GGMIPKVEACIEALEGGVkAAHIIDG 259
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
369-644 1.20e-07

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 54.91  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  369 MARSGGRMLAtlePEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRlslstsklns 435
Cdd:cd07078   9 AAFKAWAALP---PAERAAILRKLADLLEERREELaaLETleTGKPIEEALGevaraadtfRYYAGLARR---------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  436 laIGLRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPDCLP--QVAAlAIASGNGLLLKGGKEA 509
Cdd:cd07078  76 --LHGEVIPSPDPGELAIVRRE--------------PLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELT 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  510 AHSNRILHLLTQEALSIHGVkeaVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHM 586
Cdd:cd07078 136 PLTALLLAELLAEAGLPPGV---LNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPL 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6226882  587 YVDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:cd07078 213 IVFDDADLDAAVKGAVFGAFGNAGqVCTAASRLLVHES-----IYDEFVERLveRVKALKV 268
PRK00942 PRK00942
acetylglutamate kinase; Provisional
207-351 2.07e-07

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 53.19  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkdN-DSLAARLAVEMKTDLLIVLSDVEGLFDSpPGS------- 278
Cdd:PRK00942 155 LEALLEAGYIP-------VISPIGVGEDGETYNI-----NaDTAAGAIAAALGAEKLILLTDVPGVLDD-KGQliselta 221
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6226882   279 DDA-KLIdifypgDQQSVTfgtksrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgH-VITDIVEGKKVGT 351
Cdd:PRK00942 222 SEAeELI------EDGVIT---------GGMIPKVEAALDAARGGvRSVHIIDGRVP----HaLLLELFTDEGIGT 278
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
363-644 1.11e-06

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 52.05  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  363 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 429
Cdd:cd07094  23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEfakiIACEGGKPIKDARVevdraidtlRLAAEEAERIRGE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  430 TSKLNSLAIGLRQIAASSQDSVGRVLRRTriAKNLELEQVTVPIGvllvifesrPdclpqvaalAIASGNGLLLKGGKEA 509
Cdd:cd07094 103 EIPLDATQGSDNRLAWTIREPVGVVLAIT--PFNFPLNLVAHKLA---------P---------AIATGCPVVLKPASKT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  510 AHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMY 587
Cdd:cd07094 163 PLSALELAKILVEA----GVpEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVI 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  588 VDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE-----LYDEFIEAFvaAVKKLKV 293
PRK12354 PRK12354
carbamate kinase; Reviewed
230-359 1.33e-06

carbamate kinase; Reviewed


Pssm-ID: 183466  Cd Length: 307  Bit Score: 50.99  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   230 EPNSDLQGVN-VIsvkDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSppGSDDAKLIDIFYPGDQQSVTFGTksrvgmGG 307
Cdd:PRK12354 191 DADGKLHGVEaVI---DKDLAAALLAEQLDADLLLILTDVDAVYlDW--GKPTQRAIAQATPDELRELGFAA------GS 259
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6226882   308 MEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGTFFSEVKPA 359
Cdd:PRK12354 260 MGPKVEAACeFVRATGKIAGIG-------SLEDIQAILAGEA-GTRISPETAG 304
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
225-334 2.41e-06

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 49.67  E-value: 2.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  225 VVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFdsppgsDDAKLIDIFYPGDQQSVtfgtKSRVG 304
Cdd:cd04251 149 VVSPVAYSEEGEPLNV----DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERITVSDAESL----LEKAG 214
                        90       100       110
                ....*....|....*....|....*....|.
gi 6226882  305 mGGMEAKVKAALWALQGGTS-VVIANGTHPK 334
Cdd:cd04251 215 -GGMKRKLLAAAEAVEGGVReVVIGDARADS 244
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
378-762 2.62e-06

