|
Name |
Accession |
Description |
Interval |
E-value |
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
50-775 |
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: 862.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 50 RSQLKYARRLVVKLGSAVITREDNHgLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLMSLSMRETLNP 129
Cdd:TIGR01092 1 RAFLKDVKRIVVKVGTAVVTRGDGR-LALGRLGSICEQLSELNSDGREVILVTSGAVAFGRQRLRHRILVNSSFADLQKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 130 kdskefdGATLEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAV 209
Cdd:TIGR01092 80 -------QPELDGKACAAVGQSGLMALYETMFTQLDITAAQILVTDLDFRDEQFRRQLNETVHELLRMNVVPVVNENDAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 210 SPPMFIRDDEpaggarRGIpIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWEDGAKLMHTYTSDD-SNSIEFGKKS 288
Cdd:TIGR01092 153 STRAAPYSDS------QGI-FWDNDSLAALLALELKADLLILLSDVEGLYDGPPSDDDSKLIDTFYKEKhQGEITFGTKS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 289 KVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFTEATESANAVP---VEVMAENARTGSRQMQAL 365
Cdd:TIGR01092 226 RLGRGGMTAKVKAAVWAAYGGTPVIIASGTAPKNITKVVEGKKVGTLFHEDAHLWPTVEqtgERDMAVAARESSRMLQAL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 366 TPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLKQIAeDSHKNVGRVLRRTR 445
Cdd:TIGR01092 306 SSEQRKEILHDIADALEDNEDEILAENKKDVAAAQGAGYAASLVARLSMSPSKISSLAISLRQLA-AMEDPIGRVLKRTR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 446 LADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKEALATVGAEHAVSLVSTR 525
Cdd:TIGR01092 385 IADNLILEKTSVPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLVTSR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 526 EEISDLLSMENHIDLIIPRGSSDLVRSIQQqSLHIPVLGHAEGVCHVYIDRDADLEKALRIARDAKCDYPAACNAMETLL 605
Cdd:TIGR01092 465 EEIPDLLKLDDVIDLVIPRGSNKLVSQIKK-STKIPVLGHADGICHVYVDKSASVDMAKRIVRDAKCDYPAACNAMETLL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 606 IHEDLMSGAIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPAAKSLKHEYGALECCIEVVPSLDEAINHIHTYGSSHTDVI 685
Cdd:TIGR01092 544 VHKDLLRNGLLDDLIDMLRTEGVTIHGGPRFAAYLTFNISETKSFRTEYSSLACTVEIVDDVYDAIDHIHKHGSAHTDCI 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 686 VTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVEGLLTTKWILEGQDHAAADfaeGGG 765
Cdd:TIGR01092 624 VTEDENVAEFFLQHVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWLLRGKGQVVSG---DHG 700
|
730
....*....|
gi 21357643 766 RTWLHETLPL 775
Cdd:TIGR01092 701 LVYTHKDLPI 710
|
|
| PLN02418 |
PLN02418 |
delta-1-pyrroline-5-carboxylate synthase |
50-776 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate synthase
Pssm-ID: 215230 Cd Length: 718 Bit Score: 841.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 50 RSQLKYARRLVVKLGSAVITREDNHgLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLMSLSMRETLNP 129
Cdd:PLN02418 9 RAFLRDVKRVVIKVGTAVVTRDDGR-LALGRLGALCEQIKELNSDGYEVILVSSGAVGVGRQRLRYRRLVNSSFADLQKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 130 KDskEFDGatlepRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAV 209
Cdd:PLN02418 88 QM--ELDG-----KACAAVGQSELMALYDTLFSQLDVTASQLLVTDSDFRDPDFRKQLSETVESLLDLRVIPIFNENDAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 210 SppmfirddepaggARRGiPIK-------DNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWEDGAKLMHTYTSDDSNS- 281
Cdd:PLN02418 161 S-------------TRRA-PYEdssgifwDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPSSKLIHTYIKEKHQDe 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 282 IEFGKKSKVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFF-TEATESANAVPVEV--MAENARTG 358
Cdd:PLN02418 227 ITFGEKSRVGRGGMTAKVKAAVNAASAGIPVVITSGYALDNIRKVLRGERVGTLFhQDAHLWAPSKEVGAreMAVAARES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 359 SRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLKQIAeDSHKNVG 438
Cdd:PLN02418 307 SRKLQALSSEERKKILLDVADALEANEELIKAENELDVAAAQEAGYEKSLVSRLTLKPGKIASLAASIRQLA-DMEDPIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 439 RVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKEALATVGAEHA 518
Cdd:PLN02418 386 RVLKRTEVADGLVLEKTSCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAARSNAILHKVITDAIPKTVGGKL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 519 VSLVSTREEISDLLSMENHIDLIIPRGSSDLVRSIQQqSLHIPVLGHAEGVCHVYIDRDADLEKALRIARDAKCDYPAAC 598
Cdd:PLN02418 466 IGLVTSRDEIPDLLKLDDVIDLVIPRGSNKLVSQIKA-STKIPVLGHADGICHVYVDKSADMDMAKRIVVDAKTDYPAAC 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 599 NAMETLLIHEDLMSGAIFGDVCNMLKREGVKIYAGPRLNQQLTFgpPAAKSLKHEYGALECCIEVVPSLDEAINHIHTYG 678
Cdd:PLN02418 545 NAMETLLVHKDLVQNGGLNDLLVALRSAGVTLYGGPRASKLLNI--PEAQSFHHEYSSLACTVEIVDDVHAAIDHIHRHG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 679 SSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVEGLLTTKWILEGQDHAAa 758
Cdd:PLN02418 623 SAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGARFGLGAEVGISTGRIHARGPVGVEGLLTTRWILRGNGQVV- 701
|
730 740
....*....|....*....|
gi 21357643 759 dfaeGG--GRTWLHETLPLD 776
Cdd:PLN02418 702 ----DGdkGVVYTHKDLPLQ 717
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
349-753 |
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: 595.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 349 EVMAENARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLKQ 428
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDLAAAREAGLSEALLDRLLLTPERIEAMAEGLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 429 IAEdSHKNVGRVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKE 508
Cdd:cd07079 81 VAA-LPDPVGEVLRGWTLPNGLQIEKVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEALHSNRALVEIIQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 509 ALATVG-AEHAVSLVST--REEISDLLSMENHIDLIIPRGSSDLVRSIQQQSlHIPVLGHAEGVCHVYIDRDADLEKALR 585
Cdd:cd07079 160 ALEEAGlPEDAVQLIPDtdREAVQELLKLDDYIDLIIPRGGAGLIRFVVENA-TIPVIKHGDGNCHVYVDESADLEMAVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 586 IARDAKCDYPAACNAMETLLIHEDLMSgAIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPA-AKSLKHEYGALECCIEVV 664
Cdd:cd07079 239 IVVNAKTQRPSVCNALETLLVHRDIAE-EFLPKLAEALREAGVELRGDEETLAILPGAKPAtEEDWGTEYLDLILAVKVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 665 PSLDEAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVEGLL 744
Cdd:cd07079 318 DSLDEAIAHINRYGSGHTEAIVTENYETAERFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLEELT 397
|
....*....
