|
Name |
Accession |
Description |
Interval |
E-value |
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
1-582 |
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: 1005.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQ 80
Cdd:TIGR01092 140 MNVVPVVNENDAVSTRAAPYSDSQGI----FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKH 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 81 Q-SVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFSEVKPAGPTVEQQGE--- 156
Cdd:TIGR01092 216 QgEITFGTKSRLGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTLFHEDAHLWPTVEQTGErdm 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 157 --MARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAA 233
Cdd:TIGR01092 292 avAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARLSMSPSKISSLAISLRQLAA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 234 SsQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALS 313
Cdd:TIGR01092 372 M-EDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIP 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 314 IHGVKEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 393
Cdd:TIGR01092 451 IHVGKKLIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHVYVDKSASVDMAKRIVRDAK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 394 CEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAI 473
Cdd:TIGR01092 530 CDYPAACNAMETLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAI 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 474 DHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLR 553
Cdd:TIGR01092 610 DHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLR 689
|
570 580
....*....|....*....|....*....
gi 1020738643 554 GKDHVVSdfSEHGsLKYLHENLPIPQRNT 582
Cdd:TIGR01092 690 GKGQVVS--GDHG-LVYTHKDLPIPQRNT 715
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
1-577 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 667.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVPPAEPNSDLQGVnvisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYP-GD 79
Cdd:PLN02418 148 LRVIPIFNENDAVSTRRAPYEDSSGI----FWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKeKH 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 80 QQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFFseVKPAG---PTVEQQG- 155
Cdd:PLN02418 224 QDEITFGEKSRVGRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF--HQDAHlwaPSKEVGAr 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 156 EMA---RSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKRLSLSTSKLNSLAIGLRQI 231
Cdd:PLN02418 298 EMAvaaRESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSRLTLKPGKIASLAASIRQL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 232 AASsQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEA 311
Cdd:PLN02418 378 ADM-EDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDA 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 312 LSIHGVKEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRD 391
Cdd:PLN02418 457 IPKTVGGKLIGLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICHVYVDKSADMDMAKRIVVD 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 392 SKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLRTEYGDLELCIEVVDNVQD 471
Cdd:PLN02418 536 AKTDYPAACNAMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFHHEYSSLACTVEIVDDVHA 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 472 AIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWL 551
Cdd:PLN02418 614 AIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWI 693
|
570 580
....*....|....*....|....*.
gi 1020738643 552 LRGKDHVVSdfSEHGSLkYLHENLPI 577
Cdd:PLN02418 694 LRGNGQVVD--GDKGVV-YTHKDLPL 716
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
152-554 |
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: 592.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 152 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 230
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 231 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 310
Cdd:cd07079 81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 311 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 387
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 388 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 466
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 467 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 546
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397
|
....*...
gi 1020738643 547 TTKWLLRG 554
Cdd:cd07079 398 TYKYIVRG 405
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
150-560 |
3.34e-176 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 504.60 E-value: 3.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 150 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 228
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANgLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 229 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 308
Cdd:PRK00197 85 RQVAALP-DPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 309 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 385
Cdd:PRK00197 164 QEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENAT-VPVIEHGDGICHIYVDESADLDKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 386 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTF-SPSEVKSLRTEYGDLELCIE 464
Cdd:PRK00197 243 LKIVLNAKTQRPSVCNALETLLVHEAIAEEFL-PKLAEALAEAGVELRGDEAALALLPDvVPATEEDWDTEYLDLILAVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 465 VVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEG 544
Cdd:PRK00197 322 VVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEE 401
|
410
....*....|....*.
