|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
1-467 |
0e+00 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 726.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 1 MNQQDIEQVVKAVLLKM--KDSSQPVSAVQEMGVFASLDDAVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAE 76
Cdd:PRK15398 1 MNQQDIEQVVKAVLAEMlsSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYqqKSLAMRQRIIDAIREALLPHAEELAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 77 LAVTETGMGRVEDKFAKNVAQARGTPGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSV 156
Cdd:PRK15398 81 LAVEETGMGRVEDKIAKNVAAAEKTPGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 157 VFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKhTNKRLIAAG 236
Cdd:PRK15398 161 VFSPHPGAKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK-SGKKAIGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 237 AGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNider 316
Cdd:PRK15398 240 AGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKN---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 317 gKGTVSRDWVGRDAGKIAAAIGLNVPEQTRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHHTAAM 396
Cdd:PRK15398 316 -GGTVNKKWVGKDAAKILEAAGINVPKDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNRHTAIM 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489128223 397 HSRNIDNMNRMANAIDTSIFVKNGPCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV 467
Cdd:PRK15398 395 HSRNVDNLNKMARAIQTSIFVKNGPSYAGLGLGGEGFTTFTIATPTGEGVTSARTFTRRRRCVLVDGFRIR 465
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
31-461 |
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: 656.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 31 GVFASLDDAVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTPGVECLS 108
Cdd:cd07121 1 GVFATVDDAVAAAKAAQKQYrkCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 109 PQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANL 188
Cdd:cd07121 81 TTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 189 LVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTnKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNII 268
Cdd:cd07121 161 VVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG-KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 269 CADEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNIDErgkGTVSRDWVGRDAGKIAAAIGLNVPEQTRLL 348
Cdd:cd07121 240 CIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNKG---ATPNKKWVGKDASKILKAAGIEVPADIRLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 349 FVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHHTAAMHSRNIDNMNRMANAIDTSIFVKNGPCIAGLGL 428
Cdd:cd07121 317 IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGLGV 396
|
410 420 430
....*....|....*....|....*....|...
gi 489128223 429 GGEGWTTMTITTPTGEGVTSARTFVRLRRCVLV 461
Cdd:cd07121 397 GGEGYTTFTIAGPTGEGLTSARTFTRRRRCVLV 429
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
36-461 |
0e+00 |
|
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: 568.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTPGVEC--LSPQV 111
Cdd:cd07081 1 LDDAVAAAKVAQQGLscKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKdeKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 112 LTGD-NGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLV 190
Cdd:cd07081 81 LTGDeNGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 191 TVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTnKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICA 270
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 271 DEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNIDergkgtVSRDWVGRDAGKIAAAIGLNVPEQTRLLFV 350
Cdd:cd07081 240 SEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGD------VNRDIVGQDAYKIAAAAGLKVPQETRILIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 351 ETS--ATHPFAVTELMMPVLPVVRVANVDEAIE--LAVKLEGGCHHTAAMHSRN---IDNMNRMANAIDTSIFVKNGPC- 422
Cdd:cd07081 314 EVTslAEHEPFAHEKLSPVLAMYRAANFADADAkaLALKLEGGCGHTSAMYSDNikaIENMNQFANAMKTSRFVKNGPCs 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489128223 423 IAGLGLGGE--GWTTMTIT--TPTGEGVTS---ARTFVRLRRCVLV 461
Cdd:cd07081 394 QGGLGDLYNfrGWPSMTLGcgTWGGNSVSEnvgPKHLVNLKTVALR 439
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
41-460 |
1.98e-142 |
|
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: 413.54 E-value: 1.98e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 41 AAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETG-------------MGRVEDKFAKNVAQARGTPGVE 105
Cdd:cd07077 1 ESAKNAQRTLavNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 CLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAAtVINNAISLIAAGNSVVFAPHPAAKkVSQRAITLLNQAVVAAGGP 185
Cdd:cd07077 81 GHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 186 ANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTN-KRLIAAGAGNPPVVVDETADLARAAQSVVKGASFD 264