gi 21357643 745 TTKWILEGQ 753
Cdd:cd07079 398 TYKYIVRGD 406
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
49-337 |
0e+00 |
|
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.
Pssm-ID: 239789 [Multi-domain] Cd Length: 284 Bit Score: 521.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 49 ERSQLKYARRLVVKLGSAVITREDNHGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLMSLSMRETLN 128
Cdd:cd04256 1 SRSELKHAKRIVVKLGSAVVTREDECGLALGRLASIVEQVSELQSQGREVILVTSGAVAFGKQRLRHEILLSSSMRQTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 129 PKDSKEFDGATLEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDA 208
Cdd:cd04256 81 SGQLKDMPQMELDGRACAAVGQSGLMALYEAMFTQYGITVAQVLVTKPDFYDEQTRRNLNGTLEELLRLNIIPIINTNDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 209 VSPPMFiRDDEPAGgarrGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWEDGAKLMHTYTSDDSNSIEFGKKS 288
Cdd:cd04256 161 VSPPPE-PDEDLQG----VISIKDNDSLAARLAVELKADLLILLSDVDGLYDGPPGSDDAKLIHTFYPGDQQSITFGTKS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 21357643 289 KVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFT 337
Cdd:cd04256 236 RVGTGGMEAKVKAALWALQGGTSVVITNGMAGDVITKILEGKKVGTFFT 284
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
347-755 |
8.56e-176 |
|
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: 510.70 E-value: 8.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 347 PVEVMAENARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGL 426
Cdd:COG0014 2 YLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDLEAARENGLSEALLDRLKLTEERIEAMAEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 427 KQIAE--DShknVGRVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALME 504
Cdd:COG0014 82 RQVAAlpDP---VGEVLDGWTRPNGLQIGRVRVPLGVIGIIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 505 LVKEALATVG-AEHAVSLVST--REEISDLLSMENHIDLIIPRGSSDLVRSIQQQSLhIPVLGHAEGVCHVYIDRDADLE 581
Cdd:COG0014 159 VIQEALEEAGlPEDAVQLVPTtdREAVGELLTLDGYIDVIIPRGGAGLIRRVVENAT-VPVIEHGDGNCHVYVDASADLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 582 KALRIARDAKCDYPAACNAMETLLIHEDLMSgAIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPA-AKSLKHEYGALECC 660
Cdd:COG0014 238 MAVDIVVNAKTQRPGVCNALETLLVHRDIAA-EFLPRLAAALAEAGVELRGDERTRAILPDVKPAtEEDWGTEYLDLILA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 661 IEVVPSLDEAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGV 740
Cdd:COG0014 317 VKVVDSLDEAIAHINRYGSGHTEAIVTEDYAAARRFLREVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGL 396
|
410
....*....|....*
gi 21357643 741 EGLLTTKWILEGQDH 755
Cdd:COG0014 397 EELTTYKYVVRGDGQ 411
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
348-755 |
2.36e-175 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 509.61 E-value: 2.36e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 348 VEVMAENARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLK 427
Cdd:PRK00197 6 LEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDLAAARANGLSAAMLDRLLLTEARIEGIAEGLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 428 QIAE--DShknVGRVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMEL 505
Cdd:PRK00197 86 QVAAlpDP---VGEVLDGWTLPNGLRIGRVRVPLGVIGVIYESRPNVTVDAAALCLKSGNAVILRGGSEAIHSNRALVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 506 VKEALATVGA-EHAVSLVST--REEISDLLSMENHIDLIIPRGSSDLVRSIQQQSlHIPVLGHAEGVCHVYIDRDADLEK 582
Cdd:PRK00197 163 IQEALEEAGLpADAVQLVETtdRAAVGELLKLDGYVDVIIPRGGAGLIRRVVENA-TVPVIEHGDGICHIYVDESADLDK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 583 ALRIARDAKCDYPAACNAMETLLIHEDLMSgAIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPA-AKSLKHEYGALECCI 661
Cdd:PRK00197 242 ALKIVLNAKTQRPSVCNALETLLVHEAIAE-EFLPKLAEALAEAGVELRGDEAALALLPDVVPAtEEDWDTEYLDLILAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 662 EVVPSLDEAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVE 741
Cdd:PRK00197 321 KVVDSLDEAIAHINRYGSGHTEAIVTEDYAAAERFLNEVDSAAVYVNASTRFTDGGEFGLGAEIGISTQKLHARGPMGLE 400
|
410
....*....|....
