|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
459-967 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 760.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 459 FVNAANSDYARASQREAIQAALIHVHRQLGQTYTPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKA 538
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 539 AQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRNFPGETN 618
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 619 HYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYL 698
Cdd:cd07124 161 RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 699 TQHPDVHLIAFTGSQEVGCRIIAEAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSR 778
Cdd:cd07124 241 VEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 779 VIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEM---GYFVSPTIF 855
Cdd:cd07124 321 VIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELaaeGYFVQPTIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 856 TNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQP 935
Cdd:cd07124 401 ADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQP 480
|
490 500 510
....*....|....*....|....*....|..
gi 22294137 936 FGGFKLSGIGSKAGGRDYLLQFLEPRVITENV 967
Cdd:cd07124 481 FGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
461-966 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 680.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 461 NAANSDYARASQREAIQAALIHVHRQLGQTYTPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQ 540
Cdd:TIGR01237 3 HEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 541 AQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRN-FPGETNH 619
Cdd:TIGR01237 83 EAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNsREGETNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 620 YHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLT 699
Cdd:TIGR01237 163 YVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 700 QHPDVHLIAFTGSQEVGCRIIAEAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRV 779
Cdd:TIGR01237 243 DHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 780 IVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS-VPVPEMGYFVSPTIFTNV 858
Cdd:TIGR01237 323 VVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGgCGDDSKGYFIGPTIFADV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 859 PPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGG 938
Cdd:TIGR01237 403 DRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGG 482
|
490 500
....*....|....*....|....*...
gi 22294137 939 FKLSGIGSKAGGRDYLLQFLEPRVITEN 966
Cdd:TIGR01237 483 FKMSGTDSKAGGPDYLALFMQAKTVTEM 510
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
465-965 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 645.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 465 SDYARASQREAIQAALIHVHRQLGQTYTPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQ 544
Cdd:PRK03137 11 TDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 545 QTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSG---YDRnfPGETNHYH 621
Cdd:PRK03137 91 KWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGkpvESR--PGEHNRYF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 622 YQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQH 701
Cdd:PRK03137 169 YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDVHLIAFTGSQEVGCRIIAEAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIV 781
Cdd:PRK03137 249 PKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 782 LESIYKPFVERLVAATQSLNIGPAHLPsTRVGPVVTAAARDRIQEYIAKGQQEAELLL-SVPVPEMGYFVSPTIFTNVPP 860
Cdd:PRK03137 329 HEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEGRLVLgGEGDDSKGYFIQPTIFADVDP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 861 TATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFK 940
Cdd:PRK03137 408 KARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFN 487
|
490 500
....*....|....*....|....*
gi 22294137 941 LSGIGSKAGGRDYLLQFLEPRVITE 965
Cdd:PRK03137 488 MSGTDSKAGGPDYLLLFLQAKTVSE 512
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
117-971 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 564.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 117 LAHKYIAGETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYCDRYLDLMEHL------SPLGQREGVnpvqvSVK 190
Cdd:PRK11904 176 MGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIgraaggADLPARPGI-----SIK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 191 LTAFYSQFDPldvsGCRAKV-GE--P-IRRLLHRAQELGVAVHFDMEQYAYKDITLAILKDILLEPEFRDRADIGLTLQA 266
Cdd:PRK11904 251 LSALHPRYEA----AQRERVlAElvPrVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 267 YlrdsyQD-AQDLITWV----QQRGTPITVRVVKGAYWDQELIKAVQHHWP-LPVYQHKQNTDANFERIIELLLSHHTVL 340
Cdd:PRK11904 327 Y-----QKrALPVLDWLadlaRRQGRRIPVRLVKGAYWDSEIKRAQELGLPgYPVFTRKAATDVSYLACARKLLSARGAI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 341 RTAIASHNVRSQARAIAIAQRQHIpptamECQVLYGMADKLAKALVEA-GQTVRVYCPYG---DLIPgmaYLIRRLLENT 416
Cdd:PRK11904 402 YPQFATHNAHTVAAILEMAGHRGF-----EFQRLHGMGEALYDALLDApGIPCRIYAPVGshkDLLP---YLVRRLLENG 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 417 ANSSFLRQQLGA-VAIEELLAPPEPTA-DFEA---------VNVHLTTGKTSTFVNAANSdyaraSQREAIQAAlIHVHR 485
Cdd:PRK11904 474 ANSSFVHRLVDPdVPIEELVADPVEKLrSFETlpnpkiplpRDIFGPERKNSKGLNLNDR-----SELEPLAAA-IAAFL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 486 QLGQTYTPIINGDRvnprEYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQ 565
Cdd:PRK11904 548 EKQWQAGPIINGEG----EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEAN 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 566 RHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSS------GYDrnfpGETNHYHYQGRGLAVVISPWNFPLA 639
Cdd:PRK11904 624 RAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGapeklpGPT----GESNELRLHGRGVFVCISPWNFPLA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 640 IPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRI 719
Cdd:PRK11904 700 IFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETA-RI 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 720 IAEAavLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACsRVIVL-ESIYKPFVERLVAATQ 798
Cdd:PRK11904 779 INRT--LAARDGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSAL-RVLFVqEDIADRVIEMLKGAMA 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 799 SLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVP---EMGYFVSPTIFTnvppTATIAQ--EEIFGPV 873
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPagtENGHFVAPTAFE----IDSISQleREVFGPI 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 874 LAVLR--AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSKAGGR 951
Cdd:PRK11904 932 LHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGP 1011
|
890 900
....*....|....*....|
gi 22294137 952 DYLLQFLEPRVITENVQRQG 971
Cdd:PRK11904 1012 HYLLRFATEKTVTVNTTAAG 1031
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
489-966 |
1.56e-178 |
|
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: 527.00 E-value: 1.56e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 489 QTYTPIINGDRVNPR--EYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQR 566
Cdd:COG1012 4 PEYPLFIGGEWVAAAsgETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 567 HELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRN-FPGETNHYHYQGRGLAVVISPWNFPLAIPTGMT 645
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 646 AAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAv 725
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 726 lqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPA 805
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 806 HLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL--SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETF 882
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEgAELLTggRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 883 TQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAiVDRQPFGGFKLSGIGSKaGGRDYLLQFLEPRV 962
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
....
gi 22294137 963 ITEN 966
Cdd:COG1012 475 VTIR 478
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
457-971 |
1.81e-178 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 528.30 E-value: 1.81e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 457 STFVNAANSDYARAsqrEAIQAALIHVHRQLGQTYtPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAA 536
Cdd:cd07125 3 SSFVNRIFDLEVPL---EALADALKAFDEKEWEAI-PIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 537 KAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRNFP-G 615
Cdd:cd07125 79 AAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPtG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 616 ETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIG 695
Cdd:cd07125 159 ELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 696 PYLTQHPDVHLIAFTGSQEVGCRIiaeAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSA 775
Cdd:cd07125 239 EALVAHPRIDGVIFTGSTETAKLI---NRALAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 776 CSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEM-GYFVSPTI 854
Cdd:cd07125 316 LRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGnGYFVAPGI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 855 FTNVppTATIAQEEIFGPVLAVLRAETFT--QALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVD 932
Cdd:cd07125 396 IEIV--GIFDLTTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVG 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 22294137 933 RQPFGGFKLSGIGSKAGGRDYLLQFLEPRVITENVQRQG 971
Cdd:cd07125 474 RQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTAAG 512
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
507-963 |
6.05e-168 |
|
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: 498.98 E-value: 6.05e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSqPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:pfam00171 10 EVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVV 666
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 667 AAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAI 746
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA------QNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 747 IIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQE 826
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 827 YIAKGQQE-AELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRT 904
Cdd:pfam00171 323 YVEDAKEEgAKLLTgGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22294137 905 PSHIQQAKAQFAVGNLYINRGITGAIVDRqPFGGFKLSGIGsKAGGRDYLLQFLEPRVI 963
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
5-977 |
4.35e-166 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 511.90 E-value: 4.35e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 5 YEAETIAIARQLWAASQEsrnffsqlrEQMRIEDKLLGWAMEHPGLRVQLFRLIDCLPSLRSQTEVARHLQEYLSDPSVE 84
Cdd:COG0506 9 LRARAVALARRLVEAIRA---------APEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 85 LPPGLKKLLNFAQPDSLPAQAAATTFTTAVQALAHKYIAGETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYCD 164
Cdd:COG0506 80 LVNASTWGLMLTLVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 165 RYLDLMEHLSplgqREGVNPVQVSVKLTAFYSQFDPLDVSGCRAKVGEPIRRLLHRAQELGVAVHFDMEQYAYKDITLAI 244
Cdd:COG0506 160 AYLEALEAIG----AAGVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 245 LKDILLEPEFRDRADIGLTLQAYLRDSYQDAQDLITWVQQRGTPITVRVVKGAYWDQELIKAVQHHWPLPVYQHKQNTDA 324
Cdd:COG0506 236 FERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 325 NFERIIELLLSHHTVLRTAIASHNVRSQARAIAIAQRQHIPPTAMECQVLYGMADKLAKALV-EAGQTVRVYCPYGDLIP 403
Cdd:COG0506 316 NYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERGRPPDRFEFQMLYGMGEDLQRALAaVDGGRLLLYCPVVAPVG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 404 GMAYLIRRLLENTANSSFLRQQLGAVAIEELLAPPEPTADFEAVNVHLTTGKTST-------FVNAANSDYARASQREAI 476
Cdd:COG0506 396 GDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPplrrqrrRRRRARGGALAAALAAAA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 477 QAALIHVHRQLGQTYTPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLR 556
Cdd:COG0506 476 AAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 557 RAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGRGLAVVISPWNF 636
Cdd:COG0506 556 AAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 637 PLAIPTGMTAAALVTGNCTILkpadpaavvaaKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVG 716
Cdd:COG0506 636 AAAAAAAAAAAAAAAAAAAAA-----------AAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 717 CRIIAEAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIY---------K 787
Cdd:COG0506 705 AAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLalllldadlV 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 788 PFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATIAQE 867
Cdd:COG0506 785 ILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVL 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 868 EIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSK 947
Cdd:COG0506 865 LEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 944
|
970 980 990
....*....|....*....|....*....|
gi 22294137 948 AGGRDYLLQFLEPRVITENVQRQGFAPIAG 977
Cdd:COG0506 945 GGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
121-960 |
1.59e-156 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 493.23 E-value: 1.59e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 121 YIAGETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYcdrYLDLMEHLSPLGQR---EGV--NPvQVSVKLTAFY 195
Cdd:PRK11905 179 FVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERY---YRDYERAIHAIGKAatgRGVydGP-GISVKLSALH 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 196 SQFdpldvsgCRAKVGEPIRRLLHRAQEL-------GVAVHFDMEQYAYKDITLAILKDILLEPEFRDRADIGLTLQAYL 268
Cdd:PRK11905 255 PRY-------ERAQRERVMAELLPRLKALallakayDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQAYQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 269 RDsyqdAQDLITWV----QQRGTPITVRVVKGAYWDQElIKAVQ----HHWPlpVYQHKQNTDANFERIIELLLSHHTVL 340
Cdd:PRK11905 328 KR----CPFVIDYLidlaRRSGRRLMVRLVKGAYWDAE-IKRAQvdglEGFP--VFTRKVHTDVSYIACARKLLAARDVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 341 RTAIASHNVRSQARAIAIAQrqhiPPTAMECQVLYGMADKLAKALVEAGQT---VRVYCPYG---DLipgMAYLIRRLLE 414
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAG----GKGDFEFQCLHGMGEPLYDQVVGKEKLgrpCRIYAPVGtheTL---LAYLVRRLLE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 415 NTANSSFLRQQL-GAVAIEELLAPPEPTADFEAVNVHLTTGKTSTFVNAA--NS---DYARASQREAIQAALIhVHRQLG 488
Cdd:PRK11905 474 NGANSSFVNRIVdENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPErrNSkglDLSDEATLAALDEALN-AFAAKT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 489 QTYTPIINGDRVnPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHE 568
Cdd:PRK11905 553 WHAAPLLAGGDV-DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 569 LVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRnfpgetnhyhyQGRGLAVVISPWNFPLAIPTGMTAAA 648
Cdd:PRK11905 632 LFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGH-----------KPLGPVVCISPWNFPLAIFTGQIAAA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 649 LVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAeAAVLQR 728
Cdd:PRK11905 701 LVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVA-RLIQ-RTLAKR 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 729 GQSHIKrVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACsRVIVL-ESIYKPFVERLVAATQSLNIG-PAH 806
Cdd:PRK11905 779 SGPPVP-LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVLCLqEDVADRVLTMLKGAMDELRIGdPWR 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 807 LpSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVP---EMGYFVSPTIFTnvppTATIAQ--EEIFGPVLAVLR--A 879
Cdd:PRK11905 857 L-STDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPaetEKGTFVAPTLIE----IDSISDleREVFGPVLHVVRfkA 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 880 ETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSKAGGRDYLLQFLE 959
Cdd:PRK11905 932 DELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVR 1011
|
.
gi 22294137 960 P 960
Cdd:PRK11905 1012 E 1012
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
473-966 |
8.98e-152 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 458.58 E-value: 8.98e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 473 REAIQAALIHVHRQLGQTYTPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERA 552
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 553 TLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYD--RNFPGETNHYHYQGRGLAVV 630
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVevVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 631 ISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFT 710
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 711 GSQEVGCRIIAEAAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFV 790
Cdd:cd07083 241 GSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 791 ERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPE-MGYFVSPTIFTNVPPTATIAQEEI 869
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 870 FGPVLAVLR--AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSK 947
Cdd:cd07083 401 FGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAK 480
|
490
....*....|....*....
gi 22294137 948 AGGRDYLLQFLEPRVITEN 966
Cdd:cd07083 481 TGGPHYLRRFLEMKAVAER 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
124-971 |
1.34e-144 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 460.56 E-value: 1.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 124 GETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYCDRYLDLMEH-----LSPLGQREGVNPVQVSVKLTAFYSQF 198
Cdd:COG4230 183 GFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAaiaaaGGGSGGPGPSISSSLSVLLSARHPRY 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 199 DPLDvsgcRAKVGEPIRRLLHRAQELGVAVHFDMEQYAYKDITLAILKDILLEPEFRDRADIGLTLQAYLRDSYQDAQDL 278
Cdd:COG4230 263 RRRR----EERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAKALLLV 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 279 ITWVQQRGTPITVRVVKGAYWDQELIKAVQHHWPL-----PVYQHKQNTDANFERIIELLLSHHTVLRTAIASHNVrsqa 353
Cdd:COG4230 339 LDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLgyvvyPVTTRKVLYDAAALALALLLLAAQPAFAPQFATHAA---- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 354 rAIAIAQRQHIPPTAMECQVLYGMADKLAKALVEA--GQTVRVYCPYG---DLipgMAYLIRRLLENTANSSFLRQQL-G 427
Cdd:COG4230 415 -ATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVGRGklGRPCRIYAPVGsheDL---LAYLVRRLLENGANSSFVNRIAdE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 428 AVAIEELLAPPeptadFEAVnvhlttGKTSTFVNAA-------------NS---DYARASQREAIQAALihvHRQLGQTY 491
Cdd:COG4230 491 DVPVEELIADP-----VEKA------RALGGAPHPRiplprdlygperrNSaglDLSDEAVLAALSAAL---AAAAEKQW 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 492 --TPIINGDrVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHEL 569
Cdd:COG4230 557 qaAPLIAGE-AASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 570 VAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSgydrnfpgetNHYHYQGRGLAVVISPWNFPLAIPTGMTAAAL 649
Cdd:COG4230 636 MALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 650 VTGNCTIlkpadpaavvaAKLAE-----------ILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcR 718
Cdd:COG4230 706 AAGNTVL-----------AKPAEqtpliaaravrLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETA-R 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 719 IIAeAAVLQRgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACsRVIVL-ESIYKPFVERLVAAT 797
Cdd:COG4230 774 LIN-RTLAAR-DGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSAL-RVLCVqEDIADRVLEMLKGAM 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 798 QSLNIG-PAHLpSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEM---GYFVSPTIFTnvppTATIAQ--EEIFG 871
Cdd:COG4230 851 AELRVGdPADL-STDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEEcanGTFVAPTLIE----IDSISDleREVFG 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 872 PVLAVLR--AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSKAG 949
Cdd:COG4230 926 PVLHVVRykADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAG 1005
|
890 900
....*....|....*....|..
