|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
1-464 |
0e+00 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 831.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 1 MNTSELETLIRTILSEQLTTPAQ-TPVQPQGKGIFQSVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAE 79
Cdd:PRK15398 1 MNQQDIEQVVKAVLAEMLSSQTVsPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 80 ESANETGMGNKEDKFLKNKAALDNTPGVEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSV 159
Cdd:PRK15398 81 LAVEETGMGRVEDKIAKNVAAAEKTPGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 160 YFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGIVAMGMKSGKKVIGAGA 239
Cdd:PRK15398 161 VFSPHPGAKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 240 GNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLSPTDTDKLRAVCLPEGQ-AN 318
Cdd:PRK15398 241 GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGGtVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 319 KKLVGKSPSAMLEAAGIAVPaKAPRLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNV 398
Cdd:PRK15398 321 KKWVGKDAAKILEAAGINVP-KDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNRHTAIMHSRNV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447020428 399 SRLNLAARTLQTSIFVKNGPSYAGIGVGGEGFTTFTIATPTGEGTTSARTFARSRRCVLTNGFSIR 464
Cdd:PRK15398 400 DNLNKMARAIQTSIFVKNGPSYAGLGLGGEGFTTFTIATPTGEGVTSARTFTRRRRCVLVDGFRIR 465
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
32-458 |
0e+00 |
|
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: 677.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 32 GIFQSVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKFLKNKAALDNTPGVEDLT 111
Cdd:cd07121 1 GVFATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 112 TTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNL 191
Cdd:cd07121 81 TTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 192 VVTVAEPTFEATQQMMAHPRIAVLAITGGPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPC 271
Cdd:cd07121 161 VVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 272 IAEKSLIVVESVAERLVQQMQTFGALLLSPTDTDKLRAVCL---PEGQANKKLVGKSPSAMLEAAGIAVPAKaPRLLIAV 348
Cdd:cd07121 241 IAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLltnKGATPNKKWVGKDASKILKAAGIEVPAD-IRLIIVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 349 VNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNVSRLNLAARTLQTSIFVKNGPSYAGIGVGGE 428
Cdd:cd07121 320 TDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGLGVGGE 399
|
410 420 430
....*....|....*....|....*....|
gi 447020428 429 GFTTFTIATPTGEGTTSARTFARSRRCVLT 458
Cdd:cd07121 400 GYTTFTIAGPTGEGLTSARTFTRRRRCVLV 429
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
39-457 |
1.29e-111 |
|
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: 336.55 E-value: 1.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 39 EAIDAAHQAFLRYQQcplKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKFLKNKAALDNTPGVE--DLTTTALT 116
Cdd:cd07081 6 AAAKVAQQGLSCKSQ---EMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYkdEKTCGVLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 GDG-GMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTV 195
Cdd:cd07081 83 GDEnGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 196 AEPTFEATQQMMAHPRIAVLAITGGPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEK 275
Cdd:cd07081 163 DNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 276 SLIVVESVAERLVQQMQTFGALLLSPTDTDKLRAVCLPEGQANKKLVGKSPSAMLEAAGIAVPaKAPRLLIAVVN--ADD 353
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVP-QETRILIGEVTslAEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 354 PWVTSEQLMPMLPVVKVSDFDSAL--ALALKVEEGLHHTAIMHSQNVS---RLNLAARTLQTSIFVKNGP-SYAGIGVGG 427
Cdd:cd07081 322 EPFAHEKLSPVLAMYRAANFADADakALALKLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKNGPcSQGGLGDLY 401
|
410 420 430
....*....|....*....|....*....|....*..
gi 447020428 428 E--GFTTFTIATPT--GEGTTS---ARTFARSRRCVL 457
Cdd:cd07081 402 NfrGWPSMTLGCGTwgGNSVSEnvgPKHLVNLKTVAL 438
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
77-432 |
1.77e-90 |
|
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: 281.69 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 77 LAEESANETGMGNKEDKFLKNKAAL---------DNTPGV--EDLTTtaltgdgGMVlfEY-SPFGVIGSVAPSTNPTET 144
Cdd:cd07122 41 LAKMAVEETGMGVVEDKVIKNHFASeyvyndikdMKTVGVieEDEEK-------GIV--EIaEPVGVIAALIPSTNPTST 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 145 IINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiAFRCCGI-RNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGI 223
Cdd:cd07122 112 AIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMRE-AAVAAGApEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 224 VAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLSPTD 303
Cdd:cd07122 191 VKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKRRGAYFLNEEE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 304 TDKLRAVCLPEGQA-NKKLVGKSPSAMLEAAGIAVPAKApRLLIA---VVNADDPWvTSEQLMPMLPVVKVSDFDSALAL 379
Cdd:cd07122 271 KEKLEKALFDDGGTlNPDIVGKSAQKIAELAGIEVPEDT-KVLVAeetGVGPEEPL-SREKLSPVLAFYRAEDFEEALEK 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447020428 380 ALKV--EEGLHHTAIMHSQNVSRLNLAARTLQTSIFVKNGPSyagiGVGGEGFTT 432
Cdd:cd07122 349 ARELleYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPS----SLGGIGDTY 399
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
77-424 |
1.76e-66 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 228.53 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 77 LAEESANETGMGNKEDKFLKNKAAL---------DNTPGV--EDLTTtaltgdGGMVLFEysPFGVIGSVAPSTNPTETI 145
Cdd:PRK13805 54 LAKMAVEETGRGVVEDKVIKNHFASeyiynsykdEKTVGVieEDDEF------GIIEIAE--PVGVIAGITPTTNPTSTA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 146 INNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIA-VLAiTGGPGIV 224
Cdd:PRK13805 126 IFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIAlILA-TGGPGMV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 225 AMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLSPTDT 304
Cdd:PRK13805 205 KAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKEL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 305 DKLRAVCLPE--GQANKKLVGKSPSAMLEAAGIAVPAKApRLLIAV---VNADDPWvTSEQLMPMLPVVKVSDFDSALAL 379
Cdd:PRK13805 285 KKLEKFIFGKenGALNADIVGQSAYKIAEMAGFKVPEDT-KILIAEvkgVGESEPL-SHEKLSPVLAMYKAKDFEDAVEK 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 447020428 380 ALKVEE--GLHHTAIMHSQNVSRLNLAARTLQTS-IFVkNGP-SYAGIG 424
Cdd:PRK13805 363 AEKLVEfgGLGHTAVIYTNDDELIKEFGLRMKACrILV-NTPsSQGGIG 410
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
59-457 |
1.04e-65 |
|
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: 216.32 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 59 RSAIISAMRQELTPLLATLAEESANETG-------------MGNKEDKFLKNKAALDNTPGVEDLTTTALTGDGGMVLFE 125
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITASVGHIQDVLLPDNGETYVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTeTIINNSISMLAAGNSVYFSPHPGAkKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQ 205
Cdd:cd07077 98 AFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSA-PFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHPRIAVLAITGGPGIVAMGMKS--GKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDyNLPCIAEKSLIVVESV 283
Cdd:cd07077 176 LLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDDV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 284 AERLVQQMQTFGALllsptdtdklravclpegqankklvgkspsamleaAGIAVPAKaPRLLIAVVNADDPWVTSEQLMP 363
Cdd:cd07077 255 LDPLYEEFKLKLVV-----------------------------------EGLKVPQE-TKPLSKETTPSFDDEALESMTP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 364 MLPVVKVSDFDSALALALKV--EEGLHHTAIMHSQNVSRLNLAARTLQTSIFVKNGPS--YAGIGVGGEGFTTFTIATPT 439
Cdd:cd07077 299 LECQFRVLDVISAVENAWMIieSGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSkkGRGAFAGKGVERIVTSGMNN 378
|
410
....*....|....*....
gi 447020428 440 GEGT-TSARTFARSRRCVL 457
Cdd:cd07077 379 IFGAgVGHDALRPLKRLVR 397
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
62-446 |
9.60e-60 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 203.17 E-value: 9.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 62 IISAMRQELTPLLATLAEESANETGMGNKEDKFLKNK-AALDNTPGVEDLTTTA-LTGDGGMVLFEYS-PFGVIGSVAPS 138
Cdd:TIGR02518 35 IVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVfAATIVYDSIKDMKTIGiLSEDKEKKVIEIAvPVGVVAGLIPS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 139 TNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAIT 218
Cdd:TIGR02518 115 TNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCITVPTIEGTNELMKNKDTSLILAT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 219 GGPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALL 298
Cdd:TIGR02518 195 GGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQSIIVEECNKDAVVEELKKQGGYF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 299 LSPTDTDKL-RAVCLPEGQANKKLVGKSPSAMLEAAGIAVPAKApRLLIA---VVNADDPWvTSEQLMPMLPVVKVSDFD 374
Cdd:TIGR02518 275 LTAEEAEKLgKFILRPNGTMNPQIVGKSPQVIANLAGLTVPEDA-KVLIGeqnGVGNKNPY-SREKLTTILAFYTEENWH 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447020428 375 SALALALKV--EEGLHHTAIMHSQNVSRL-NLAARTLQTSIFVKNGPSYAGIGVGGEGFTTFTIATPTGEGTTSA 446
Cdd:TIGR02518 353 EACELSIELlqNEGAGHTLIIHSENKDIVrEFALKKPVSRMLVNTGGSLGGIGATTNLVPAFTLGCGAVGGSSTS 427
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
42-457 |
2.18e-43 |
|
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: 156.62 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 42 DAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETG--MGNKEDKFLKNKAALDNTPGVEDL---TTTALT 116
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKlggPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 GDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRccgiRNLVVTVA 196
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLP----PGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 197 EPTFEATQQMMAHPRIAVLAITGGPG----IVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCI 272
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAvgkaIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 273 AEKSLIVVESVAERLVQQMQTfgalllsptdtdklravclpegqankklvgkspsamleaagiavpakaprlLIAVVNAD 352
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT---------------------------------------------------VLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 353 DPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQTSIFVKNGPSyagigVGGEGFTT 432
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGL--TAGVFTRDLNRALRVAERLRAGTVYINDSS-----IGVGPEAP 338
|
410 420
....*....|....*....|....*....