Cdd:cd07077 159 KILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 265 NNiICADEKVLIVVDSVADELMRLMESQHAVklttaqaeqlqpvllknidergkgtvsrdwvgrdagkiaaaIGLNVPEQ 344
Cdd:cd07077 239 QN-ACASEQNLYVVDDVLDPLYEEFKLKLVV-----------------------------------------EGLKVPQE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 345 TRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIE--LAVKLEGGCHHTAAMHSRNIDNMNRMANAIDTSIFVKNGPC 422
Cdd:cd07077 277 TKPLSKETTPSFDDEALESMTPLECQFRVLDVISAVEnaWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESS 356
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489128223 423 IA--GLGLGGEGWTTMTITTPTGEG-VTSARTFVRLRRCVL 460
Cdd:cd07077 357 KKgrGAFAGKGVERIVTSGMNNIFGaGVGHDALRPLKRLVR 397
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
36-427 |
7.58e-99 |
|
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: 303.64 E-value: 7.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLKSVAMRQL--AITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTpgVECLSPQVLT 113
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVdkIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYV--YNDIKDMKTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 114 G------DNGLTLIEnAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPAN 187
Cdd:cd07122 79 GvieedeEKGIVEIA-EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 188 LLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKhTNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNI 267
Cdd:cd07122 158 LIQWIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYS-SGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 268 ICADEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNidergKGTVSRDWVGRDAGKIAAAIGLNVPEQTRL 347
Cdd:cd07122 237 ICASEQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDD-----GGTLNPDIVGKSAQKIAELAGIEVPEDTKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 348 LFVET---SATHPFAVtELMMPVLPVVRVANVDEAIELAVKL--EGGCHHTAAMHSRNIDNMNRMANAIDTSIFVKNGP- 421
Cdd:cd07122 312 LVAEEtgvGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARELleYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPs 390
|
....*.
gi 489128223 422 CIAGLG 427
Cdd:cd07122 391 SLGGIG 396
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
17-421 |
1.22e-74 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 250.87 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 17 MKDSSQPVSAVQEmgvfasLDDAVAAAKLAQQGLKSVAMRQL-AIT-ALREAGEKHARELAELAVTETGMGRVEDKFAKN 94
Cdd:PRK13805 1 MTKEEMAVTNVAE------LDALVEKAKKAQEEFATFTQEQVdKIVrAAALAALDARIPLAKMAVEETGRGVVEDKVIKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 95 -VA--------QARGTPGVeclspqvLTGDNGLTLIENA-PWGVVASVTPSTNPAATVINNAisLIAA--GNSVVFAPHP 162
Cdd:PRK13805 75 hFAseyiynsyKDEKTVGV-------IEEDDEFGIIEIAePVGVIAGITPTTNPTSTAIFKA--LIALktRNPIIFSFHP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 163 AAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKhTNKRLIAAGAGNPPV 242
Cdd:PRK13805 146 RAQKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYS-SGKPALGVGAGNVPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 243 VVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNIDergkGTVS 322
Cdd:PRK13805 225 YIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGKEN----GALN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 323 RDWVGRDAGKIAAAIGLNVPEQTRLLFVETSAT---HPFAVtELMMPVLPVVRVANVDEAIELAVKL--EGGCHHTAAMH 397
Cdd:PRK13805 301 ADIVGQSAYKIAEMAGFKVPEDTKILIAEVKGVgesEPLSH-EKLSPVLAMYKAKDFEDAVEKAEKLveFGGLGHTAVIY 379
|
410 420
....*....|....*....|....*
gi 489128223 398 SRNIDNMNRMANAIDTS-IFVkNGP 421
Cdd:PRK13805 380 TNDDELIKEFGLRMKACrILV-NTP 403
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
38-427 |
8.64e-67 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 222.05 E-value: 8.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 38 DAVAAAKLAQQGLKSVAMRQL--AITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTpgVECLSPQ----V 111
Cdd:TIGR02518 12 NLIRSAKVAQKKLANMTQEQIdkIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIV--YDSIKDMktigI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 112 LTGDNGLTLIENA-PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLV 190
Cdd:TIGR02518 90 LSEDKEKKVIEIAvPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 191 TVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKhTNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICA 270
Cdd:TIGR02518 170 CITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYS-SGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 271 DEKVLIVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNidergKGTVSRDWVGRDAGKIAAAIGLNVPEQTRLLFV 350
Cdd:TIGR02518 249 SEQSIIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRP-----NGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 351 E---TSATHPFAvTELMMPVLPVVRVANVDEAIELAVKL--EGGCHHTAAMHSRNIDNMNRMANAIDTS-IFVKNGPCIA 424
Cdd:TIGR02518 324 EqngVGNKNPYS-REKLTTILAFYTEENWHEACELSIELlqNEGAGHTLIIHSENKDIVREFALKKPVSrMLVNTGGSLG 402
|
...