gi 22294137 950 GRDYLLQFLEPRVITENVQRQG 971
Cdd:COG4230 1006 GPHYLLRFATERTVTVNTTAAG 1027
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
546-965 |
9.02e-144 |
|
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: 435.48 E-value: 9.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSG-YDRNFPGETNHYHYQG 624
Cdd:cd07078 17 LPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEvIPSPDPGELAIVRREP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDV 704
Cdd:cd07078 97 LGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 HLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:cd07078 177 DKISFTGSTAVG-KAIMRAA-----AENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL--SVPVPEMGYFVSPTIFTNVPPT 861
Cdd:cd07078 251 IYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEgAKLLCggKRLEGGKGYFVPPTVLTDVDPD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 862 ATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAiVDRQPFGGFKL 941
Cdd:cd07078 331 MPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA-EPSAPFGGVKQ 409
|
410 420
....*....|....*....|....
gi 22294137 942 SGIGsKAGGRDYLLQFLEPRVITE 965
Cdd:cd07078 410 SGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
130-424 |
4.38e-135 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 407.26 E-value: 4.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 130 VLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYCDRYLDLMEHLSPLGQREGVNP-VQVSVKLTAFYSQFDPLDVSGCRA 208
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPrPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 209 KVGEPIRRLLHRAQELGVAVHFDMEQYAYKDITLAILKDILLEPEFRDRADIGLTLQAYLRDSYQDAQDLITWVQQRGTP 288
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 289 ITVRVVKGAYWDQELIKAVQHHWPLPVYQHKQNTDANFERIIELLLSHHTVLRTAIASHNVRSQARAIAIAQRQHIPPTA 368
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEELGIPPRR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 22294137 369 MECQVLYGMADKLAKALVEAGQTVRVYCPYGDLIPGMAYLIRRLLENTANSSFLRQ 424
Cdd:pfam01619 241 FEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
495-952 |
1.80e-129 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 399.70 E-value: 1.80e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMC 574
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 575 YEVGKVVAEGDAEVSEAVDFCRYYADEMERLssgydrnfPGET------NHYHYQGR---GLAVVISPWNFPLAIPTGMT 645
Cdd:cd07097 85 REEGKTLPEARGEVTRAGQIFRYYAGEALRL--------SGETlpstrpGVEVETTReplGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 646 AAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAV 725
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVG-RRIAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 726 lqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPA 805
Cdd:cd07097 236 -----ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 806 HLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLLS---VPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAET 881
Cdd:cd07097 311 LDEGVDIGPVVSERQLEKDLRYIEIARSEgAKLVYGgerLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22294137 882 FTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGaiVDRQ-PFGGFKLSGIGSKAGGRD 952
Cdd:cd07097 391 YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEA 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
495-966 |
7.98e-122 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 379.77 E-value: 7.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVN--PREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAW 572
Cdd:cd07131 3 IGGEWVDsaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 573 MCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLssgYDRNFPGE-TNHYHY---QGRGLAVVISPWNFPLAIPTGMTAAA 648
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRL---FGETVPSElPNKDAMtrrQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 649 LVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAVlqr 728
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVG-ERIGETCA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 729 gqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLP 808
Cdd:cd07131 236 --RPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 809 STRVGPVVTAAARDRIQEYIAKGQQE-AELLL-----SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETF 882
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEgATLLLggerlTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 883 TQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVdRQPFGGFKLSGIGSKAGGRDYLLQFLEPRV 962
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTEWKA 472
|
....
gi 22294137 963 ITEN 966
Cdd:cd07131 473 VYVD 476
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
121-961 |
8.30e-121 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 399.73 E-value: 8.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 121 YIAGETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEAQQYCDRYldlMEHLSPLGQR-------EGVNpvqVSVKLTA 193
Cdd:PRK11809 259 FVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASY---EQAIHAIGKAsngrgiyEGPG---ISIKLSA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 194 FYSQFdpldvsgCRAKVGEPIRRLLHR-------AQELGVAVHFDMEQYAYKDITLAILKDILLEPEFRDRADIGLTLQA 266
Cdd:PRK11809 333 LHPRY-------SRAQYDRVMEELYPRlksltllARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 267 YLRDSYQDAQDLITWVQQRGTPITVRVVKGAYWDQElIKAVQHHW--PLPVYQHKQNTDANFERIIELLLSHHTVLRTAI 344
Cdd:PRK11809 406 YQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSE-IKRAQVDGleGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQF 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 345 ASHNVRSQAraiAIAQR--QHIPPTAMECQVLYGMADKLAKALVEA------GQTVRVYCPYGDLIPGMAYLIRRLLENT 416
Cdd:PRK11809 485 ATHNAHTLA---AIYHLagQNYYPGQYEFQCLHGMGEPLYEQVVGKvadgklNRPCRIYAPVGTHETLLAYLVRRLLENG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 417 ANSSFL-RQQLGAVAIEELLAppEPTADFEAVnvHLTTGKT---------------STFVNAANSDYARASQREAIQAAL 480
Cdd:PRK11809 562 ANTSFVnRIADTSLPLDELVA--DPVEAVEKL--AQQEGQLglphpkiplprdlygKGRANSAGLDLANEHRLASLSSAL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 481 IHVHRQLGQTyTPIInGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAAD 560
Cdd:PRK11809 638 LASAHQKWQA-APML-EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAAD 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 561 LLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERlssgydrNFPGETNhyhyqgRGLAVV--ISPWNFPL 638
Cdd:PRK11809 716 LMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD-------DFDNDTH------RPLGPVvcISPWNFPL 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 639 AIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVgcr 718
Cdd:PRK11809 783 AIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV--- 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 719 iiaeAAVLQRG-------QSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACsRVIVL-ESIYKPFV 790
Cdd:PRK11809 860 ----ARLLQRNlagrldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSAL-RVLCLqDDVADRTL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 791 ERLVAATQSLNIG-PAHLpSTRVGPVVTAAARDRIQEYI----AKGQqeaelllSVPVPEMGYFVSPTIFTNVPPT---- 861
Cdd:PRK11809 935 KMLRGAMAECRMGnPDRL-STDIGPVIDAEAKANIERHIqamrAKGR-------PVFQAARENSEDWQSGTFVPPTliel 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 862 ATIA--QEEIFGPVLAVLR--AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFG 937
Cdd:PRK11809 1007 DSFDelKREVFGPVLHVVRynRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFG 1086
|
890 900
....*....|....*....|....
gi 22294137 938 GFKLSGIGSKAGGRDYLLQFLEPR 961
Cdd:PRK11809 1087 GEGLSGTGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
495-964 |
2.07e-113 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 357.20 E-value: 2.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNP--REYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAW 572
Cdd:cd07138 3 IDGAWVAPagTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 573 MCYEVGK-VVAEGDAEVSEAVDFCRYYADEMerlssgydRNFPGET----NHYHYQGRGLAVVISPWNFPLAIPTGMTAA 647
Cdd:cd07138 82 ITLEMGApITLARAAQVGLGIGHLRAAADAL--------KDFEFEErrgnSLVVREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 648 ALVTGnCT-ILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvl 726
Cdd:cd07138 154 ALAAG-CTvVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 727 qrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAH 806
Cdd:cd07138 231 ----DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 807 LPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL---LSVPV-PEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAET 881
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEgARLVaggPGRPEgLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 882 FTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgitGAIVDRQ-PFGGFKLSGIGsKAGGRDYLLQFLEP 960
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG-REWGRYGLEEFLEV 461
|
....
gi 22294137 961 RVIT 964
Cdd:cd07138 462 KSIQ 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
546-965 |
1.34e-109 |
|
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: 343.44 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLS-SGYDRNFPGETNHYHYQG 624
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGgPELPSPDPGGEAYVRREP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDV 704
Cdd:cd06534 93 LGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 HLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:cd06534 173 DKISFTGSTAVG-KAIMKAA-----AENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVaatqslnigpahlpstrvgpvvtaaardriqeyiakgqqeaelllsvpvpemgyfvspTIFTNVPPTATI 864
Cdd:cd06534 247 IYDEFVEKLV----------------------------------------------------------TVLVDVDPDMPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 865 AQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAiVDRQPFGGFKLSGI 944
Cdd:cd06534 269 AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEAPFGGVKNSGI 347
|
410 420
....*....|....*....|.
gi 22294137 945 GSkAGGRDYLLQFLEPRVITE 965
Cdd:cd06534 348 GR-EGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
495-966 |
7.69e-109 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 345.70 E-value: 7.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGD-RVNPREYSESLNPSQPEEIVgRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWM 573
Cdd:cd07086 3 IGGEwVGSGGETFTSRNPANGEPIA-RVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 574 CYEVGKVVAEGDAEVSEAVDFCRYYADEMERLssgYDRNFPGE-TNHYHYQGR---GLAVVISPWNFPLAIPTGMTAAAL 649
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRML---YGLTIPSErPGHRLMEQWnplGVVGVITAFNFPVAVPGWNAAIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 650 VTGNCTILKPADPAAVVAAKLAEILMAA----GFPPGVFQFLPGRGSViGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAv 725
Cdd:cd07086 159 VCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVG-RRVGETV- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 726 lqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPA 805
Cdd:cd07086 236 ----ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 806 HLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL---SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAET 881
Cdd:cd07086 312 LDEGTLVGPLINQAAVEKYLNAIEIAKSQgGTVLTggkRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 882 FTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAV--GNLYINRGITGAIVDrQPFGGFKLSGIGSKAgGRDYLLQFLE 959
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNIPTSGAEIG-GAFGGEKETGGGRES-GSDAWKQYMR 469
|
....*..
gi 22294137 960 PRVITEN 966
Cdd:cd07086 470 RSTCTIN 476
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
546-964 |
3.73e-107 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 340.31 E-value: 3.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA-EVSEAVDFCRYYADemeRLSSGYDRNFPGETNHYHYQG 624
Cdd:cd07093 38 MSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFAD---YILQLDGESYPQDGGALNYVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 R---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQH 701
Cdd:cd07093 115 RqpvGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDVHLIAFTGSQEVGCRIIAEAAVlqrgqsHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIV 781
Cdd:cd07093 195 PDVDLISFTGETATGRTIMRAAAP------NLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 782 LESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLLSVPVPEM-----GYFVSPTIF 855
Cdd:cd07093 269 QRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEgATILTGGGRPELpdlegGYFVEPTVI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 856 TNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgiTGAIVD-RQ 934
Cdd:cd07093 349 TGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN---CWLVRDlRT 425
|
410 420 430
....*....|....*....|....*....|
gi 22294137 935 PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07093 426 PFGGVKASGIG-REGGDYSLEFYTELKNVC 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
509-964 |
8.00e-107 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 339.41 E-value: 8.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSqPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEV 588
Cdd:cd07103 2 INPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 589 SEAVDFCRYYADEMERLssgYDR----NFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGnCT-ILKPADPA 663
Cdd:cd07103 81 DYAASFLEWFAEEARRI---YGRtipsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAG-CTvVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 664 AVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGk 743
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 744 NA-IIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARD 822
Cdd:cd07103 230 NApFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 823 RIQEYI----AKGqqeAELLLS-VPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALT 897
Cdd:cd07103 310 KVEALVedavAKG---AKVLTGgKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22294137 898 GGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVdrQPFGGFKLSGIGSKaGGRDYLLQFLEPRVIT 964
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLGRE-GGKEGLEEYLETKYVS 450
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
507-964 |
6.89e-104 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 332.64 E-value: 6.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSQpEEIVGRVGLATIEDAEHAIRAAKA--AQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG 584
Cdd:cd07091 22 PTINPAT-EEVICQVAEADEEDVDAAVKAARAafETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 585 -DAEVSEAVDFCRYYA---DEMErlssgyDRNFPGETNHYHYQGR---GLAVVISPWNFPLAIPTGMTAAALVTGNCTIL 657
Cdd:cd07091 101 aKGDVALSIKCLRYYAgwaDKIQ------GKTIPIDGNFLAYTRRepiGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 658 KPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAvlqrGQSHIKRVI 737
Cdd:cd07091 175 KPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVG-RTIMEAA----AKSNLKKVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 738 AEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVT 817
Cdd:cd07091 250 LELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 818 AAARDRIQEYIAKGQQE-AELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYA 895
Cdd:cd07091 330 KAQFDKILSYIESGKKEgATLLTgGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYG 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 896 LTGGLYSRTPSHIQQAKAQFAVGNLYINrgiTGAIVDRQ-PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07091 410 LAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFG-RELGEEGLEEYTQVKAVT 475
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
495-963 |
4.81e-100 |
|
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: 321.91 E-value: 4.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNPR--EYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAW 572
Cdd:cd07088 2 INGEFVPSSsgETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 573 MCYEVGKVVAEGDAEVSEAVDFCRYYAD-----EMERLSSgyDRnfPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAA 647
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEwarriEGEIIPS--DR--PNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 648 ALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVlq 727
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 728 rgqsHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHL 807
Cdd:cd07088 235 ----NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 808 PSTRVGPVVTAAARDRIQEYIAKG-QQEAELLL--SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQ 884
Cdd:cd07088 311 AATDMGPLVNEAALDKVEEMVERAvEAGATLLTggKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 885 ALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIvdrQPF-GGFKLSGIGSkAGGRDYLLQFLEPRVI 963
Cdd:cd07088 391 AIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM---QGFhAGWKKSGLGG-ADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
550-961 |
8.59e-100 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 321.04 E-value: 8.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 550 ERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYA---DEMErlssgyDRNFPGETNHYH-YQGR 625
Cdd:cd07114 44 ERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAglaDKIE------GAVIPVDKGDYLnFTRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 ---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHP 702
Cdd:cd07114 118 eplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 DVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVL 782
Cdd:cd07114 198 LVAKIAFTGGTETGRHIARAAA------ENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 783 ESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL-----LSVPVPEMGYFVSPTIFT 856
Cdd:cd07114 272 RSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEgARVLtggerPSGADLGAGYFFEPTILA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 857 NVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN--RgitgAIVDRQ 934
Cdd:cd07114 352 DVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNtyR----ALSPSS 427
|
410 420
....*....|....*....|....*..