gi 447020428 433 FTIATPTGEG----TTSARTFARSRRCVL 457
Cdd:cd06534 339 FGGVKNSGIGreggPYGLEEYTRTKTVVI 367
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
39-419 |
2.92e-27 |
|
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: 113.07 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 39 EAIDAAHQAFLRYQQCPLKTRSAIISAMRQEL---TPLLATLA--------EESANETGMGNKEDKFLKnKAALDNTPgv 107
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLeerREELAALEtletgkpiEEALGEVARAADTFRYYA-GLARRLHG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 108 edlTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiafrcCG 187
Cdd:cd07078 79 ---EVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE-----AG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 188 I-RNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPG----IVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIING 262
Cdd:cd07078 151 LpPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 263 ASFDYNLPCIAEKSLIVVESVA----ERLVQQMQTF--GALLLSPTDTDKLravcLPEGQANK--KLV--GKSPSAMLEA 332
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYdefvERLVERVKALkvGNPLDPDTDMGPL----ISAAQLDRvlAYIedAKAEGAKLLC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 333 AGIAVPAKAPRL----LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTL 408
Cdd:cd07078 307 GGKRLEGGKGYFvpptVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGL--AAGVFTRDLERALRVAERL 384
|
410
....*....|.
gi 447020428 409 QTSIFVKNGPS 419
Cdd:cd07078 385 EAGTVWINDYS 395
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-400 |
5.69e-24 |
|
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: 103.97 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKFLKNKAA---------------- 100
Cdd:cd07145 23 VREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIrlfklaaeeakvlrge 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 101 ---LDNTPGVEdltttaltgdGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISL 177
Cdd:cd07145 103 tipVDAYEYNE----------RRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 178 IEEIAFRcCGIRNLVVTVAEptfEATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLV 253
Cdd:cd07145 173 LEEAGLP-PGVINVVTGYGS---EVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 254 KAAEDIINGaSFDY-NLPCIAEKSLIVVESVAERLVQQM-QTFGALLL-SPTDTD-------KLRAVCLPEGQANKKlVG 323
Cdd:cd07145 249 RAVSIAVRG-RFENaGQVCNAVKRILVEEEVYDKFLKLLvEKVKKLKVgDPLDEStdlgpliSPEAVERMENLVNDA-VE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447020428 324 KSPSAMLEAAGIAVPAKAPRLLiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHhtAIMHSQNVSR 400
Cdd:cd07145 327 KGGKILYGGKRDEGSFFPPTVL-ENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ--ASVFTNDINR 400
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
37-429 |
4.66e-23 |
|
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: 101.45 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedkflKNKA-ALDNTPGV-------- 107
Cdd:pfam00171 31 VDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG---------KPLAeARGEVDRAidvlryya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 108 ---EDLTTTALTGDGGMVLFE-YSPFGVIGSVAPSTNPtetiINNSISM----LAAGNSVYFSPHPGAKKVSLKLISLIE 179
Cdd:pfam00171 102 glaRRLDGETLPSDPGRLAYTrREPLGVVGAITPWNFP----LLLPAWKiapaLAAGNTVVLKPSELTPLTALLLAELFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 180 EIAFRCcGIRNLVVTVAEptfEATQQMMAHPRIAVLAITGGPG----IVAMGMKSGKKVIGAGAGNPPCIVDETADLVKA 255
Cdd:pfam00171 178 EAGLPA-GVLNVVTGSGA---EVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQ------TFGalllSPTDTD-KLRAVClPEGQANK--KLV--GK 324
Cdd:pfam00171 254 VEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVeaakklKVG----DPLDPDtDMGPLI-SKAQLERvlKYVedAK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 325 SPSAMLEAAGIAVPAK----APrLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSR 400
Cdd:pfam00171 329 EEGAKLLTGGEAGLDNgyfvEP-TVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL--AAGVFTSDLER 405
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 447020428 401 LNLAARTLQT--------SIFVKNGPSYAGI---GVGGEG 429
Cdd:pfam00171 406 ALRVARRLEAgmvwindyTTGDADGLPFGGFkqsGFGREG 445
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
37-431 |
1.10e-22 |
|
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: 100.20 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKF--------LKNKAALDNTPGVE 108
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdraidtLRLAAEEAERIRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 109 DLTTTALTGDGG-MVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiafrcCG 187
Cdd:cd07094 103 EIPLDATQGSDNrLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVE-----AG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 188 IRNLVVTVAEPTFEATQQMMA-HPRIAVLAITGGpGIVAMGMKS---GKKVIGAGAGNPPCIVDETADLVKAAEDIINGA 263
Cdd:cd07094 178 VPEGVLQVVTGEREVLGDAFAaDERVAMLSFTGS-AAVGEALRAnagGKRIALELGGNAPVIVDRDADLDAAIEALAKGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 264 SFDYNLPCIAEKSLIVVESVAERLVQ---------------QMQTFGALLLSPTDTDKLRAVCLPEGQANKKLV--GKSP 326
Cdd:cd07094 257 FYHAGQVCISVQRIYVHEELYDEFIEafvaavkklkvgdplDEDTDVGPLISEEAAERVERWVEEAVEAGARLLcgGERD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 327 SAMLEAAgiavpakaprlLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNVSrLNLAAR 406
Cdd:cd07094 337 GALFKPT-----------VLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA-FKAAEK 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 447020428 407 TLQTSIFVKNGPSY------------AGIGVGGEGFT 431
Cdd:cd07094 405 LEVGGVMVNDSSAFrtdwmpfggvkeSGVGREGVPYA 441
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
37-410 |
5.40e-19 |
|
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: 88.92 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAE-ESANeTGMgnkedkfLKNKAALDNTPGVEDLT---T 112
Cdd:cd07092 21 VDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAAlESRN-TGK-------PLHLVRDDELPGAVDNFrffA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 113 TALTGDGGMVLFEYS----------PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07092 93 GAARTLEGPAAGEYLpghtsmirrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRccGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITGGPGivamgmkSGKKVIGAGA-----------GNPPCIVDETAD 251
Cdd:cd07092 173 PP--GVVNVVCGGGASAGDA---LVAHPRVRMVSLTGSVR-------TGKKVARAAAdtlkrvhlelgGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 252 LVKAAEDIINGASFDYNLPCIAEKSLIVVESV----AERLVQQMQTFgaLLLSPTDTDKLRAVCLPEGQANK--KLVGKS 325
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVydefVAALVEAVSAI--RVGDPDDEDTEMGPLNSAAQRERvaGFVERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 326 PS-AMLEAAGIAVPAK----APRLLIAVVNADDPwVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSR 400
Cdd:cd07092 319 PAhARVLTGGRRAEGPgyfyEPTVVAGVAQDDEI-VQEEIFGPVVTVQPFDDEDEAIELANDVEYGL--ASSVWTRDVGR 395
|
410
....*....|
gi 447020428 401 LNLAARTLQT 410
Cdd:cd07092 396 AMRLSARLDF 405
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
37-434 |
9.41e-19 |
|
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: 88.64 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedkflKNKA-ALDNTPGVEDL----- 110
Cdd:COG1012 45 VDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETG---------KPLAeARGEVDRAADFlryya 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 111 --------TTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTeTIINNSISM-LAAGNSVYFSPHPGAKKVSLKLISLIEEI 181
Cdd:COG1012 116 gearrlygETIPSDAPGTRAYVRREPLGVVGAITPWNFPL-ALAAWKLAPaLAAGNTVVLKPAEQTPLSALLLAELLEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 182 -----AFrccgirNLVVTVAEptfEATQQMMAHPRIAVLAITGGPG----IVAMGMKSGKKVIGAGAGNPPCIVDETADL 252
Cdd:COG1012 195 glpagVL------NVVTGDGS---EVGAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 253 VKAAEDIINGAsFDYNl-pCIAEKSLIVVESVAERLVQQM-QTFGALLL-SPTDTDklrAVCLP---EGQANK--KLV-- 322
Cdd:COG1012 266 DAAVEAAVRGA-FGNAgqrCTAASRLLVHESIYDEFVERLvAAAKALKVgDPLDPG---TDMGPlisEAQLERvlAYIed 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 323 GKSPSAMLEAAGIAVPAKAPRL----LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNV 398
Cdd:COG1012 342 AVAEGAELLTGGRRPDGEGGYFveptVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGL--AASVFTRDL 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 447020428 399 SRLNLAARTLQT-SIFVKNGPSYA------------GIGV--GGEGFTTFT 434
Cdd:COG1012 420 ARARRVARRLEAgMVWINDGTTGAvpqapfggvkqsGIGRegGREGLEEYT 470
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-429 |
1.63e-17 |
|
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: 84.60 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKFLKNKA----------ALDNTPG 106
Cdd:cd07147 23 IEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAidtfriaaeeATRIYGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 107 VEDLTTTAlTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiafrcC 186
Cdd:cd07147 103 VLPLDISA-RGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAE-----T 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 187 GIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPgIVAMGMKS---GKKVIGAGAGNPPCIVDETADLVKAAEDIINGA 263
Cdd:cd07147 177 GLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSP-AVGWDLKAragKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 264 SFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLS--PTDTDKLRAVCLPEGQAnKKLVGKSPSAMLEAAGIAVPAK- 340
Cdd:cd07147 256 FYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTgdPKDDATDVGPMISESEA-ERVEGWVNEAVDAGAKLLTGGKr 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 341 -----APRLLiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHhtAIMHSQNVSRLNLAARTLQ-TSIFV 414
Cdd:cd07147 335 dgallEPTIL-EDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ--AGVFTRDLEKALRAWDELEvGGVVI 411
|
410 420
....*....|....*....|....*
gi 447020428 415 KNGPS-------YAGI---GVGGEG 429
Cdd:cd07147 412 NDVPTfrvdhmpYGGVkdsGIGREG 436
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
128-425 |
1.97e-17 |
|
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: 84.55 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPtetiINNSISMLA----AGNSVYFSPhpgAKKVSLKLISLIEeiAFRCCGI-RNLVVTVAEPTFEA 202
Cdd:cd07082 141 PLGVVLAIGPFNYP----LNLTVSKLIpaliMGNTVVFKP---ATQGVLLGIPLAE--AFHDAGFpKGVVNVVTGRGREI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 203 TQQMMAHPRIAVLAITGGPGIVAMGMKSGKK---VIGAGAGNPpCIVDETADLVKAAEDIINGAsFDYN-LPCIAEKSLI 278
Cdd:cd07082 212 GDPLVTHGRIDVISFTGSTEVGNRLKKQHPMkrlVLELGGKDP-AIVLPDADLELAAKEIVKGA-LSYSgQRCTAIKRVL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 279 VVESVAERLVQQMQ------TFGalllSPTDtDKLRAVCLPEgqankklvGKSPSAMLEAAGIAVpAKAPRLLI------ 346
Cdd:cd07082 290 VHESVADELVELLKeevaklKVG----MPWD-NGVDITPLID--------PKSADFVEGLIDDAV-AKGATVLNgggreg 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 347 ------AVVNADDP-----WVtsEQLMPMLPVVKVSDFDSALALALKVEEGLHhtAIMHSQNVSRLNLAARTLQT-SIFV 414
Cdd:cd07082 356 gnliypTLLDPVTPdmrlaWE--EPFGPVLPIIRVNDIEEAIELANKSNYGLQ--ASIFTKDINKARKLADALEVgTVNI 431
|
330
....*....|.
