|
Name |
Accession |
Description |
Interval |
E-value |
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
1-681 |
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: 1165.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 1 MMLVTSGAVAFGKQRLRHEILLSQSVRQALHSGqnqlkemaiPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTN 80
Cdd:TIGR01092 48 VILVTSGAVAFGRQRLRHRILVNSSFADLQKPQ---------PELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 81 LDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVisVKDNDSLAARLAVEMKTDLLIVLSDVEGLFD 160
Cdd:TIGR01092 119 LDFRDEQFRRQLNETVHELLRMNVVPVVNENDAVSTRAAPYSDSQGI--FWDNDSLAALLALELKADLLILLSDVEGLYD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 161 SPPGSDDAKLIDIFYPGDQQ-SVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTF 239
Cdd:TIGR01092 197 GPPSDDDSKLIDTFYKEKHQgEITFGTKSRLGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKN----ITKVVEGKKVGTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 240 FSEVKPAGPTVEQQGE-----MARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRL 313
Cdd:TIGR01092 273 FHEDAHLWPTVEQTGErdmavAARESSRMLQALSSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAgYAASLVARL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 314 SLSTSKLNSLAIGLRQIAASsQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGG 393
Cdd:TIGR01092 353 SMSPSKISSLAISLRQLAAM-EDPIGRVLKRTRIADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 394 KEAAHSNRILHLLTQEALSIHGVKEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHM 473
Cdd:TIGR01092 432 KEAARSNAILHKVITEAIPIHVGKKLIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKKSTK-IPVLGHADGICHV 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 474 YVDSEASVDKVTRLVRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRT 553
Cdd:TIGR01092 511 YVDKSASVDMAKRIVRDAKCDYPAACNAMETLLVHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRT 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 554 EYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRI 633
Cdd:TIGR01092 591 EYSSLACTVEIVDDVYDAIDHIHKHGSAHTDCIVTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRI 670
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1020738497 634 HARGPVGLEGLLTTKWLLRGKDHVVSdfSEHGsLKYLHENLPIPQRNT 681
Cdd:TIGR01092 671 HARGPVGVEGLLTTRWLLRGKGQVVS--GDHG-LVYTHKDLPIPQRNT 715
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
2-676 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 770.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 2 MLVTSGAVAFGKQRLRHEILLSQSVRQaLHSGQNQLKEMAipvlearaCAAAGQSGLMALYEAMFTQYSICAAQILVTNL 81
Cdd:PLN02418 57 ILVSSGAVGVGRQRLRYRRLVNSSFAD-LQKPQMELDGKA--------CAAVGQSELMALYDTLFSQLDVTASQLLVTDS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 82 DFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVISvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDS 161
Cdd:PLN02418 128 DFRDPDFRKQLSETVESLLDLRVIPIFNENDAVSTRRAPYEDSSGIFW--DNDSLAALLALELKADLLILLSDVEGLYTG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 162 PPGSDDAKLIDIFYP-GDQQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVsghvITDIVEGKKVGTFF 240
Cdd:PLN02418 206 PPSDPSSKLIHTYIKeKHQDEITFGEKSRVGRGGMTAKVKAAVNAASAGIPVVITSGYALDN----IRKVLRGERVGTLF 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 241 seVKPAG---PTVEQQG-EMA---RSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAE-GRLAAPLLKR 312
Cdd:PLN02418 282 --HQDAHlwaPSKEVGArEMAvaaRESSRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQeAGYEKSLVSR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 313 LSLSTSKLNSLAIGLRQIAASsQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKG 392
Cdd:PLN02418 360 LTLKPGKIASLAASIRQLADM-EDPIGRVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 393 GKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICH 472
Cdd:PLN02418 439 GKEAARSNAILHKVITDAIPKTVGGKLIGLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKASTK-IPVLGHADGICH 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 473 MYVDSEASVDKVTRLVRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSpsEVKSLR 552
Cdd:PLN02418 518 VYVDKSADMDMAKRIVVDAKTDYPAACNAMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNIP--EAQSFH 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 553 TEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSR 632
Cdd:PLN02418 596 HEYSSLACTVEIVDDVHAAIDHIHRHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGR 675
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1020738497 633 IHARGPVGLEGLLTTKWLLRGKDHVVSdfSEHGSLkYLHENLPI 676
Cdd:PLN02418 676 IHARGPVGVEGLLTTRWILRGNGQVVD--GDKGVV-YTHKDLPL 716
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
251-653 |
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: 592.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 251 EQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQ 329
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAgLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 330 IAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQE 409
Cdd:cd07079 81 VAALP-DPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 410 ALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTR 486
Cdd:cd07079 160 ALEEAGLpEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENAT-IPVIKHGDGNCHVYVDESADLEMAVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 487 LVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFS-PSEVKSLRTEYGDLELCIEVV 565
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAEEFL-PKLAEALREAGVELRGDEETLAILPGAkPATEEDWGTEYLDLILAVKVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 566 DNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLL 645
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397
|
....*...