gi 21357643 742 GLLTTKWILEGQDH 755
Cdd:PRK00197 401 ELTTYKYIVLGDGQ 414
|
|
| proA |
TIGR00407 |
gamma-glutamyl phosphate reductase; The related model TIGR01092 describes a full-length fusion ... |
355-747 |
2.52e-130 |
|
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: 393.38 E-value: 2.52e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 355 ARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLKQIAEDSH 434
Cdd:TIGR00407 1 AKQAANILAQLSTAEKNDALSKIADGLEAQAPAILAANAKDIAVAKENGLADALLDRLLLTEGRLKGIADGVKDVIELAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 435 KnVGRVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKEALATVG 514
Cdd:TIGR00407 81 P-VGKVIDGRELDSGLTLERVRVPLGVLGVIYEARPNVTVDIASLCLKTGNAVILRGGKEAVRSNKALVEVIQDALAQTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 515 -AEHAVSLVST--REEISDLLSMENHIDLIIPRGSSDLVRSIQQQSlHIPVLGHAEGVCHVYIDRDADLEKALRIARDAK 591
Cdd:TIGR00407 160 lPVGAVQLIETpsRELVSELLDLDEYIDLLIPRGGNGLVRLIKQTS-TIPVLGHGDGICHIYLDESADLIKAIKVIVNAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 592 CDYPAACNAMETLLIHEDLmsGAIFGDV-CNMLKREGVKIYAGPRLNQQLTFGPP-----AAKSLKHEYGALECCIEVVP 665
Cdd:TIGR00407 239 TQRPSTCNAIETLLVNKAI--AREFLPVlENQLLEKGVTIHADAYALKLLELGPAteaivCKTDFDKEFLSLDLSVKIVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 666 SLDEAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVEGLLT 745
Cdd:TIGR00407 317 SLEAAIQHINQYGTQHSDAILTENKANAEQFQNGVDSAAVYHNASTRFTDGFRFGFGAEVGISTQKLHARGPMGLEALTS 396
|
..
gi 21357643 746 TK 747
Cdd:TIGR00407 397 YK 398
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
58-337 |
4.80e-104 |
|
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: 319.77 E-value: 4.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 58 RLVVKLGSAVITREDNhGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLmslsmretlnPKDSKEfdg 137
Cdd:cd04242 1 RIVVKVGSSLLTDEDG-GLDLGRLASLVEQIAELRNQGKEVILVSSGAVAAGRQRLGLEKR----------PKTLPE--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 138 atlePRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAVSPpmfird 217
Cdd:cd04242 67 ----KQALAAVGQSLLMALYEQLFAQYGIKVAQILLTRDDFEDRKRYLNARNTLETLLELGVIPIINENDTVAT------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 218 DEPAGGarrgipikDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDsNSIEF---GKKSKVGTG 293
Cdd:cd04242 137 EEIRFG--------DNDRLSALVAGLVNADLLILLSDVDGLYDKNPRENpDAKLIPEVEEIT-DEIEAmagGSGSSVGTG 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 21357643 294 GMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFT 337
Cdd:cd04242 208 GMRTKLKAARIATEAGIPVVIANGRKPDVLLDILAGEAVGTLFL 251
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
353-750 |
1.20e-97 |
|
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: 308.38 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 353 ENARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSgLAKPLLSRLSLNPAKLKNLSVGLKQIAed 432
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRS-LIANWIAMMGCSESKLYKNIDTERGIT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 433 shKNVGRVLRRTRlADQLELKQVTVPIGVLLVIFESRPD-SLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKEALA 511
Cdd:cd07077 78 --ASVGHIQDVLL-PDNGETYVRAFPIGVTMHILPSTNPlSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 512 TVGAEHAVSLVSTR--EEISDLLSMENhIDLIIPRGSSDLVRSIQQQSLHIPVLGHAEGVCHVYIDRDADLEKALRIARD 589
Cdd:cd07077 155 AHGPKILVLYVPHPsdELAEELLSHPK-IDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 590 AKCDYPAACNAMETLLIHEDLMSgAIFGDVCNMLKREGVKIYAGPRLNQQLTFgPPAAKSLKHEYGALECCIEVVPSLDE 669
Cdd:cd07077 234 SKFFDQNACASEQNLYVVDDVLD-PLYEEFKLKLVVEGLKVPQETKPLSKETT-PSFDDEALESMTPLECQFRVLDVISA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 670 ---AINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARG-PVGVEGLLT 745
Cdd:cd07077 312 venAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGVERIVTSGMNNIFGaGVGHDALRP 391
|
....*
gi 21357643 746 TKWIL 750
Cdd:cd07077 392 LKRLV 396
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
50-345 |
2.39e-75 |
|
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: 248.80 E-value: 2.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 50 RSQLKYARRLVVKLGSAVITREDnHGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAqellmsLSMRetlnP 129
Cdd:COG0263 1 REALAKARRIVVKIGSSLLTDEG-GGLDRARLAALADQIAALRAAGKEVVLVSSGAVAAGRGRLG------LPKR----P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 130 KDSKEfdgatlePRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAV 209
Cdd:COG0263 70 KTLPE-------KQAAAAVGQGLLMQAYEEAFARHGLTVAQVLLTRDDLEDRRRYLNARNTLETLLELGVVPIINENDTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 210 SppmfirDDEpaggarrgipIK--DNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDSnSIEF-- 284