gi 447020428 415 KNGPSYaGIGV 425
Cdd:cd07082 432 NSKCQR-GPDH 441
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
28-429 |
3.50e-16 |
|
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: 80.45 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 28 PQGKGifQSVSEAIDAAHQAFLRYQQCPLKTRSAII----SAMRQELTPLLATLAEESANETGMGNKEDKF----LKNKA 99
Cdd:cd07150 16 AVGSR--QDAERAIAAAYDAFPAWAATTPSERERILlkaaEIMERRADDLIDLLIDEGGSTYGKAWFETTFtpelLRAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 100 ALDNTPGVEDLTTTAlTGDGGMVLfeYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIE 179
Cdd:cd07150 94 GECRRVRGETLPSDS-PGTVSMSV--RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 180 EIAFRcCGIRNLVVTVAEptfEATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKA 255
Cdd:cd07150 171 EAGLP-KGVFNVVTGGGA---EVGDELVDDPRVRMVTFTGstavGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM---------------QTFGALLLSPTDTDKLravclpEGQANKk 320
Cdd:cd07150 247 VRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFvarasklkvgdprdpDTVIGPLISPRQVERI------KRQVED- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 321 lvgkspsAMLEAAGIAVPAK------APRLLIAVvnADDPWVTSEQLM-PMLPVVKVSDFDSALALALKVEEGLhhTAIM 393
Cdd:cd07150 320 -------AVAKGAKLLTGGKydgnfyQPTVLTDV--TPDMRIFREETFgPVTSVIPAKDAEEALELANDTEYGL--SAAI 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 447020428 394 HSQNVSRLNLAARTLQTSIFVKNGPS--------YAGI---GVGGEG 429
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHINDPTildeahvpFGGVkasGFGREG 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
37-387 |
7.04e-16 |
|
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: 79.60 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAI-------ISAMRQELTPLLA-----TLAEESANETGMGNkedkFLKNKAALD-N 103
Cdd:cd07097 39 ADAAIAAAAAAFPAWRRTSPEARADIldkagdeLEARKEELARLLTreegkTLPEARGEVTRAGQ----IFRYYAGEAlR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 104 TPGvedltTTALTGDGGMVLFEY-SPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07097 115 LSG-----ETLPSTRPGVEVETTrEPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRCcGIRNLVVTvaePTFEATQQMMAHPRIAVLAITGGpgiVAMGMKSGKKVIGAGA-------GNPPCIVDETADLVKA 255
Cdd:cd07097 190 LPA-GVFNLVMG---SGSEVGQALVEHPDVDAVSFTGS---TAVGRRIAAAAAARGArvqlemgGKNPLVVLDDADLDLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM-QTFGAL-----LLSPTDTdklrAVCLPEGQANKKL----VGKS 325
Cdd:cd07097 263 VECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALvERTKALkvgdaLDEGVDI----GPVVSERQLEKDLryieIARS 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447020428 326 PSAMLEAAGIAVPAK------APRLLIAVVNadDPWVTSEQLM-PMLPVVKVSDFDSALALALKVEEGL 387
Cdd:cd07097 339 EGAKLVYGGERLKRPdegyylAPALFAGVTN--DMRIAREEIFgPVAAVIRVRDYDEALAIANDTEFGL 405
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
37-419 |
3.53e-15 |
|
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: 77.23 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKF--------LKNKAALDNTPGVE 108
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFnvdlaagmLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 109 DLTTTAlTGDGGMVLFEysPFGVIGSVAPSTNPtetII--NNSISM-LAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRC 185
Cdd:cd07105 82 SIPSDK-PGTLAMVVKE--PVGVVLGIAPWNAP---VIlgTRAIAYpLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 186 cGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGpgivamgMKSGKKVIGAGA-----------GNPPCIVDETADLVK 254
Cdd:cd07105 156 -GVLNVVTHSPEDAPEVVEALIAHPAVRKVNFTGS-------TRVGRIIAETAAkhlkpvllelgGKAPAIVLEDADLDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 255 AAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM-QTFGALLLSPTDTDKLRAVclPEGQANKKLVGKSPS--AMLE 331
Cdd:cd07105 228 AANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLkAAAEKLFAGPVVLGSLVSA--AAADRVKELVDDALSkgAKLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 332 AAGIAV----PAKAPRLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSR-LNLAAR 406
Cdd:cd07105 306 VGGLADespsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGL--SAAVFTRDLARaLAVAKR 383
|
410
....*....|...
gi 447020428 407 tLQTSIFVKNGPS 419
Cdd:cd07105 384 -IESGAVHINGMT 395
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
35-409 |
5.93e-15 |
|
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: 76.61 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 35 QSVSEAIDAAHQAF----------LRYQQcpLKTRSAIISAMRQELTPLLAT----LAEESANETGMGNKEdkfLKNKAA 100
Cdd:cd07120 19 AEAEAAIAAARRAFdetdwahdprLRARV--LLELADAFEANAERLARLLALengkILGEARFEISGAISE---LRYYAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 101 LD-NTPGvedltTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIE 179
Cdd:cd07120 94 LArTEAG-----RMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 180 EIAFRCCGIRNLVvtvAEPTFEATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKA 255
Cdd:cd07120 169 EIPSLPAGVVNLF---TESGSEGAAHLVASPDVDVISFTGstatGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM-QTFGAL--------------LLSPTDTDKLRAVCLPEGQANKK 320
Cdd:cd07120 246 LPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLaARLAAVkvgpgldpasdmgpLIDRANVDRVDRMVERAIAAGAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 321 LV--GKSPSAMLEAAGIAVPAkaprlLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNV 398
Cdd:cd07120 326 VVlrGGPVTEGLAKGAFLRPT-----LLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGL--AASVWTRDL 398
|
410
....*....|.
gi 447020428 399 SRLNLAARTLQ 409
Cdd:cd07120 399 ARAMRVARAIR 409
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
34-434 |
8.21e-15 |
|
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: 76.13 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 34 FQSVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMG----NKEDKFLKNKAA--LDNTPGV 107
Cdd:cd07102 17 LEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPiaqaGGEIRGMLERARymISIAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 108 edLTTTALTGDGGMVLF-EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIafrcc 186
Cdd:cd07102 97 --LADIRVPEKDGFERYiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEA----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 187 GIRNLVVTVAEPTFEATQQMMAHPRIAVLAITG------------GPGIVAMGMKSGkkvigagaGNPPCIVDETADLVK 254
Cdd:cd07102 170 GLPEGVFQVLHLSHETSAALIADPRIDHVSFTGsvaggraiqraaAGRFIKVGLELG--------GKDPAYVRPDADLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 255 AAEDIINGASFDYNLPCIAEKSLIVVESV----AERLVQQMQTFgaLLLSPTDTD-------KLRAVCLPEGQAnKKLVG 323
Cdd:cd07102 242 AAESLVDGAFFNSGQSCCSIERIYVHESIydafVEAFVAVVKGY--KLGDPLDPSttlgpvvSARAADFVRAQI-ADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 324 KSPSAMLEAAGIAVPAK-----APRLLIAvVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNV 398
Cdd:cd07102 319 KGARALIDGALFPEDKAggaylAPTVLTN-VDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGL--TASVWTKDI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 447020428 399 SRLNLAARTLQTSIFVKN------------GPSYAGIGV--GGEGFTTFT 434
Cdd:cd07102 396 ARAEALGEQLETGTVFMNrcdyldpalawtGVKDSGRGVtlSRLGYDQLT 445
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-410 |
2.19e-14 |
|
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: 75.03 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedkflknKAALDNTPGvEDLTT---- 112
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-----------KTMVDASLG-EILVTceki 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 113 --------TAL---TGDGGMVLF------EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLI 175
Cdd:cd07098 88 rwtlkhgeKALrpeSRPGGLLMFykrarvEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 176 SLIEEiAFRCCGI-RNLVVTVaePTF-EATQQMMAHPRIAVLAITGGPGIvamgmksGKKVIGAGA-----------GNP 242
Cdd:cd07098 168 SIIRE-CLAACGHdPDLVQLV--TCLpETAEALTSHPVIDHITFIGSPPV-------GKKVMAAAAesltpvvlelgGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 243 PCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQ------TFGALLLSPTDtdkLRAVCLPEgQ 316
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTdrvqalRQGPPLDGDVD---VGAMISPA-R 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 317 ANKK--LVGKSPS--AMLEAAGiaVPAKAPRL---------LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKV 383
Cdd:cd07098 314 FDRLeeLVADAVEkgARLLAGG--KRYPHPEYpqghyfpptLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420
....*....|....*....|....*..