gi 1020738497 646 TTKWLLRG 653
Cdd:cd07079 398 TYKYIVRG 405
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
249-659 |
1.80e-174 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 503.83 E-value: 1.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 249 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 327
Cdd:PRK00197 5 YLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANgLSAAMLDRLLLTEARIEGIAEGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 328 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 407
Cdd:PRK00197 85 RQVAALP-DPVGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 408 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 484
Cdd:PRK00197 164 QEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENAT-VPVIEHGDGICHIYVDESADLDKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 485 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTF-SPSEVKSLRTEYGDLELCIE 563
Cdd:PRK00197 243 LKIVLNAKTQRPSVCNALETLLVHEAIAEEFL-PKLAEALAEAGVELRGDEAALALLPDvVPATEEDWDTEYLDLILAVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 564 VVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEG 643
Cdd:PRK00197 322 VVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEE 401
|
410
....*....|....*.
gi 1020738497 644 LLTTKWLLRGKDHVVS 659
Cdd:PRK00197 402 LTTYKYIVLGDGQIRA 417
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
255-652 |
4.67e-173 |
|
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: 499.83 E-value: 4.67e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 255 EMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASs 334
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 335 qdsVGRVLRRTRIAkNLELEQVTVPIGVLLVIFESRPDCL-PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSI 413
Cdd:cd07077 80 ---VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLSgITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 414 HGVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDS 491
Cdd:cd07077 156 HGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 492 KCEYPAACNALETLLIHRDLLrTPLFDQIIDMLRVEQVKIHAGPKFASYLTFsPSEVKSLRTEYGDLELCIEVVDN---V 568
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVL-DPLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVisaV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 569 QDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARG-PVGLEGLLTT 647
Cdd:cd07077 313 ENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRPL 392
|
....*
gi 1020738497 648 KWLLR 652
Cdd:cd07077 393 KRLVR 397
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
249-659 |
3.59e-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: 497.99 E-value: 3.59e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 249 TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGL 327
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENgLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 328 RQIAASSqDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLT 407
Cdd:COG0014 82 RQVAALP-DPVGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 408 QEALSIHGV-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKV 484
Cdd:COG0014 161 QEALEEAGLpEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 485 TRLVRDSKCEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLtfspSEVK-----SLRTEYGDLE 559
Cdd:COG0014 240 VDIVVNAKTQRPGVCNALETLLVHRDIAAEFL-PRLAAALAEAGVELRGDERTRAIL----PDVKpateeDWGTEYLDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 560 LCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPV 639
Cdd:COG0014 315 LAVKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPM 394
|
410 420
....*....|....*....|
gi 1020738497 640 GLEGLLTTKWLLRGKDHVVS 659
Cdd:COG0014 395 GLEELTTYKYVVRGDGQIRP 414
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
1-241 |
1.31e-152 |
|
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: 443.03 E-value: 1.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 1 MMLVTSGAVAFGKQRLRHEILLSQSVRQALHSgqNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTN 80
Cdd:cd04256 50 VILVTSGAVAFGKQRLRHEILLSSSMRQTLKS--GQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 81 LDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFD 160
Cdd:cd04256 128 PDFYDEQTRRNLNGTLEELLRLNIIPIINTNDAVSPPPEPDEDLQGVISIKDNDSLAARLAVELKADLLILLSDVDGLYD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 161 SPPGSDDAKLIDIFYPGDQQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHpkvsGHVITDIVEGKKVGTFF 240
Cdd:cd04256 208 GPPGSDDAKLIHTFYPGDQQSITFGTKSRVGTGGMEAKVKAALWALQGGTSVVITNGMA----GDVITKILEGKKVGTFF 283
|
.