gi 22294137 935 PFGGFKLSGIGsKAGGRDYLLQFLEPR 961
Cdd:cd07114 428 PFGGFKDSGIG-RENGIEAIREYTQTK 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
508-967 |
1.51e-99 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 320.16 E-value: 1.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 508 SLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DA 586
Cdd:cd07115 1 TLNPATGELI-ARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYAdemerlssGYDRNFPGET--------NHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILK 658
Cdd:cd07115 80 DVPRAADTFRYYA--------GWADKIEGEVipvrgpflNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 659 PADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVlqrgqsHIKRVIA 738
Cdd:cd07115 152 PAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG------NLKRVSL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 739 EMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTA 818
Cdd:cd07115 226 ELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 819 AARDRIQEYIAKGQQEAELLLS--VPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYAL 896
Cdd:cd07115 306 AQFDRVLDYVDVGREEGARLLTggKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22294137 897 TGGLYSRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFKLSGIGsKAGGRDYLLQFLEPRVITENV 967
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSVWVNL 453
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
461-961 |
1.54e-97 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 316.47 E-value: 1.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 461 NAANSDYARASQREAIQAALihvHRQLGQTY--TPIINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKA 538
Cdd:TIGR01238 9 NSLGIDLDNESELKPLEAQI---HAWADKTWqaAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 539 AQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERlssgydrNFPGETn 618
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRD-------VLGEFS- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 619 hyhYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYL 698
Cdd:TIGR01238 158 ---VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 699 TQHPDVHLIAFTGSQEVGCRIiaEAAVLQRGQSHIKrVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSR 778
Cdd:TIGR01238 235 TSDPRIAGVAFTGSTEVAQLI--NQTLAQREDAPVP-LIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 779 VIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYI----AKGQQEAELLLSVPVP-EMGYFVSPT 853
Cdd:TIGR01238 312 LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIehmsQTQKKIAQLTLDDSRAcQHGTFVAPT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 854 IFtNVPPTATIaQEEIFGPVLAVLR--AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIV 931
Cdd:TIGR01238 392 LF-ELDDIAEL-SEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVV 469
|
490 500 510
....*....|....*....|....*....|
gi 22294137 932 DRQPFGGFKLSGIGSKAGGRDYLLQFLEPR 961
Cdd:TIGR01238 470 GVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
460-966 |
2.57e-95 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 311.06 E-value: 2.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 460 VNAANSDYARAS-QREAIQAALihvHRQLGQTYT-P-IINGDRVNPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAA 536
Cdd:cd07123 2 VNEPVLSYAPGSpERAKLQEAL---AELKSLTVEiPlVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 537 KAAQAQWQQTSVAERATLLRRAADLLEAQ-RHELVAWMCYEVGKVV--AEGDAeVSEAVDFCR---YYADEMERlsSGYD 610
Cdd:cd07123 79 LEARKEWARMPFEDRAAIFLKAADLLSGKyRYELNAATMLGQGKNVwqAEIDA-ACELIDFLRfnvKYAEELYA--QQPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 611 RNFPGETNHYHYQG-RGLAVVISPWNFPlAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPG 689
Cdd:cd07123 156 SSPAGVWNRLEYRPlEGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 690 RGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAV-LQRGQShIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGY 768
Cdd:cd07123 235 DGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnLDRYRT-YPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 769 SGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYI--AKGQQEAELLL------S 840
Cdd:cd07123 314 QGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIdhAKSDPEAEIIAggkcddS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 841 VpvpemGYFVSPTIFTNVPPTATIAQEEIFGPVLAVL--RAETFTQALAIANATA-YALTGGLYSRTPSHIQQAKA--QF 915
Cdd:cd07123 394 V-----GYFVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDalRN 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 22294137 916 AVGNLYINRGITGAIVDRQPFGGFKLSGIGSKAGGRDYLLQFLEPRVITEN 966
Cdd:cd07123 469 AAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKET 519
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
510-965 |
2.81e-95 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 308.90 E-value: 2.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 510 NPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVS 589
Cdd:cd07110 3 NPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 590 EAVDFCRYYADEMERLSSGYDRNFP----GETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAV 665
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAKAERAVPlpseDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 666 VAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVLqrgqshIKRVIAEMGGKNA 745
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 746 IIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQ 825
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 826 EYIAKGQQE-AELLLSVPVPEM---GYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLY 901
Cdd:cd07110 316 SFIARGKEEgARLLCGGRRPAHlekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22294137 902 SRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFKLSGIGSKAG--GrdyLLQFLEPRVITE 965
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIGRELGewG---LDNYLEVKQITR 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
515-964 |
8.16e-95 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 308.35 E-value: 8.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 515 EEIVGRVGLATIEDAEHAIRAAKAA--QAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVA-EGDAEVSEA 591
Cdd:cd07139 24 EEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwSRRAQGPGP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 592 VDFCRYYAD-------EMERLSSGydrnfpGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAA 664
Cdd:cd07139 104 AALLRYYAAlardfpfEERRPGSG------GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 665 VVAAKLAEILMAAGFPPGVFQFLPGrGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKN 744
Cdd:cd07139 178 LDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG------ERLARVTLELGGKS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 745 AIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRI 824
Cdd:cd07139 251 AAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 825 QEYIAKGQQE-AELLLSVPVPE---MGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGL 900
Cdd:cd07139 331 EGYIAKGRAEgARLVTGGGRPAgldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSV 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 901 YSRTPSHIQQAKAQFAVGNLYINrgitGAIVDRQ-PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07139 411 WTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGPEGLDAYLETKSIY 470
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
546-964 |
1.64e-94 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 305.99 E-value: 1.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYyADEMERLSSG--YDRNFPGETNHYHYQ 623
Cdd:cd07104 19 TPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILRE-AAGLPRRPEGeiLPSDVPGKESMVRRV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 624 GRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILK-PADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHP 702
Cdd:cd07104 98 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKpDSRTPVTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALVEHP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 DVHLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVL 782
Cdd:cd07104 178 RVRMISFTGSTAVG-RHIGELA-----GRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 783 ESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLLSVPVPemGYFVSPTIFTNVPPT 861
Cdd:cd07104 252 ESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAgARLLTGGTYE--GLFYQPTVLSDVTPD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 862 ATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrGIT---GAIVdrqPFGG 938
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-DQTvndEPHV---PFGG 405
|
410 420
....*....|....*....|....*.
gi 22294137 939 FKLSGIGSkAGGRDYLLQFLEPRVIT 964
Cdd:cd07104 406 VKASGGGR-FGGPASLEEFTEWQWIT 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
516-945 |
4.33e-94 |
|
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: 305.67 E-value: 4.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07149 10 EVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMERLSsGYDRNFPGETNHYHYQG------RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAK 669
Cdd:cd07149 90 RLSAEEAKRLA-GETIPFDASPGGEGRIGftirepIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 670 LAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAVLqrgqshiKRVIAEMGGKNAIIID 749
Cdd:cd07149 169 LAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVG-EAIARKAGL-------KKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 750 ESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIA 829
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 830 KGQQE-AELLLsvPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHI 908
Cdd:cd07149 321 EAVEGgARLLT--GGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430
....*....|....*....|....*....|....*..
gi 22294137 909 QQAKAQFAVGNLYINrGITGAIVDRQPFGGFKLSGIG 945
Cdd:cd07149 399 LKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
546-949 |
1.25e-93 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 304.54 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLssgYDRNFP---GETNHYHY 622
Cdd:cd07109 39 LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKL---HGETIPlgpGYFVYTVR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 623 QGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHP 702
Cdd:cd07109 116 EPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 DVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVL 782
Cdd:cd07109 196 GVDHISFTGSVETGIAVMRAAA------ENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 783 ESIYKPFVERLVAATQSLNIGPAhLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS-----VPVPEMGYFVSPTIFTN 857
Cdd:cd07109 270 RSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARARARGARIVAggriaEGAPAGGYFVAPTLLDD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 858 VPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRqPFG 937
Cdd:cd07109 349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFG 427
|
410
....*....|..
gi 22294137 938 GFKLSGIGSKAG 949
Cdd:cd07109 428 GVKKSGHGREKG 439
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
509-963 |
4.60e-93 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 303.01 E-value: 4.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSQpEEIVGRVGLATIEDAEHAIRAAKAA-QAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGK-VVAEGDA 586
Cdd:cd07089 2 INPAT-EEVIGTAPDAGAADVDAAIAAARRAfDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYADemerLSSGYDRNFP-GETNHYHYQGRGLAV--------VISPWNFPLAIPTGMTAAALVTGNCTIL 657
Cdd:cd07089 81 QVDGPIGHLRYFAD----LADSFPWEFDlPVPALRGGPGRRVVRrepvgvvaAITPWNFPFFLNLAKLAPALAAGNTVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 658 KPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVLqrgqshIKRVI 737
Cdd:cd07089 157 KPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 738 AEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVT 817
Cdd:cd07089 231 LELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 818 AAARDRIQEYIAKGQQE-AELLLSVPVP---EMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATA 893
Cdd:cd07089 311 AAQRDRVEGYIARGRDEgARLVTGGGRPaglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 894 YALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIvdRQPFGGFKLSGIGsKAGGRDYLLQFLEPRVI 963
Cdd:cd07089 391 YGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
549-959 |
6.56e-93 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 302.60 E-value: 6.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 549 AERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYADEMERLssgYDRNFPGETNHYHYQGR-- 625
Cdd:cd07112 48 AERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVDVPSAANTFRWYAEAIDKV---YGEVAPTGPDALALITRep 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 -GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDV 704
Cdd:cd07112 125 lGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 HLIAFTGSQEVGCRIIAEAavlqrGQSHIKRVIAEMGGKNA-IIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLE 783
Cdd:cd07112 205 DALAFTGSTEVGRRFLEYS-----GQSNLKRVWLECGGKSPnIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 784 SIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLL----SVPVPEMGYFVSPTIFTNVP 859
Cdd:cd07112 280 SIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVaggkRVLTETGGFFVEPTVFDGVT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 860 PTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIvdRQPFGGF 939
Cdd:cd07112 360 PDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDI--TTPFGGF 437
|
410 420
....*....|....*....|
gi 22294137 940 KLSGigskaGGRDYLLQFLE 959
Cdd:cd07112 438 KQSG-----NGRDKSLHALD 452
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
516-949 |
1.70e-91 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 298.83 E-value: 1.70e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMERLSsGYDRNFPGETnhYHYQGR---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAE 672
Cdd:cd07090 88 EYYAGLAPTLS-GEHVPLPGGS--FAYTRReplGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 673 ILMAAGFPPGVFQFLPGRGSViGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESA 752
Cdd:cd07090 165 ILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 753 DLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQ 832
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 833 QE-AELL---LSVPVP---EMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRtp 905
Cdd:cd07090 318 QEgAKVLcggERVVPEdglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR-- 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 22294137 906 sHIQQAK---AQFAVGNLYINR-GITGAIVdrqPFGGFKLSGIGSKAG 949
Cdd:cd07090 396 -DLQRAHrviAQLQAGTCWINTyNISPVEV---PFGGYKQSGFGRENG 439
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
509-963 |
2.11e-90 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 295.59 E-value: 2.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEV 588
Cdd:cd07106 2 INPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 589 SEAVDFCRYYADeMERLSSGYDRNFPG--ETnhyHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVV 666
Cdd:cd07106 81 GGAVAWLRYTAS-LDLPDEVIEDDDTRrvEL---RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 667 AAKLAEILMAAgFPPGVFQFLPGRGSViGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAI 746
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAA------KTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 747 IIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQE 826
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 827 YI--AKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSrt 904
Cdd:cd07106 309 LVedAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS-- 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22294137 905 pSHIQQAKA---QFAVGNLYINRgiTGAIVDRQPFGGFKLSGIGSkAGGRDYLLQFLEPRVI 963
Cdd:cd07106 387 -SDLERAEAvarRLEAGTVWINT--HGALDPDAPFGGHKQSGIGV-EFGIEGLKEYTQTQVI 444
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
546-959 |
4.74e-89 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 292.32 E-value: 4.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYAdemerlssGYDRNFPGETnhYHYQGR 625
Cdd:cd07118 40 MSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA--------SLARTLHGDS--YNNLGD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 G-LAVV----------ISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVI 694
Cdd:cd07118 110 DmLGLVlrepigvvgiITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 695 GPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCS 774
Cdd:cd07118 190 GQAMTEHPDVDMVSFTGSTRVGKAIAAAAA------RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 775 ACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL--SVPVPEMGYFVS 851
Cdd:cd07118 264 SGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEgATLLLggERLASAAGLFYQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 852 PTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIv 931
Cdd:cd07118 344 PTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP- 422
|
410 420
....*....|....*....|....*...
gi 22294137 932 dRQPFGGFKLSGIGSKAgGRDYLLQFLE 959
Cdd:cd07118 423 -ELPFGGFKQSGIGREL-GRYGVEEYTE 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
495-965 |
7.33e-89 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 292.50 E-value: 7.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRV--NPREYSESLNPSqPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAW 572
Cdd:cd07085 5 INGEWVesKTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 573 MCYEVGKVVAEGDAEVS---EAVDFC-----RYYADEMERLSSGYDrnfpgetNHYHYQGRGLAVVISPWNFPLAIPTGM 644
Cdd:cd07085 84 ITLEHGKTLADARGDVLrglEVVEFAcsiphLLKGEYLENVARGID-------TYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 645 TAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTqHPDVHLIAFTGSQEVGCRIiaeaa 724
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYI----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 725 vLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGP 804
Cdd:cd07085 231 -YERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 805 AHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL-----SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLR 878
Cdd:cd07085 310 GDDPGADMGPVISPAAKERIEGLIESGVEEgAKLVLdgrgvKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 879 AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITgAIVDRQPFGGFKLSGIGS-KAGGRDYLLQF 957
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDlHFYGKDGVRFY 468
|
....*...
gi 22294137 958 LEPRVITE 965
Cdd:cd07085 469 TQTKTVTS 476
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
546-945 |
5.52e-88 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 288.20 E-value: 5.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGR 625
Cdd:cd07100 18 TSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEPIETDAGKAYVRYEPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPL------AIPtgmtaaALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGpYLT 699
Cdd:cd07100 98 GVVLGIMPWNFPFwqvfrfAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVE-AII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 700 QHPDVHLIAFTGSQEVGcRIIAEAAvlqrGQsHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRV 779
Cdd:cd07100 171 ADPRVRGVTLTGSERAG-RAVAAEA----GK-NLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 780 IVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKG-QQEAELLL-SVPVPEMGYFVSPTIFTN 857
Cdd:cd07100 245 IVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAvAAGATLLLgGKRPDGPGAFYPPTVLTD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 858 VPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrGITGAivD-RQPF 936
Cdd:cd07100 325 VTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN-GMVKS--DpRLPF 401
|
....*....