gi 1020738643 545 LLTTKWLLRGKDHVVS 560
Cdd:PRK00197 402 LTTYKYIVLGDGQIRA 417
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
156-553 |
3.42e-174 |
|
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: 499.06 E-value: 3.42e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 156 EMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASs 235
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 236 qdsVGRVLRRTRIAkNLELEQVTVPIGVLLVIFESRPDCL-PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSI 314
Cdd:cd07077 80 ---VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLSgITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 315 HGVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDS 392
Cdd:cd07077 156 HGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 393 KCEYPAACNALETLLIHRDLLrTPLFDQIIDMLRVEQVKIHAGPKFASYLTFsPSEVKSLRTEYGDLELCIEVVDN---V 469
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVL-DPLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVisaV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 470 QDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARG-PVGLEGLLTT 548
Cdd:cd07077 313 ENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPL 392
|
....*
gi 1020738643 549 KWLLR 553
Cdd:cd07077 393 KRLVR 397
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
150-560 |
5.80e-174 |
|
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: 498.76 E-value: 5.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 150 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 228
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 229 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 308
Cdd:COG0014 82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 309 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 385
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 386 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 460
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 461 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 540
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
|
410 420
....*....|....*....|
gi 1020738643 541 GLEGLLTTKWLLRGKDHVVS 560
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
158-549 |
6.24e-129 |
|
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: 383.37 E-value: 6.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 158 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAaSSQ 236
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENgLADALLDRLLLTEGRLKGIADGVKDVI-ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 237 DSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHG 316
Cdd:TIGR00407 80 DPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 317 V-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 393
Cdd:TIGR00407 160 LpVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTST-IPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 394 CEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFSPSEV-----KSLRTEYGDLELCIEVVDN 468
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAIAREFL-PVLENQLLEKGVTIHADAYALKLLELGPATEaivckTDFDKEFLSLDLSVKIVES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 469 VQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTT 548
Cdd:TIGR00407 318 LEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSY 397
|
.
gi 1020738643 549 K 549
Cdd:TIGR00407 398 K 398
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
1-142 |
4.43e-81 |
|
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: 256.21 E-value: 4.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVPPAEPNSDLQGVnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQ 80
Cdd:cd04256 149 LNIIPIINTNDAVSPPPEPDEDLQGV--ISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYPGDQ 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1020738643 81 QSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHpkvsGHVITDIVEGKKVGTFFS 142
Cdd:cd04256 227 QSITFGTKSRVGTGGMEAKVKAALWALQGGTSVVITNGMA----GDVITKILEGKKVGTFFT 284
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
158-553 |
2.64e-60 |
|
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: 204.39 E-value: 2.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 158 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEeaegrlaapllKRLSLSTSKLNSLAIGLRQIAASSQD 237
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-----------KPIEEALGEVARAIDTFRYAAGLADK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 238 SVGrvLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCL--PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSih 315
Cdd:cd06534 72 LGG--PELPSPDPGGEAYVRREPLGVVGVITPWNFPLLlaAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 316 gVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHMYVDSEASVDKVTRLVRD 391
Cdd:cd06534 148 -PPGVVNVVPGGgdEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 392 SKCEY-PAACNALETLLIHRDLlrtplFDQIIDMLRveQVKIHAGPKFasyltfspsevKSLRTEYGDLELCIEVVDNVQ 470
Cdd:cd06534 226 GAFFNaGQICTAASRLLVHESI-----YDEFVEKLV--TVLVDVDPDM-----------PIAQEEIFGPVLPVIRFKDEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 471 DAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYR-FGlgaevGISTSRIHAR-GPVGLEGLLTT 548
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFG-----GVKNSGIGREgGPYGLEEYTRT 362
|
....*
gi 1020738643 549 KWLLR 553
Cdd:cd06534 363 KTVVI 367
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
1-141 |
2.27e-43 |
|
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: 155.29 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVppaepnsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD 79
Cdd:cd04242 122 LGVIPIINENDTVA-----------TEEIRFGDNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENpDAKLIPEVEEIT 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738643 80 Q--QSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 141
Cdd:cd04242 191 DeiEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKP----DVLLDILAGEAVGTLF 250
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
1-141 |
5.81e-30 |
|
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: 121.30 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVppaepnsdlqgVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDI---FY 76
Cdd:COG0263 130 LGVVPIINENDTVA-----------TDEIRFGDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDpDAKLIPEveeIT 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1020738643 77 PGDQQSVTfGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFF 141