gi 1020738497 241 S 241
Cdd:cd04256 284 T 284
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
257-648 |
1.09e-127 |
|
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: 383.75 E-value: 1.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 257 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGR-LAAPLLKRLSLSTSKLNSLAIGLRQIAaSSQ 335
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENgLADALLDRLLLTEGRLKGIADGVKDVI-ELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 336 DSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHG 415
Cdd:TIGR00407 80 DPVGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 416 V-KEAVQLVNT--REEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKgIPVMGHSEGICHMYVDSEASVDKVTRLVRDSK 492
Cdd:TIGR00407 160 LpVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTST-IPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 493 CEYPAACNALETLLIHRDLLRTPLfDQIIDMLRVEQVKIHAGPKFASYLTFSPSEV-----KSLRTEYGDLELCIEVVDN 567
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAIAREFL-PVLENQLLEKGVTIHADAYALKLLELGPATEaivckTDFDKEFLSLDLSVKIVES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 568 VQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTT 647
Cdd:TIGR00407 318 LEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTSY 397
|
.
gi 1020738497 648 K 648
Cdd:TIGR00407 398 K 398
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
1-240 |
3.47e-80 |
|
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: 255.06 E-value: 3.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 1 MMLVTSGAVAFGKQRLRheillsqsvrqalhsgqnqLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTN 80
Cdd:cd04242 40 VILVSSGAVAAGRQRLG-------------------LEKRPKTLPEKQALAAVGQSLLMALYEQLFAQYGIKVAQILLTR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 81 LDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAepnsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFD 160
Cdd:cd04242 101 DDFEDRKRYLNARNTLETLLELGVIPIINENDTVATEE---------IRFGDNDRLSALVAGLVNADLLILLSDVDGLYD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 161 SPPGSD-DAKLIDIFYPGDQ--QSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVG 237
Cdd:cd04242 172 KNPRENpDAKLIPEVEEITDeiEAMAGGSGSSVGTGGMRTKLKAARIATEAGIPVVIANGRKP----DVLLDILAGEAVG 247
|
...
gi 1020738497 238 TFF 240
Cdd:cd04242 248 TLF 250
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
257-652 |
1.64e-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: 204.39 E-value: 1.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 257 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEeaegrlaapllKRLSLSTSKLNSLAIGLRQIAASSQD 336
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETG-----------KPIEEALGEVARAIDTFRYAAGLADK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 337 SVGrvLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCL--PQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSih 414
Cdd:cd06534 72 LGG--PELPSPDPGGEAYVRREPLGVVGVITPWNFPLLlaAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 415 gVKEAVQLVNTR--EEVEDLCRLDKmIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHMYVDSEASVDKVTRLVRD 490
Cdd:cd06534 148 -PPGVVNVVPGGgdEVGAALLSHPR-VDKISFTGSTAVGKAIMKAAAEnlKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 491 SKCEY-PAACNALETLLIHRDLlrtplFDQIIDMLRveQVKIHAGPKFasyltfspsevKSLRTEYGDLELCIEVVDNVQ 569
Cdd:cd06534 226 GAFFNaGQICTAASRLLVHESI-----YDEFVEKLV--TVLVDVDPDM-----------PIAQEEIFGPVLPVIRFKDEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 570 DAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYR-FGlgaevGISTSRIHAR-GPVGLEGLLTT 647
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFG-----GVKNSGIGREgGPYGLEEYTRT 362
|
....*
gi 1020738497 648 KWLLR 652
Cdd:cd06534 363 KTVVI 367
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
3-240 |
2.36e-53 |
|
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: 187.94 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 3 LVTSGAVAFGKQRLRheillsqsvrqaLHSGQNQLKEmaipvleARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLD 82
Cdd:COG0263 50 LVSSGAVAAGRGRLG------------LPKRPKTLPE-------KQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 83 FHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVpPAEpnsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSP 162
Cdd:COG0263 111 LEDRRRYLNARNTLETLLELGVVPIINENDTVA-TDE--------IRFGDNDRLAALVANLVEADLLVLLTDVDGLYDAD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 163 PGSD-DAKLIDI---FYPGDQQSVTfGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGT 238
Cdd:COG0263 182 PRKDpDAKLIPEveeITPEIEAMAG-GAGSGLGTGGMATKLEAARIATRAGIPTVIASGREP----NVLLRILAGERVGT 256
|
..