gi 22294137 937 GGFKLSGIG 945
Cdd:cd07100 402 GGVKRSGYG 410
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
495-954 |
1.00e-87 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 289.60 E-value: 1.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNP--REYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAA--QAQWQQTSVAERATLLRRAADLLEAQRHELV 570
Cdd:cd07119 2 IDGEWVEAasGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 571 AWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSSG-YDRNFPGETNHYHyQGRGLAVVISPWNFPLAIPTGMTAAAL 649
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEvYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 650 VTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrg 729
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 730 qSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPS 809
Cdd:cd07119 235 -GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 810 TRVGPVVTAAARDRIQEYIAKGQQE-AELL-----LSVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFT 883
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEgARLVcggkrPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 884 QALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINR-GITGAivdRQPFGGFKLSGIG---SKAGGRDYL 954
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFA---EAPWGGYKQSGIGrelGPTGLEEYQ 465
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
507-964 |
1.32e-86 |
|
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: 285.38 E-value: 1.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:cd07150 2 DDLNPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYADEMerlssgydRNFPGETNHYHYQGR---------GLAVVISPWNFPLAIPTGMTAAALVTGNCTIL 657
Cdd:cd07150 81 ETTFTPELLRAAAGEC--------RRVRGETLPSDSPGTvsmsvrrplGVVAGITPFNYPLILATKKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 658 KPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVlqrgqsHIKRVI 737
Cdd:cd07150 153 KPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR------HLKKIT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 738 AEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVT 817
Cdd:cd07150 227 LELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 818 AAARDRIQEYI----AKGqqeAELLlsVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATA 893
Cdd:cd07150 307 PRQVERIKRQVedavAKG---AKLL--TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTE 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22294137 894 YALTGGLYSRtpsHIQQAkAQFA----VGNLYINrGITgaIVDRQ--PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07150 382 YGLSAAILTN---DLQRA-FKLAerleSGMVHIN-DPT--ILDEAhvPFGGVKASGFG-REGGEWSMEEFTELKWIT 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
488-949 |
2.22e-84 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 280.45 E-value: 2.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 488 GQTYT-PI---INGDRVNPREYS--ESLNPSQPEEIVgRVGLATIEDAEHAIRAAKAA-QAQWQQTSVAERATLLRRAAD 560
Cdd:cd07144 1 GKSYDqPTglfINNEFVKSSDGEtiKTVNPSTGEVIA-SVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 561 LLEAQRHELVAWMCYEVGK-VVAEGDAEVSEAVDFCRYYADEMERLssgYDRNFPGETNHYHY---QGRGLAVVISPWNF 636
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKpYHSNALGDLDEIIAVIRYYAGWADKI---QGKTIPTSPNKLAYtlhEPYGVCGQIIPWNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 637 PLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVG 716
Cdd:cd07144 157 PLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 717 cRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAA 796
Cdd:cd07144 237 -RLVMKAAA-----QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 797 T-QSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLL-----SVPVPEMGYFVSPTIFTNVPPTATIAQEEIF 870
Cdd:cd07144 311 VkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVyggekAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22294137 871 GPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIvdRQPFGGFKLSGIGSKAG 949
Cdd:cd07144 391 GPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIGRELG 467
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
494-966 |
3.58e-84 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 281.67 E-value: 3.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 494 IINGDRV-NPREYSESLNPSQPEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQ-RHELVA 571
Cdd:TIGR01236 35 VIGGEEVyDSNERIPQVNPHNHQAVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSGPyRYEILA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 572 WMCYEVGKVV--AEGDAeVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQG-RGLAVVISPWNFpLAIPTGMTAAA 648
Cdd:TIGR01236 115 ATMLGQSKTVyqAEIDA-VAELIDFFRFNVKYARELYAQQPISAPGEWNRTEYRPlEGFVYAISPFNF-TAIAGNLAGAP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 649 LVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAV-LQ 727
Cdd:TIGR01236 193 ALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQnLD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 728 RGQSHiKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHL 807
Cdd:TIGR01236 273 RYHNF-PRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 808 PSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPE----MGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLR--AET 881
Cdd:TIGR01236 352 FRGFMGAVIDEQSFDKIVKYIEDAKKDPEALTILYGGKyddsQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVypDDK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 882 FTQAL-AIANATAYALTGGLYSRTPSHIQQA--KAQFAVGNLYINRGITGAIVDRQPFGGFKLSGIGSKAGGRDYLLQFL 958
Cdd:TIGR01236 432 YKEILdLVDSTSQYGLTGAVFAKDRKAILEAdkKLRFAAGNFYINDKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWT 511
|
....*...
gi 22294137 959 EPRVITEN 966
Cdd:TIGR01236 512 SPRSIKET 519
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
547-964 |
3.09e-83 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 276.41 E-value: 3.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 547 SVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERL----SSGYDRNFPGETNHYHY 622
Cdd:cd07099 38 GVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVlaprKVPTGLLMPNKKATVEY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 623 QGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSViGPYLTQHP 702
Cdd:cd07099 118 RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 dVHLIAFTGSQEVGCRIIAEAAvlqrgqshiKRVI---AEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRV 779
Cdd:cd07099 197 -VDKVAFTGSVATGRKVMAAAA---------ERLIpvvLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 780 IVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAA----ARDRIQEYIAKGqqeAELLL-SVPVPEMGYFVSPTI 854
Cdd:cd07099 267 YVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqldiVRRHVDDAVAKG---AKALTgGARSNGGGPFYEPTV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 855 FTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQ 934
Cdd:cd07099 344 LTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPAL 423
|
410 420 430
....*....|....*....|....*....|
gi 22294137 935 PFGGFKLSGIGSKaGGRDYLLQFLEPRVIT 964
Cdd:cd07099 424 PFGGVKDSGGGRR-HGAEGLREFCRPKAIA 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
509-953 |
5.02e-83 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 275.74 E-value: 5.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DAE 587
Cdd:cd07092 2 VDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVrDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 588 VSEAVDFCRYYADE---MERLSSG-YdrnFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPA 663
Cdd:cd07092 81 LPGAVDNFRFFAGAartLEGPAAGeY---LPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 664 AVVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGK 743
Cdd:cd07092 158 PLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA------DTLKRVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 744 NAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDR 823
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 824 IQEYIAKGQQEAELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYS 902
Cdd:cd07092 311 VAGFVERAPAHARVLTgGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 22294137 903 RTPSHIQQAKAQFAVGNLYINRGITgaIVDRQPFGGFKLSGIG---SKAGGRDY 953
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYGkdlSIYALEDY 442
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
510-963 |
1.04e-82 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 275.00 E-value: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 510 NPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVS 589
Cdd:cd07145 5 NPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 590 EAVDFCRYYADEMERLssgYDRNFPGETnhYHYQGRGLA--------VV--ISPWNFPLAIPTGMTAAALVTGNCTILKP 659
Cdd:cd07145 84 RTIRLFKLAAEEAKVL---RGETIPVDA--YEYNERRIAftvrepigVVgaITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 660 ADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAE 739
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 740 MGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAA 819
Cdd:cd07145 233 LGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 820 ARDRIQEYIAKGQQE-AELLLSVPVPEmGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTG 898
Cdd:cd07145 313 AVERMENLVNDAVEKgGKILYGGKRDE-GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 899 GLYSRTPSHIQQAKAQFAVGNLYINrGITGAIVDRQPFGGFKLSGIGsKAGGRDYLLQFLEPRVI 963
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGIG-REGVRYTMLEMTEEKTI 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
507-945 |
1.40e-82 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 274.95 E-value: 1.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSQPEEIVgRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:cd07151 13 DVLNPYTGETLA-EIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCR---YYADEMERLSSGYDrnFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPA 663
Cdd:cd07151 92 EWGAAMAITReaaTFPLRMEGRILPSD--VPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 664 AVVAAKL-AEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGG 742
Cdd:cd07151 170 PITGGLLlAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG-RHIGELAG-----RHLKKVALELGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 743 KNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARD 822
Cdd:cd07151 244 NNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 823 RIQEYIAKGQQE-AELLLSVPVpeMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLY 901
Cdd:cd07151 324 GLLDKIEQAVEEgATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVF 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22294137 902 SRTPSHIQQAKAQFAVGNLYINrgiTGAIVDRQ--PFGGFKLSGIG 945
Cdd:cd07151 402 TSDLERGVQFARRIDAGMTHIN---DQPVNDEPhvPFGGEKNSGLG 444
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
508-964 |
8.81e-82 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 272.71 E-value: 8.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 508 SLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAE 587
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 588 VSEAVDFCRYYADEMERLSSgydRNFPGETNHYHYQGR---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAA 664
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKG---ETIPVGGRNLHYTLRepyGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 665 VVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKN 744
Cdd:cd07107 157 LSALRLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA------EGIKHVTLELGGKN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 745 AIIIDESADLDQAVAGVVQSA-FGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDR 823
Cdd:cd07107 230 ALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 824 IQEYIAKGQQEAELLL------SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALT 897
Cdd:cd07107 310 VMHYIDSAKREGARLVtgggrpEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 898 GGLYSRTPSHIQQAKAQFAVGNLYIN---RGITGAivdrqPFGGFKLSGIGSKAgGRDYLLQFLEPRVIT 964
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIGREE-CLEELLSYTQEKNVN 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
509-959 |
7.66e-81 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 271.56 E-value: 7.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSQPEEI--VGRVGLATIEDAehaIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:PLN02278 45 YNPATGEVIanVPCMGRAETNDA---IASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYADEMERLSsgydrnfpGETNHYHYQGRGLAVV---------ISPWNFPLAIPTGMTAAALVTGNCTIL 657
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVY--------GDIIPSPFPDRRLLVLkqpvgvvgaITPWNFPLAMITRKVGPALAAGCTVVV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 658 KPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVI 737
Cdd:PLN02278 194 KPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATVKRVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 738 AEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVT 817
Cdd:PLN02278 268 LELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLIN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 818 AAARDRI----QEYIAKGqqeAELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANAT 892
Cdd:PLN02278 348 EAAVQKVeshvQDAVSKG---AKVLLgGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDT 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22294137 893 AYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVdrQPFGGFKLSGIGsKAGGRDYLLQFLE 959
Cdd:PLN02278 425 EAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGVKQSGLG-REGSKYGIDEYLE 488
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
491-966 |
1.25e-80 |
|
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: 269.83 E-value: 1.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 491 YTPIINGD-RVNPREYSESLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQT-SVAERATLLRRAADLLEAQRHE 568
Cdd:cd07082 2 FKYLINGEwKESSGKTIEVYSPIDGEVI-GSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 569 LVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERL---SSGYDRnFPGETNHYHYQGR---GLAVVISPWNFPLAIPT 642
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLdgdSLPGDW-FPGTKGKIAQVRReplGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 643 GMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAe 722
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 723 aavlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNI 802
Cdd:cd07082 239 -------QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 803 GPAHLPSTRVGPVVTAAARDRIQEYI----AKGqqeAELLLSVpVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLR 878
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIddavAKG---ATVLNGG-GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 879 AETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN----RGItgaivDRQPFGGFKLSGIGSKaGGRDYL 954
Cdd:cd07082 388 VNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIGTQ-GIGDAL 461
|
490
....*....|..
gi 22294137 955 LQFLEPRVITEN 966
Cdd:cd07082 462 RSMTRRKGIVIN 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
516-965 |
3.04e-80 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 268.41 E-value: 3.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMERLSSgyDRNFPG-----ETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKL 670
Cdd:cd07101 87 RYYARRAERLLK--PRRRRGaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 671 AEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDvhLIAFTGSQEVGcRIIAEAAVlqrgqshiKRVI---AEMGGKNAII 747
Cdd:cd07101 165 VELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATG-RVVAERAG--------RRLIgcsLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 748 IDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEY 827
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 828 I----AKGqqeAELLL-SVPVPEMG-YFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLY 901
Cdd:cd07101 314 VddavAKG---ATVLAgGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22294137 902 SRTPSHIQQAKAQFAVGNLYINRGITGAI--VDrQPFGGFKLSGIGSKAgGRDYLLQFLEPRVITE 965
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGYAAAWasID-APMGGMKDSGLGRRH-GAEGLLKYTETQTVAV 454
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
516-951 |
1.65e-79 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 266.15 E-value: 1.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEhaiRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07146 10 EVVGTVPAGTEEALR---EALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMER-----LSSGYDRNFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKL 670
Cdd:cd07146 87 RFAAAEALRddgesFSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 671 AEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqshIKRVIAEMGGKNAIIIDE 750
Cdd:cd07146 167 ADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 751 SADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAK 830
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 831 GQQEAELLLSVPVPEmGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQ 910
Cdd:cd07146 319 AIAQGARVLLGNQRQ-GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22294137 911 AKAQFAVGNLYINrGITGAIVDRQPFGGFKLSGIGSKAGGR 951
Cdd:cd07146 398 LVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVR 437
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
489-945 |
1.79e-79 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 267.52 E-value: 1.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 489 QTYTPIINGDRVNPR--EYSESLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQR 566
Cdd:PRK13252 5 PLQSLYIDGAYVEATsgETFEVINPATGEVL-ATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 567 HELVAWMCYEVGKVVAEgdAEVSEAV---DFCRYYAD-------EMERLSSG---YDRNFPgetnhyhyqgRGLAVVISP 633
Cdd:PRK13252 84 DELAALETLDTGKPIQE--TSVVDIVtgaDVLEYYAGlapalegEQIPLRGGsfvYTRREP----------LGVCAGIGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 634 WNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSViGPYLTQHPDVHLIAFTGSQ 713
Cdd:PRK13252 152 WNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 714 EVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERL 793
Cdd:PRK13252 231 PTGKKVMAAAA------ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 794 VAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL-----LSVPVPEMGYFVSPTIFTNVPPTATIAQE 867
Cdd:PRK13252 305 LERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEgARLLcggerLTEGGFANGAFVAPTVFTDCTDDMTIVRE 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22294137 868 EIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINR-GITGAivdRQPFGGFKLSGIG 945
Cdd:PRK13252 385 EIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
516-964 |
3.67e-79 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 264.93 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYyADEM------ERLSSGydrnfPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVA-A 668
Cdd:cd07152 82 HE-AAGLptqpqgEILPSA-----PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 669 KLAEILMAAGFPPGVFQFLPGrGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIII 748
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVG-RKVGEAA-----GRHLKKVSLELGGKNALIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 749 DESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYI 828
Cdd:cd07152 229 LDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 829 AKGQQEAELLLSVPVPEmGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHI 908
Cdd:cd07152 309 DDSVAAGARLEAGGTYD-GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 22294137 909 QQAKAQFAVGNLYINRG--ITGAIVdrqPFGGFKLSGIGSKAGGRDYLLQFLEPRVIT 964
Cdd:cd07152 388 MALADRLRTGMLHINDQtvNDEPHN---PFGGMGASGNGSRFGGPANWEEFTQWQWVT 442
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
516-964 |
1.07e-78 |
|
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: 264.29 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMERLssgYDRNFPGETNHYHYQGRGLAV--------VISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVA 667
Cdd:cd07094 90 RLAAEEAERI---RGEEIPLDATQGSDNRLAWTIrepvgvvlAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 668 AKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqshIKRVIAEMGGKNAII 747
Cdd:cd07094 167 LELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 748 IDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEY 827
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 828 IAKGQQEAELLLSVPVPEmGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSH 907
Cdd:cd07094 319 VEEAVEAGARLLCGGERD-GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22294137 908 IQQAKAQFAVGNLYINRGiTGAIVDRQPFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTVV 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
485-949 |
4.81e-78 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 263.90 E-value: 4.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 485 RQLgqtytpIINGDRVNP--REYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQ-----QTSVAERATLLRR 557
Cdd:PLN02467 8 RQL------FIGGEWREPvlGKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAFKRNKgkdwaRTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 558 AADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLSS--GYDRNFPGETNHYHYQGRGLAVV--ISP 633
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqKAPVSLPMETFKGYVLKEPLGVVglITP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 634 WNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQ 713
Cdd:PLN02467 161 WNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 714 EVGCRIIAEAAVLqrgqshIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERL 793
Cdd:PLN02467 241 ATGRKIMTAAAQM------VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 794 VAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLLSVPVPE---MGYFVSPTIFTNVPPTATIAQEEI 869
Cdd:PLN02467 315 VKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEgATILCGGKRPEhlkKGFFIEPTIITDVTTSMQIWREEV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 870 FGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFKLSGIGSKAG 949
Cdd:PLN02467 395 FGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELG 472
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
509-948 |
7.13e-78 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 261.91 E-value: 7.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 509 LNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVV-AEGDAE 587
Cdd:cd07108 2 INPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 588 VSEAVDFCRYY---ADEMErlssgyDRNFPGETNHYHYQGRG-LAVV--ISPWNFPLAIPTGMTAAALVTGNCTILKPAD 661
Cdd:cd07108 81 AAVLADLFRYFgglAGELK------GETLPFGPDVLTYTVREpLGVVgaILPWNAPLMLAALKIAPALVAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 662 PAAVVAAKLAEIlMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMG 741
Cdd:cd07108 155 DAPLAVLLLAEI-LAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVG-KIIYRAAA-----DRLIPVSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 742 GKNAIIIDESADLDQAVAGVVQSA-FGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAA 820
Cdd:cd07108 228 GKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 821 RDRIQEYIAKG--QQEAELLLSVPVP-----EMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATA 893
Cdd:cd07108 308 FAKVCGYIDLGlsTSGATVLRGGPLPgegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 894 YALTGGLYSRTPSHIQQAKAQFAVGNLYINRGitGAIVDRQPFGGFKLSGIGSKA 948
Cdd:cd07108 388 YGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLGREA 440
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
549-964 |
1.58e-77 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 261.90 E-value: 1.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 549 AERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYA---DEMERLSSGYDRNFPGETNHyhyQG 624
Cdd:cd07141 69 SERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAgwaDKIHGKTIPMDGDFFTYTRH---EP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDV 704
Cdd:cd07141 146 VGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 HLIAFTGSQEVGcRIIAEAAvlqrGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:cd07141 226 DKVAFTGSTEVG-KLIQQAA----GKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQES 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELLL-SVPVPEMGYFVSPTIFTNVPPTA 862
Cdd:cd07141 301 IYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEgAKLECgGKRHGDKGYFIQPTVFSDVTDDM 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 863 TIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSR------TPSHIQQAkaqfavGNLYINrgITGAIVDRQPF 936
Cdd:cd07141 381 RIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKdidkaiTFSNALRA------GTVWVN--CYNVVSPQAPF 452
|
410 420
....*....|....*....|....*...