gi 489128223 425 GLG 427
Cdd:TIGR02518 403 GIG 405
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
41-460 |
3.56e-63 |
|
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: 209.01 E-value: 3.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 41 AAAKLAQQGLK--SVAMRQLAITALREAGEKHARELAELAVTETG--MGRVEDKFAKNVAQARGTPGVECL---SPQVLT 113
Cdd:cd06534 1 AAARAAFKAWAalPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKlggPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 114 GDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLnqavVAAGGPANLLVTVA 193
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 194 NPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKH---TNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICA 270
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAaaeNLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 271 DEKVLIVVDSVADELMRlmesqhavKLTTaqaeqlqpvllknidergkgtvsrdwvgrdagkiaaaiglnvpeqtrlLFV 350
Cdd:cd06534 237 AASRLLVHESIYDEFVE--------KLVT------------------------------------------------VLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 351 ETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGchHTAAMHSRNIDNMNRMANAIDTSIFVKNGPCI------- 423
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYG--LTAGVFTRDLNRALRVAERLRAGTVYINDSSIgvgpeap 338
|
410 420 430
....*....|....*....|....*....|....*...
gi 489128223 424 -AGLGLGGEGWTTmtittptgeGVTSARTFVRLRRCVL 460
Cdd:cd06534 339 fGGVKNSGIGREG---------GPYGLEEYTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
37-433 |
4.79e-30 |
|
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: 121.48 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVEC------ 106
Cdd:pfam00171 32 DAAIAAARAAFPAwrKTPAAERAAILRKAADLLEERKDELAELETLENG---------KPLAEARGevDRAIDVlryyag 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 107 ----LSPQVLTGDNG-LTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVA 181
Cdd:pfam00171 103 larrLDGETLPSDPGrLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTAL----LLAELFEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV-----VDAARkhTNKRLIAAGAGNPPVVVDETADLARAAQS 256
Cdd:pfam00171 179 AGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVgrhiaEAAAQ--NLKRVTLELGGKNPLIVLEDADLDAAVEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 257 VVKGASFDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLTT----------------AQAEQLQPVLLKNIDERGKGT 320
Cdd:pfam00171 257 AVFGAFGNAGQVCTATSRLLVHESIYDEFVEKL-VEAAKKLKVgdpldpdtdmgpliskAQLERVLKYVEDAKEEGAKLL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 321 VSRDWVGRDAGKIAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGchHTAAMHSRN 400
Cdd:pfam00171 336 TGGEAGLDNGYFVEPTVLANVTPDMRIAQEEI-----FG------PVLSVIRFKDEEEAIEIANDTEYG--LAAGVFTSD 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489128223 401 IDNMNRMANAIDTSIFVKNGPCIAGL-----------GLGGEGW 433
Cdd:pfam00171 403 LERALRVARRLEAGMVWINDYTTGDAdglpfggfkqsGFGREGG 446
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
37-421 |
8.30e-30 |
|
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: 120.39 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETG----MGRVE-----DKFAKNVAQARGTPGVE 105
Cdd:cd07078 1 DAAVAAARAAFKAwaALPPAERAAILRKLADLLEERREELAALETLETGkpieEALGEvaraaDTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 CLSPqvltGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQavvaAGGP 185
Cdd:cd07078 81 IPSP----DPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE----AGLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 186 ANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNKRLIAAGAGNPPVVVDETADLARAAQSVVKGA 261
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALASHPRVDKISFTGstavGKAIMRAAAEN-LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 262 SFDNNIICADEKVLIVVDSVADELMRLMESQH-AVK--------------LTTAQAEQLQPVLLKNIDERGKGTVSRDWV 326
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVkALKvgnpldpdtdmgplISAAQLDRVLAYIEDAKAEGAKLLCGGKRL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 GRDAG-KIAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMN 405
Cdd:cd07078 312 EGGKGyFVPPTVLTDVDPDMPIAQEEI-----FG------PVLPVIPFKDEEEAIELANDTEYGL--AAGVFTRDLERAL 378
|
410
....*....|....*.