gi 1020738497 239 FF 240
Cdd:COG0263 257 LF 258
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
3-244 |
1.29e-49 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 174.27 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 3 LVTSGAVAFGKQRLR-HEILLSQSVRQALhsgqnqlkemaipvlearacAAAGQSGLMALYEAMFTQYSICAAQILVTNL 81
Cdd:PRK12314 52 LVSSGAIGAGLTKLKlDKRPTSLAEKQAL--------------------AAVGQPELMSLYSKFFAEYGIVVAQILLTRD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 82 DFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVppaepNSDLQGVISvkDNDSLAARLAVEMKTDLLIVLSDVEGLFDS 161
Cdd:PRK12314 112 DFDSPKSRANVKNTFESLLELGILPIVNENDAVA-----TDEIDTKFG--DNDRLSAIVAKLVKADLLIILSDIDGLYDK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 162 PP-GSDDAKLIDIFYPGDQQ--SVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPkvsgHVITDIVEGKKVGT 238
Cdd:PRK12314 185 NPrINPDAKLRSEVTEITEEilALAGGAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNP----SDILDFLEGESIGT 260
|
....*.
gi 1020738497 239 FFSEVK 244
Cdd:PRK12314 261 LFAPKK 266
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
1-240 |
1.31e-43 |
|
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: 160.55 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 1 MMLVTSGAVAFGKQRLrheillsqsvrqalhsGQNQL-KEMAipvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVT 79
Cdd:TIGR01027 41 VVIVSSGAIAAGFEAL----------------GLPERpKTLA----EKQALAAVGQVRLMQLYEQLFSQYGIKVAQILLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 80 NLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVpPAEpnsdlqgvISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF 159
Cdd:TIGR01027 101 RADFSDRERYLNARNTLEALLELGVVPIINENDTVA-TEE--------IKFGDNDTLSALVAILVGADLLVLLTDVDGLY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 160 DSPPGSD-DAKLIDIFYPGD--QQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKV 236
Cdd:TIGR01027 172 DADPRTNpDAKLIPVVEEITdlLLGVAGDSGSSVGTGGMRTKLQAADLATRAGVPVIIASGSKPE----KIADALEGAPV 247
|
....
gi 1020738497 237 GTFF 240
Cdd:TIGR01027 248 GTLF 251
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
1-240 |
4.51e-42 |
|
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: 152.98 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 1 MMLVTSGAVAFGKQRLRHEILLsqsvrqalhsgqNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTN 80
Cdd:cd02115 32 VVVVHGAGPQITDELLAHGELL------------GYARGLRITDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 81 LDFHD------EQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEpnsdlqGVISVKDNDSLAARLAVEMKTDLLIVLSD 154
Cdd:cd02115 100 AGFASpnqghvGKITKVSTDRLKSLLENGILPILSGFGGTDEKET------GTLGRGGSDSTAALLAAALKADRLVILTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 155 VEGLFDSPP-GSDDAKLIDIFYPGDQQSVTfgtksrvGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSghvitDIVEG 233
Cdd:cd02115 174 VDGVYTADPrKVPDAKLLSELTYEEAAELA-------YAGAMVLKPKAADPAARAGIPVRIANTENPGAL-----ALFTP 241
|
....*..
gi 1020738497 234 KKVGTFF 240
Cdd:cd02115 242 DGGGTLI 248
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
41-216 |
1.47e-28 |
|
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: 114.39 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 41 AIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVvppaep 120
Cdd:pfam00696 66 TLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGI------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 121 nsDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVtfgTKSRVGMGGMEAKV 199
Cdd:pfam00696 140 --DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDELLEL---LASGLATGGMKVKL 214
|
170
....*....|....*...