gi 447020428 384 EEGLhhTAIMHSQNVSRLNLAARTLQT 410
Cdd:cd07098 392 EYGL--GASVFGKDIKRARRIASQLET 416
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
37-297 |
2.38e-14 |
|
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: 74.97 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAF----------LRyQQCPLktrsAIISAMRQELTPLLATLAEES----ANETGM--GNKEDKFLKNKAA 100
Cdd:cd07089 21 VDAAIAAARRAFdtgdwstdaeER-ARCLR----QLHEALEARKEELRALLVAEVgapvMTARAMqvDGPIGHLRYFADL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 101 LDNTPGVEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEE 180
Cdd:cd07089 96 ADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 181 IAFRcCGIRNLVVTVAEptfEATQQMMAHPRIAVLAITGGPGIvamgmksGKKVIGAGA-----------GNPPCIVDET 249
Cdd:cd07089 176 TDLP-AGVVNVVTGSDN---AVGEALTTDPRVDMVSFTGSTAV-------GRRIMAQAAatlkrvllelgGKSANIVLDD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447020428 250 ADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM-QTFGAL 297
Cdd:cd07089 245 ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALaAAFEAL 293
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
126-409 |
3.53e-14 |
|
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: 74.57 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEptfEATQQ 205
Cdd:cd07124 164 YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPP-GVVNFLPGPGE---EVGDY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHPRIAVLAITG----GPGI------VAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGAsFDYN-LPCIAE 274
Cdd:cd07124 240 LVEHPDVRFIAFTGsrevGLRIyeraakVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSA-FGFQgQKCSAC 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 275 KSLIVVESV----AERLVQ-----------QMQTFGALLLSPTDTDKLRAVcLPEGQANKKLVGKSPSAMLEAAGIAVPa 339
Cdd:cd07124 319 SRVIVHESVydefLERLVErtkalkvgdpeDPEVYMGPVIDKGARDRIRRY-IEIGKSEGRLLLGGEVLELAAEGYFVQ- 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 340 kaPrLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQ 409
Cdd:cd07124 397 --P-TIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGL--TGGVFSRSPEHLERARREFE 461
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
37-430 |
4.76e-14 |
|
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: 73.79 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedkflKNKAALdntpGVEDLTTTALT 116
Cdd:cd07099 20 VAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETG---------KPRADA----GLEVLLALEAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 G---------------DGGMVLF------EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLI 175
Cdd:cd07099 87 DwaarnaprvlaprkvPTGLLMPnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 176 SLIEEIafrccGIRNLVVTVAEpTFEATQQMMAHPRIAVLAITGGPGivamgmkSGKKVIGAGA-----------GNPPC 244
Cdd:cd07099 167 EAWAAA-----GPPQGVLQVVT-GDGATGAALIDAGVDKVAFTGSVA-------TGRKVMAAAAerlipvvlelgGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 245 IVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMqTFGALLLSPTDTDKLRAVCLP---EGQAnkKL 321
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARL-VAKARALRPGADDIGDADIGPmttARQL--DI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 322 VGKSPSAMLEAAGIAV----------PAKAPRLLiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTA 391
Cdd:cd07099 311 VRRHVDDAVAKGAKALtggarsngggPFYEPTVL-TDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGL--SA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 447020428 392 IMHSQNVSRLNLAARTLQT-SIFVKNGPSYAGI------GVGGEGF 430
Cdd:cd07099 388 SVFSRDLARAEAIARRLEAgAVSINDVLLTAGIpalpfgGVKDSGG 433
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
37-409 |
2.31e-13 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 71.86 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLA-EESANeTGmgnkedkflK-NKAAL-DNTPGVEDLT-- 111
Cdd:PRK13473 41 VDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFArLESLN-CG---------KpLHLALnDEIPAIVDVFrf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 112 -TTALTGDGGMVLFEYS----------PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEE 180
Cdd:PRK13473 111 fAGAARCLEGKAAGEYLeghtsmirrdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAAD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 181 IAFRccGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITGGPGivamgmkSGKKVIGAGA-----------GNPPCIVDET 249
Cdd:PRK13473 191 ILPP--GVLNVVTGRGATVGDA---LVGHPKVRMVSLTGSIA-------TGKHVLSAAAdsvkrthlelgGKAPVIVFDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 250 ADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLL--SPTDTDKLRAVCLPEGQANK--KLVGKS 325
Cdd:PRK13473 259 ADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKvgDPDDEDTELGPLISAAHRDRvaGFVERA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 326 PSamLEAAGIAVPAKAPRL--------LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQN 397
Cdd:PRK13473 339 KA--LGHIRVVTGGEAPDGkgyyyeptLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGL--ASSVWTRD 414
|
410
....*....|..
gi 447020428 398 VSRLNLAARTLQ 409
Cdd:PRK13473 415 VGRAHRVSARLQ 426
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
126-406 |
2.60e-13 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 71.89 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiAFRCCGIRNLVVTVAEptfEATQQ 205
Cdd:PRK03137 169 YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEE-AGLPAGVVNFVPGSGS---EVGDY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHPRIAVLAITGG----------PGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGAsFDYN-LPCIAE 274
Cdd:PRK03137 245 LVDHPKTRFITFTGSrevglriyerAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASA-FGFSgQKCSAC 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 275 KSLIVVESVAERLVQQMQTFGALLL--SPTDTDKLRAVcLPEGQANKKL----VGKSpSAMLEAAGIAVPAKA----PRl 344
Cdd:PRK03137 324 SRAIVHEDVYDEVLEKVVELTKELTvgNPEDNAYMGPV-INQASFDKIMsyieIGKE-EGRLVLGGEGDDSKGyfiqPT- 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447020428 345 LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAAR 406
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGL--TGAVISNNREHLEKARR 460
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
37-292 |
2.67e-13 |
|
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: 71.34 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISA----MRQELTPLLATLAEEsanetgMGnkedKFLK------NKAAL----- 101
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKladlLRERKDELARLITLE------MG----KPIAearaevEKCAWicryy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 102 -DNtpGVEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLklisLIEE 180
Cdd:cd07100 71 aEN--AEAFLADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCAL----AIEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 181 IaFRCCGI-----RNLVVTVaeptfEATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVI---GagaGNPPCIVDE 248
Cdd:cd07100 145 L-FREAGFpegvfQNLLIDS-----DQVEAIIADPRVRGVTLTGseraGRAVAAEAGKNLKKSVlelG---GSDPFIVLD 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447020428 249 TADLVKAAEDII------NGASfdynlpCIAEKSLIVVESVA----ERLVQQMQ 292
Cdd:cd07100 216 DADLDKAVKTAVkgrlqnAGQS------CIAAKRFIVHEDVYdeflEKFVEAMA 263
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
128-420 |
3.41e-13 |
|
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: 71.24 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPgakKVSLKLISLIEeiAFRCCGI--RNLVVTVAEPTfEATQQ 205
Cdd:cd07146 120 PLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE---KTPLSAIYLAD--LLYEAGLppDMLSVVTGEPG-EIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHPRIAVLAITGGpgiVAMG-----MKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVV 280
Cdd:cd07146 194 LITHPDVDLVTFTGG---VAVGkaiaaTAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 281 ESVAERLV---------------QQMQTFGALLLSPTDTDKLRAVCL-PEGQANKKLVGKspsamlEAAGIAVpakAPRL 344
Cdd:cd07146 271 ESVADEFVdllveksaalvvgdpMDPATDMGTVIDEEAAIQIENRVEeAIAQGARVLLGN------QRQGALY---APTV 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447020428 345 LiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQT-SIFVKNGPSY 420
Cdd:cd07146 342 L-DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGL--SSGVCTNDLDTIKRLVERLDVgTVNVNEVPGF 415
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
37-450 |
2.12e-12 |
|
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: 68.91 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKflknkaaLDNTPGVEdlTTTALT 116
Cdd:cd07131 39 VDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGR-------GDVQEAID--MAQYAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 GDGGMVL-----------FEYS---PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07131 110 GEGRRLFgetvpselpnkDAMTrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRCcGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAED 258
Cdd:cd07131 190 LPP-GVVNVVHGRGEEVGEA---LVEHPDVDVVSFTGstevGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 259 IINGASFDYNLPCIAEKSLIVVESVAERLVQQM--QTFGALLLSPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEA 332
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFveRAKRLRVGDGLDEETDMGPLINEAQLEKVLnyneIGKEEGATLLL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 333 AGIAVPAKAPR-------LLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhHTAImHSQNVSRLNLAA 405
Cdd:cd07131 346 GGERLTGGGYEkgyfvepTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGL-SSAI-YTEDVNKAFRAR 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 447020428 406 RTLQTSIFVKNGPSyagigVGGEGFTTFTIATPTGEGTTSARTFA 450
Cdd:cd07131 424 RDLEAGITYVNAPT-----IGAEVHLPFGGVKKSGNGHREAGTTA 463
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
37-387 |
2.29e-12 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 68.83 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETG------------MGNKEDkfLKNKAALDNT 104
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGkplweaatevtaMINKIA--ISIQAYHERT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 105 PgvedlTTTALTGDGGMVLfEYSPFGVIGSVAPSTNPTEtIINNSI-SMLAAGNSVYFSPHPGAKKVSLKLISLIEEiAF 183
Cdd:PRK09457 117 G-----EKRSEMADGAAVL-RHRPHGVVAVFGPYNFPGH-LPNGHIvPALLAGNTVVFKPSELTPWVAELTVKLWQQ-AG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 184 RCCGIRNLVVTVAEpTFEAtqqMMAHPRIAVLAITGG--------------PG-IVAMGMksgkkvigagAGNPPCIVDE 248
Cdd:PRK09457 189 LPAGVLNLVQGGRE-TGKA---LAAHPDIDGLLFTGSantgyllhrqfagqPEkILALEM----------GGNNPLVIDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 249 TADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVA-----ERLV------------QQMQTFGALLLSPTDTDKLRAvc 311
Cdd:PRK09457 255 VADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgdaflARLVavakrltvgrwdAEPQPFMGAVISEQAAQGLVA-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 312 lpegqANKKLVGKSPSAMLEA------AGIAVPAkaprlLIAVVNADDPwVTSEQLMPMLPVVKVSDFDSALALALKVEE 385
Cdd:PRK09457 333 -----AQAQLLALGGKSLLEMtqlqagTGLLTPG-----IIDVTGVAEL-PDEEYFGPLLQVVRYDDFDEAIRLANNTRF 401
|
..
gi 447020428 386 GL 387
Cdd:PRK09457 402 GL 403
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
37-427 |
3.40e-12 |
|
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: 68.17 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETG-----MGNKEDKFLknkAALDNTPG-VEDL 110
Cdd:cd07107 21 VDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGnpvsaMLGDVMVAA---ALLDYFAGlVTEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 111 TTTALTGDGGMVLF-EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRccGIR 189
Cdd:cd07107 98 KGETIPVGGRNLHYtLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPP--GVF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 190 NLVVTVAEptfEATQQMMAHPRIAVLAITGGPGivamgmkSGKKVIGAGA-----------GNPPCIVDETADLVKAAED 258
Cdd:cd07107 176 NILPGDGA---TAGAALVRHPDVKRIALIGSVP-------TGRAIMRAAAegikhvtlelgGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 259 IINGASFDY-NLPCIAEKSLIVVESVAERLVQQM-QTFGALLLS-PTDTDKLRAVCLPEGQANKKL----VGKSPSAMLE 331
Cdd:cd07107 246 AVAGMNFTWcGQSCGSTSRLFVHESIYDEVLARVvERVAAIKVGdPTDPATTMGPLVSRQQYDRVMhyidSAKREGARLV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 332 AAGIAVPAKAPR---LLIAVVNADdpwVTS-------EQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRL 401
Cdd:cd07107 326 TGGGRPEGPALEggfYVEPTVFAD---VTPgmriareEIFGPVLSVLRWRDEAEMVAQANGVEYGL--TAAIWTNDISQA 400
|
410 420
....*....|....*....|....*...