Cdd:COG0263 143 A------TDE----------IRfgDNDRLAALVANLVEADLLVLLTDVDGLYDADPRKDpDAKLIPEVEEITP-EIEAma 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357643 285 -GKKSKVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFTEATESANA 345
Cdd:COG0263 206 gGAGSGLGTGGMATKLEAARIATRAGIPTVIASGREPNVLLRILAGERVGTLFLPSGEPLSA 267
|
|
| PRK12314 |
PRK12314 |
gamma-glutamyl kinase; Provisional |
50-337 |
3.43e-72 |
|
gamma-glutamyl kinase; Provisional
Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 236.68 E-value: 3.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 50 RSQLKYARRLVVKLGSAVITREdNHGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQEllmslsmretlnp 129
Cdd:PRK12314 3 RRQLENAKRIVIKVGSSTLSYE-NGKINLERIEQLVFVISDLMNKGKEVILVSSGAIGAGLTKLKLD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 130 KDSKEFdgatLEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAV 209
Cdd:PRK12314 69 KRPTSL----AEKQALAAVGQPELMSLYSKFFAEYGIVVAQILLTRDDFDSPKSRANVKNTFESLLELGILPIVNENDAV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 210 SPpmfirdDEpaggarrgIPIK--DNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWE-DGAKLMHTYTSDDSNSIEF-- 284
Cdd:PRK12314 145 AT------DE--------IDTKfgDNDRLSAIVAKLVKADLLIILSDIDGLYDKNPRInPDAKLRSEVTEITEEILALag 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 21357643 285 GKKSKVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFT 337
Cdd:PRK12314 211 GAGSKFGTGGMVTKLKAAKFLMEAGIKMVLANGFNPSDILDFLEGESIGTLFA 263
|
|
| proB |
TIGR01027 |
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
57-336 |
1.60e-62 |
|
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: 214.09 E-value: 1.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 57 RRLVVKLGSAVITREDNhGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAqellmsLSMRetlnPKDSKEfd 136
Cdd:TIGR01027 1 QRIVVKVGSSSLTGSSG-SLDRSHIAELVEQVAALHAAGHEVVIVSSGAIAAGFEALG------LPER----PKTLAE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 137 gatlePRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAVsppmfir 216
Cdd:TIGR01027 68 -----KQALAAVGQVRLMQLYEQLFSQYGIKVAQILLTRADFSDRERYLNARNTLEALLELGVVPIINENDTV------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 217 ddepaggARRGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTY--TSDDSNSIEFGKKSKVGTG 293
Cdd:TIGR01027 136 -------ATEEIKFGDNDTLSALVAILVGADLLVLLTDVDGLYDADPRTNpDAKLIPVVeeITDLLLGVAGDSGSSVGTG 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 21357643 294 GMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFF 336
Cdd:TIGR01027 209 GMRTKLQAADLATRAGVPVIIASGSKPEKIADALEGAPVGTLF 251
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
355-751 |
1.37e-41 |
|
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: 155.85 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 355 ARTGSRQMQALTPAQRASAVNTLADLLvsrekfilDANAKDLAEAQKSGLAKPLLSRLslnpAKLKNLSVGLKQIAEDSH 434
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLL--------EERREELAALETLETGKPIEEAL----GEVARAIDTFRYAAGLAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 435 KNVGRVLRRTRlaDQLELKQVTVPIGVLLVIFESR-PDSLP-QVAALAMASANGLLLKGGKEAAHSNKALMELVKEALAT 512
Cdd:cd06534 71 KLGGPELPSPD--PGGEAYVRREPLGVVGVITPWNfPLLLAaWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 513 VGAehaVSLVSTR-EEISDLLSMENHIDLIIPRGSSDLVRSIQQQS--LHIPVLGHAEGVCHVYIDRDADLEKALRIARD 589
Cdd:cd06534 149 PGV---VNVVPGGgDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAaeNLKPVTLELGGKSPVIVDEDADLDAAVEGAVF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 590 AKC-DYPAACNAMETLLIHEDLMsgaifgdvcNMLKREGVKIYAGPrlnqqltfgPPAAKSLKHEYGALECCIEVVPSLD 668
Cdd:cd06534 226 GAFfNAGQICTAASRLLVHESIY---------DEFVEKLVTVLVDV---------DPDMPIAQEEIFGPVLPVIRFKDEE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 669 EAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFR-FGLGAEVGIStaRIHarGPVGVEGLLTTK 747
Cdd:cd06534 288 EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEApFGGVKNSGIG--REG--GPYGLEEYTRTK 363
|
....
gi 21357643 748 WILE 751
Cdd:cd06534 364 TVVI 367
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
57-316 |
5.13e-34 |
|
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: 130.18 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 57 RRLVVKLGSAVITREDnhglalgRLASIVEQVAECHLEGREVMMVTSGAvAFGKQKLAqelLMSLSMRETLNPKDSKefd 136
Cdd:pfam00696 1 KRVVIKLGGSSLTDKE-------RLKRLADEIAALLEEGRKLVVVHGGG-AFADGLLA---LLGLSPRFARLTDAET--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 137 GATLEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAVSPPmfir 216
Cdd:pfam00696 67 LEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDDVVTRIDTEALEELLEAGVVPVITGFIGIDPE---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 217 ddepaGGARRGipikDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDsnsIEFGKKSKVGTGGM 295
Cdd:pfam00696 143 -----GELGRG----SSDTLAALLAEALGADKLIILTDVDGVYTADPRKVpDAKLIPEISYDE---LLELLASGLATGGM 210
|
250 260
....*....|....*....|..