gi 1020738497 200 KAALWALQ-GGTSVVIAN 216
Cdd:pfam00696 215 PAALEAARrGGIPVVIVN 232
|
|
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
17-219 |
1.22e-16 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 80.44 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 17 RHEILLSQSVRQALHSGQNQLKEMAIPvlEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTL 96
Cdd:PTZ00489 44 KYEVILVTSGAVAAGYTKKEMDKSYVP--NKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 97 HELLRMNIVPIVNTNDAVVppaepnsdLQGVIsVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSPPGSDDAKLIDIFY 175
Cdd:PTZ00489 122 EVLISHKVIPIINENDATA--------LHELV-FGDNDRLSALVAHHFKADLLVILSDIDGYYtENPRTSTDAKIRSVVH 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1020738497 176 PGDQQSVTFGT--KSRVGMGGMEAKVKAALWALQGGTSVVIANGTH 219
Cdd:PTZ00489 193 ELSPDDLVAEAtpNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFH 238
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
95-238 |
4.31e-10 |
|
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: 60.74 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 95 TLHELLRMNIVPIVNtNDAVVppaepnsDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGsdDAKLIDIF 174
Cdd:cd04241 119 VIKELLDRGFVPVLH-GDVVL-------DEGGGITILSGDDIVVELAKALKPERVIFLTDVDGVYDKPPP--DAKLIPEI 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738497 175 YPGDQQSVTFGTKSRVG--MGGMEAKVKAALWALQGGTSVVIANGTHPKvsghVITDIVEGKKVGT 238
Cdd:cd04241 189 DVGSLEDILAALGSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPE----NLYRALLGNFIGT 250
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
96-217 |
6.66e-09 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 57.22 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 96 LHELLRMNIVPIVNtndavvPPAEpnsDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIFY 175
Cdd:PRK14058 142 LKLLLKAGYLPVVA------PPAL---SEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGSLIERIT 210
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1020738497 176 PGDqqsvtFGTKSRVGMGGMEAKVKAALWALQGG-TSVVIANG 217
Cdd:PRK14058 211 PEE-----AEELSKAAGGGMKKKVLMAAEAVEGGvGRVIIADA 248
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
96-238 |
2.79e-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: 55.21 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 96 LHELLRMNIVPIVNtndavvPPAepnSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFY 175
Cdd:cd04238 131 LETLLEAGYIPVIA------PIA---VDEDGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELT 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738497 176 PGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGG-TSVVIANGTHPkvsgHVITDIVEGKK-VGT 238
Cdd:cd04238 197 PKEaEELIEDGVIS----GGMIPKVEAALEALEGGvRKVHIIDGRVP----HSLLLELFTDEgIGT 254
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
119-246 |
1.32e-07 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 53.68 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 119 EPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLF-DSppGSDDAKLIDIFYPGDQQSVTFGTksrvgmGGMEA 197
Cdd:PRK12354 191 DADGKLHGVEAVIDKDLAAALLAEQLDADLLLILTDVDAVYlDW--GKPTQRAIAQATPDELRELGFAA------GSMGP 262
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1020738497 198 KVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGTFFSEVKPA 246
Cdd:PRK12354 263 KVEAACeFVRATGKIAGIG-------SLEDIQAILAGEA-GTRISPETAG 304
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
256-531 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 256 MARSGGRMLAtlePEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRlslstsklns 322
Cdd:cd07078 9 AAFKAWAALP---PAERAAILRKLADLLEERREELaaLETleTGKPIEEALGevaraadtfRYYAGLARR---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 323 laIGLRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPDCLP--QVAAlAIASGNGLLLKGGKEA 396
Cdd:cd07078 76 --LHGEVIPSPDPGELAIVRRE--------------PLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 397 AHSNRILHLLTQEALSIHGVkeaVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKG--IPVMGHSEGICHM 473
Cdd:cd07078 136 PLTALLLAELLAEAGLPPGV---LNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEnlKRVTLELGGKSPL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1020738497 474 YVDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 531
Cdd:cd07078 213 IVFDDADLDAAVKGAVFGAFGNAGqVCTAASRLLVHES-----IYDEFVERLveRVKALKV 268
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
115-238 |