gi 489128223 406 RMANAIDTSIFVKNGP 421
Cdd:cd07078 379 RVAERLEAGTVWINDY 394
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
36-425 |
1.40e-27 |
|
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: 114.84 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLK--SVAMRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVECL---- 107
Cdd:COG1012 45 VDAAVAAARAAFPAWAatPPAERAAILLRAADLLEERREELAALLTLETG---------KPLAEARGevDRAADFLryya 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 108 ----------SPQVLTGDNGLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAkkvsQRAITLLNQ 177
Cdd:COG1012 116 gearrlygetIPSDAPGTRAYVRRE--PLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQT----PLSALLLAE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 178 AVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNKRLIAAGAGNPPVVVDETADLARA 253
Cdd:COG1012 190 LLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGstavGRRIAAAAAEN-LKRVTLELGGKNPAIVLDDADLDAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLT----TAQAEQLQPVllknIDERGKGTVsRDWV--G 327
Cdd:COG1012 269 VEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERL-VAAAKALKvgdpLDPGTDMGPL----ISEAQLERV-LAYIedA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 328 RDAG-KIAAaiGLNVPEQTRLLFVE------TSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRN 400
Cdd:COG1012 343 VAEGaELLT--GGRRPDGEGGYFVEptvladVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGL--AASVFTRD 418
|
410 420
....*....|....*....|....*
gi 489128223 401 IDNMNRMANAIDTSIFVKNGPCIAG 425
Cdd:COG1012 419 LARARRVARRLEAGMVWINDGTTGA 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
32-412 |
2.77e-23 |
|
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: 102.05 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 32 VFASLDDAVAAAKLAQQGLKSVAMRQLAITALREAGE---KHARELAELAVTETG---------MGRVEDKFAKNVAQAR 99
Cdd:cd07146 15 VPAGTEEALREALALAASYRSTLTRYQRSAILNKAAAlleARREEFARLITLESGlclkdtryeVGRAADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 100 GTPGvECLSPQVLTGDN---GLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakKVSQRAItLLN 176
Cdd:cd07146 95 RDDG-ESFSCDLTANGKarkIFTLRE--PLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE---KTPLSAI-YLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 177 QAVVAAGGPANLL-VTVANPDiETAQRLFKYPGIGLLVVTGGEAVVDA-ARKHTNKRLIAAGAGNPPVVVDETADLARAA 254
Cdd:cd07146 168 DLLYEAGLPPDMLsVVTGEPG-EIGDELITHPDVDLVTFTGGVAVGKAiAATAGYKRQLLELGGNDPLIVMDDADLERAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 255 QSVVKGASFDNNIICADEKVLIVVDSVADELMRLMEsQHAVKLTT----------------AQAEQLQPVLLKNIDeRGK 318
Cdd:cd07146 247 TLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLV-EKSAALVVgdpmdpatdmgtvideEAAIQIENRVEEAIA-QGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 319 GTVSRDwvGRDAGKIAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGChhTAAMHS 398
Cdd:cd07146 325 RVLLGN--QRQGALYAPTVLDHVPPDAELVTEET-----FG------PVAPVIRVKDLDEAIAISNSTAYGL--SSGVCT 389
|
410
....*....|....