Cdd:COG0263 199 PEIEAMAG-GAGSGLGTGGMATKLEAARIATRAGIPTVIASGREP----NVLLRILAGERVGTLF 258
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
1-145 |
5.88e-28 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 113.03 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVppaepnsdlqgVNVISVK--DNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYP 77
Cdd:PRK12314 132 LGILPIVNENDAVA-----------TDEIDTKfgDNDRLSAIVAKLVKADLLIILSDIDGLYDKNPrINPDAKLRSEVTE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 78 GDQQ--SVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGTFFSEVK 145
Cdd:PRK12314 201 ITEEilALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP----SDILDFLEGESIGTLFAPKK 266
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
1-141 |
3.13e-24 |
|
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: 104.31 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVvppaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD 79
Cdd:TIGR01027 123 LGVVPIINENDTV-----------ATEEIKFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNpDAKLIPVVEEIT 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738643 80 --QQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGTFF 141
Cdd:TIGR01027 192 dlLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPE----KIADALEGAPVGTLF 251
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
1-141 |
1.76e-23 |
|
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: 99.82 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVPPaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPP-GSDDAKLIDIFYPGD 79
Cdd:cd02115 127 NGILPILSGFGGTDEK--------ETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPrKVPDAKLLSELTYEE 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1020738643 80 QQSVTfgtksrvGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSghvitDIVEGKKVGTFF 141
Cdd:cd02115 199 AAELA-------YAGAMVLKPKAADPAARAGIPVRIANTENPGAL-----ALFTPDGGGTLI 248
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
1-117 |
2.73e-13 |
|
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: 69.70 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 1 MNIVPIVNTNDAVVPPAEpnsdlqgvnvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGD 79
Cdd:pfam00696 127 AGVVPVITGFIGIDPEGE----------LGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDE 196
|
90 100 110
....*....|....*....|....*....|....*....
gi 1020738643 80 QQSVtfgTKSRVGMGGMEAKVKAALWALQ-GGTSVVIAN 117
Cdd:pfam00696 197 LLEL---LASGLATGGMKVKLPAALEAARrGGIPVVIVN 232
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
26-118 |
6.02e-09 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 57.22 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 26 VNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIFYPGDqqsvtFGTKSRVGMGGMEAKVKAALW 105
Cdd:PRK14058 166 LNV----DGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGSLIERITPEE-----AEELSKAAGGGMKKKVLMAAE 234
|
90
....*....|....
gi 1020738643 106 ALQGG-TSVVIANG 118
Cdd:PRK14058 235 AVEGGvGRVIIADA 248
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
3-139 |
8.90e-09 |
|
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: 56.50 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 3 IVPIVNtNDAVVppaepnSDLQGVNVISvkdNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGsdDAKLIDIFYPGDQQS 82
Cdd:cd04241 128 FVPVLH-GDVVL------DEGGGITILS---GDDIVVELAKALKPERVIFLTDVDGVYDKPPP--DAKLIPEIDVGSLED 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1020738643 83 VTFGTKSRVG--MGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGT 139
Cdd:cd04241 196 ILAALGSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPE----NLYRALLGNFIGT 250
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
13-139 |
1.08e-08 |
|
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: 56.36 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 13 VVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFYPGD-QQSVTFGTKSrv 91
Cdd:cd04238 142 VIAPIAVDEDGETYNV----NADTAAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELTPKEaEELIEDGVIS-- 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1020738643 92 gmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgHVITDIVEGKK-VGT 139
Cdd:cd04238 211 --GGMIPKVEAALEALEGGvRKVHIIDGRVP----HSLLLELFTDEgIGT 254
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
157-432 |
1.24e-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: 54.14 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 157 MARSGGRMLAtlePEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRlslstsklns 223
Cdd:cd07078 9 AAFKAWAALP---PAERAAILRKLADLLEERREELaaLETleTGKPIEEALGevaraadtfRYYAGLARR---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 224 laIGLRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPDCLP--QVAAlAIASGNGLLLKGGKEA 297
Cdd:cd07078 76 --LHGEVIPSPDPGELAIVRRE--------------PLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 298 AHSNRILHLLTQEALSIHGVkeaVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHM 374
Cdd:cd07078 136 PLTALLLAELLAEAGLPPGV---LNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020738643 375 YVDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 432
Cdd:cd07078 213 IVFDDADLDAAVKGAVFGAFGNAGqVCTAASRLLVHES-----IYDEFVERLveRVKALKV 268
|
|
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
3-120 |
3.16e-07 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 51.94 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 3 IVPIVNTNDAVvppaepnsdlqGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSPPGSDDAKLIDIFYPGDQQ 81
Cdd:PTZ00489 129 VIPIINENDAT-----------ALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTDAKIRSVVHELSPD 197
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1020738643 82 SVTFGT--KSRVGMGGMEAKVKAALWALQGGTSVVIANGTH 120
Cdd:PTZ00489 198 DLVAEAtpNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFH 238
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
13-118 |
9.05e-07 |
|
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: 50.58 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 13 VVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIFYPGD-QQSVTFGTKSrv 91
Cdd:cd04250 162 VIAPVGVGEDGETYNI----NADTAAGAIAAALKAEKLILLTDVAGVLDDPN--DPGSLISEISLKEaEELIADGIIS-- 233
|
90 100
....*....|....*....|....*...