6.96e-07 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 51.54 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 115 VPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSpPGSDDAKLIDIFYPgdQQSVTFGTKSRVGMGG 194
Cdd:PRK12454 196 IPVIEEDGELKGVEAVIDKDLASELLAEELNADIFIILTDVEKVYLN-YGKPDQKPLDKVTV--EEAKKYYEEGHFKAGS 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1020738497 195 MEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGkKVGT 238
Cdd:PRK12454 273 MGPKILAAIrFVENGGKRAIIA-------SLEKAVEALEG-KTGT 309
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
250-531 |
1.78e-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: 50.89 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 250 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 316
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEfakiIACEGGKPIKDARVevdraidtlRLAAEEAERIRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 317 TSKLNSLAIGLRQIAASSQDSVGRVLRRTriAKNLELEQVTVPIGvllvifesrPdclpqvaalAIASGNGLLLKGGKEA 396
Cdd:cd07094 103 EIPLDATQGSDNRLAWTIREPVGVVLAIT--PFNFPLNLVAHKLA---------P---------AIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 397 AHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMY 474
Cdd:cd07094 163 PLSALELAKILVEA----GVpEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 475 VDSEASVDKVTRLVRDSKCEYPA-ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 531
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEE-----LYDEFIEAFvaAVKKLKV 293
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
265-649 |
4.34e-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: 49.84 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 265 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSlstsklnslaiGlrQIA 331
Cdd:pfam00171 46 RKTPAAERAAILRKAADLLEERKDELaeLETleNGKPLAEARGevdraidvlRYYAGLARRLD-----------G--ETL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 332 ASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI--FESrPDCLP--QVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 407
Cdd:pfam00171 113 PSDPGRLAYTRRE--------------PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPLTALLLAELF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 408 QEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHSegicHMYVDSE 478
Cdd:pfam00171 177 EEA----GLpAGVLNVVTGsgAEVGEALVE-HPDVRKVSFTGSTAVGRHIAEAAaqNLKRVTlelgGKN----PLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 479 ASVDKVTRLVRDSKCEYP-AACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI--------HAGP--------KFAS 539
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES-----IYDEFVEKLveAAKKLKVgdpldpdtDMGPliskaqleRVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 540 Y-----------------------------LTFSPSEVKSLRTE-YGDLeLCIEVVDNVQDAIDHIH--KYGssHTDVIV 587
Cdd:pfam00171 323 YvedakeegaklltggeagldngyfveptvLANVTPDMRIAQEEiFGPV-LSVIRFKDEEEAIEIANdtEYG--LAAGVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738497 588 TEDENTAEFFLQHVDSACVFWNASTRFS-DGYRFGlgaevGISTSRI-HARGPVGLEGLLTTKW 649
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDaDGLPFG-----GFKQSGFgREGGPYGLEEYTEVKT 458
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
132-221 |
5.12e-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: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 132 DNDSLAARLAVEMKTDLLIVLSDVEGLFdsppgsDDAKLIDIFYPGDQQSVtfgtKSRVGmGGMEAKVKAALWALQGGTS 211
Cdd:cd04251 165 DGDRAAAAIAAALKAERLILLTDVEGLY------LDGRVIERITVSDAESL----LEKAG-GGMKRKLLAAAEAVEGGVR 233
|
90
....*....|.
gi 1020738497 212 -VVIANGTHPK 221
Cdd:cd04251 234 eVVIGDARADS 244
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
134-238 |
5.58e-06 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 48.57 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 134 DSLAARLAVEMKTDLLIVLSDVEGLFDSpPGS-------DDA-KLIdifypgDQQSVTfgtksrvgmGGMEAKVKAALWA 205
Cdd:PRK00942 184 DTAAGAIAAALGAEKLILLTDVPGVLDD-KGQliseltaSEAeELI------EDGVIT---------GGMIPKVEAALDA 247
|
90 100 110
....*....|....*....|....*....|....*
gi 1020738497 206 LQGG-TSVVIANGTHPkvsgH-VITDIVEGKKVGT 238
Cdd:PRK00942 248 ARGGvRSVHIIDGRVP----HaLLLELFTDEGIGT 278
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
134-217 |
6.94e-06 |
|
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: 48.27 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 134 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPgsDDAKLIDIFYPGD-QQSVTFGTKSrvgmGGMEAKVKAALWALQGGT-S 211
Cdd:cd04250 180 DTAAGAIAAALKAEKLILLTDVAGVLDDPN--DPGSLISEISLKEaEELIADGIIS----GGMIPKVEACIEALEGGVkA 253
|
....*.