gi 22294137 937 GGFKLSGIGSKAgGRDYLLQFLEPRVIT 964
Cdd:cd07141 453 GGYKMSGNGREL-GEYGLQEYTEVKTVT 479
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
516-980 |
5.04e-76 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 259.04 E-value: 5.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKvvAEGDA--EVSEAVD 593
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK--ARRHAfeEVLDVAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 594 FCRYYADEMERLSSGYDRN--FPGET-NHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKL 670
Cdd:PRK09407 121 TARYYARRAPKLLAPRRRAgaLPVLTkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 671 AEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDvhLIAFTGSQEVGcRIIAEAAVlqrgqshiKRVI---AEMGGKNAII 747
Cdd:PRK09407 201 VELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATG-RVLAEQAG--------RRLIgfsLELGGKNPMI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 748 IDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEY 827
Cdd:PRK09407 270 VLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 828 I----AKGqqeAELLL-SVPVPEMG-YFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLY 901
Cdd:PRK09407 350 VddavAKG---ATVLAgGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVW 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 902 SRTPSHIQQAKAQFAVGNLYINRGITGAI--VDrQPFGGFKLSGIGSKAgGRDYLLQFLEPRVITEnvQR-QGFAPIAGV 978
Cdd:PRK09407 427 TGDTARGRAIAARIRAGTVNVNEGYAAAWgsVD-APMGGMKDSGLGRRH-GAEGLLKYTESQTIAT--QRvLPLAPPPGM 502
|
..
gi 22294137 979 DD 980
Cdd:PRK09407 503 PY 504
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
491-945 |
9.78e-76 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 256.89 E-value: 9.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 491 YTPIINGDRVNPR--EYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHE 568
Cdd:cd07559 1 YDNFINGEWVAPSkgEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 569 LVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYADEMeRLSSGYDRNFPGETNHYHYQgRGLAVV--ISPWNFPLAIPTGMT 645
Cdd:cd07559 80 LAVAETLDNGKPIRETlAADIPLAIDHFRYFAGVI-RAQEGSLSEIDEDTLSYHFH-EPLGVVgqIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 646 AAALVTGNCTILKPADPAAVVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAV 725
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELI-GDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVG-RLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 726 lqrgqSHIKRVIAEMGGKNAIIIDESAD------LDQAVAGVVQSAFGySGQKCSACSRVIVLESIYKPFVERLVAATQS 799
Cdd:cd07559 236 -----ENLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAFN-QGEVCTCPSRALVQESIYDEFIERAVERFEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 800 LNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL-----LSVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPV 873
Cdd:cd07559 310 IKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEgAEVLtggerLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 874 LAVLRAETFTQALAIANATAYALTGGLYSRtpsHIQQAkaqfavgnLYINRGI-TG--------AIVDRQPFGGFKLSGI 944
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTR---DINRA--------LRVARGIqTGrvwvncyhQYPAHAPFGGYKKSGI 458
|
.
gi 22294137 945 G 945
Cdd:cd07559 459 G 459
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
467-960 |
2.56e-74 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 253.09 E-value: 2.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 467 YARASQ-REAIQAALIHVHRQLGqtytPIINGDRVNP--REYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQW 543
Cdd:cd07111 1 YGPAPEsAACALAWLDAHDRSFG----HFINGKWVKPenRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 544 QQTSVAERATLLRRAADLLeaQRHELVAWMCYEV--GKVVAEG-DAEVSEAVDFCRYYADEMERLssgyDRNFPGetnhy 620
Cdd:cd07111 76 SALPGHVRARHLYRIARHI--QKHQRLFAVLESLdnGKPIRESrDCDIPLVARHFYHHAGWAQLL----DTELAG----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 621 hYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSViGPYLTQ 700
Cdd:cd07111 145 -WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALAN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 701 HPDVHLIAFTGSQEVGcRIIAEAAVlqrGQShiKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVI 780
Cdd:cd07111 223 HPGVDKVAFTGSTEVG-RALRRATA---GTG--KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 781 VLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL-LSVPVPEMGYFVSPTIFTNV 858
Cdd:cd07111 297 VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEgADVFqPGADLPSKGPFYPPTLFTNV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 859 PPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN-RGITGAIVdrqPFG 937
Cdd:cd07111 377 PPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFG 453
|
490 500
....*....|....*....|...
gi 22294137 938 GFKLSGIGsKAGGRDYLLQFLEP 960
Cdd:cd07111 454 GYRESGFG-REGGKEGLYEYLRP 475
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
495-954 |
8.26e-74 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 251.37 E-value: 8.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNPREYSES-LNPSQPEEIVgRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWM 573
Cdd:PRK13473 7 INGELVAGEGEKQPvYNPATGEVLA-EIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 574 CYEVGK---VVAEGdaEVSEAVDFCRYYADE---MERLSSG-YDrnfPGETNHYHYQGRGLAVVISPWNFPLaiptgMTA 646
Cdd:PRK13473 86 SLNCGKplhLALND--EIPAIVDVFRFFAGAarcLEGKAAGeYL---EGHTSMIRRDPVGVVASIAPWNYPL-----MMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 647 A-----ALVTGNCTILKPADPAAVVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIA 721
Cdd:PRK13473 156 AwklapALAAGNTVVLKPSEITPLTALKLAELA-ADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 722 EAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVqsAFGY--SGQKCSACSRVIVLESIYKPFVERLVAATQS 799
Cdd:PRK13473 235 AAA------DSVKRTHLELGGKAPVIVFDDADLDAVVEGIR--TFGYynAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 800 LNIGPAHLPSTRVGPVVTAAARDRIQEYI--AKGQQEAELLLSVPVPEM-GYFVSPTIFTNVPPTATIAQEEIFGPVLAV 876
Cdd:PRK13473 307 LKVGDPDDEDTELGPLISAAHRDRVAGFVerAKALGHIRVVTGGEAPDGkGYYYEPTLLAGARQDDEIVQREVFGPVVSV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 877 LRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITgaIVDRQPFGGFKLSGIG---SKAGGRDY 953
Cdd:PRK13473 387 TPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYGkdmSLYGLEDY 464
|
.
gi 22294137 954 L 954
Cdd:PRK13473 465 T 465
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
516-962 |
2.15e-73 |
|
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: 249.47 E-value: 2.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 516 EIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFC 595
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 596 RYYADEMERLS---------------SGYDRNFPgetnhyhyqgRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPA 660
Cdd:cd07147 90 RIAAEEATRIYgevlpldisargegrQGLVRRFP----------IGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 661 DPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSvIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAavlqrGQshiKRVIAEM 740
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRD-DADLLVTDERIKLLSFTGSPAVGWDLKARA-----GK---KKVVLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 741 GGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAA 820
Cdd:cd07147 231 GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 821 RDRIQEYIAKG-QQEAELLlsVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGG 899
Cdd:cd07147 311 AERVEGWVNEAvDAGAKLL--TGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22294137 900 LYSRTPSHIQQAKAQFAVGNLYINRgITGAIVDRQPFGGFKLSGIGsKAGGRDYLLQFLEPRV 962
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSGIG-REGVRYAIEEMTEPRL 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
550-949 |
2.18e-73 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 250.49 E-value: 2.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 550 ERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGD-AEVSEAVDFCRYYA---DEMERLSSGYDRNFPGETNHyhyQGR 625
Cdd:cd07142 66 ERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAgwaDKIHGMTLPADGPHHVYTLH---EPI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVH 705
Cdd:cd07142 143 GVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 LIAFTGSQEVGcRIIAEAAvlqrGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESI 785
Cdd:cd07142 223 KVAFTGSTEVG-KIIMQLA----AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 786 YKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS--VPVPEMGYFVSPTIFTNVPPTAT 863
Cdd:cd07142 298 YDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITggDRIGSKGYYIQPTIFSDVKDDMK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 864 IAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN--RGITGAIvdrqPFGGFKL 941
Cdd:cd07142 378 IARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI----PFGGYKM 453
|
....*...
gi 22294137 942 SGIGSKAG 949
Cdd:cd07142 454 SGIGREKG 461
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
495-949 |
4.77e-73 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 249.37 E-value: 4.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNPREYS--ESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSV--AERATLLRRAADLLEAQRHELV 570
Cdd:cd07143 11 INGEFVDSVHGGtvKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFETDWGLKVsgSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 571 AWMCYEVGK-VVAEGDAEVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAAL 649
Cdd:cd07143 90 SIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 650 VTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrg 729
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 730 QSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPS 809
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 810 TRVGPVVTAAARDRIQEYIAKGQQEAELLLS--VPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALA 887
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETggKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22294137 888 IANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgiTGAIVDRQ-PFGGFKLSGIGSKAG 949
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN---CYNLLHHQvPFGGYKQSGIGRELG 464
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
546-964 |
1.14e-71 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 244.02 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYAdemERLSSgydrnFPGETNHYHYQGR 625
Cdd:cd07105 19 TPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA---SLITQ-----IIGGSIPSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 gLAVV----------ISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFL---PGRGS 692
Cdd:cd07105 91 -LAMVvkepvgvvlgIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 693 VIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAvlqrGQsHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQK 772
Cdd:cd07105 170 EVVEALIAHPAVRKVNFTGSTRVG-RIIAETA----AK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 773 CSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLpstrvGPVVTAAARDRIQEYI----AKGqqeAELLLSVP--VPEM 846
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVddalSKG---AKLVVGGLadESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 847 GYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgi 926
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN--- 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22294137 927 tGAIVDRQ---PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07105 393 -GMTVHDEptlPHGGVKSSGYG-RFNGKWGIDEFTETKWIT 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
508-964 |
1.63e-71 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 244.56 E-value: 1.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 508 SLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAE-RATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:cd07120 1 SIDPATGEVI-GTYADGGVAEAEAAIAAARRAFDETDWAHDPRlRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYYADeMERLSSGydRNF---PGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPA 663
Cdd:cd07120 80 EISGAISELRYYAG-LARTEAG--RMIepePGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 664 AVVAAKLAEILMAA-GFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGG 742
Cdd:cd07120 157 AQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA------PTLKRLGLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 743 KNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARD 822
Cdd:cd07120 231 KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 823 RIQEYIAKG-QQEAELLL-SVPVPEM---GYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALT 897
Cdd:cd07120 311 RVDRMVERAiAAGAEVVLrGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22294137 898 GGLYSRTPSHIQQAKAQFAVGNLYINRgiTGAIVDRQPFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVWIND--WNKLFAEAEEGGYRQSGLG-RLHGVAALEDFIEYKHIY 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
546-943 |
3.31e-71 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 242.95 E-value: 3.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEA---VDFCryYADEMERLSsgyDRNFPGE--TNHY 620
Cdd:cd07095 19 LSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDIS--IKAYHERTG---ERATPMAqgRAVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 621 HYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSViGPYLTQ 700
Cdd:cd07095 94 RHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRET-GEALAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 701 HPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIA-EMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRV 779
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 780 IVLESIY-KPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRI----QEYIAKGqqeAELLLSVP-VPEMGYFVSPT 853
Cdd:cd07095 247 IVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYllaqQDLLALG---GEPLLAMErLVAGTAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 854 IFtNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAiVDR 933
Cdd:cd07095 324 II-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SST 401
|
410
....*....|
gi 22294137 934 QPFGGFKLSG 943
Cdd:cd07095 402 APFGGVGLSG 411
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
555-963 |
1.42e-68 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 235.02 E-value: 1.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 555 LRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYAD-----EMERLSSgyDRnfPGETNHYHYQGRGLAV 629
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEwarryEGEIIQS--DR--PGENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 630 VISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAF 709
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 710 TGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPF 789
Cdd:PRK10090 157 TGSVSAGEKIMAAAA------KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 790 VERLVAATQSLNIG-PAHLPSTRVGPVVTAAARDRIQEYIAKG-QQEAELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQ 866
Cdd:PRK10090 231 VNRLGEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVARAvEEGARVALgGKAVEGKGYYYPPTLLLDVRQEMSIMH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 867 EEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIvdrQPF-GGFKLSGIG 945
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIG 387
|
410
....*....|....*...