gi 1020738643 92 gmGGMEAKVKAALWALQGGT-SVVIANG 118
Cdd:cd04250 234 --GGMIPKVEACIEALEGGVkAAHIIDG 259
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
18-147 |
1.28e-06 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 50.60 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 18 EPNSDLQGVN-VIsvkDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSppGSDDAKLIDIFYPGDQQSVTFGTksrvgmGG 95
Cdd:PRK12354 191 DADGKLHGVEaVI---DKDLAAALLAEQLDADLLLILTDVDAVYlDW--GKPTQRAIAQATPDELRELGFAA------GS 259
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1020738643 96 MEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGTFFSEVKPA 147
Cdd:PRK12354 260 MGPKVEAACeFVRATGKIAGIG-------SLEDIQAILAGEA-GTRISPETAG 304
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
151-432 |
1.94e-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: 50.51 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 151 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 217
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEfakiIACEGGKPIKDARVevdraidtlRLAAEEAERIRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 218 TSKLNSLAIGLRQIAASSQDSVGRVLRRTriAKNLELEQVTVPIGvllvifesrPdclpqvaalAIASGNGLLLKGGKEA 297
Cdd:cd07094 103 EIPLDATQGSDNRLAWTIREPVGVVLAIT--PFNFPLNLVAHKLA---------P---------AIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 298 AHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMY 375
Cdd:cd07094 163 PLSALELAKILVEA----GVpEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 376 VDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 432
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE-----LYDEFIEAFvaAVKKLKV 293
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
13-122 |
4.37e-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: 48.52 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 13 VVPPAEPNSDLQGVNVisvkDNDSLAARLAVEMKTDLLIVLSDVEGLFdsppgsDDAKLIDIFYPGDQQSVtfgtKSRVG 92
Cdd:cd04251 149 VVSPVAYSEEGEPLNV----DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERITVSDAESL----LEKAG 214
|
90 100 110
....*....|....*....|....*....|.