gi 489128223 399 RNIDNMNRMANAID 412
Cdd:cd07146 390 NDLDTIKRLVERLD 403
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
22-432 |
1.83e-22 |
|
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: 99.65 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 22 QPVSAVqEMGVFASLDDAVAAAKLAQQGLKSVAMRQLA--ITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQAR 99
Cdd:cd07088 24 EVVATV-PAATAEDADRAVDAAEAAQKAWERLPAIERAayLRKLADLIRENADELAKLIVEEQG---------KTLSLAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 100 GTPGVEC------------LSPQVLTGD--NGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHpaak 165
Cdd:cd07088 94 VEVEFTAdyidymaewarrIEGEIIPSDrpNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 166 KVSQRAITLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPP 241
Cdd:cd07088 170 EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGsteaGQKIMEAAAENITKVSLELG-GKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 242 VVVDETADLARAAQSVVKgASFDNN-IICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAEQLQ--PVLLKNIDERG 317
Cdd:cd07088 249 AIVMKDADLDLAVKAIVD-SRIINCgQVCTCAERVYVHEDIYDEFMeKLVEKMKAVKVGDPFDAATDmgPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 318 KGTVSRdwvGRDAG-KIaaAIGLNVPEQTRLLFVE----TSATHPFAVT--ELMMPVLPVVRVANVDEAIELAVKLEGGC 390
Cdd:cd07088 328 EEMVER---AVEAGaTL--LTGGKRPEGEKGYFYEptvlTNVRQDMEIVqeEIFGPVLPVVKFSSLDEAIELANDSEYGL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489128223 391 hhTAAMHSRNIDNMNRMANAI---DTSIFVKNGPCIAGL-------GLGGEG 432
Cdd:cd07088 403 --TSYIYTENLNTAMRATNELefgETYINRENFEAMQGFhagwkksGLGGAD 452
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
38-413 |
2.20e-22 |
|
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: 99.22 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 38 DAVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETGMGRVE------------DKFAKN---VAQARG 100
Cdd:cd07099 22 AAVARARAAQRAWaaLGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADaglevllaleaiDWAARNaprVLAPRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 101 TPGVECLSPQVLTgdngltlIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVV 180
Cdd:cd07099 102 VPTGLLMPNKKAT-------VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE----LLAEAWA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 181 AAGGPANLLvTVANPDIETAQRLFKYpGIGLLVVTGGEAvvdaarkhTNKRLIAAGA-----------GNPPVVVDETAD 249
Cdd:cd07099 171 AAGPPQGVL-QVVTGDGATGAALIDA-GVDKVAFTGSVA--------TGRKVMAAAAerlipvvlelgGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 250 LARAAQSVVKGASFDNNIICADEKVLIVVDSVADELmrlmesqhaVKLTTAQAEQLQPvllkNIDERGKG---------- 319
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEF---------VARLVAKARALRP----GADDIGDAdigpmttarq 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 320 --TVSR---DWVgrDAGKIAAAIGLnvPEQTRLLFVE----TSATHPFAVT--ELMMPVLPVVRVANVDEAIELAVKLEG 388
Cdd:cd07099 308 ldIVRRhvdDAV--AKGAKALTGGA--RSNGGGPFYEptvlTDVPHDMDVMreETFGPVLPVMPVADEDEAIALANDSRY 383
|
410 420
....*....|....*....|....*
gi 489128223 389 GChhTAAMHSRNIDNMNRMANAIDT 413
Cdd:cd07099 384 GL--SASVFSRDLARAEAIARRLEA 406
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
37-413 |
3.51e-22 |
|
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: 98.80 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQG---LKSVAMRQLAITALREAGEKHARELAELAVTETG------MGRVE---DKFAKNVAQARGTPGV 104
Cdd:cd07082 41 LEAAETAYDAGRGwwpTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGktlkdaLKEVDrtiDYIRDTIEELKRLDGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 105 ECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPaatvINNAISLIA----AGNSVVFAPhpaAKKVSQRAITLLnQAVV 180
Cdd:cd07082 121 SLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYP----LNLTVSKLIpaliMGNTVVFKP---ATQGVLLGIPLA-EAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 181 AAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDA-ARKHTNKRLIAA-GAGNPPVVVDEtADLARAAQSVV 258
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRlKKQHPMKRLVLElGGKDPAIVLPD-ADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 259 KGA-SFdNNIICADEKVLIVVDSVADELMRLMESQHAvKLTTAQAEQ----LQPV-----------LLKNIDERGkGTVS 322
Cdd:cd07082 272 KGAlSY-SGQRCTAIKRVLVHESVADELVELLKEEVA-KLKVGMPWDngvdITPLidpksadfvegLIDDAVAKG-ATVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 323 RDWVGRDAGKIAAAIGLNVPEQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIELAVKLEGGCHhtAAMHSRNID 402
Cdd:cd07082 349 NGGGREGGNLIYPTLLDPVTPDMRLAWEE-----PFG------PVLPIIRVNDIEEAIELANKSNYGLQ--ASIFTKDIN 415
|
410
....*....|.