gi 447020428 402 NLAARTLQTSIFVKNGPS--YAGIGVGG 427
Cdd:cd07107 401 HRTARRVEAGYVWINGSSrhFLGAPFGG 428
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
35-388 |
5.02e-12 |
|
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: 67.62 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 35 QSVSEAIDAAHQAFLRYQQCPLKTRSAIISA----MRQELTPLLATLAEESANETGMGNKED-------KFLKNKAA--- 100
Cdd:cd07149 21 EDVEKAIAAAKEGAKEMKSLPAYERAEILERaaqlLEERREEFARTIALEAGKPIKDARKEVdraietlRLSAEEAKrla 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 101 -----LDNTPGVEDLTttaltgdgGMVLFEysPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLI 175
Cdd:cd07149 101 getipFDASPGGEGRI--------GFTIRE--PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 176 SLIEEIAFrccgIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGI-VAMGMKSG-KKVIGAGAGNPPCIVDETADLV 253
Cdd:cd07149 171 ELLLEAGL----PKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVgEAIARKAGlKKVTLELGSNAAVIVDADADLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 254 KAAEDIINGASFDYNLPCIAEKSLIVVESV----AERLVQQMQTF--GALLLSPTDTDKLravcLPEGQAN--KKLVGks 325
Cdd:cd07149 247 KAVERCVSGAFANAGQVCISVQRIFVHEDIydefLERFVAATKKLvvGDPLDEDTDVGPM----ISEAEAEriEEWVE-- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447020428 326 pSAMLEAAGIAVPAK------APRLLiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLH 388
Cdd:cd07149 321 -EAVEGGARLLTGGKrdgailEPTVL-TDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
16-416 |
5.15e-12 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 67.61 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 16 EQLTTPAQTPVQPQGKGIFQSVSEAIDAAHQAFLR--YQQCPLKTRSAIISAmrqeltplLATLAEESANETGMGNKEDK 93
Cdd:PRK09847 38 ETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNK--------LADLMEAHAEELALLETLDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 94 FLKNKAAL-DNTPGV--------EDLTT----TALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVY 160
Cdd:PRK09847 110 GKPIRHSLrDDIPGAarairwyaEAIDKvygeVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 161 FSPHPGAKKVSLKLISLIEEiafrcCGIRNLVVTVAePTF--EATQQMMAHPRIAVLAITGGPGIVAMGMKSG-----KK 233
Cdd:PRK09847 190 LKPSEKSPLSAIRLAGLAKE-----AGLPDGVLNVV-TGFghEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAgdsnmKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 234 V-IGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAE----RLVQQMQTFG-----------AL 297
Cdd:PRK09847 264 VwLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADeflaLLKQQAQNWQpghpldpattmGT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 298 LLSPTDTDKLRAVcLPEGQANKKLvgkspsaMLEAAGIAVPAKAPRLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSAL 377
Cdd:PRK09847 344 LIDCAHADSVHSF-IREGESKGQL-------LLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 447020428 378 ALALKVEEGLhhTAIMHSQNVSRLNLAARTLQT-SIFVKN 416
Cdd:PRK09847 416 QLANDSQYGL--GAAVWTRDLSRAHRMSRRLKAgSVFVNN 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
37-380 |
8.48e-12 |
|
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: 66.91 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnK-------EDKFLKNKAALDNTPGVED 109
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETG---KplweaqtEVAAMAGKIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 110 LTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIR 189
Cdd:cd07095 79 TGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP-GVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 190 NLVVTVAEptfeATQQMMAHPRIAVLAITGGpgiVAMGMKSGKKVIGAG--------AGNPPCIVDETADLVKAAEDIIN 261
Cdd:cd07095 158 NLVQGGRE----TGEALAAHEGIDGLLFTGS---AATGLLLHRQFAGRPgkilalemGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 262 GASFDYNLPCIAEKSLIVVESVA-----ERLVQQMQT------------FGALLLSPTDTDKLRavclpegqANKKLVGK 324
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVgdaflERLVEAAKRlrigapdaeppfMGPLIIAAAAARYLL--------AQQDLLAL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 447020428 325 SPSAMLEAAgiAVPAKAPRL---LIAVVNADDPwVTSEQLMPMLPVVKVSDFDSALALA 380
Cdd:cd07095 303 GGEPLLAME--RLVAGTAFLspgIIDVTDAADV-PDEEIFGPLLQVYRYDDFDEAIALA 358
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
117-430 |
1.08e-11 |
|
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: 66.49 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 GDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRcCGIRNLVVTVA 196
Cdd:cd07109 106 GPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLP-AGALNVVTGLG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 197 EptfEATQQMMAHPRIAVLAITGGPGIVAMGMKS-GKKVIGAG---AGNPPCIVDETADLVKAAEDIINGASFDYNLPCI 272
Cdd:cd07109 185 A---EAGAALVAHPGVDHISFTGSVETGIAVMRAaAENVVPVTlelGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 273 AEKSLIVVESVAERLVQQM-QTFGALLLSPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEAAGIAVPAK------- 340
Cdd:cd07109 262 AGSRLLVHRSIYDEVLERLvERFRALRVGPGLEDPDLGPLISAKQLDRVEgfvaRARARGARIVAGGRIAEGApaggyfv 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 341 APRLLiAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQT-SIFVKNGPS 419
Cdd:cd07109 342 APTLL-DDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL--VAGVWTRDGDRALRVARRLRAgQVFVNNYGA 418
|
330
....*....|....*.
gi 447020428 420 YAGI-----GVGGEGF 430
Cdd:cd07109 419 GGGIelpfgGVKKSGH 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
37-429 |
1.29e-11 |
|
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: 66.52 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELT----PLLATLAEESANETGMGNKEDKFlknkaALDNTpgvEDLTT 112
Cdd:cd07088 37 ADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRenadELAKLIVEEQGKTLSLARVEVEF-----TADYI---DYMAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 113 TALTGDGGMV----------LFEySPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07088 109 WARRIEGEIIpsdrpnenifIFK-VPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRCcGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITGGpgivamgMKSGKKVIGAGA-----------GNPPCIVDETAD 251
Cdd:cd07088 188 LPA-GVLNIVTGRGSVVGDA---LVAHPKVGMISLTGS-------TEAGQKIMEAAAenitkvslelgGKAPAIVMKDAD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 252 LVKAAEDIINGASFDYNLPCIAEKSLIVVESVA----ERLVQQMQ--TFGalllSPTDtDKLRAVCLPEGQANKKLVGKS 325
Cdd:cd07088 257 LDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYdefmEKLVEKMKavKVG----DPFD-AATDMGPLVNEAALDKVEEMV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 326 PSAMLEAAGIAVPAKAPRL---------LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQ 396
Cdd:cd07088 332 ERAVEAGATLLTGGKRPEGekgyfyeptVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGL--TSYIYTE 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 447020428 397 NVSRLNLAARTLQ---TSIFVKNGPSYAGI-------GVGGEG 429
Cdd:cd07088 410 NLNTAMRATNELEfgeTYINRENFEAMQGFhagwkksGLGGAD 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
37-412 |
2.11e-11 |
|
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: 65.45 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedKFLKNKAA-LDNTPG--------V 107
Cdd:cd07110 21 VDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNG------KPLDEAAWdVDDVAGcfeyyadlA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 108 EDLTTTA-----LTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07110 95 EQLDAKAeravpLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRCcGIRNLVVTVAEptfEATQQMMAHPRIAVLAITGGpgivamgMKSGKKVIGAGA-----------GNPPCIVDETAD 251
Cdd:cd07110 175 LPP-GVLNVVTGTGD---EAGAPLAAHPGIDKISFTGS-------TATGSQVMQAAAqdikpvslelgGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 252 LVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFG-ALLLSPTDTDKLRAVCL-PEGQANKKL----VGKS 325
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAeAIRVGDPLEEGVRLGPLvSQAQYEKVLsfiaRGKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 326 PSAMLeAAGIAVPAKAPR------LLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAImhSQNVS 399
Cdd:cd07110 324 EGARL-LCGGRRPAHLEKgyfiapTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI--SRDAE 400
|
410
....*....|...
gi 447020428 400 RLNLAARTLQTSI 412
Cdd:cd07110 401 RCDRVAEALEAGI 413
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
113-409 |
2.27e-11 |
|
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: 65.70 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 113 TALTGDGGMVLFEYSPFGVIGSVAPSTNPtetiinnsISM--------LAAGNSVYFSPhpgAKKVSLKLISLiEEIAFR 184
Cdd:cd07112 109 VAPTGPDALALITREPLGVVGAVVPWNFP--------LLMaawkiapaLAAGNSVVLKP---AEQSPLTALRL-AELALE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 185 cCGIRNLVVTVAePTF--EATQQMMAHPRIAVLAITGGPGIVAMGMK-SG----KKVIGAGAGNPPCIV-DETADLVKAA 256
Cdd:cd07112 177 -AGLPAGVLNVV-PGFghTAGEALGLHMDVDALAFTGSTEVGRRFLEySGqsnlKRVWLECGGKSPNIVfADAPDLDAAA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 257 EDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLL--SPTDTDKLRAVCLPEGQANKKL----VGKSPSAML 330
Cdd:cd07112 255 EAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpgDPLDPATRMGALVSEAHFDKVLgyieSGKAEGARL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 331 EAAGIAVPAKAPRLLIA-----VVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHhtAIMHSQNVSRLNLAA 405
Cdd:cd07112 335 VAGGKRVLTETGGFFVEptvfdGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA--ASVWTSDLSRAHRVA 412
|
....
gi 447020428 406 RTLQ 409
Cdd:cd07112 413 RRLR 416
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
128-429 |
3.02e-11 |
|
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: 65.15 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEptfEATQQMM 207
Cdd:cd07115 117 PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPA-GVLNVVTGFGE---VAGAALV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 208 AHPRIAVLAITGGPGIvamgmksGKKVIGAGAGN-----------PPCIVDETADLVKAAEDIINGASFDYNLPCIAEKS 276
Cdd:cd07115 193 EHPDVDKITFTGSTAV-------GRKIMQGAAGNlkrvslelggkSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 277 LIVVESVAERLVQQMQTFGALLL--SPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEAAGIAVPAKA---PRLLIA 347
Cdd:cd07115 266 LLVHESIYDEFLERFTSLARSLRpgDPLDPKTQMGPLVSQAQFDRVLdyvdVGREEGARLLTGGKRPGARGffvEPTIFA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 348 VVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQ-------TSIFVKNGPSY 420
Cdd:cd07115 346 AVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGL--AAGVWTRDLGRAHRVAAALKagtvwinTYNRFDPGSPF 423
|
....*....