gi 1020738643 93 mGGMEAKVKAALWALQGGTS-VVIANGTHPK 122
Cdd:cd04251 215 -GGMKRKLLAAAEAVEGGVReVVIGDARADS 244
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
35-139 |
5.28e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 48.57 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 35 DSLAARLAVEMKTDLLIVLSDVEGLFDSpPGS-------DDA-KLIdifypgDQQSVTfgtksrvgmGGMEAKVKAALWA 106
Cdd:PRK00942 184 DTAAGAIAAALGAEKLILLTDVPGVLDD-KGQliseltaSEAeELI------EDGVIT---------GGMIPKVEAALDA 247
|
90 100 110
....*....|....*....|....*....|....*
gi 1020738643 107 LQGG-TSVVIANGTHPkvsgH-VITDIVEGKKVGT 139
Cdd:PRK00942 248 ARGGvRSVHIIDGRVP----HaLLLELFTDEGIGT 278
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
166-550 |
5.91e-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: 49.07 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 166 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSlstsklnslaiGlrQIA 232
Cdd:pfam00171 46 RKTPAAERAAILRKAADLLEERKDELaeLETleNGKPLAEARGevdraidvlRYYAGLARRLD-----------G--ETL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 233 ASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI--FESrPDCLP--QVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 308
Cdd:pfam00171 113 PSDPGRLAYTRRE--------------PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPLTALLLAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 309 QEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHSegicHMYVDSE 379
Cdd:pfam00171 177 EEA----GLpAGVLNVVTGsgAEVGEALVE-HPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTlelgGKN----PLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 380 ASVDKVTRLVRDSKCEYP-AACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI--------HAGP--------KFAS 440
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES-----IYDEFVEKLveAAKKLKVgdpldpdtDMGPliskaqleRVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 441 Y-----------------------------LTFSPSEVKSLRTE-YGDLeLCIEVVDNVQDAIDHIH--KYGssHTDVIV 488
Cdd:pfam00171 323 YvedakeegaklltggeagldngyfveptvLANVTPDMRIAQEEiFGPV-LSVIRFKDEEEAIEIANdtEYG--LAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738643 489 TEDENTAEFFLQHVDSACVFWNASTRFS-DGYRFGlgaevGISTSRI-HARGPVGLEGLLTTKW 550
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFG-----GFKQSGFgREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
158-432 |
7.61e-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: 48.58 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 158 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLA----NKKDLEEAEG---------RLAAPLLKRLSlstsklnsl 224
Cdd:COG1012 52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAALltleTGKPLAEARGevdraadflRYYAGEARRLY--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 225 aiGlRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPdcLPQVA---ALAIASGNGLLLKGGKEA 297
Cdd:COG1012 123 --G-ETIPSDAPGTRAYVRRE--------------PLGVVGAItpwnF---P--LALAAwklAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 298 AHSNRILHLLTQEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHS 368
Cdd:COG1012 181 PLSALLLAELLEEA----GLpAGVLNVVTGdgSEVGAALVA-HPDVDKISFTGSTAVGRRIAAAAaeNLKRVTlelgGKN 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738643 369 egicHMYVDSEASVDKVTRLVRDSKCEYpA--ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 432
Cdd:COG1012 256 ----PAIVLDDADLDAAVEAAVRGAFGN-AgqRCTAASRLLVHES-----IYDEFVERLvaAAKALKV 313
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
14-139 |
1.31e-05 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 47.30 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 14 VPPAEPNSDLQGVNviSVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSpPGSDDAKLIDIFYPgdQQSVTFGTKSRVGM 93
Cdd:PRK12454 196 IPVIEEDGELKGVE--AVIDKDLASELLAEELNADIFIILTDVEKVYLN-YGKPDQKPLDKVTV--EEAKKYYEEGHFKA 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1020738643 94 GGMEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGkKVGT 139
Cdd:PRK12454 271 GSMGPKILAAIrFVENGGKRAIIA-------SLEKAVEALEG-KTGT 309
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
35-121 |
3.57e-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: 45.79 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 35 DSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFYPGDQQSVTfgtKSRVGMGGMEAKVKAALWALQGGT-SV 113
Cdd:COG0548 186 DTVAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELTAAEAEELI---ADGVISGGMIPKLEAALDAVRGGVkRV 257
|
....*...
gi 1020738643 114 VIANGTHP 121
Cdd:COG0548 258 HIIDGRVP 265
|
|
| AAK_NAGK-NC |
cd04249 |
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
22-139 |
5.73e-04 |
|
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: 42.02 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 22 DLQG--VNVisvkDNDSLAARLAVEMKTDLlIVLSDVEGLFDSppgsdDAKLIDIFypgDQQSVTFGTKSRVGMGGMEAK 99
Cdd:cd04249 147 DDQGqlMNV----NADQAATAIAQLLNADL-VLLSDVSGVLDA-----DKQLISEL---NAKQAAELIEQGVITDGMIVK 213
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1020738643 100 VKAALWALQG-GTSVVIANGTHPKvsghVITDIVEGKKVGT 139
Cdd:cd04249 214 VNAALDAAQSlRRGIDIASWQYPE----QLTALLAGEPVGT 250
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
166-366 |
8.82e-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: 42.17 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 166 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSLSTSKLNslaiglrqIA 232
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVanLLMweIGKTLKDALKevdrtidyiRDTIEELKRLDGDSLPGD--------WF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 233 ASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI-------FESrpdclpqVAALAIA--SGNGLLLKGGKEAAhsnrI 303
Cdd:cd07082 128 PGTKGKIAQVRR--------------EPLGVVLAIgpfnyplNLT-------VSKLIPAliMGNTVVFKPATQGV----L 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738643 304 LHLLTQEALSIHGV-KEAVQLVNTR-EEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP-VMG 366
Cdd:cd07082 183 LGIPLAEAFHDAGFpKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRlVLE 248
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
35-140 |
8.94e-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: 41.08 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 35 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVTFGTKSRVGmggmeAKVKAALWALQ----G 109
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAG-----SNEPFDPLAAKiierS 192
|
90 100 110
....*....|....*....|....*....|.