gi 489128223 403 NMNRMANAIDT 413
Cdd:cd07082 416 KARKLADALEV 426
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-411 |
4.62e-22 |
|
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: 98.19 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSvaMRQLAITA----LREAGE---KHARELAELAVTETGM----GRVE--------DKFAKN 94
Cdd:cd07145 18 LSREEVREAIEVAEKAKDV--MSNLPAYKrykiLMKVAElieRRKEELAKLLTIEVGKpikqSRVEvertirlfKLAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 95 VAQARG-TPGVEclspQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFapHPAAKkvSQRAIT 173
Cdd:cd07145 96 AKVLRGeTIPVD----AYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV--KPSSN--TPLTAI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 174 LLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV---VDAARKHTNKRLIAAGAGNPPVVVDETADL 250
Cdd:cd07145 168 ELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVgllIASKAGGTGKKVALELGGSDPMIVLKDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 251 ARAAQSVVKGaSFDN-NIICADEKVLIVVDSVADE-LMRLMESQHAVKLTTAQAEQ--LQPVLLKNIDERGKGTVsRDWV 326
Cdd:cd07145 248 ERAVSIAVRG-RFENaGQVCNAVKRILVEEEVYDKfLKLLVEKVKKLKVGDPLDEStdLGPLISPEAVERMENLV-NDAV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 G----------RDAGKIAAAIGLNVPEQTRLLFVEtsathpfavtELMMPVLPVVRVANVDEAIELAVKLEGGCHhtAAM 396
Cdd:cd07145 326 EkggkilyggkRDEGSFFPPTVLENDTPDMIVMKE----------EVFGPVLPIAKVKDDEEAVEIANSTEYGLQ--ASV 393
|
410
....*....|....*
gi 489128223 397 HSRNIDNMNRMANAI 411
Cdd:cd07145 394 FTNDINRALKVAREL 408
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
34-383 |
4.23e-21 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 95.29 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETG----MGRVEDKFAknVAQARGTPGVEcL 107
Cdd:cd07106 19 AQLDQAVAAAKAAFPGwsATPLEERRAALLAIADAIEANAEELARLLTLEQGkplaEAQFEVGGA--VAWLRYTASLD-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 108 SPQVLT-GDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVvaaggPA 186
Cdd:cd07106 96 PDEVIEdDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVL-----PP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 187 NLLVTVANPDiETAQRLFKYPGIGLLVVTG----GEAVVDAARKhTNKRLIAAGAGNPPVVVDETADLARAAQSVVKGAS 262
Cdd:cd07106 171 GVLNVVSGGD-ELGPALTSHPDIRKISFTGstatGKKVMASAAK-TLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 263 FDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLTT----AQAEQLQPVLLKNIDERGKGTVsrDWVGRDAGKIAA--- 335
Cdd:cd07106 249 INSGQVCAAIKRLYVHESIYDEFCEAL-VALAKAAVVgdglDPGTTLGPVQNKMQYDKVKELV--EDAKAKGAKVLAgge 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489128223 336 -----------AIGLNVPEQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIELA 383
Cdd:cd07106 326 pldgpgyfippTIVDDPPEGSRIVDEE-----QFG------PVLPVLKYSDEDEVIARA 373
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
24-414 |
5.65e-21 |
|
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: 95.19 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 24 VSAVQEMGVFASLDDAVAAAKlaqqglksvAMRQLAIT----ALREAG---EKHARELAELAVTETGMGRVE-------- 88
Cdd:cd07094 15 VPADDRADAEEALATARAGAE---------NRRALPPHermaILERAAdllKKRAEEFAKIIACEGGKPIKDarvevdra 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 89 -DKFAKNVAQARGTPGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKV 167
Cdd:cd07094 86 iDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 168 SQRaitlLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTN-KRLIAAGAGNPPVVVDE 246
Cdd:cd07094 166 ALE----LAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGgKRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 247 TADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQhAVKLTTAQAEQLQPVLLKNIDErGKGTVSRDWV 326
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAA-VKKLKVGDPLDEDTDVGPLISE-EAAERVERWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 GRDAGKIAAAIGLNVPEQTrlLFVETSATHP-----FAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHhtAAMHSRNI 401
Cdd:cd07094 320 EEAVEAGARLLCGGERDGA--LFKPTVLEDVprdtkLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ--AGIFTRDL 395
|
410
....*....|...