gi 21357643 296 DSKVKAATWALDRGV-SVVICN 316
Cdd:pfam00696 211 KVKLPAALEAARRGGiPVVIVN 232
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
60-336 |
9.45e-28 |
|
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: 112.54 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 60 VVKLGSAVITREDnhglalgRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLMSLSMRETLNPKdskefdgat 139
Cdd:cd02115 1 VIKFGGSSVSSEE-------RLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDR--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 140 lEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDF------YNEETRNNLFCTLSELISLNIVPIINTNDAVSPPm 213
Cdd:cd02115 65 -ETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFaspnqgHVGKITKVSTDRLKSLLENGILPILSGFGGTDEK- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 214 firddepaggARRGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWE-DGAKLMHTYTSDDSNSIEfgkkskvGT 292
Cdd:cd02115 143 ----------ETGTLGRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKvPDAKLLSELTYEEAAELA-------YA 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 21357643 293 GGMDSKVKAATWALDRGVSVVICNGMQEKAIKtIIGGRKVGTFF 336
Cdd:cd02115 206 GAMVLKPKAADPAARAGIPVRIANTENPGALA-LFTPDGGGTLI 248
|
|
| PTZ00489 |
PTZ00489 |
glutamate 5-kinase; Provisional |
53-343 |
1.27e-27 |
|
glutamate 5-kinase; Provisional
Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 112.80 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 53 LKYARRLVVKLGSAVITreDNHGLALGRLASIVEQVAEchLEGR-EVMMVTSGAVAFGKQKlaqellmslsmretlnpkd 131
Cdd:PTZ00489 5 LKSVKRIVVKVGSSILV--DNQEIAAHRIEALCRFIAD--LQTKyEVILVTSGAVAAGYTK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 132 sKEFDGATL-EPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAVs 210
Cdd:PTZ00489 62 -KEMDKSYVpNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDAT- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 211 ppmfirddepaggARRGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWEDG----AKLMHTYTSDDSNSiEFGK 286
Cdd:PTZ00489 140 -------------ALHELVFGDNDRLSALVAHHFKADLLVILSDIDGYYTENPRTSTdakiRSVVHELSPDDLVA-EATP 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21357643 287 KSKVGTGGMDSKVKAATWALDRGVSVVICNGMQ-EKAIKTIIGG-RKVGTFFTEATESA 343
Cdd:PTZ00489 206 NNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHlEKARDFLIGGsHEIGTLFYPRVSSA 264
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
58-334 |
5.89e-14 |
|
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: 72.29 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 58 RLVVKLGSAVITREDNHGLA-LGRLASIVEQVAECHlegREVMMVTSGAVAFGKQKLAQELLMS--------------LS 122
Cdd:cd04241 1 MIILKLGGSVITDKDRPETIrEENLERIARELAEAI---DEKLVLVHGGGSFGHPKAKEYGLPDgdgsfsaegvaethEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 123 MREtLNPKDSKEFDGATLEPraaaavgqsglmslydamfaqYGVKIAQVLVTkpdfynEETRNNLFCT--LSELISLNIV 200
Cdd:cd04241 78 MLE-LNSIVVDALLEAGVPA---------------------VSVPPSSFFVT------ENGRIVSFDLevIKELLDRGFV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 201 PIINtNDAVSppmfirDDEPaggarrGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPweDGAKLMHTYTSDDSN 280
Cdd:cd04241 130 PVLH-GDVVL------DEGG------GITILSGDDIVVELAKALKPERVIFLTDVDGVYDKPP--PDAKLIPEIDVGSLE 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 21357643 281 SIEFGKKSKVG--TGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGT 334
Cdd:cd04241 195 DILAALGSAGTdvTGGMAGKIEELLELARRGIEVYIFNGDKPENLYRALLGNFIGT 250
|
|
| COG1608 |
COG1608 |
Isopentenyl phosphate kinase [Lipid transport and metabolism]; |
178-334 |
2.18e-12 |
|
Isopentenyl phosphate kinase [Lipid transport and metabolism];
Pssm-ID: 441216 [Multi-domain] Cd Length: 254 Bit Score: 67.94 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 178 FYNEETRNNLFCT--LSELISLNIVPIINtNDAVSppmfirDDEpaggarRGIPIKDNDSLSAMLAAEVQADLLILMSDV 255
Cdd:COG1608 105 AVRDNGRILSFDTepIKEMLEEGFVPVLH-GDVVF------DAE------RGFTILSGDEIVVYLAKELKPERVGLATDV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 256 DGIYNKPPwedGAKLMHTYTSDDSNSIEFGKKSKVG---TGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKV 332
Cdd:COG1608 172 DGVYDDDP---KGKLIPEITRSNFDEVLDALGGSAGtdvTGGMAGKVEELLELAKPGVEVYIFNGNKPGNLSAALRGEEV 248
|
...
gi 21357643 333 -GT 334
Cdd:COG1608 249 rGT 251
|
|
| IPPK_Arch |
NF040647 |
isopentenyl phosphate kinase; |
240-336 |
8.63e-12 |
|
isopentenyl phosphate kinase;
Pssm-ID: 468614 [Multi-domain] Cd Length: 258 Bit Score: 66.08 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 240 LAAEVQADLLILMSDVDGIYNK-PPWEDGAKLMHTYTS-DDSNSIEFGKKSKVgTGGMDSKVKAATWALDRGVSVVICNG 317
Cdd:NF040647 160 LAKKLKPDRVILGSDVDGVYDKnPKKYPDAKLIDKVNSlDDLESLEGTNNVDV-TGGMYGKVKELLKLAELGIESYIING 238
|
90 100
....*....|....*....|
gi 21357643 318 MQEKAIKTIIGGRKV-GTFF 336
Cdd:NF040647 239 NKPENIYKALGGEKViGTVI 258
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
191-334 |
1.42e-11 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 65.69 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 191 LSELISLNIVPIintndaVSPPMFirDDEpaggarrGIPIK-DNDSLSAMLAAEVQADLLILMSDVDGIYNKPPweDGAK 269
Cdd:PRK14058 142 LKLLLKAGYLPV------VAPPAL--SEE-------GEPLNvDGDRAAAAIAGALKAEALVLLSDVPGLLRDPP--DEGS 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357643 270 LMHTYTSDdsnsiEFGKKSKVGTGGMDSKVKAATWALDRGVS-VVICNGMQEKAIKTIIGGRkvGT 334
Cdd:PRK14058 205 LIERITPE-----EAEELSKAAGGGMKKKVLMAAEAVEGGVGrVIIADANVDDPISAALAGE--GT 263
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
234-334 |
1.95e-11 |
|
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: 64.84 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYnkppwEDGAKLMHTYTSDDSNSIefgKKSKVGTGGMDSKVKAATWALDRGV-SV 312
Cdd:cd04238 160 DTAAGAIAAALKAEKLILLTDVPGVL-----DDPGSLISELTPKEAEEL---IEDGVISGGMIPKVEAALEALEGGVrKV 231
|
90 100
....*....|....*....|...