gi 22294137 946 SkAGGRDYLLQFLEPRVI 963
Cdd:PRK10090 388 G-ADGKHGLHEYLQTQVV 404
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
510-964 |
4.30e-68 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 235.80 E-value: 4.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 510 NPSQpEEIVGRVGLATIEDAEHAIRAAKAA-QAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA-E 587
Cdd:cd07113 21 NPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 588 VSEAVDFCRYYAdemerlssGYDRNFPGETNHYHYQGRG------------LAVV--ISPWNFPLAIPTGMTAAALVTGN 653
Cdd:cd07113 100 VGQSANFLRYFA--------GWATKINGETLAPSIPSMQgerytaftrrepVGVVagIVPWNFSVMIAVWKIGAALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 654 CTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSViGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAVlqrgqSHI 733
Cdd:cd07113 172 TIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATG-KKIGRQAA-----SDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 734 KRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVG 813
Cdd:cd07113 245 TRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 814 PVVTAAARDRIQEYI--AKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANA 891
Cdd:cd07113 325 PLANQPHFDKVCSYLddARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLIND 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22294137 892 TAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgiTGAIVDRQ-PFGGFKLSGIGsKAGGRDYLLQFLEPRVIT 964
Cdd:cd07113 405 TPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDPAvPFGGMKQSGIG-REFGSAFIDDYTELKSVM 474
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
550-954 |
7.13e-68 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 235.19 E-value: 7.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 550 ERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLssgYDRNFPGETNHYHY----QGR 625
Cdd:PRK11241 71 ERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRI---YGDTIPGHQADKRLivikQPI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVH 705
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 LIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESI 785
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCA------KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 786 YKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEM--GYFVSPTIFTNVPPTAT 863
Cdd:PRK11241 302 YDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHElgGNFFQPTILVDVPANAK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 864 IAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVdrQPFGGFKLSG 943
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASG 459
|
410
....*....|....
gi 22294137 944 I---GSKAGGRDYL 954
Cdd:PRK11241 460 LgreGSKYGIEDYL 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
547-964 |
5.70e-67 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 233.17 E-value: 5.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 547 SVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA-EVSEAVDFCRYYA---DEMERLSSGYDRNFPGETNHyhy 622
Cdd:PLN02766 80 SGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAgaaDKIHGETLKMSRQLQGYTLK--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 623 QGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHP 702
Cdd:PLN02766 157 EPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 DVHLIAFTGSQEVGcRIIAEAAvlqrGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVL 782
Cdd:PLN02766 237 DVDKVSFTGSTEVG-RKIMQAA----ATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 783 ESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS--VPVPEMGYFVSPTIFTNVPP 860
Cdd:PLN02766 312 EGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTggKPCGDKGYYIEPTIFTDVTE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 861 TATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFK 940
Cdd:PLN02766 392 DMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYK 469
|
410 420
....*....|....*....|....*
gi 22294137 941 LSGIGsKAGGRDYLLQFLEPR-VIT 964
Cdd:PLN02766 470 MSGFG-RDQGMDALDKYLQVKsVVT 493
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
495-964 |
9.19e-66 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 229.30 E-value: 9.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 495 INGDRVNP---REYsESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVA--ERATLLRRAADLLEAQRHEL 569
Cdd:cd07140 10 INGEFVDAeggKTY-NTINPTD-GSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNarDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 570 VAWMCYEVGKVVAEG-DAEVSEAVDFCRYYA---DEMERLSSGYDRNFPgeTNHYHYQGR---GLAVVISPWNFPLAIPT 642
Cdd:cd07140 88 ATIESLDSGAVYTLAlKTHVGMSIQTFRYFAgwcDKIQGKTIPINQARP--NRNLTLTKRepiGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 643 GMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAE 722
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 723 AAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNI 802
Cdd:cd07140 246 CAV-----SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 803 GPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLL--SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAE 880
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVygGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 881 T--FTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgiTGAIVD-RQPFGGFKLSGIGsKAGGRDYLLQF 957
Cdd:cd07140 401 DgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN---TYNKTDvAAPFGGFKQSGFG-KDLGEEALNEY 476
|
....*..
gi 22294137 958 LEPRVIT 964
Cdd:cd07140 477 LKTKTVT 483
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
507-910 |
6.18e-65 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 226.70 E-value: 6.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSQPEEIVgRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:cd07130 15 TSISPANGEPIA-RVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVDFCRYyademerlSSGYDRNFPGET------NHYHY---QGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTIL 657
Cdd:cd07130 94 EVQEMIDICDF--------AVGLSRQLYGLTipserpGHRMMeqwNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 658 KPADP---AAVVAAKL-AEILMAAGFPPGVFQFLPGrGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAvlqrgQSHI 733
Cdd:cd07130 166 KPSPTtplTAIAVTKIvARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVG-RQVGQAV-----AARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 734 KRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVG 813
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 814 PVVTAAARDRIQEYIAKGQ-QEAELLLSVPVPEM-GYFVSPTIFTnVPPTATIAQEEIFGPVLAVLRAETFTQALAIANA 891
Cdd:cd07130 319 PLHTKAAVDNYLAAIEEAKsQGGTVLFGGKVIDGpGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410
....*....|....*....
gi 22294137 892 TAYALTGGLYSRTPSHIQQ 910
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFR 416
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
546-945 |
6.58e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 226.16 E-value: 6.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERL---------SSGYDRNFpge 616
Cdd:PRK09406 42 TTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALladepadaaAVGASRAY--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 617 tnhYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQ-FLPGRGSVIG 695
Cdd:PRK09406 119 ---VRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQtLLVGSGAVEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 696 pyLTQHPDVHLIAFTGSQEVGcRIIAEAAvlqrGQShIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSA 775
Cdd:PRK09406 196 --ILRDPRVAAATLTGSEPAG-RAVAAIA----GDE-IKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 776 CSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKG-QQEAELLLSVPVPEM-GYFVSPT 853
Cdd:PRK09406 268 AKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAvAAGATILCGGKRPDGpGWFYPPT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 854 IFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrGITgAIVDR 933
Cdd:PRK09406 348 VITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMT-VSYPE 425
|
410
....*....|..
gi 22294137 934 QPFGGFKLSGIG 945
Cdd:PRK09406 426 LPFGGVKRSGYG 437
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
546-946 |
1.27e-63 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 222.51 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMER-LSSGYDRNFPGETNHYHYQG 624
Cdd:cd07102 37 VPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEaLADIRVPEKDGFERYIRREP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPyLTQHPDV 704
Cdd:cd07102 117 LGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 HLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:cd07102 196 DHVSFTGSVAGG-RAIQRAA-----AGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHES 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAA----RDRIQEYIAKGqqeAELLL---SVPVP-EMGYFVSPTIFT 856
Cdd:cd07102 270 IYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAadfvRAQIADAIAKG---ARALIdgaLFPEDkAGGAYLAPTVLT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 857 NVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGItgaIVD-RQP 935
Cdd:cd07102 347 NVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCD---YLDpALA 423
|
410
....*....|.
gi 22294137 936 FGGFKLSGIGS 946
Cdd:cd07102 424 WTGVKDSGRGV 434
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
547-959 |
1.93e-63 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 223.23 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 547 SVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGR 625
Cdd:PRK09847 79 SPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVH 705
Cdd:PRK09847 159 GVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDID 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 LIAFTGSQEVGCRIIAEAavlqrGQSHIKRVIAEMGGKNA-IIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:PRK09847 239 AIAFTGSTRTGKQLLKDA-----GDSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATI 864
Cdd:PRK09847 314 IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 865 AQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVdrQPFGGFKLSGi 944
Cdd:PRK09847 394 SREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG- 470
|
410
....*....|....*
gi 22294137 945 gskaGGRDYLLQFLE 959
Cdd:PRK09847 471 ----NGRDKSLHALE 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
491-945 |
1.11e-62 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 220.40 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 491 YTPIINGDRVNPR--EYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHE 568
Cdd:cd07117 1 YGLFINGEWVKGSsgETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 569 LVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYAdemerlssGYDRNFPGETNHYHYQGRGLA------VV--ISPWNFPLA 639
Cdd:cd07117 80 LAMVETLDNGKPIRETrAVDIPLAADHFRYFA--------GVIRAEEGSANMIDEDTLSIVlrepigVVgqIIPWNFPFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 640 IPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRI 719
Cdd:cd07117 152 MAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKII-QDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVG-RD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 720 IAEAAVlqrgqshiKRVIA---EMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAA 796
Cdd:cd07117 230 VAIAAA--------KKLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 797 TQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL-----LSVPVPEMGYFVSPTIFTNVPPTATIAQEEIF 870
Cdd:cd07117 302 FENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEgAKILtgghrLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIF 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 871 GPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFKLSGIG 945
Cdd:cd07117 382 GPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
491-945 |
8.88e-60 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 212.31 E-value: 8.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 491 YTPIINGDRVNPR--EYSESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHE 568
Cdd:cd07116 1 YDNFIGGEWVAPVkgEYFDNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 569 LVAWMCYEVGKVVAEG-DAEVSEAVDFCRYYADEMeRLSSGYDRNFPGETNHYHYQgRGLAVV--ISPWNFPLAIPTGMT 645
Cdd:cd07116 80 LAVAETWDNGKPVRETlAADIPLAIDHFRYFAGCI-RAQEGSISEIDENTVAYHFH-EPLGVVgqIIPWNFPLLMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 646 AAALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGcRIIaeaav 725
Cdd:cd07116 158 APALAAGNCVVLKPAEQTPASILVLME-LIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTG-RLI----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 726 LQRGQSHIKRVIAEMGGKN-----AIIIDESAD-LDQAVAGVVQSAFGySGQKCSACSRVIVLESIYKPFVERLVAATQS 799
Cdd:cd07116 231 MQYASENIIPVTLELGGKSpniffADVMDADDAfFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 800 LNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQE-AELL------LSVPVPEMGYFVSPTIFTNvpPTATIAQEEIFGP 872
Cdd:cd07116 310 IKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEgAEVLtggernELGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGP 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22294137 873 VLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINrgITGAIVDRQPFGGFKLSGIG 945
Cdd:cd07116 388 VLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
550-949 |
6.32e-59 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 211.59 E-value: 6.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 550 ERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEG-DAEVSEAVDFCRYY---ADEMERLSSGYDRNFPGETNHyhyQGR 625
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYYagwADKIHGLTVPADGPHHVQTLH---EPI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVH 705
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 LIAFTGSQEVGcRIIAEAAvlqrGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESI 785
Cdd:PLN02466 277 KLAFTGSTDTG-KIVLELA----AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 786 YKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS--VPVPEMGYFVSPTIFTNVPPTAT 863
Cdd:PLN02466 352 YDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECggDRFGSKGYYIQPTVFSNVQDDML 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 864 IAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN--RGITGAIvdrqPFGGFKL 941
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFDAAI----PFGGYKM 507
|
....*...
gi 22294137 942 SGIGSKAG 949
Cdd:PLN02466 508 SGIGREKG 515
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
491-955 |
3.14e-58 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 207.93 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 491 YTPIINGDRVNPR-EYSESLNPSQPEEIVgRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHEL 569
Cdd:TIGR03374 2 HKLLINGELVSGEgEKQPVYNPATGEVIL-EIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 570 VAWMCYEVGKVV-AEGDAEVSEAVDFCRYYADEMERLS-SGYDRNFPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAA 647
Cdd:TIGR03374 81 AELESRNCGKPLhSVFNDEIPAIVDVFRFFAGAARCLSgLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 648 ALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlq 727
Cdd:TIGR03374 161 ALAAGNCVVLKPSEITPLTALKLAE-LAKDIFPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHILSHTA--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 728 rgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHL 807
Cdd:TIGR03374 237 ---PSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 808 PSTRVGPVVTAAARDRIQEYIakgqQEAELLLSVPV-------PEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAE 880
Cdd:TIGR03374 314 ESTELGPLSSLAHLERVMKAV----EEAKALGHIKVitggekrKGNGYYFAPTLLAGAKQDDAIVQKEVFGPVVSITSFD 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22294137 881 TFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITgaIVDRQPFGGFKLSGIG---SKAGGRDYLL 955
Cdd:TIGR03374 390 DEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYGkdmSLYGLEDYTV 465
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
546-966 |
2.70e-57 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 204.84 E-value: 2.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAegDAEVSEAVDFC---RYYADEMERLSSGYDRnfPGETNHYH- 621
Cdd:cd07098 37 TSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMV--DASLGEILVTCekiRWTLKHGEKALRPESR--PGGLLMFYk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 622 -----YQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPA----AVVAAKLAEILMAAGFPPGVFQFLPGRGS 692
Cdd:cd07098 113 rarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssGFFLSIIRECLAACGHDPDLVQLVTCLPE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 693 ViGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQK 772
Cdd:cd07098 193 T-AEALTSHPVIDHITFIGSPPVGKKVMAAAA------ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 773 CSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKG-QQEAELLLS---VPVPEM-- 846
Cdd:cd07098 266 CIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAvEKGARLLAGgkrYPHPEYpq 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 847 GYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINR-G 925
Cdd:cd07098 346 GHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDfG 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22294137 926 ITGAIVDrQPFGGFKLSGIGsKAGGRDYLLQFLEPRVITEN 966
Cdd:cd07098 426 VNYYVQQ-LPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
546-947 |
2.43e-55 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 200.37 E-value: 2.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMER-LSSG---YDRNFPG-ETNHY 620
Cdd:PLN00412 72 TPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRiLGEGkflVSDSFPGnERNKY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 621 HYQGR---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPY 697
Cdd:PLN00412 152 CLTSKiplGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 698 LTQHPDVHLIAFTGSqEVGCRIIAEAAV--LQrgqshikrviAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSA 775
Cdd:PLN00412 232 LTMHPGVNCISFTGG-DTGIAISKKAGMvpLQ----------MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 776 CSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTrVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEmGYFVSPTIF 855
Cdd:PLN00412 301 VKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCD-ITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE-GNLIWPLLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 856 TNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN----RGitgaiV 931
Cdd:PLN00412 379 DNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsapaRG-----P 453
|
410
....*....|....*.