gi 489128223 402 DNMNRMANAIDTS 414
Cdd:cd07094 396 NVAFKAAEKLEVG 408
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
33-413 |
1.14e-19 |
|
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: 91.15 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 33 FASLDDAVAAAKLAQQGLKSVAM--RQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGTPGV------ 104
Cdd:cd07102 17 LEAVRAALERARAAQKGWRAVPLeeRKAIVTRAVELLAANTDEIAEELTWQMG---------RPIAQAGGEIRGmlerar 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 105 -------ECLSPQVLTGDNGLTL-IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRaitlLN 176
Cdd:cd07102 88 ymisiaeEALADIRVPEKDGFERyIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER----FA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 177 QAVVAAGGPANLLVtVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAG---AGNPPVVVDETADLARA 253
Cdd:cd07102 164 AAFAEAGLPEGVFQ-VLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDN-NIICADEKVLI---VVDSVADELMRLMESQhavKL-------TT----AQAEQLQPVLLKNIDERGK 318
Cdd:cd07102 243 AESLVDGAFFNSgQSCCSIERIYVhesIYDAFVEAFVAVVKGY---KLgdpldpsTTlgpvVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 319 G----TVSRDWVGRDAGK--IAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGChh 392
Cdd:cd07102 320 GaralIDGALFPEDKAGGayLAPTVLTNVDHSMRVMREET-----FG------PVVGIMKVKSDAEAIALMNDSEYGL-- 386
|
410 420
....*....|....*....|.
gi 489128223 393 TAAMHSRNIDNMNRMANAIDT 413
Cdd:cd07102 387 TASVWTKDIARAEALGEQLET 407
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
20-419 |
1.79e-18 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 87.64 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 20 SSQPVSAVQEmGVFASLDDAVAAAK-LAQQG---LKSVAMRQLAITALREAGEKHARELAELAVTETG------------ 83
Cdd:PRK09847 44 TQAPLAKIAR-GKSVDIDRAVSAARgVFERGdwsLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGkpirhslrddip 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 84 -MGRVEDKFAKNVAQARGTpgvecLSPqvlTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhp 162
Cdd:PRK09847 123 gAARAIRWYAEAIDKVYGE-----VAT---TSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 163 aAKKVSQRAITLLNQAvVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGG-----EAVVDAARKHTNKRLIAAGA 237
Cdd:PRK09847 193 -SEKSPLSAIRLAGLA-KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGStrtgkQLLKDAGDSNMKRVWLEAGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 238 GNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMEsQHAVKLTTAQAEQLQPVLLKNIDE-- 315
Cdd:PRK09847 271 KSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLK-QQAQNWQPGHPLDPATTMGTLIDCah 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 316 -----------RGKGTVSRDwvGRDAGkIAAAIGLNVpeqtrllFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAV 384
Cdd:PRK09847 350 adsvhsfiregESKGQLLLD--GRNAG-LAAAIGPTI-------FVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
|
410 420 430
....*....|....*....|....*....|....*.
gi 489128223 385 KLEGGChhTAAMHSRNIDNMNRMANAIDT-SIFVKN 419
Cdd:PRK09847 420 DSQYGL--GAAVWTRDLSRAHRMSRRLKAgSVFVNN 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-411 |
7.86e-18 |
|
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: 85.73 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG----LKSVAMRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGT--PGV--- 104
Cdd:cd07112 24 ADVDRAVAAARRAFESgvwsRLSPAERKAVLLRLADLIEAHRDELALLETLDMG---------KPISDALAVdvPSAant 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 105 -----ECL-------SPqvlTGDNGLTLIENAPWGVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPhpaAKKVSQ 169
Cdd:cd07112 95 frwyaEAIdkvygevAP---TGPDALALITREPLGVVGAVVPWNFPllmAAWKIAPAL---AAGNSVVLKP---AEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 170 RAITLLNQAVvAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV-----VDAARkhTN-KRL-IAAGAGNPPV 242
Cdd:cd07112 166 TALRLAELAL-EAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVgrrflEYSGQ--SNlKRVwLECGGKSPNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 243 VVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLTTAQAEQLQPVLLKNIDERGKGTVs 322
Cdd:cd07112 243 VFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKV-VAAAREWKPGDPLDPATRMGALVSEAHFDKV- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 323 RDWV--GRDAGKIAAAIGLNVPEQTRLLFVE------TSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHhtA 394
Cdd:cd07112 321 LGYIesGKAEGARLVAGGKRVLTETGGFFVEptvfdgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA--A 398
|
410
....*....|....*..