gi 21357643 313 VICNGMQEKAIKTIIGGRK-VGT 334
Cdd:cd04238 232 HIIDGRVPHSLLLELFTDEgIGT 254
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
355-648 |
3.58e-11 |
|
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: 66.08 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 355 ARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDlaeaqksgLAKPLlsrlslnPAKLKNLSVGLKQI---AE 431
Cdd:cd07078 7 ARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLE--------TGKPI-------EEALGEVARAADTFryyAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 432 DSHKNVGRVLRRTRLADQLELKQvtVPIGVLLVI----FesrPDSLP--QVAAlAMASANGLLLKGGKEAAHSNKALMEL 505
Cdd:cd07078 72 LARRLHGEVIPSPDPGELAIVRR--EPLGVVGAItpwnF---PLLLAawKLAP-ALAAGNTVVLKPSELTPLTALLLAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 506 VKEALATVGaehAVSLVS-TREEISDLLSMENHIDLIIPRGSSDLVRSIQQ---QSLhIPV---LGhaeGVCHVYIDRDA 578
Cdd:cd07078 146 LAEAGLPPG---VLNVVTgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRaaaENL-KRVtleLG---GKSPLIVFDDA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357643 579 DLEKAL-RIARDAKCDYPAACNAMETLLIHEDlmsgaIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPAAK 648
Cdd:cd07078 219 DLDAAVkGAVFGAFGNAGQVCTAASRLLVHES-----IYDEFVERLVERVKALKVGNPLDPDTDMGPLISA 284
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
341-610 |
2.18e-09 |
|
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: 60.52 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 341 ESANAVPVEVMAENARTGSRQMQALTPAQRASAVNTLADLLVSREkfilDANAKDLA-EAQKsglakpllsrlslnPAKL 419
Cdd:cd07094 16 PADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRA----EEFAKIIAcEGGK--------------PIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 420 KNLSV-----GLKQIAEDSHKNVGRVL-------RRTRLAdqlelkqVTV--PIGVLLVIFE-SRPDSLPQV-AALAMAS 483
Cdd:cd07094 78 ARVEVdraidTLRLAAEEAERIRGEEIpldatqgSDNRLA-------WTIrePVGVVLAITPfNFPLNLVAHkLAPAIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 484 ANGLLLKGGKEAAHSNKALMELVKEALATVGAEHAVslVSTREEISDLLSMENHIDLIIPRGSSDLVRSIQQQSLHIPVL 563
Cdd:cd07094 151 GCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVV--TGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 21357643 564 GHAEGVCHVYIDRDADLEKALRIARDAKCDYPA-ACNAMETLLIHEDL 610
Cdd:cd07094 229 LELGGNAPVIVDRDADLDAAIEALAKGGFYHAGqVCISVQRIYVHEEL 276
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
58-334 |
1.05e-08 |
|
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays 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 kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, 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 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. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239772 [Multi-domain] Cd Length: 229 Bit Score: 56.39 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 58 RLVVKLGSAVITrEDNHGLALGRLASIVEQVAECHLEGREVMMVT-SGAVAFGKQKLAqellmslsmretlnpkdsKEFD 136
Cdd:cd04239 1 RIVLKLSGEALA-GEGGGIDPEVLKEIAREIKEVVDLGVEVAIVVgGGNIARGYIAAA------------------RGMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 137 GATLEPRAAAAVGQSGLMsLYDAMfAQYGVKiAQVLVTKPDFYNEETRNnlFCTLSELISLNIVPIIntndavsppmfir 216
Cdd:cd04239 62 RATADYIGMLATVMNALA-LQDAL-EKLGVK-TRVMSAIPMQGVAEPYI--RRRAIRHLEKGRIVIF------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 217 ddepAGGArrGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDSNSIEfgkkSKVgtggM 295
Cdd:cd04239 124 ----GGGT--GNPGFTTDTAAALRAEEIGADVLLKATNVDGVYDADPKKNpDAKKYDRISYDELLKKG----LKV----M 189
|
250 260 270
....*....|....*....|....*....|....*....
gi 21357643 296 DSkvKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGT 334
Cdd:cd04239 190 DA--TALTLCRRNKIPIIVFNGLKPGNLLRALKGEHVGT 226
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
209-329 |
1.14e-08 |
|
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: 56.61 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 209 VSPPMFirddepaggARRGIPIK-DNDSLSAMLAAEVQADLLILMSDVDGIYnkppwEDGAKLMHTYTSDDSNSIEfgkk 287
Cdd:cd04251 150 VSPVAY---------SEEGEPLNvDGDRAAAAIAAALKAERLILLTDVEGLY-----LDGRVIERITVSDAESLLE---- 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 21357643 288 sKVGtGGMDSKVKAATWALDRGVS-VVICNGMQEKAIKTIIGG 329
Cdd:cd04251 212 -KAG-GGMKRKLLAAAEAVEGGVReVVIGDARADSPISSALNG 252
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
234-317 |
2.11e-08 |
|
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 56.36 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYNKppWEDGAKLMHTYTSDDSNSIefgKKSKVGTGGMDSKVKAATWALDRGV-SV 312
Cdd:cd04250 180 DTAAGAIAAALKAEKLILLTDVAGVLDD--PNDPGSLISEISLKEAEEL---IADGIISGGMIPKVEACIEALEGGVkAA 254
|
....*
gi 21357643 313 VICNG 317
Cdd:cd04250 255 HIIDG 259
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
343-609 |
3.40e-07 |
|
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: 53.30 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 343 ANAVPVEVMAENARTGSRQMQALTPAQRASAVNTLADLLvsrekfilDANAKDLAEAQKSGLAKPL-LSRLSLNPAKLKn 421
Cdd:pfam00171 26 ATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLL--------EERKDELAELETLENGKPLaEARGEVDRAIDV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 422 lsvgLKQIAEDSHKNVGRVLRRTRLADQLELKQvtvPIGVLLVI--FESrPDSLP--QVAAlAMASANGLLLKGGKEAAH 497
Cdd:pfam00171 97 ----LRYYAGLARRLDGETLPSDPGRLAYTRRE---PLGVVGAItpWNF-PLLLPawKIAP-ALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 498 SNKALMELVKEALATVGaehAVSLVSTR-EEISDLLSMENHIDLIIPRGSSDLVRSIQQQS--LHIPV---LGhaeGVCH 571
Cdd:pfam00171 168 TALLLAELFEEAGLPAG---VLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAaqNLKRVtleLG---GKNP 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 21357643 572 VYIDRDADLEKALRIARDAKCDYP-AACNAMETLLIHED 609
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAgQVCTATSRLLVHES 280
|
|
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
240-334 |
5.00e-07 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 52.03 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 240 LAAEVQADLLILMSDVDGIYNKPpwedgAKLMHTYTSDDsnsIEFGKKSKVGTGGMDSKVKAATWALDRGV-SVVICNGM 318
Cdd:PRK00942 190 IAAALGAEKLILLTDVPGVLDDK-----GQLISELTASE---AEELIEDGVITGGMIPKVEAALDAARGGVrSVHIIDGR 261
|
90
....*....|....*..