gi 1020738497 212 VVIANG 217
Cdd:cd04250 254 AHIIDG 259
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
257-531 |
9.32e-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: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 257 ARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLA----NKKDLEEAEG---------RLAAPLLKRLSlstsklnsl 323
Cdd:COG1012 52 ARAAFPAWAATPPAERAAILLRAADLLEERREELAALltleTGKPLAEARGevdraadflRYYAGEARRLY--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 324 aiGlRQIAASSQDSVGRVLRRtriaknleleqvtvPIGVLLVI----FesrPdcLPQVA---ALAIASGNGLLLKGGKEA 396
Cdd:COG1012 123 --G-ETIPSDAPGTRAYVRRE--------------PLGVVGAItpwnF---P--LALAAwklAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 397 AHSNRILHLLTQEAlsihGV-KEAVQLVNT--REEVEDLCRlDKMIDLIIPRGSSQLVRDIQKAA--KGIPVM----GHS 467
Cdd:COG1012 181 PLSALLLAELLEEA----GLpAGVLNVVTGdgSEVGAALVA-HPDVDKISFTGSTAVGRRIAAAAaeNLKRVTlelgGKN 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1020738497 468 egicHMYVDSEASVDKVTRLVRDSKCEYpA--ACNALETLLIHRDllrtpLFDQIIDML--RVEQVKI 531
Cdd:COG1012 256 ----PAIVLDDADLDAAVEAAVRGAFGN-AgqRCTAASRLLVHES-----IYDEFVERLvaAAKALKV 313
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
134-220 |
4.04e-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: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 134 DSLAARLAVEMKTDLLIVLSDVEGLFDsppgsDDAKLIDIFYPGDQQSVTfgtKSRVGMGGMEAKVKAALWALQGGT-SV 212
Cdd:COG0548 186 DTVAGAIAAALKAEKLILLTDVPGVLD-----DPGSLISELTAAEAEELI---ADGVISGGMIPKLEAALDAVRGGVkRV 257
|
....*...
gi 1020738497 213 VIANGTHP 220
Cdd:COG0548 258 HIIDGRVP 265
|
|
| AAK_NAGK-NC |
cd04249 |
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
96-238 |
8.69e-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: 44.71 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 96 LHELLRMNIVPIVNTNDAvvppaepnsDLQGVISVKDNDSLAARLAVEMKTDLlIVLSDVEGLFDSppgsdDAKLIDIFy 175
Cdd:cd04249 129 LNDLLKAGFLPIISSIGA---------DDQGQLMNVNADQAATAIAQLLNADL-VLLSDVSGVLDA-----DKQLISEL- 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1020738497 176 pgDQQSVTFGTKSRVGMGGMEAKVKAALWALQG-GTSVVIANGTHPKvsghVITDIVEGKKVGT 238
Cdd:cd04249 193 --NAKQAAELIEQGVITDGMIVKVNAALDAAQSlRRGIDIASWQYPE----QLTALLAGEPVGT 250
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
265-465 |
5.97e-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: 42.94 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 265 ATLEPEQRAEIIHHLADLLTDQRDEI--LLA--NKKDLEEAEG---------RLAAPLLKRLSLSTSKLNslaiglrqIA 331
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVanLLMweIGKTLKDALKevdrtidyiRDTIEELKRLDGDSLPGD--------WF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 332 ASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI-------FESrpdclpqVAALAIA--SGNGLLLKGGKEAAhsnrI 402
Cdd:cd07082 128 PGTKGKIAQVRR--------------EPLGVVLAIgpfnyplNLT-------VSKLIPAliMGNTVVFKPATQGV----L 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020738497 403 LHLLTQEALSIHGV-KEAVQLVNTR-EEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP-VMG 465
Cdd:cd07082 183 LGIPLAEAFHDAGFpKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRlVLE 248
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
134-239 |
7.66e-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: 41.46 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 134 DSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSD-DAKLIDIFYPGDQQSVTFGTKSRVGmggmeAKVKAALWALQ----G 208
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAG-----SNEPFDPLAAKiierS 192
|
90 100 110
....*....|....*....|....*....|.