gi 22294137 932 DRQPFGGFKLSGIGSK 947
Cdd:PLN00412 454 DHFPFQGLKDSGIGSQ 469
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
507-943 |
4.51e-52 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 190.55 E-value: 4.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 507 ESLNPSQPEEIVGRVGlATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDA 586
Cdd:PRK09457 18 ESRNPVSGEVLWQGND-ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 587 EVSEAVD----FCRYYAdemERlsSGYDRN-FPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPAD 661
Cdd:PRK09457 97 EVTAMINkiaiSIQAYH---ER--TGEKRSeMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 662 PAAVVAAKLAEILMAAGFPPGVFQFLPGrGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIA-EM 740
Cdd:PRK09457 172 LTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFA------GQPEKILAlEM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 741 GGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIY-KPFVERLVAATQSLNIGPAHL-PSTRVGPVVTA 818
Cdd:PRK09457 245 GGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDAePQPFMGAVISE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 819 AARDRI----QEYIAKGqqeAELLLSVPVPEMGY-FVSPTIF--TNVpptATIAQEEIFGPVLAVLRAETFTQALAIANA 891
Cdd:PRK09457 325 QAAQGLvaaqAQLLALG---GKSLLEMTQLQAGTgLLTPGIIdvTGV---AELPDEEYFGPLLQVVRYDDFDEAIRLANN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 22294137 892 TAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDrQPFGGFKLSG 943
Cdd:PRK09457 399 TRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSA-APFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
502-945 |
1.71e-50 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 185.45 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 502 PREYSESLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVV 581
Cdd:PRK13968 5 PATHAISVNPATGEQL-SVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 582 AEGDAEVSEAVDFCRYYADEMERLSSGYDRNFPGETNHYHYQGRGLAVVISPWNFPL------AIPTgmtaaaLVTGNCT 655
Cdd:PRK13968 84 NQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLwqvmrgAVPI------LLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 656 ILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPYLTQhPDVHLIAFTGSQEVGCRIIAEAAvlqrgqSHIKR 735
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAG------AALKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 736 VIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPV 815
Cdd:PRK13968 231 CVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 816 VTAAARDRIQEYIAKGQQE-AELLL-SVPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATA 893
Cdd:PRK13968 311 ARFDLRDELHHQVEATLAEgARLLLgGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 22294137 894 YALTGGLYSRTPSHIQQAKAQFAVGNLYINrGITgAIVDRQPFGGFKLSGIG 945
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLECGGVFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
508-949 |
2.30e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 183.11 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 508 SLNPSQPEEIvGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAE 587
Cdd:PLN02315 38 SVNPANNQPI-AEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 588 VSEAVDFCRYYADEMERLSSGYdrnFPGE-TNHYH---YQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPA 663
Cdd:PLN02315 117 VQEIIDMCDFAVGLSRQLNGSI---IPSErPNHMMmevWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 664 ---AVVAAKL-AEILMAAGFPPGVFQFLPGrGSVIGPYLTQHPDVHLIAFTGSQEVGcrIIAEAAVLQRgqshIKRVIAE 739
Cdd:PLN02315 194 pliTIAMTKLvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG--LMVQQTVNAR----FGKCLLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 740 MGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAA 819
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 820 ARDRIQEYIAKGQQEAELLL---SVPVPEmGYFVSPTIfTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYAL 896
Cdd:PLN02315 347 SKKNFEKGIEIIKSQGGKILtggSAIESE-GNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGL 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 897 TGGLYSRTPSHIQQAKAQFA--VGNLYINRGITGAIVDrQPFGGFKLSGIGSKAG 949
Cdd:PLN02315 425 SSSIFTRNPETIFKWIGPLGsdCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
551-949 |
1.29e-48 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 178.87 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 551 RATLLRRAADLLEA-----QRHELVAWMCyEVGKVVAEGDaevseavDFCRYYADEMERLSSGYDRNFPGETNHYHYQGR 625
Cdd:cd07087 30 KRMLTENEEEIAAAlyadlGKPPAEAYLT-EIAVVLGEID-------HALKHLKKWMKPRRVSVPLLLQPAKAYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFP--LAIPTgmTAAALVTGNCTILKPADPAAVVAAKLAEILmAAGFPPGVFQFLPGRGSVIGPYLTQHPD 703
Cdd:cd07087 102 GVVLIIGPWNYPlqLALAP--LIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVEGGVEVATALLAEPFD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 704 vhLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLE 783
Cdd:cd07087 179 --HIFFTGSPAVG-KIVMEAAA-----KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 784 SIYKPFVERLVAATQSLnIGPAHLPSTRVGPVVTAAARDRIQEYIA------KGQQEAELLlsvpvpemgyFVSPTIFTN 857
Cdd:cd07087 251 SIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDdgkvviGGQVDKEER----------YIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 858 VPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFG 937
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
|
410
....*....|....*
gi 22294137 938 GFKLSGIGS---KAG 949
Cdd:cd07087 400 GVGNSGMGAyhgKAG 414
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
546-949 |
5.45e-47 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 174.34 E-value: 5.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGD-AEV----SEAVDFCRYYADEMERLSSGYDRNFPGETNHY 620
Cdd:cd07134 17 STAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEIlpvlSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 621 HYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAgFPP---GVFQflpGrGSVIGPY 697
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEdevAVFE---G-DAEVAQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 698 LTQHPDVHlIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACS 777
Cdd:cd07134 172 LLELPFDH-IFFTGSPAVG-KIVMAAAA-----KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 778 RVIVLESIYKPFVERLVAAT-QSLNIGPAHLPSTRVGPVVTAAARDRIQEYI----AKGqqeAELLLSVPVPEMGYFVSP 852
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIeKFYGKDAARKASPDLARIVNDRHFDRLKGLLddavAKG---AKVEFGGQFDAAQRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 853 TIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVD 932
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNP 401
|
410
....*....|....*..
gi 22294137 933 RQPFGGFKLSGIGSKAG 949
Cdd:cd07134 402 NLPFGGVNNSGIGSYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
612-946 |
3.38e-45 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 170.59 E-value: 3.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 612 NFPGETnHYHYQGRGLAVVISPWNFPL---AIPTgmtAAALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLP 688
Cdd:PTZ00381 98 FGPGKS-YIIPEPLGVVLVIGAWNYPLnltLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVIE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 689 GRGSVIGPYLTQHPDvhLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGY 768
Cdd:PTZ00381 173 GGVEVTTELLKEPFD--HIFFTGSPRVG-KLVMQAAA-----ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 769 SGQKCSACSRVIVLESIYKPFVERLVAATQSLnIGPAHLPSTRVGPVVTAAARDRIQEYIA--KGQqeaeLLLSVPVPEM 846
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGK----VVYGGEVDIE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 847 GYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGI 926
Cdd:PTZ00381 320 NKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCV 399
|
330 340
....*....|....*....|
gi 22294137 927 TGAIVDRQPFGGFKLSGIGS 946
Cdd:PTZ00381 400 FHLLNPNLPFGGVGNSGMGA 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
550-945 |
1.82e-44 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) 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: 143466 [Multi-domain] Cd Length: 455 Bit Score: 167.60 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 550 ERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEmerLSSGYDRNFP-----GETNHYHYQG 624
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADE---LGQLGGREIPmgltpASAGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 R---GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGrGSVIGPYLTQH 701
Cdd:cd07148 122 RepiGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDVHLIAFTGSQEVGCRIIAEAAVlqrGQshikRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIV 781
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLAP---GT----RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 782 LESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYI----AKGqqeAELLL-SVPVPEMGYfvSPTIFT 856
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVneavAAG---ARLLCgGKRLSDTTY--APTVLL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 857 NVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGiTGAIVDRQPF 936
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPF 427
|
....*....
gi 22294137 937 GGFKLSGIG 945
Cdd:cd07148 428 AGRRQSGYG 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
494-923 |
9.15e-44 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 168.77 E-value: 9.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 494 IINGDRVNPREYS--ESLNPSQpEEIVGRVGLATIEDAEHAIRAAKAAQAQWQQTSVAERATLLRRAADLLEAQRHELVA 571
Cdd:PLN02419 117 LIGGSFVESQSSSfiDVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 572 WMCYEVGKVVAEGDAEVSEAVDFCRYyADEMERLSSG-YDRNFPGETNHYHY-QGRGLAVVISPWNFPLAIPTGMTAAAL 649
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEH-ACGMATLQMGeYLPNVSNGVDTYSIrEPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 650 VTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVFQFLPGRGSVIGPyLTQHPDVHLIAFTGSQEVGCRIIAEAAVlqRG 729
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAA--KG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 730 qshiKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLESIyKPFVERLVAATQSLNIGPAHLPS 809
Cdd:PLN02419 352 ----KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLVERAKALKVTCGSEPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 810 TRVGPVVTAAARDRIQEYIAKGQQE-AELLLS-----VPVPEMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFT 883
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDgAKLLLDgrdivVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 22294137 884 QALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYIN 923
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
625-949 |
6.73e-38 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 147.75 E-value: 6.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAgFPPGVFQFLPGRGSVIGPYLTQHPDv 704
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKFD- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 hLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIVLES 784
Cdd:cd07135 187 -KIFYTGSGRVG-RIIAEAAA-----KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLNIGPAHlPSTRVGPVVTAAARDRIQEYIAK--------GQQEAELLlsvpvpemgyFVSPTIFT 856
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGGAN-ASPDYTRIVNPRHFNRLKSLLDTtkgkvvigGEMDEATR----------FIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 857 NVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPF 936
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPF 408
|
330
....*....|...
gi 22294137 937 GGFKLSGIGSKAG 949
Cdd:cd07135 409 GGVGDSGYGAYHG 421
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
613-946 |
7.62e-36 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 141.47 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 613 FPGETNHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLPGrGS 692
Cdd:cd07133 90 FLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAE-LLAEYFDEDEVAVVTG-GA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 693 VIGPYLTQHPDVHLIaFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQK 772
Cdd:cd07133 168 DVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAA------ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 773 CSACSRVIVLESIYKPFVERLVAATQSlnigpaHLPSTRVGP----VVTAAARDRIQEYI----AKGQQEAELLLSVPVP 844
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAK------MYPTLADNPdytsIINERHYARLQGLLedarAKGARVIELNPAGEDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 845 EMGYFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALtgGLY--SRTPSHIQQAKAQFAVGNLYI 922
Cdd:cd07133 315 AATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPL--ALYyfGEDKAEQDRVLRRTHSGGVTI 392
|
330 340
....*....|....*....|....
gi 22294137 923 NRGITGAIVDRQPFGGFKLSGIGS 946
Cdd:cd07133 393 NDTLLHVAQDDLPFGGVGASGMGA 416
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
549-963 |
5.88e-35 |
|
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: 139.30 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 549 AERATLLRRAADLLEAQRHELVAwmcyevGKVVAEGDAEVSeAVDFC------RYYADEmerLSSGYDRNFPGET----- 617
Cdd:cd07084 21 PKRADFLARIIQRLAAKSYDIAA------GAVLVTGKGWMF-AENICgdqvqlRARAFV---IYSYRIPHEPGNHlgqgl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 618 ---NHYHYQGRGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAG-FPPGVFQFLPGRGSV 693
Cdd:cd07084 91 kqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 694 iGPYLTQHPDVHLIAFTGSQEVGCRIIAEAavlqrgqsHIKRVIAEMGGKNAIIIDESADLDQAVA-GVVQSAFGYSGQK 772
Cdd:cd07084 171 -MQALLLHPNPKMVLFTGSSRVAEKLALDA--------KQARIYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 773 CSACSRVIVLESIYK-PFVERLVA--ATQSLN---IGPAHLPSTRVGpvvTAAARDRIQEYIAKGQQEAELLLSVPVPem 846
Cdd:cd07084 242 CTAQSMLFVPENWSKtPLVEKLKAllARRKLEdllLGPVQTFTTLAM---IAHMENLLGSVLLFSGKELKNHSIPSIY-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 847 GYFVSPTIFTNVPP---TATIAQEEIFGPVLAVLRAETFTQALAIANAT--AYALTGGLYSRTPSHIQQAKAQFAV-GNL 920
Cdd:cd07084 317 GACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLALVLELLErmHGSLTAAIYSNDPIFLQELIGNLWVaGRT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22294137 921 Y-INRGITGAIVDRQPFGGFKLSGIGSKAGGRDYLLQFLEPRVI 963
Cdd:cd07084 397 YaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
612-946 |
3.46e-33 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 134.17 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 612 NFPGETnHYHYQGRGLAVVISPWNFP--LAI-PTgmtAAALVTGNCTILKPADPAAVVAAKLAEILMAAgFPPGVFQFLP 688
Cdd:cd07136 89 NFPSKS-YIYYEPYGVVLIIAPWNYPfqLALaPL---IGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 689 GRGSVIGPYLTQHPDvhLIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGY 768
Cdd:cd07136 164 GGVEENQELLDQKFD--YIFFTGSVRVG-KIVMEAAA-----KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 769 SGQKCSACSRVIVLESIYKPFVERLVAATQSLNiGPAHLPSTRVGPVVTAAARDRIQEYIAK------GQQEAELLlsvp 842
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLLDNgkivfgGNTDRETL---- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 843 vpemgyFVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYI 922
Cdd:cd07136 311 ------YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI 384
|
330 340
....*....|....*....|....
gi 22294137 923 NRGITGAIVDRQPFGGFKLSGIGS 946
Cdd:cd07136 385 NDTIMHLANPYLPFGGVGNSGMGS 408
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
626-946 |
2.10e-30 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 125.41 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILmaagfP----PGVFQFLPGRGSVIGPYLTQH 701
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PkyldKECYPVVLGGVEETTELLKQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDvhLIAFTGSQEVGcRIIAEAAvlqrgQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIV 781
Cdd:cd07132 177 FD--YIFYTGSTSVG-KIVMQAA-----AKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 782 LESIYKPFVERLVAATQSL-NIGPAHLPStrVGPVVTAAARDRIQEYIAKGQ-------QEAELllsvpvpemgyFVSPT 853
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEFyGEDPKESPD--YGRIINDRHFQRLKKLLSGGKvaiggqtDEKER-----------YIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 854 IFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDR 933
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDS 395
|
330
....*....|...