gi 21357643 319 QEKAIKT-IIGGRKVGT 334
Cdd:PRK00942 262 VPHALLLeLFTDEGIGT 278
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
240-323 |
7.50e-07 |
|
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: 51.57 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 240 LAAEVQADLLILMSDVDGIYNKPpwedgAKLMHTYTSDDSNSIefgKKSKVGTGGMDSKVKAATWALDRGV-SVVICNGM 318
Cdd:COG0548 192 IAAALKAEKLILLTDVPGVLDDP-----GSLISELTAAEAEEL---IADGVISGGMIPKLEAALDAVRGGVkRVHIIDGR 263
|
....*
gi 21357643 319 QEKAI 323
Cdd:COG0548 264 VPHAL 268
|
|
| PRK12354 |
PRK12354 |
carbamate kinase; Reviewed |
221-302 |
6.23e-05 |
|
carbamate kinase; Reviewed
Pssm-ID: 183466 Cd Length: 307 Bit Score: 45.59 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 221 AGGArrGIPIK--------------DNDSLSAMLAAEVQADLLILMSDVDGIY---NKPpwedGAKLMHTYTSDDSNSIE 283
Cdd:PRK12354 181 AGGG--GIPVVydadgklhgveaviDKDLAAALLAEQLDADLLLILTDVDAVYldwGKP----TQRAIAQATPDELRELG 254
|
90
....*....|....*....
gi 21357643 284 FGKkskvgtGGMDSKVKAA 302
Cdd:PRK12354 255 FAA------GSMGPKVEAA 267
|
|
| PyrH |
COG0528 |
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ... |
234-334 |
6.35e-05 |
|
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440294 [Multi-domain] Cd Length: 238 Bit Score: 45.01 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDsnSIEfgKKSKVgtggMDSkvKAATWALDRGVSV 312
Cdd:COG0528 143 DTAAALRAIEIGADVLLKATKVDGVYDADPKKNpDAKKYDRLTYDE--VLA--KGLKV----MDA--TAFSLCRDNNLPI 212
|
90 100
....*....|....*....|..
gi 21357643 313 VICNGMQEKAIKTIIGGRKVGT 334
Cdd:COG0528 213 IVFNMNKPGNLLRAVLGEKIGT 234
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
355-629 |
7.54e-05 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 46.08 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 355 ARTGSRQMQALTPAQRASAVNTLADLLVSREKFIL------DANAKDLAE------AQKSGLAKpLLSRLSLNPAKLKNL 422
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAagavlvTGKGWMFAEnicgdqVQLRARAF-VIYSYRIPHEPGNHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 423 SVGLKQiaeDSHKnvgrvlrrtrladqlelkqVTVPIGVLLVIFESR-PDS--LPQVAAlAMASANGLLLKGGKEAAHSN 499
Cdd:cd07084 87 GQGLKQ---QSHG-------------------YRWPYGPVLVIGAFNfPLWipLLQLAG-ALAMGNPVIVKPHTAVSIVM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 500 KALMELVKEALATVGAehAVSLVSTREEISDLLSMENHIDLIIPRGSSDLVRSIQQQSLHIPVLGHAEGVCHVYIDRDAD 579
Cdd:cd07084 144 QIMVRLLHYAGLLPPE--DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQ 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 21357643 580 LEKAL--RIARDAKCDYPAACNAMETLLIHEDLMSGAIFGDVCNMLKREGVK 629
Cdd:cd07084 222 AVDYVawQCVQDMTACSGQKCTAQSMLFVPENWSKTPLVEKLKALLARRKLE 273
|
|
| PRK12353 |
PRK12353 |
putative amino acid kinase; Reviewed |
221-302 |
1.68e-04 |
|
putative amino acid kinase; Reviewed
Pssm-ID: 237071 Cd Length: 314 Bit Score: 44.38 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 221 AGGArrGIP-IKDNDSL------------SAMLAAEVQADLLILMSDVDGI---YNKPpwedGAKLMHTYTSDDS----N 280
Cdd:PRK12353 191 AGGG--GIPvIREGGGLkgveavidkdfaSAKLAELVDADLLIILTAVDKVyinFGKP----NQKKLDEVTVSEAekyiE 264
|
90 100
....*....|....*....|..
gi 21357643 281 SIEFGKkskvgtGGMDSKVKAA 302
Cdd:PRK12353 265 EGQFAP------GSMLPKVEAA 280
|
|
| AAK_CK |
cd04235 |
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
221-302 |
1.69e-04 |
|
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: 44.42 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 221 AGGArrGIP-IKDNDSL------------SAMLAAEVQADLLILMSDVDGIY---NKPpweDGAKLMHTYTSDDSNSIEF 284
Cdd:cd04235 187 AGGG--GIPvVREGGGLkgveavidkdlaSALLAEEINADLLVILTDVDNVYinfGKP---NQKALEQVTVEELEKYIEE 261
|
90
....*....|....*...
gi 21357643 285 GKKSKvgtGGMDSKVKAA 302
Cdd:cd04235 262 GQFAP---GSMGPKVEAA 276
|
|
| AAK_UMPK-PyrH-Ec |
cd04254 |
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ... |
234-334 |
2.56e-04 |
|
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays 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 E. coli (Ec) 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 and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs 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: 239787 [Multi-domain] Cd Length: 231 Bit Score: 43.25 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDSNSiefgKKSKVgtggMDSkvKAATWALDRGVSV 312
Cdd:cd04254 137 DTAAALRAIEINADVILKATKVDGVYDADPKKNpNAKRYDHLTYDEVLS----KGLKV----MDA--TAFTLCRDNNLPI 206
|
90 100
....*....|....*....|..