gi 1020738497 209 GTSVVIANGTHPKvsghVITDIVEGKKVGTF 239
Cdd:cd04253 193 GIKTIVVDGRDPE----NLERALKGEFVGTI 219
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|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
250-458 |
1.27e-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: 41.81 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 250 VEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEG---------RLAAPLLKRLSLS 316
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEfartIALEAGKPIKDARKevdraietlRLSAEEAKRLAGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 317 TSKLNSlaiglrqiAASSQDSVGRVLRrtriaknleleqvtVPIGVLLVI--FEsrpDCLPQVA---ALAIASGNGLLLK 391
Cdd:cd07149 103 TIPFDA--------SPGGEGRIGFTIR--------------EPIGVVAAItpFN---FPLNLVAhkvGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 392 GGKEAAHSNRILHLLTQEAlsihGV-KEAVQLVN-TREEVED-LCRlDKMIDLIIPRGSSQLVRDIQKAA 458
Cdd:cd07149 158 PASQTPLSALKLAELLLEA----GLpKGALNVVTgSGETVGDaLVT-DPRVRMISFTGSPAVGEAIARKA 222
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
265-537 |
1.46e-03 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 41.55 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 265 ATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLeeaegrlaapllkRLSLSTSKLNSLAIGLRQIAASSQDsvgrvlrr 344
Cdd:PTZ00381 24 KTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDL-------------GRHPFETKMTEVLLTVAEIEHLLKH-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 345 trIAKNLELEQVTV--------------PIGVLLVIFE-SRP--DCLPQVAAlAIASGNGLLLKGGKEAAHSNRILHLLT 407
Cdd:PTZ00381 83 --LDEYLKPEKVDTvgvfgpgksyiipePLGVVLVIGAwNYPlnLTLIPLAG-AIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 408 QEALSihgvKEAVQLVNT-REEVEDLCRLDkmIDLIIPRGSSQLVRDIQKAA--KGIPVMGHSEGICHMYVDSEASVDKV 484
Cdd:PTZ00381 160 TKYLD----PSYVRVIEGgVEVTTELLKEP--FDHIFFTGSPRVGKLVMQAAaeNLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1020738497 485 TRLVRDSKC-EYPAACNALETLLIHRDLLrtplfDQIIDMLRvEQVKIHAGPKF 537
Cdd:PTZ00381 234 ARRIAWGKFlNAGQTCVAPDYVLVHRSIK-----DKFIEALK-EAIKEFFGEDP 281
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
237-530 |
1.75e-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: 41.46 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 237 GTFFSEVKPAGP-TVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDE----ILLANKKDLEEAEGRLAApllk 311
Cdd:cd07147 9 GEVVARVALAGPdDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEElaetIVLEAGKPIKDARGEVAR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 312 rlslstsklnslAIGLRQIAA-SSQDSVGRVLRRTRIAKNLELEQVT--VPIGVLLVIfesRPDCLP--QVA---ALAIA 383
Cdd:cd07147 85 ------------AIDTFRIAAeEATRIYGEVLPLDISARGEGRQGLVrrFPIGPVSAI---TPFNFPlnLVAhkvAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 384 SGNGLLLKggkeAAHSNRILHLLTQEALSIHGV-KEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIP 462
Cdd:cd07147 150 AGCPFVLK----PASRTPLSALILGEVLAETGLpKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020738497 463 VMGHSEGICHMYVDSEASVDK-VTRLVRDSKCEYPAACNALETLLIHRDllrtpLFDQIIDMLrVEQVK 530
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFaAQRIIFGAFYQAGQSCISVQRVLVHRS-----VYDEFKSRL-VARVK 288
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
115-238 |
2.03e-03 |
|
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239768 Cd Length: 308 Bit Score: 40.96 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020738497 115 VPPAEPNSDLQGVISVKDNDSLAARLAVEMKTDLLIVLSDVEGL---FDSPpgsDDAKLIDIFYpgdQQSVTFGTKSRVG 191
Cdd:cd04235 192 IPVVREGGGLKGVEAVIDKDLASALLAEEINADLLVILTDVDNVyinFGKP---NQKALEQVTV---EELEKYIEEGQFA 265
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1020738497 192 MGGMEAKVKAAL-WALQGGTSVVIAngthpkvSGHVITDIVEGKKvGT 238
Cdd:cd04235 266 PGSMGPKVEAAIrFVESGGKKAIIT-------SLENAEAALEGKA-GT 305
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