gi 447020428 421 AGIGVGGEG 429
Cdd:cd07115 424 GGYKQSGFG 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
93-406 |
7.82e-11 |
|
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: 63.85 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 93 KFLKNKAALDNTPGVEDLTTTAltgdGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSL 172
Cdd:cd07152 79 GELHEAAGLPTQPQGEILPSAP----GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 173 KLISLIEEIAfrccGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGI-VAMGMKSG---KKVIGAGAGNPPCIVDE 248
Cdd:cd07152 155 VVIARLFEEA----GLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVgRKVGEAAGrhlKKVSLELGGKNALIVLD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 249 TADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLL--SPTDTDKLRAVCLPEGQANK--KLVGK 324
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPvgDPATGQVALGPLINARQLDRvhAIVDD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 325 S--PSAMLEAAGIAVPAKAPRLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSR-L 401
Cdd:cd07152 311 SvaAGARLEAGGTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGL--SAGIISRDVGRaM 388
|
....*
gi 447020428 402 NLAAR 406
Cdd:cd07152 389 ALADR 393
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
37-456 |
8.93e-11 |
|
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: 63.80 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTP----------LLATLAEESANETGMGNKEDKFLknkAALDNTPG 106
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAksydiaagavLVTGKGWMFAENICGDQVQLRAR---AFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 107 VEDLTTTALTGDGGM-VLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiafrc 185
Cdd:cd07084 78 IPHEPGNHLGQGLKQqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHY----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 186 CGIRNL-VVTVAEPTFEATQQMMAHPRIAVLAITGGPGiVAMGMKSGKKVI---GAGAGNPPCIVDETADLVKA-AEDII 260
Cdd:cd07084 153 AGLLPPeDVTLINGDGKTMQALLLHPNPKMVLFTGSSR-VAEKLALDAKQAriyLELAGFNWKVLGPDAQAVDYvAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 261 NGASFDYNLPCIAEKSLIV---------VESVAERLVQqmQTFGALLLSP--TDTDKLRAVCLPEGQANKKLVGKSPSAM 329
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVpenwsktplVEKLKALLAR--RKLEDLLLGPvqTFTTLAMIAHMENLLGSVLLFSGKELKN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 330 LEAAGIAVPAKAPRLLIAV--VNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNVSRLN-LAAR 406
Cdd:cd07084 310 HSIPSIYGACVASALFVPIdeILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQeLIGN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 447020428 407 TLQTSIFVKNGPSYAGIGVG---GEGFTtftiATPTGEGTTSARTFARSRRCV 456
Cdd:cd07084 390 LWVAGRTYAILRGRTGVAPNqnhGGGPA----ADPRGAGIGGPEAIKLVWRCH 438
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
37-406 |
9.67e-11 |
|
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: 63.32 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETG----MGNKEDKF----LKNKAALDNTPGVE 108
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGAaiaiLREAAGLPRRPEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 109 DLTTTAltgDGGMVLFEYSPFGVIGSVAPSTNPTetiinnSISM------LAAGNSVYFSPHPGAKKVSLKLISLIEEIA 182
Cdd:cd07104 82 ILPSDV---PGKESMVRRVPLGVVGVISPFNFPL------ILAMrsvapaLALGNAVVLKPDSRTPVTGGLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 183 FRCCGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITG----GPGIVAMGMKSGKKV---IGagaGNPPCIVDETADLVKA 255
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDA---LVEHPRVRMISFTGstavGRHIGELAGRHLKKValeLG---GNNPLIVLDDADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM---------------QTFGALLLSPTDTDKLravclpegqanKK 320
Cdd:cd07104 227 VSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLvakakalpvgdprdpDTVIGPLINERQVDRV-----------HA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 321 LVGKSPS--AMLEAAGIAVPAKAPRLLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNV 398
Cdd:cd07104 296 IVEDAVAagARLLTGGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGL--SAAVFTRDL 373
|
....*....
gi 447020428 399 SR-LNLAAR 406
Cdd:cd07104 374 ERaMAFAER 382
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
125-378 |
1.69e-10 |
|
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: 62.54 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 125 EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSlKLIS-LIEEiafrccGIRNLVVTVAEPTFEAT 203
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATS-ALLAkLIPK------YFDPEAVAVVEGGVEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 204 QQMMAHPRIAVLaITGGPGIvamgmksGKKVIGAGA-----------GNPPCIVDETADLVKAAEDIINGASFDYNLPCI 272
Cdd:cd07087 170 TALLAEPFDHIF-FTGSPAV-------GKIVMEAAAkhltpvtlelgGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 273 AEKSLIVVESVAERLVQQMQT-----FGALLLSPTDTDKLravcLPEGQANkKLVGkspsaMLEAAGIAVPAK------- 340
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKaikefYGEDPKESPDYGRI----INERHFD-RLAS-----LLDDGKVVIGGQvdkeery 311
|
250 260 270
....*....|....*....|....*....|....*....
gi 447020428 341 -APRLLIaVVNADDPWVTSEQLMPMLPVVKVSDFDSALA 378
Cdd:cd07087 312 iAPTILD-DVSPDSPLMQEEIFGPILPILTYDDLDEAIE 349
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
117-409 |
2.18e-10 |
|
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: 62.35 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 117 GDG--GMVLFEysPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVT 194
Cdd:cd07118 108 GDDmlGLVLRE--PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPA-GVVNIVTG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 195 VAEPtfeATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLP 270
Cdd:cd07118 185 YGAT---VGQAMTEHPDVDMVSFTGstrvGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGEC 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 271 CIAEKSLIVVESVAE----RLVQQMQ--TFGalllSPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEAAGIAVPAK 340
Cdd:cd07118 262 CNSGSRLLVHESIADafvaAVVARSRkvRVG----DPLDPETKVGAIINEAQLAKITdyvdAGRAEGATLLLGGERLASA 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447020428 341 APRL----LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQ 409
Cdd:cd07118 338 AGLFyqptIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL--SAGVWSKDIDTALTVARRIR 408
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
147-431 |
5.72e-10 |
|
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: 61.04 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 147 NNSISMLAaGNSVYFSPHPGAKKVSLKLISLIEEiAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGpgiVAM 226
Cdd:cd07086 153 NAAIALVC-GNTVVWKPSETTPLTAIAVTKILAE-VLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGS---TEV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 227 GMKSGKKVIGAGA-------GNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLL 299
Cdd:cd07086 228 GRRVGETVARRFGrvllelgGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 300 --SPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEAAGIAVPAKAPRL-----LIAVVNADDPWVTSEQLMPMLPVV 368
Cdd:cd07086 308 igDPLDEGTLVGPLINQAAVEKYLnaieIAKSQGGTVLTGGKRIDGGEPGNyveptIVTGVTDDARIVQEETFAPILYVI 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447020428 369 KVSDFDSALALALKVEEGLhHTAIMhSQNVSRLN--LAARTLQTSI-FVKNGPSYAGIG--VGGEGFT 431
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGL-SSSIF-TEDLREAFrwLGPKGSDCGIvNVNIPTSGAEIGgaFGGEKET 453
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
126-444 |
7.76e-10 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 60.81 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPH---PGAKKVSLKLIS-LIEEIAFRCCgirnlvvtvaEPTFE 201
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSelsPHTSKLMAKLLTkYLDPSYVRVI----------EGGVE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 202 ATQQMMAHPrIAVLAITGGPgivamgmKSGKKVIGAGA-----------GNPPCIVDETADLVKAAEDIINGASFDYNLP 270
Cdd:PTZ00381 177 VTTELLKEP-FDHIFFTGSP-------RVGKLVMQAAAenltpctlelgGKSPVIVDKSCNLKVAARRIAWGKFLNAGQT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 271 CIAEKSLIVVESVAERLVQQMQTFGALLLSP---TDTDKLRAVclpEGQANKKLVGkspsaMLEA----------AGIAV 337
Cdd:PTZ00381 249 CVAPDYVLVHRSIKDKFIEALKEAIKEFFGEdpkKSEDYSRIV---NEFHTKRLAE-----LIKDhggkvvyggeVDIEN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 338 PAKAPRlLIAVVNADDPWVTSEQLMPMLPVVKVSDFDSAL--------ALAL-----------KVEEGLHHTAIMHsqNV 398
Cdd:PTZ00381 321 KYVAPT-IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLefinsrpkPLALyyfgedkrhkeLVLENTSSGAVVI--ND 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447020428 399 SRLNLAARTLQtsiFVKNGPSyaGIGV--GGEGFTTFTIATPTGEGTT 444
Cdd:PTZ00381 398 CVFHLLNPNLP---FGGVGNS--GMGAyhGKYGFDTFSHPKPVLNKST 440
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
127-420 |
8.93e-10 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 60.52 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 127 SPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEptfEATQQM 206
Cdd:PRK10090 70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPK-GVFNLVLGRGE---TVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 207 MAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVES 282
Cdd:PRK10090 146 AGNPKVAMVSMTGsvsaGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 283 VAERLVQQMQ------TFGalllSPTDTDKLRAVCLPEGQANKKLVGKSPSAMLEAAGIAVPAKA---------PRLLIA 347
Cdd:PRK10090 226 IYDQFVNRLGeamqavQFG----NPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAvegkgyyypPTLLLD 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447020428 348 VVNaDDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNvsrLNLAARTLQTsifVKNGPSY 420
Cdd:PRK10090 302 VRQ-EMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGL--TSSIYTQN---LNVAMKAIKG---LKFGETY 365
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
125-290 |
1.44e-09 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 59.87 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 125 EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAkkvsLKLISLIEEIaFRCCGIRNLVVTVAEPTFEATQ 204
Cdd:PRK13968 123 EYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV----MGCAQLIAQV-FKDAGIPQGVYGWLNADNDGVS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 205 QMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVV 280
Cdd:PRK13968 198 QMINDSRIAAVTVTGsvraGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIE 277
|
170
....*....|
gi 447020428 281 ESVAERLVQQ 290
Cdd:PRK13968 278 EGIASAFTER 287
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
37-291 |
2.15e-09 |
|
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: 59.25 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLR--YQQCPLKTRSAIISAMRQELTPLLATLAE-ESANeTGmgnkedKFLKnKAALDntpgVEDLTTT 113
Cdd:cd07119 37 AKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARlETLN-TG------KTLR-ESEID----IDDVANC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 114 ------ALTGDGG-----------MVLFEysPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLIS 176
Cdd:cd07119 105 fryyagLATKETGevydvpphvisRTVRE--PVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 177 LIEEIAFRcCGIRNLVVTVAEptfEATQQMMAHPRIAVLAITGgpgivamGMKSGKKVIGAGAGN-----------PPCI 245
Cdd:cd07119 183 LIEEAGLP-AGVVNLVTGSGA---TVGAELAESPDVDLVSFTG-------GTATGRSIMRAAAGNvkkvalelggkNPNI 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447020428 246 VDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQM 291
Cdd:cd07119 252 VFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAAL 297
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
111-293 |
2.37e-09 |
|
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: 59.16 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 111 TTTALTGDGGMVLFEysPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiAFRccgiRN 190
Cdd:cd07134 85 TPLLLFGTKSKIRYE--PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIRE-AFD----ED 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 191 LVvTVAEPTFEATQQMMAHPRIAVLaITGGPGIvamgmksGKKVIGAGA-----------GNPPCIVDETADLVKAAEDI 259
Cdd:cd07134 158 EV-AVFEGDAEVAQALLELPFDHIF-FTGSPAV-------GKIVMAAAAkhlasvtlelgGKSPTIVDETADLKKAAKKI 228
|
170 180 190
....*....|....*....|....*....|....