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 50.61  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    378 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSlstsklnslaiGlrQIA 444
Cdd:pfam00171  46 RKTPAAERAAILRKAADLLEERKDELaeLETleNGKPLAEARGevdraidvlRYYAGLARRLD-----------G--ETL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    445 ASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI--FESrPDCLP--QVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:pfam00171 113 PSDPGRLAYTRRE--------------PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPLTALLLAELF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    521 QEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHSegicHMYVDSE 591
Cdd:pfam00171 177 EEA----GLpAGVLNVVTGsgAEVGEALVE-HPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTlelgGKN----PLIVLED 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    592 ASVDKVTRLVRDSKCEYP-AACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI--------HAGP--------KFAS 652
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES-----IYDEFVEKLveAAKKLKVgdpldpdtDMGPliskaqleRVLK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882    653 Y-----------------------------LTFSPSEVKSLRTE-YGDLeLCIEVVDNVQDAIDHIH--KYGssHTDVIV 700
Cdd:pfam00171 323 YvedakeegaklltggeagldngyfveptvLANVTPDMRIAQEEiFGPV-LSVIRFKDEEEAIEIANdtEYG--LAAGVF 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6226882    701 TEDENTAEFFLQHVDSACVFWNASTRFS-DGYRFGlgaevGISTSRI-HARGPVGLEGLLTTKW 762
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFG-----GFKQSGFgREGGPYGLEEYTEVKT 458
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
370-644 5.77e-06

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 49.74  E-value: 5.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  370 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLA----NKKDLEEAEG---------RLAAPLLKRLSlstsklnsl 436
Cdd:COG1012  52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAALltleTGKPLAEARGevdraadflRYYAGEARRLY--------- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  437 aiGlRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPdcLPQVA---ALAIASGNGLLLKGGKEA 509
Cdd:COG1012 123 --G-ETIPSDAPGTRAYVRRE--------------PLGVVGAItpwnF---P--LALAAwklAPALAAGNTVVLKPAEQT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  510 AHSNRILHLLTQEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHS 580
Cdd:COG1012 181 PLSALLLAELLEEA----GLpAGVLNVVTGdgSEVGAALVA-HPDVDKISFTGSTAVGRRIAAAAaeNLKRVTlelgGKN 255
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226882  581 egicHMYVDSEASVDKVTRLVRDSKCEYpA--ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 644
Cdd:COG1012 256 ----PAIVLDDADLDAAVEAAVRGAFGN-AgqRCTAASRLLVHES-----IYDEFVERLvaAAKALKV 313
PRK12454 PRK12454
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
226-351 9.29e-06

carbamate kinase-like carbamoyl phosphate synthetase; Reviewed


Pssm-ID: 183535  Cd Length: 313  Bit Score: 48.46  E-value: 9.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   226 VPPAEPNSDLQGVNviSVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSpPGSDDAKLIDIFYPgdQQSVTFGTKSRVGM 305
Cdd:PRK12454 196 IPVIEEDGELKGVE--AVIDKDLASELLAEELNADIFIILTDVEKVYLN-YGKPDQKPLDKVTV--EEAKKYYEEGHFKA 270
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 6226882   306 GGMEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGkKVGT 351
Cdd:PRK12454 271 GSMGPKILAAIrFVENGGKRAIIA-------SLEKAVEALEG-KTGT 309
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
207-333 1.39e-05

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 47.72  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  207 LHELLRMNIVPivntndaVVPPAEPNSDLQGVNVisvkdN-DSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLID 285
Cdd:COG0548 157 IRALLDAGYIP-------VISPIGYSPTGEVYNI-----NaDTVAGAIAAALKAEKLILLTDVPGVLD-----DPGSLIS 219
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6226882  286 IFYPGDQQSVTfgtKSRVGMGGMEAKVKAALWALQGGT-SVVIANGTHP 333
Cdd:COG0548 220 ELTAAEAEELI---ADGVISGGMIPKLEAALDAVRGGVkRVHIIDGRVP 265
AAK_NAGK-NC cd04249
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ...
207-351 5.13e-05

AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239782 [Multi-domain]  Cd Length: 252  Bit Score: 45.48  E-value: 5.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  207 LHELLRMNIVPIVNTNDAvvppaepnsDLQG--VNVisvkDNDSLAARLAVEMKTDLlIVLSDVEGLFDSppgsdDAKLI 284
Cdd:cd04249 129 LNDLLKAGFLPIISSIGA---------DDQGqlMNV----NADQAATAIAQLLNADL-VLLSDVSGVLDA-----DKQLI 189
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226882  285 DIFypgDQQSVTFGTKSRVGMGGMEAKVKAALWALQG-GTSVVIANGTHPKvsghVITDIVEGKKVGT 351
Cdd:cd04249 190 SEL---NAKQAAELIEQGVITDGMIVKVNAALDAAQSlRRGIDIASWQYPE----QLTALLAGEPVGT 250
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
378-578 5.18e-04