gi 21357643 313 VICNGMQEKAIKTIIGGRKVGT 334
Cdd:cd04254 207 VVFNINEPGNLLKAVKGEGVGT 228
|
|
| AAK_UMPK-PyrH-Pf |
cd04253 |
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
234-337 |
6.92e-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: 41.85 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYNKPPWED-GAKLMHTYTSDDSNSIEFGKKSKVGTGG-MDskVKAATWALDRGVS 311
Cdd:cd04253 118 DAVAALLAERLGADLLINATNVDGVYSKDPRKDpDAKKFDRLSADELIDIVGKSSWKAGSNEpFD--PLAAKIIERSGIK 195
|
90 100
....*....|....*....|....*.
gi 21357643 312 VVICNGMQEKAIKTIIGGRKVGTFFT 337
Cdd:cd04253 196 TIVVDGRDPENLERALKGEFVGTIIE 221
|
|
| PRK12454 |
PRK12454 |
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
221-334 |
1.55e-03 |
|
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed
Pssm-ID: 183535 Cd Length: 313 Bit Score: 41.52 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 221 AGGArrGIPIK-------------DNDSLSAMLAAEVQADLLILMSDVDGI---YNKP--PWEDGAKLmhtytsddSNSI 282
Cdd:PRK12454 191 SGGG--GIPVIeedgelkgveaviDKDLASELLAEELNADIFIILTDVEKVylnYGKPdqKPLDKVTV--------EEAK 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 21357643 283 EFGKKSKVGTGGMDSKVKAAT-WALDRGVSVVIcnGMQEKAIKTIIGgrKVGT 334
Cdd:PRK12454 261 KYYEEGHFKAGSMGPKILAAIrFVENGGKRAII--ASLEKAVEALEG--KTGT 309
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
341-610 |
2.35e-03 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 41.16 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 341 ESANAVPVEVMAENARtGSRQ--MQALTPAQRAsaVNTLADLLVS-REKFILDAnaKDLAEAQKSGLAkPLLSRLSLNPA 417
Cdd:cd07150 2 DDLNPADGSVYARVAV-GSRQdaERAIAAAYDA--FPAWAATTPSeRERILLKA--AEIMERRADDLI-DLLIDEGGSTY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 418 KLKNLSVG-----LKQIAEDSHKNVGRVLRrtrlADQLELKQVTV--PIGVLLVIfesRPDSLPQV-----AALAMASAN 485
Cdd:cd07150 76 GKAWFETTftpelLRAAAGECRRVRGETLP----SDSPGTVSMSVrrPLGVVAGI---TPFNYPLIlatkkVAFALAAGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 486 GLLLKGGKEAAHSNKALMELVKEAlatvGAEHAVSLVST--REEISDLLSMENHIDLIIPRGSSDLVRSIQQQS--LHIP 561
Cdd:cd07150 149 TVVLKPSEETPVIGLKIAEIMEEA----GLPKGVFNVVTggGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAgrHLKK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 21357643 562 V---LGhaeGVCHVYIDRDADLEKALRIA-RDAKCDYPAACNAMETLLIHEDL 610
Cdd:cd07150 225 ItleLG---GKNPLIVLADADLDYAVRAAaFGAFMHQGQICMSASRIIVEEPV 274
|
|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
215-262 |
2.62e-03 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 40.83 E-value: 2.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 21357643 215 IRDDepaGGARRGIP--IkDNDSLSAMLAAEVQADLLILMSDVDGIY---NKP 262
Cdd:COG0549 198 VRDE---DGGLKGVEavI-DKDLASALLAEELDADLLLILTDVDKVYinfGKP 246
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
234-329 |
5.17e-03 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 39.67 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 234 DSLSAMLAAEVQADLLILMSDVDGIYnkppwEDGAKLMHTYTSDDSNSIEFGKKSKVGTGGMDSKVKAATWALDRGV-SV 312
Cdd:PLN02512 208 DTAAGEIAAALGAEKLILLTDVAGVL-----EDKDDPGSLVKELDIKGVRKLIADGKIAGGMIPKVECCVRSLAQGVkTA 282
|
90 100
....*....|....*....|....*..
gi 21357643 313 VICNG----------MQEKAIKTIIGG 329
Cdd:PLN02512 283 HIIDGrvphsllleiLTDEGAGTMITG 309
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
329-618 |
8.95e-03 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 39.17 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 329 GRKVGTFfteatESANAVPVEVMAENARTGSRQMQALTPAQRASAVNTLADLLvsrekfilDANAKDLAEAqksglakpl 408
Cdd:cd07088 23 GEVVATV-----PAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLI--------RENADELAKL--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 409 lsrLSLNPAKLKNLSVG--------LKQIAEDSHKNVGRVLRRTRLADQLELKQVtvPIGVLLVIFesrPDSLP-----Q 475
Cdd:cd07088 81 ---IVEEQGKTLSLARVeveftadyIDYMAEWARRIEGEIIPSDRPNENIFIFKV--PIGVVAGIL---PWNFPffliaR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 476 VAALAMASANGLLLKGGKEAAHSNKALMELVKEALATVGAehaVSLVSTR-EEISDLLSMENHIDLIIPRGSSDLVRSI- 553
Cdd:cd07088 153 KLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGV---LNIVTGRgSVVGDALVAHPKVGMISLTGSTEAGQKIm 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357643 554 QQQSLHI-PV---LGhaeGVCHVYIDRDADLEKALRIARDAKCDYPA-ACNAMETLLIHEDL-----------MSGAIFG 617
Cdd:cd07088 230 EAAAENItKVsleLG---GKAPAIVMKDADLDLAVKAIVDSRIINCGqVCTCAERVYVHEDIydefmeklvekMKAVKVG 306
|
.
gi 21357643 618 D 618
Cdd:cd07088 307 D 307
|
|
| |