gi 447020428 260 INGASFDYNLPCIAEKSLIVVESVAERLVQQMQT 293
Cdd:cd07134 229 AWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKA 262
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
128-412 |
1.06e-08 |
|
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: 57.18 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPtetIINNSISM---LAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRcCGIRNLVVTVAEPTFEAtq 204
Cdd:cd07114 119 PLGVVAAITPWNSP---LLLLAKKLapaLAAGNTVVLKPSEHTPASTLELAKLAEEAGFP-PGVVNVVTGFGPETGEA-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 205 qMMAHPRIAVLAITGGPgivamgmKSGKKVIGAGA-----------GNPPCIVDETADLVKAAEDIINGASFDYNLPCIA 273
Cdd:cd07114 193 -LVEHPLVAKIAFTGGT-------ETGRHIARAAAenlapvtlelgGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 274 EKSLIVVESVAERLVQQMQTFGALLL--SPTDTD-KLRAVCLPegQANKKLVGKSPSAMLEAAGIAVPAKAPRL------ 344
Cdd:cd07114 265 GSRLLVQRSIYDEFVERLVARARAIRvgDPLDPEtQMGPLATE--RQLEKVERYVARAREEGARVLTGGERPSGadlgag 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447020428 345 ------LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQTSI 412
Cdd:cd07114 343 yffeptILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL--AAGIWTRDLARAHRVARAIEAGT 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
37-389 |
1.81e-08 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 56.69 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAII----SAMRQELTPLLATLAEESAnetgmgnkedkflknKAALDNTPGVE---D 109
Cdd:PLN00412 55 VNKAMESAKAAQKAWAKTPLWKRAELLhkaaAILKEHKAPIAECLVKEIA---------------KPAKDAVTEVVrsgD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 110 LTTTA------LTGDGGMV--------------LFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKK 169
Cdd:PLN00412 120 LISYTaeegvrILGEGKFLvsdsfpgnernkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 170 VSLKLISlieeiAFRCCGI-RNLVVTVAEPTFEATQQMMAHPRIAVLAITGG---------PGIVAMGMKSGkkvigaga 239
Cdd:PLN00412 200 AALHMVH-----CFHLAGFpKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGdtgiaiskkAGMVPLQMELG-------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 240 GNPPCIVDETADLVKAAEDIINGAsFDYN-LPCIAEKSLIVVESVAERLVQQMQtfgalllspTDTDKLRaVCLPEGQAN 318
Cdd:PLN00412 267 GKDACIVLEDADLDLAAANIIKGG-FSYSgQRCTAVKVVLVMESVADALVEKVN---------AKVAKLT-VGPPEDDCD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 319 -KKLVGKSPSAMLEaaGIAVPAKAP----------------RLLIAVVNADDPWVTSEQLMPMLPVVKVSDfdsalalal 381
Cdd:PLN00412 336 iTPVVSESSANFIE--GLVMDAKEKgatfcqewkregnliwPLLLDNVRPDMRIAWEEPFGPVLPVIRINS--------- 404
|
....*...
gi 447020428 382 kVEEGLHH 389
Cdd:PLN00412 405 -VEEGIHH 411
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
37-430 |
1.02e-07 |
|
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: 54.12 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRS-------AIISAMRQELTPLLATLAEESANETGMGNKE--DKFLKN-KAALD-NTP 105
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRArlllkaaDLLRRRRRELIATLTYEVGKNWVEAIDDVAEaiDFIRYYaRAALRlRYP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 106 GVEDLTTTALTGDggmvLFeYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRC 185
Cdd:cd07083 137 AVEVVPYPGEDNE----SF-YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 186 cGIRNLVVTVAePTFEATqqMMAHPRIAVLAITGGPGI----------VAMGMKSGKKVIGAGAGNPPCIVDETADLVKA 255
Cdd:cd07083 212 -GVVQFLPGVG-EEVGAY--LTEHERIRGINFTGSLETgkkiyeaaarLAPGQTWFKRLYVETGGKNAIIVDETADFELV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 256 AEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQ-TFGALLLSPTDTDK--LRAVCLPEGQANKKL---VGKSPSAM 329
Cdd:cd07083 288 VEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLkRAERLSVGPPEENGtdLGPVIDAEQEAKVLSyieHGKNEGQL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 330 LeaAGIAVPAK-----APrlliAVVNADDPWV---TSEQLMPMLPVVKVSDFDSALALALKVEEGLHHTAIMHSQNVSRL 401
Cdd:cd07083 368 V--LGGKRLEGegyfvAP----TVVEEVPPKAriaQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHL 441
|
410 420
....*....|....*....|....*....
gi 447020428 402 NLAARTLQTSIFVKNGPSYAGIgVGGEGF 430
Cdd:cd07083 442 EEARREFHVGNLYINRKITGAL-VGVQPF 469
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
36-416 |
1.10e-07 |
|
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: 54.12 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 36 SVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedKFLKN-----KAALD-----NTP 105
Cdd:cd07125 70 DVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAG------KTLADadaevREAIDfcryyAAQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 106 GVEDLTTTALTGDGGMV-LFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLieeiaFR 184
Cdd:cd07125 144 ARELFSDPELPGPTGELnGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL-----LH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 185 CCGI-RNLVVTVAEPTFEATQQMMAHPRIAVLAITGGpgiVAMGMKSGKKVIGAGAGNPP----------CIVDETADLV 253
Cdd:cd07125 219 EAGVpRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGS---TETAKLINRALAERDGPILPliaetggknaMIVDSTALPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 254 KAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQtfGALLL----SPTD--TD-----------KLRAVCLpEGQ 316
Cdd:cd07125 296 QAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLK--GAMASlkvgDPWDlsTDvgplidkpagkLLRAHTE-LMR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 317 ANKKLVGKSPsamleaagiaVPAKAPRL----LIAVVNADDpwVTSEQLMPMLPVV--KVSDFDSALALALKVEEGLhhT 390
Cdd:cd07125 373 GEAWLIAPAP----------LDDGNGYFvapgIIEIVGIFD--LTTEVFGPILHVIrfKAEDLDEAIEDINATGYGL--T 438
|
410 420
....*....|....*....|....*.
gi 447020428 391 AIMHSQNVSRlnlaARTLQTSIFVKN 416
Cdd:cd07125 439 LGIHSRDERE----IEYWRERVEAGN 460
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
126-400 |
1.85e-07 |
|
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: 53.30 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEPTFEAtqq 205
Cdd:cd07143 142 HEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPP-GVINVVSGYGRTCGNA--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHPRIAVLAITGGPGIVAMGMKSG-----KKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVV 280
Cdd:cd07143 218 ISSHMDIDKVAFTGSTLVGRKVMEAAaksnlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 281 ESVAERLVQQM--QTFGALLLSPTDTDKLRAVCLPEGQANKKLV----GKSPSAMLEAAGIAVPAKA----PRLLiAVVN 350
Cdd:cd07143 298 EGIYDKFVKRFkeKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSyiesGKAEGATVETGGKRHGNEGyfiePTIF-TDVT 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447020428 351 ADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSR 400
Cdd:cd07143 377 EDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGL--AAAVFTNNINN 424
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
128-429 |
2.26e-07 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 52.99 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEptfEATQQMM 207
Cdd:PRK11241 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPA-GVFNVVTGSAG---AVGGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 208 AHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESV 283
Cdd:PRK11241 222 SNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 284 AERLVQQM-QTFGALLLSPTDTDKLRAVCLPEGQANKKLVGKSPSAMLEAAGIAVPAKAPRL--------LIAVVNADDP 354
Cdd:PRK11241 302 YDRFAEKLqQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELggnffqptILVDVPANAK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 355 WVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQ-------TSIFVKNGPSYAGI---G 424
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGL--AAYFYARDLSRVFRVGEALEygivginTGIISNEVAPFGGIkasG 459
|
....*
gi 447020428 425 VGGEG 429
Cdd:PRK11241 460 LGREG 464
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
125-424 |
2.62e-06 |
|
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: 49.61 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 125 EYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiafrcCGI-RNLVVTVAEPTFEAT 203
Cdd:cd07101 115 NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIE-----AGLpRDLWQVVTGPGSEVG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 204 QQMMAHprIAVLAITGGPG---IVAMGMksGKKVIGAGA---GNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSL 277
Cdd:cd07101 190 GAIVDN--ADYVMFTGSTAtgrVVAERA--GRRLIGCSLelgGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 278 IVVESVAERLV-------QQMQTFGALLLSP-----TDTDKLRAVCLPEGQANKKlvgkspSAMLEAAGIAVPAKAPRL- 344
Cdd:cd07101 266 YVHESVYDEFVrrfvartRALRLGAALDYGPdmgslISQAQLDRVTAHVDDAVAK------GATVLAGGRARPDLGPYFy 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 345 ---LIAVVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLHhtAIMHSQNVSRLNLAARTLQT-SIFVKNG--P 418
Cdd:cd07101 340 eptVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN--ASVWTRDGARGRRIAARLRAgTVNVNEGyaA 417
|
....*.