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 43.33  E-value: 5.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  378 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSLSTSKLNslaiglrqIA 444
Cdd:cd07082  56 PTMPLEERIDCLHKFADLLKENKEEVanLLMweIGKTLKDALKevdrtidyiRDTIEELKRLDGDSLPGD--------WF 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  445 ASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI-------FESrpdclpqVAALAIA--SGNGLLLKGGKEAAhsnrI 515
Cdd:cd07082 128 PGTKGKIAQVRR--------------EPLGVVLAIgpfnyplNLT-------VSKLIPAliMGNTVVFKPATQGV----L 182
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6226882  516 LHLLTQEALSIHGV-KEAVQLVNTR-EEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP-VMG 578
Cdd:cd07082 183 LGIPLAEAFHDAGFpKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRlVLE 248
AAK_UMPK-PyrH-Pf cd04253
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ...
247-352 5.93e-04

AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239786 [Multi-domain]  Cd Length: 221  Bit Score: 42.24  E-value: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  247 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVTFGTKSRVGmggmeAKVKAALWALQ----G 321
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAG-----SNEPFDPLAAKiierS 192
                        90       100       110
                ....*....|....*....|....*....|.
gi 6226882  322 GTSVVIANGTHPKvsghVITDIVEGKKVGTF 352
Cdd:cd04253 193 GIKTIVVDGRDPE----NLERALKGEFVGTI 219
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
363-571 9.43e-04

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 42.58  E-value: 9.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  363 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 429
Cdd:cd07149  23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEfartIALEAGKPIKDARKevdraietlRLSAEEAKRLAGE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  430 TSKLNSlaiglrqiAASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI--FEsrpDCLPQVA---ALAIASGNGLLLK 504
Cdd:cd07149 103 TIPFDA--------SPGGEGRIGFTIR--------------EPIGVVAAItpFN---FPLNLVAhkvGPAIAAGNAVVLK 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  505 GGKEAAHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVED-LCRlDKMIDLIIPRGSSQLVRDIQKAA 571
Cdd:cd07149 158 PASQTPLSALKLAELLLEA----GLpKGALNVVTgSGETVGDaLVT-DPRVRMISFTGSPAVGEAIARKA 222
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
350-643 1.22e-03

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 42.23  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  350 GTFFSEVKPAGP-TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEGRLAapllk 424
Cdd:cd07147   9 GEVVARVALAGPdDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEElaetIVLEAGKPIKDARGEVA----- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  425 RlslstsklnslAIGLRQIAA-SSQDSVGRVLRRTRIAKNLELEQVT--VPIGVLLVIfesRPDCLP--QVA---ALAIA 496
Cdd:cd07147  84 R-----------AIDTFRIAAeEATRIYGEVLPLDISARGEGRQGLVrrFPIGPVSAI---TPFNFPlnLVAhkvAPAIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882  497 SGNGLLLKggkeAAHSNRILHLLTQEALSIHGV-KEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP 575
Cdd:cd07147 150 AGCPFVLK----PASRTPLSALILGEVLAETGLpKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKK 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6226882  576 VMGHSEGICHMYVDSEASVDK-VTRLVRDSKCEYPAACNALETLLIHRDllrtpLFDQIIDMLrVEQVK 643
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFaAQRIIFGAFYQAGQSCISVQRVLVHRS-----VYDEFKSRL-VARVK 288
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
378-650 1.77e-03

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 41.55  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   378 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLeeaegrlaapllkRLSLSTSKLNSLAIGLRQIAASSQDsvgrvlrr 457
Cdd:PTZ00381  24 KTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDL-------------GRHPFETKMTEVLLTVAEIEHLLKH-------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   458 trIAKNLELEQVTV--------------PIGVLLVIFE-SRP--DCLPQVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 520
Cdd:PTZ00381  83 --LDEYLKPEKVDTvgvfgpgksyiipePLGVVLVIGAwNYPlnLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226882   521 QEALSihgvKEAVQLVNT-REEVEDLCRLDkmIDLIIPRGSSQLVRDIQKAA--KGIPVMGHSEGICHMYVDSEASVDKV 597
Cdd:PTZ00381 160 TKYLD----PSYVRVIEGgVEVTTELLKEP--FDHIFFTGSPRVGKLVMQAAaeNLTPCTLELGGKSPVIVDKSCNLKVA 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6226882   598 TRLVRDSKC-EYPAACNALETLLIHRDLLrtplfDQIIDMLRvEQVKIHAGPKF 650
Cdd:PTZ00381 234 ARRIAWGKFlNAGQTCVAPDYVLVHRSIK-----DKFIEALK-EAIKEFFGEDP 281
 
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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