gi 22294137 934 QPFGGFKLSGIGS 946
Cdd:cd07132 396 LPFGGVGNSGMGA 408
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
547-911 |
7.08e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.12 E-value: 7.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 547 SVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYAD------------EMERLSSGYDRNFP 614
Cdd:PRK11903 61 TYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaalgdarllrDGEAVQLGKDPAFQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 615 GEtnHYHYQGRGLAVVISPWNFPlaiPTGM---TAAALVTGNCTILKPADPAAVVAAKLAEILMAAG-FPPGVFQFLPGR 690
Cdd:PRK11903 141 GQ--HVLVPTRGVALFINAFNFP---AWGLwekAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 691 GSVIGPYLtQHPDVhlIAFTGSQEVGCRIIAEAAVLQRGQshikRVIAEMGGKNAIII--DESAD---LDQAVAGVVQSA 765
Cdd:PRK11903 216 SAGLLDHL-QPFDV--VSFTGSAETAAVLRSHPAVVQRSV----RVNVEADSLNSALLgpDAAPGseaFDLFVKEVVREM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 766 FGYSGQKCSACSRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLS----V 841
Cdd:PRK11903 289 TVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDgggfA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 842 PV---PEMGYFVSPTIF-TNVPPTATIAQE-EIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQA 911
Cdd:PRK11903 369 LVdadPAVAACVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
123-428 |
3.95e-27 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 115.95 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 123 AGETTEQVLKTIGRLRKQGMLVTMDILGEAVITEAEaqqyCDRYL------------------------------DLMEH 172
Cdd:PLN02681 90 AGEDAEEAARTVRRLWELGLGGILDYAAEDAGDNAA----CDRNLekflaairaaatlppssssaavkitalcppSLLER 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 173 LSPLGQREGVNP------VQVSVKLTAFYSQF-------DPLDVSGCR--AKVGEPIRRLLHRAQELGVAVHFDMEQY-- 235
Cdd:PLN02681 166 VSDLLRWQDRDPngklpwKQWSFPLFADSSPLyhatsepEPLTAEEERllELAHERLQKLCERAAQLGVPLLIDAEYTsl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 236 --AYKDITLAilkdilLEPEF---RDRADIGLTLQAYLRDSYQDAQDLITWVQQRGTPITVRVVKGAYWDQELIKAVQHH 310
Cdd:PLN02681 246 qpAIDYITYD------LAREFnkgKDRPIVYGTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 311 WPLPVYQHKQNTDANFERIIELLL-----SHHTVLrtaIASHNVRSQARAIAIAQRQHIPP---TAMECQvLYGMADKLA 382
Cdd:PLN02681 320 VPSPVHDTIQDTHACYNRCAEFLLekasnGDGEVM---LATHNVESGELAAAKMNELGLHKgdpRVQFAQ-LLGMSDNLS 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 22294137 383 KALVEAGQTVRVYCPYGDLIPGMAYLIRRLLEN---TANSSFLRQQLGA 428
Cdd:PLN02681 396 FGLGNAGFRVSKYLPYGPVEEVIPYLLRRAEENrglLSGSAIDRQLLRK 444
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
626-949 |
2.10e-25 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 110.19 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVh 705
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIEGGVPETTALLEQKWDK- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 lIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGY-SGQKCSACSRVIVLES 784
Cdd:cd07137 181 -IFFTGSPRVG-RIIMAAAA-----KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 IYKPFVERLVAATQSLnIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATI 864
Cdd:cd07137 254 FAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDSSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 865 AQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGI 944
Cdd:cd07137 333 MTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
....*
gi 22294137 945 GSKAG 949
Cdd:cd07137 413 GAYHG 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
546-902 |
2.41e-25 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 110.71 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 546 TSVAERATLLRRAADLLEAQRHELVAWMCYEVGKVVAEGDAEVSEAVDFCRYYADEMERLS--------SGYDRNFPGET 617
Cdd:cd07129 18 LSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSwldaridpADPDRQPLPRP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 618 NHYHYQGR-GLAVVISPWNFPLAIPT--GMTAAALVTGNCTILKPADPAAVVAAKLAEILMAA----GFPPGVFQFLPGR 690
Cdd:cd07129 98 DLRRMLVPlGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 691 GSVIGPYLTQHPDVHLIAFTGSQEVGcRIIAEAAvLQRGQShiKRVIAEMGGKNAIIIDESA---DLDQAVAGVVQSAFG 767
Cdd:cd07129 178 GREVGVALVKHPAIKAVGFTGSRRGG-RALFDAA-AARPEP--IPFYAELGSVNPVFILPGAlaeRGEAIAQGFVGSLTL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 768 YSGQKCSACSRVIVLESI-YKPFVERLVAATQslnigpAHLPSTRVGPVVTAAARDRIQEyiAKGQQEAELLLSVPVPEM 846
Cdd:cd07129 254 GAGQFCTNPGLVLVPAGPaGDAFIAALAEALA------AAPAQTMLTPGIAEAYRQGVEA--LAAAPGVRVLAGGAAAEG 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 847 GYFVSPTIFTnVPPTATIA----QEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYS 902
Cdd:cd07129 326 GNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHG 384
|
|
| PutA_N |
pfam18083 |
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) ... |
6-121 |
4.67e-25 |
|
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) proteins present in Geobacter sulfurreducens. PutA are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of l-proline to l-glutamate and couple the oxidation of imported proline imported to the reduction of membrane-associated quinones. This domain is located at the N-terminus and is referred to as the alpha domain. The hydrocarbon tail of Zwittergent 3-12 binds to an exposed hydrophobic patch of the alpha domain which contains aromatic and nonpolar residues. The domain may be involved in membrane association.
Pssm-ID: 436258 Cd Length: 113 Bit Score: 100.51 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 6 EAETIAIARQLWAASQ-ESRNFFsqlrEQMRIEDKLLGWAMEHPGLRVQLFRLIDCLPSLRSQTEVARHLQEYLSDPSVE 84
Cdd:pfam18083 1 EARTQRIGRELFAALSgERPSLF----DRRWWDDKLMEWAMKDEQLKVQLFRFVDVLPALKTPAEVARHLREYLGDVQDE 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 22294137 85 LPPGLKKLLNFAQPDSLPAQAAATTFTTAVQALAHKY 121
Cdd:pfam18083 77 LPQPLRWALRAADGGSLGGRALAKAARKGAEQMARRF 113
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
625-923 |
6.92e-25 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 110.05 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 625 RGLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAG-FPPGVFQFLPGRGsviGPYLTQ--H 701
Cdd:cd07128 145 RGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSV---GDLLDHlgE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDVhlIAFTGSQEVGCRIIAEAAVLQRGqshiKRVIAEMGGKNAIIIDESA-----DLDQAVAGVVQSAFGYSGQKCSAC 776
Cdd:cd07128 222 QDV--VAFTGSAATAAKLRAHPNIVARS----IRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 777 SRVIVLESIYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPV--------PEMGY 848
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDrfevvgadAEKGA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22294137 849 FVSPTIFTNVPPTATIA--QEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFA--VGNLYIN 923
Cdd:cd07128 376 FFPPTLLLCDDPDAATAvhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAApyHGRLLVL 454
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
626-945 |
2.23e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 95.56 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILmAAGFPPGVFQFLPGrGSVIGPYLTQHP-DV 704
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEG-GPAVGEQLLQHKwDK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 705 hlIAFTGSQEVGcRIIAEAAVlqrgqSHIKRVIAEMGGKNAIIID---ESADLDQAVAGVVQSAFGY-SGQKCSACSRVI 780
Cdd:PLN02203 188 --IFFTGSPRVG-RIIMTAAA-----KHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 781 VLESiYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEMGYFVSPTIFTNVPP 860
Cdd:PLN02203 260 VEER-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEPTILLNPPL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 861 TATIAQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFK 940
Cdd:PLN02203 339 DSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVG 418
|
....*
gi 22294137 941 LSGIG 945
Cdd:PLN02203 419 ESGFG 423
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
626-949 |
8.53e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 90.88 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEiLMAAGFPPGVFQFLPGRGSVIGPYLTQHPDVh 705
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVVEGAVTETTALLEQKWDK- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 706 lIAFTGSQEVGCRIIAEAAvlqrgqSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFG-YSGQKCSACSRVIVLES 784
Cdd:PLN02174 192 -IFYTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 785 iYKPFVERLVAATQSLNIGPAHLPSTRVGPVVTAAARDRIQEYIAKGQQEAELLLSVPVPEMGYFVSPTIFTNVPPTATI 864
Cdd:PLN02174 265 -YAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 865 AQEEIFGPVLAVLRAETFTQALAIANATAYALTGGLYSRTPSHIQQAKAQFAVGNLYINRGITGAIVDRQPFGGFKLSGI 944
Cdd:PLN02174 344 MSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGM 423
|
....*
gi 22294137 945 GSKAG 949
Cdd:PLN02174 424 GAYHG 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
626-913 |
9.15e-16 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 80.77 E-value: 9.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILM----AAGFPPGVFQFLPGRGSVIGPYLTQH 701
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLqaavAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 702 PDVHLIAFTGSQevgcriiaeaAVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACSRVIV 781
Cdd:cd07081 177 PGIGLLLATGGP----------AVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 782 LESIYKPFVERLvaatqslnigpahlpSTRVGPVVTAAARDRIQEYIAK---------GQQE---AELL-LSVPVPEMGY 848
Cdd:cd07081 247 VDSVYDEVMRLF---------------EGQGAYKLTAEELQQVQPVILKngdvnrdivGQDAykiAAAAgLKVPQETRIL 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22294137 849 FVSPTIFTNVPPTATiaqeEIFGPVLAVLRAETFTQALAIanATAYALTGGLYSRTPSHIQQAKA 913
Cdd:cd07081 312 IGEVTSLAEHEPFAH----EKLSPVLAMYRAANFADADAK--ALALKLEGGCGHTSAMYSDNIKA 370
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
617-930 |
2.20e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 74.05 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 617 TNHYHYQGRGLAVVISPWNFPL--AIPtGMTAAaLVTGNCTILK---PADPAAVVAAKLA-EILMAAGFPPGVFQFLP-G 689
Cdd:cd07127 186 EKTFTVVPRGVALVIGCSTFPTwnGYP-GLFAS-LATGNPVIVKphpAAILPLAITVQVArEVLAEAGFDPNLVTLAAdT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 690 RGSVIGPYLTQHPDVHLIAFTGSQEVGCRIIAEAAVLQrgqshikrVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYS 769
Cdd:cd07127 264 PEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYS 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 770 GQKCSACSRVIV-LESI--------YKPFVERLVAATQSLNIGPAhLPSTRVGPVVTAAARDRiqeyIAKGQQEAELLLS 840
Cdd:cd07127 336 GQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGLLADPA-RAAALLGAIQSPDTLAR----IAEARQLGEVLLA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 841 VPVPEMGYFVSPTIFTNVPPTATIAQ-----EEIFGPVLAVLRAETFTQALAIANATAY---ALTGGLYSRTPSHIQQAK 912
Cdd:cd07127 411 SEAVAHPEFPDARVRTPLLLKLDASDeaayaEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDPEVVERVQ 490
|
330 340
....*....|....*....|
gi 22294137 913 -AQFAVG-NLYINrgITGAI 930
Cdd:cd07127 491 eAALDAGvALSIN--LTGGV 508
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
611-946 |
1.71e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 70.99 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 611 RNFPGETNHYHYQGRGL------AVVISPWNFPLAIPTGMTAAALVTGNCTILKPADPAAVVAAKLAEILMAAGFPPGVF 684
Cdd:cd07126 123 RSFNVPGDHQGQQSSGYrwpygpVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 685 QFLPGRGSVIGPYLTQhPDVHLIAFTGSQEVGCRIiaeaAVLQRGQshIKrvIAEMGGKNAIIIDESADLDQAVAGVVQS 764
Cdd:cd07126 203 DLIHSDGPTMNKILLE-ANPRMTLFTGSSKVAERL----ALELHGK--VK--LEDAGFDWKILGPDVSDVDYVAWQCDQD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 765 AFGYSGQKCSACSRVIVLESIYK-PFVERLVAATQSLNigpahLPSTRVGPVVTAAARdRIQEYIAKgqqeaelLLSVPV 843
Cdd:cd07126 274 AYACSGQKCSAQSILFAHENWVQaGILDKLKALAEQRK-----LEDLTIGPVLTWTTE-RILDHVDK-------LLAIPG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 844 PEMGY-------FVSPTIFTNVPPTAT--------------IAQEEIFGP--VLAVLRAETFTQALAIANATAYALTGGL 900
Cdd:cd07126 341 AKVLFggkpltnHSIPSIYGAYEPTAVfvpleeiaieenfeLVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAV 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 22294137 901 YSRTPSHIQQAKAQFAVGNLY--INRGITGAIVDR--QPFGGFKLSGIGS 946
Cdd:cd07126 421 VSNDIRFLQEVLANTVNGTTYagIRARTTGAPQNHwfGPAGDPRGAGIGT 470
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
648-910 |
5.25e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 65.98 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 648 ALVTGNCTILKPADPAAVVAAKLAEIL----MAAGFPPGVFQFLPGRGSVIGPYLTQHPDVHLIAFTGSqevgcriiaeA 723
Cdd:cd07122 119 ALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG----------P 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 724 AVLQRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQS-AFGYsGQKCSACSRVIVLESIYKPFVERLVAAtqslni 802
Cdd:cd07122 189 GMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRAELKRR------ 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 803 GpAHLpstrvgpvVTAAARDRIQEY------------IAKGQQE-AELL-LSVPvPEMGYFVSPtiFTNVPPTATIAQEE 868
Cdd:cd07122 262 G-AYF--------LNEEEKEKLEKAlfddggtlnpdiVGKSAQKiAELAgIEVP-EDTKVLVAE--ETGVGPEEPLSREK 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22294137 869 IFgPVLAVLRAETFTQALAIANA-TAYA---LTGGLYSRTPSHIQQ 910
Cdd:cd07122 330 LS-PVLAFYRAEDFEEALEKARElLEYGgagHTAVIHSNDEEVIEE 374
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
698-889 |
1.57e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 58.02 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 698 LTQHPDVHLIAFTGSQEVGcriiaeAAVLQRGqshiKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFGYSGQKCSACS 777
Cdd:cd07121 175 LMAHPDINLLVVTGGPAVV------KAALSSG----KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEK 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 778 RVIVLESIYKPFVERL-------VAATQSLNIgpahLPSTRVGPVVTAAARDRIqeyiakGQQEAELL--LSVPVPEmgy 848
Cdd:cd07121 245 EVIAVDSVADYLIAAMqrngayvLNDEQAEQL----LEVVLLTNKGATPNKKWV------GKDASKILkaAGIEVPA--- 311
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22294137 849 fVSPTIFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIA 889
Cdd:cd07121 312 -DIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
626-793 |
2.33e-08 |
|
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: 57.23 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 626 GLAVVISPWNFPLAIPTgMTAAALVTGNCTILKPADPAAVVAAKLAEIL---MAAGFPPGVFQFLPGRGSVIGPYLTQHP 702
Cdd:cd07077 102 GVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPKILVLYVPHPSDELAEELLSHP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 703 DVHLIAFTGSQEVgcriiAEAAvlqRGQSHIKRVIAEMGGKNAIIIDESADLDQAVAGVVQSAFgYSGQKCSACSRVIVL 782
Cdd:cd07077 181 KIDLIVATGGRDA-----VDAA---VKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVV 251
|
170
....*....|.
gi 22294137 783 ESIYKPFVERL 793
Cdd:cd07077 252 DDVLDPLYEEF 262
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
698-889 |
3.28e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.22 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 698 LTQHPDVHLIAFTGSQEVGcriiaeAAVLQRGqshiKRVIAEMGGKNAIIIDESADLDQAVAGVVQSA-FGYSgQKCSAC 776
Cdd:PRK15398 207 LMKHPGIALLVVTGGPAVV------KAAMKSG----KKAIGAGAGNPPVVVDETADIEKAARDIVKGAsFDNN-LPCIAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 777 SRVIVLESIYKPFVERLVAAtQSLNIGPAHLpsTRVGPVVT----AAARDriqeYIAKgqqEAELLLS---VPVPEmgyf 849
Cdd:PRK15398 276 KEVIVVDSVADELMRLMEKN-GAVLLTAEQA--EKLQKVVLknggTVNKK----WVGK---DAAKILEaagINVPK---- 341
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22294137 850 vSPT-IFTNVPPTATIAQEEIFGPVLAVLRAETFTQALAIA 889
Cdd:PRK15398 342 -DTRlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
671-891 |
1.19e-06 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 52.49 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 671 AEIL----MAAGFPPGVFQFLPGrgsvigP------YLTQHPDVHLIAFTGsqevgcriiaeaavlqrGQSHIKrvIAEM 740
Cdd:PRK13805 155 AKIVldaaVAAGAPKDIIQWIEE------PsveltnALMNHPGIALILATG-----------------GPGMVK--AAYS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 741 GGKNAI---------IIDESADLDQAVAGVVQS-AFGYsGQKCSACSRVIVLESIYKPFVERLvaatqslnigpahlpST 810
Cdd:PRK13805 210 SGKPALgvgagnvpaYIDKTADIKRAVNDILLSkTFDN-GMICASEQAVIVDDEIYDEVKEEF---------------AS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22294137 811 RVGPVVTAAARDRIQEYIAKGQQEAellLSVPVP--------EMGYFvsptiftNVPPTATI--------------AQEE 868
Cdd:PRK13805 274 HGAYFLNKKELKKLEKFIFGKENGA---LNADIVgqsaykiaEMAGF-------KVPEDTKIliaevkgvgeseplSHEK 343
|
250 260
....*....|....*....|...
gi 22294137 869 IFgPVLAVLRAETFTQALAIANA 891
Cdd:PRK13805 344 LS-PVLAMYKAKDFEDAVEKAEK 365
|
|
| |