gi 447020428 419 SYAGIG 424
Cdd:cd07101 418 AWASID 423
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
37-292 |
3.49e-06 |
|
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: 49.14 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQEL---TPLLATLAEESANETgmgnkedkflKNKAALDNTPGVEDLTTT 113
Cdd:TIGR01238 76 VQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLelhMPELMALCVREAGKT----------IHNAIAEVREAVDFCRYY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 114 ALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRcCGIRNLVV 193
Cdd:TIGR01238 146 AKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFP-AGTIQLLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 194 TVAEPTFEAtqqMMAHPRIAVLAITGGPGIVAMGMKSGKK-------VIGAGAGNPPCIVDETADLVKAAEDIINGASFD 266
Cdd:TIGR01238 225 GRGADVGAA---LTSDPRIAGVAFTGSTEVAQLINQTLAQredapvpLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDS 301
|
250 260
....*....|....*....|....*.
gi 447020428 267 YNLPCIAEKSLIVVESVAERLVQQMQ 292
Cdd:TIGR01238 302 AGQRCSALRVLCVQEDVADRVLTMIQ 327
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
116-409 |
3.52e-06 |
|
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: 49.13 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 116 TGDGGMVLFEYSPFGVIGSVAPSTNPtetiinnsISM--------LAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcG 187
Cdd:cd07091 129 IDGNFLAYTRREPIGVCGQIIPWNFP--------LLMlawklapaLAAGNTVVLKPAEQTPLSALYLAELIKEAGFPP-G 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 188 IRNLVvtvaePTFEAT--QQMMAHPRIAVLAITG----GPGIVAMGMKSG-KKVIGAGAGNPPCIVDETADLVKAAEDII 260
Cdd:cd07091 200 VVNIV-----PGFGPTagAAISSHMDVDKIAFTGstavGRTIMEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 261 NGASFDYNLPCIAEKSLIVVESVAERLVQQM--QTFGALLLSPTDTDKLRAVCLPEGQANKKL----VGKSPSAMLEAAG 334
Cdd:cd07091 275 FGIFFNQGQCCCAGSRIFVQESIYDEFVEKFkaRAEKRVVGDPFDPDTFQGPQVSKAQFDKILsyieSGKKEGATLLTGG 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447020428 335 IAVPAKA----PRLLIAvVNADDPWVTSEQLMPMLPVVKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQ 409
Cdd:cd07091 355 ERHGSKGyfiqPTVFTD-VKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGL--AAGVFTKDINKALRVSRALK 430
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
126-293 |
5.78e-06 |
|
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: 48.65 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 126 YSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiAFRCCgirnlVVTVAEPTFEATQQ 205
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEE-TFDEE-----YVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 206 MMAHP--RIAvlaITGGPGIvamgmksGKKVIGAGA-----------GNPPCIVDETADLVKAAEDIINGASFDYNLPCI 272
Cdd:cd07136 172 LLDQKfdYIF---FTGSVRV-------GKIVMEAAAkhltpvtlelgGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
170 180
....*....|....*....|.
gi 447020428 273 AEKSLIVVESVAERLVQQMQT 293
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKE 262
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-410 |
6.04e-06 |
|
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: 48.58 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 39 EAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGmgnkedKFLKNkaALDNTpgvedltttaltgD 118
Cdd:cd07103 23 AAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQG------KPLAE--ARGEV-------------D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 119 GGMVLFEYspFG-----VIGSVAPSTNPTETII---------------NNSISM--------LAAGNSVYFSPHPGAKKV 170
Cdd:cd07103 82 YAASFLEW--FAeearrIYGRTIPSPAPGKRILvikqpvgvvaaitpwNFPAAMitrkiapaLAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 171 SLKLISLIEEiafrcCGIR----NLVVTVAEptfEATQQMMAHPRIAVLAITGGPGIvamgmksGKKVIGAGA------- 239
Cdd:cd07103 160 ALALAELAEE-----AGLPagvlNVVTGSPA---EIGEALCASPRVRKISFTGSTAV-------GKLLMAQAAdtvkrvs 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 240 ----GNPPCIVDETADLVKAAEDIIN------GASfdynlpCIAEKSLIVVESVAERLVQQMQ----------------T 293
Cdd:cd07103 225 lelgGNAPFIVFDDADLDKAVDGAIAskfrnaGQT------CVCANRIYVHESIYDEFVEKLVervkklkvgngldegtD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 294 FGALllspTDTDKLRAVclpegqanKKLVG--KSPSAMLEAAGIAVPAK----APRLLiAVVNADDPWVTSEQLMPMLPV 367
Cdd:cd07103 299 MGPL----INERAVEKV--------EALVEdaVAKGAKVLTGGKRLGLGgyfyEPTVL-TDVTDDMLIMNEETFGPVAPI 365
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 447020428 368 VKVSDFDSALALALKVEEGLhhTAIMHSQNVSRLNLAARTLQT 410
Cdd:cd07103 366 IPFDTEDEVIARANDTPYGL--AAYVFTRDLARAWRVAEALEA 406
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
128-291 |
2.70e-05 |
|
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: 46.33 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRCcGIRNLVVTVAEptfEATQQMM 207
Cdd:cd07140 147 PIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPK-GVINILPGSGS---LVGQRLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 208 AHPRIAVLAITGGPGIVAMGMKSG-----KKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVES 282
Cdd:cd07140 223 DHPDVRKLGFTGSTPIGKHIMKSCavsnlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEES 302
|
....*....
gi 447020428 283 VAERLVQQM 291
Cdd:cd07140 303 IHDEFVRRV 311
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
37-291 |
6.21e-05 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 45.11 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFLRYQQCPLKTRSAIISAMrqeltpllATLAEESANETG------MG----NKEDKFLKNKAAL----D 102
Cdd:PRK09406 25 VDAAIARAHARFRDYRTTTFAQRARWANAA--------ADLLEAEADQVAalmtleMGktlaSAKAEALKCAKGFryyaE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 103 NTPG-VEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEI 181
Cdd:PRK09406 97 HAEAlLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 182 AFRCCGIRNLVVTVAeptfeATQQMMAHPRIAVLAITG----GPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAE 257
Cdd:PRK09406 177 GFPDGCFQTLLVGSG-----AVEAILRDPRVAAATLTGsepaGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447020428 258 DII------NGASfdynlpCIAEKSLIVVESV----AERLVQQM 291
Cdd:PRK09406 252 TAVtarvqnNGQS------CIAAKRFIVHADVydafAEKFVARM 289
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
128-379 |
8.86e-05 |
|
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: 44.71 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIafrccgIRNLVVTVAEPTFEATQQMM 207
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY------LDTKAIKVIEGGVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 208 AHPRIAVLaITGGPGIvamgmksGKKVIGAGA-----------GNPPCIVDETADLVKAAEDIINGA-SFDYNLPCIAEK 275
Cdd:cd07137 175 EQKWDKIF-FTGSPRV-------GRIIMAAAAkhltpvtlelgGKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQACIAPD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 276 SLIVVESVAERLVQQMQT-----FGAlllSPTDTDKLRAVclpegqANKKLVGKSpSAMLEAAGIAvpAK--------AP 342
Cdd:cd07137 247 YVLVEESFAPTLIDALKNtlekfFGE---NPKESKDLSRI------VNSHHFQRL-SRLLDDPSVA--DKivhggerdEK 314
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 447020428 343 RLLIA---VVNA--DDPWVTSEQLMPMLPVVKVSDFDSALAL 379
Cdd:cd07137 315 NLYIEptiLLDPplDSSIMTEEIFGPLLPIITVKKIEESIEI 356
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
38-289 |
2.72e-04 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 43.14 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 38 SEAIDAAHQAFLRYQQCPLKTRSAIIS-------AMRQELTPLLaTLAE-----ESANETGMGNKEDKFLKNKAAldNTP 105
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRrwydliiANKEDLAQLM-TLEQgkplkEAIGEVAYGASFLEYFAEEAK--RVY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 106 GveDLTTTALTGDGGMVLFEysPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEIAFRC 185
Cdd:PLN02278 142 G--DIIPSPFPDRRLLVLKQ--PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 186 cGIRNLVVTVAEPTFEAtqqMMAHPRIAVLAITGGPGIVAMGMKSG----KKVIGAGAGNPPCIVDETADLVKAAEDIIN 261
Cdd:PLN02278 218 -GVLNVVMGDAPEIGDA---LLASPKVRKITFTGSTAVGKKLMAGAaatvKRVSLELGGNAPFIVFDDADLDVAVKGALA 293
|
250 260
....*....|....*....|....*...
gi 447020428 262 GASFDYNLPCIAEKSLIVVESVAERLVQ 289
Cdd:PLN02278 294 SKFRNSGQTCVCANRILVQEGIYDKFAE 321
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
37-291 |
1.70e-03 |
|
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: 40.87 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 37 VSEAIDAAHQAFL-RYQQCPLKTRSAIISAMRQELTPLLATLAEESANETGMGNKEDKFLKNKA---------ALDNTPG 106
Cdd:cd07148 23 IDKALDTAHALFLdRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAidgvelaadELGQLGG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 107 VE---DLTTTaltGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLISLIEEiaf 183
Cdd:cd07148 103 REipmGLTPA---SAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHE--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 184 rcCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGpGIVAMGMKS----GKKVIGAGAGNPPCIVDETADLVKAAEDI 259
Cdd:cd07148 177 --AGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGS-ARVGWMLRSklapGTRCALEHGGAAPVIVDRSADLDAMIPPL 253
|
250 260 270
....*....|....*....|....*....|..
gi 447020428 260 INGASFDYNLPCIAEKSLIVVESVAERLVQQM 291
Cdd:cd07148 254 VKGGFYHAGQVCVSVQRVFVPAEIADDFAQRL 285
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
128-263 |
3.08e-03 |
|
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: 39.98 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447020428 128 PFGVIGSVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLKLisliEEIaFRCCGIRNLVVTVAEPTFEATQQMM 207
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLL----AEI-LTEAGLPDGVFNVVQGGGETGQLLC 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447020428 208 AHPRIAVLAITGGpgiVAmgmkSGKKVIGAGA-----------GNPPCIVDETADLvkaaEDIINGA 263
Cdd:cd07090 191 EHPDVAKVSFTGS---VP----TGKKVMSAAAkgikhvtlelgGKSPLIIFDDADL----ENAVNGA 246
|
|
| |