gi 1020738643 110 GTSVVIANGTHPKvsghVITDIVEGKKVGTF 140
Cdd:cd04253 193 GIKTIVVDGRDPE----NLERALKGEFVGTI 219
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
166-438 |
1.19e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 41.55 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 166 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLeeaegrlaapllkRLSLSTSKLNSLAIGLRQIAASSQDsvgrvlrr 245
Cdd:PTZ00381 24 KTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDL-------------GRHPFETKMTEVLLTVAEIEHLLKH-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 246 trIAKNLELEQVTV--------------PIGVLLVIFE-SRP--DCLPQVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 308
Cdd:PTZ00381 83 --LDEYLKPEKVDTvgvfgpgksyiipePLGVVLVIGAwNYPlnLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 309 QEALSihgvKEAVQLVNT-REEVEDLCRLDkmIDLIIPRGSSQLVRDIQKAA--KGIPVMGHSEGICHMYVDSEASVDKV 385
Cdd:PTZ00381 160 TKYLD----PSYVRVIEGgVEVTTELLKEP--FDHIFFTGSPRVGKLVMQAAaeNLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738643 386 TRLVRDSKC-EYPAACNALETLLIHRDLLrtplfDQIIDMLRvEQVKIHAGPKF 438
Cdd:PTZ00381 234 ARRIAWGKFlNAGQTCVAPDYVLVHRSIK-----DKFIEALK-EAIKEFFGEDP 281
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
151-359 |
1.24e-03 |
|
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: 41.43 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 151 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 217
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEfartIALEAGKPIKDARKevdraietlRLSAEEAKRLAGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 218 TSKLNSlaiglrqiAASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI--FEsrpDCLPQVA---ALAIASGNGLLLK 292
Cdd:cd07149 103 TIPFDA--------SPGGEGRIGFTIR--------------EPIGVVAAItpFN---FPLNLVAhkvGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 293 GGKEAAHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVED-LCRlDKMIDLIIPRGSSQLVRDIQKAA 359
Cdd:cd07149 158 PASQTPLSALKLAELLLEA----GLpKGALNVVTgSGETVGDaLVT-DPRVRMISFTGSPAVGEAIARKA 222
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
138-431 |
1.68e-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: 41.08 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 138 GTFFSEVKPAGP-TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEGRLAApllk 212
Cdd:cd07147 9 GEVVARVALAGPdDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEElaetIVLEAGKPIKDARGEVAR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 213 rlslstsklnslAIGLRQIAA-SSQDSVGRVLRRTRIAKNLELEQVT--VPIGVLLVIfesRPDCLP--QVA---ALAIA 284
Cdd:cd07147 85 ------------AIDTFRIAAeEATRIYGEVLPLDISARGEGRQGLVrrFPIGPVSAI---TPFNFPlnLVAhkvAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738643 285 SGNGLLLKggkeAAHSNRILHLLTQEALSIHGV-KEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP 363
Cdd:cd07147 150 AGCPFVLK----PASRTPLSALILGEVLAETGLpKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020738643 364 VMGHSEGICHMYVDSEASVDK-VTRLVRDSKCEYPAACNALETLLIHRDllrtpLFDQIIDMLrVEQVK 431
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFaAQRIIFGAFYQAGQSCISVQRVLVHRS-----VYDEFKSRL-VARVK 288
|
|
| |