gi 489128223 395 AMHSRNIDNMNRMANAI 411
Cdd:cd07112 399 SVWTSDLSRAHRVARRL 415
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
36-400 |
8.74e-18 |
|
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: 85.74 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLKSVAMRQLAiTALREAGEKHARELAELAVT---ETGmgrvedkfaKNVAQARGTPG--------- 103
Cdd:cd07124 71 AEAAVQAARAAFPTWRRTPPEERA-RLLLRAAALLRRRRFELAAWmvlEVG---------KNWAEADADVAeaidfleyy 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 104 ---VECLSPQVLTG----DNGLTLIenaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSqraiTLLN 176
Cdd:cd07124 141 areMLRLRGFPVEMvpgeDNRYVYR---PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIA----AKLV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 177 QAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV----------VDAARKHTnKRLIAAGAGNPPVVVDE 246
Cdd:cd07124 214 EILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVglriyeraakVQPGQKWL-KRVIAEMGGKNAIIVDE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 247 TADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESqhAVKLTTAQAEQ----LQPVLLKNIDERGKGTV 321
Cdd:cd07124 293 DADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLeRLVER--TKALKVGDPEDpevyMGPVIDKGARDRIRRYI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 322 SrdwVGRDAGKIAAaiGLNVPE-QTRLLFVETS------ATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTA 394
Cdd:cd07124 371 E---IGKSEGRLLL--GGEVLElAAEGYFVQPTifadvpPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGL--TG 443
|
....*.
gi 489128223 395 AMHSRN 400
Cdd:cd07124 444 GVFSRS 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
36-421 |
9.37e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 85.58 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGL------KSVAMRQLAITALREagekHARELAELAVTETGMG----RVEDKFAKNVAQARGTPGVE 105
Cdd:PLN00412 55 VNKAMESAKAAQKAWaktplwKRAELLHKAAAILKE----HKAPIAECLVKEIAKPakdaVTEVVRSGDLISYTAEEGVR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 CLSP-QVLTGD-------NGLTLIENAPWGVVASVTPSTNPaatvINNAISLIA----AGNSVVFAPHpaakkvSQRAIT 173
Cdd:PLN00412 131 ILGEgKFLVSDsfpgnerNKYCLTSKIPLGVVLAIPPFNYP----VNLAVSKIApaliAGNAVVLKPP------TQGAVA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 174 LLN--QAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLA 251
Cdd:PLN00412 201 ALHmvHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 252 RAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQHAvKLTTAQAE---QLQPVLLKN---------IDERGKG 319
Cdd:PLN00412 281 LAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA-KLTVGPPEddcDITPVVSESsanfieglvMDAKEKG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 320 TVSRDWVGRDAGKIAAAIGLNVPEQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIELAVK----LEgGCHHTaa 395
Cdd:PLN00412 360 ATFCQEWKREGNLIWPLLLDNVRPDMRIAWEE-----PFG------PVLPVIRINSVEEGIHHCNAsnfgLQ-GCVFT-- 425
|
410 420
....*....|....*....|....*.
gi 489128223 396 mhsRNIDNMNRMANAIDTSIFVKNGP 421
Cdd:PLN00412 426 ---RDINKAILISDAMETGTVQINSA 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
34-383 |
2.68e-17 |
|
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: 83.83 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG---LKSVAMRQLAITALREAGEKHARELAELAVTETGMGRV----------EDKFAKNVAQARG 100
Cdd:cd07089 19 ADVDAAIAAARRAFDTgdwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtaramqvdgpIGHLRYFADLADS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 101 TPGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkVSQRAITLLNQAVV 180
Cdd:cd07089 99 FPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP----DTPLSALLLGEIIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 181 AAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV---VDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQSV 257
Cdd:cd07089 175 ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVgrrIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 258 VKGASFDNNIICADEKVLIVVDSVADElmrlmesqhAVKLTTAQAEQLqPVLlkniDERGKGTVS--------RDWV--- 326
Cdd:cd07089 255 VGVCMHNAGQGCALTTRLLVPRSRYDE---------VVEALAAAFEAL-PVG----DPADPGTVMgplisaaqRDRVegy 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489128223 327 ---GRDAGKIAAAIGLNVP--------EQTRLLFVETSAThpFAVTELMMPVLPVVRVANVDEAIELA 383
Cdd:cd07089 321 iarGRDEGARLVTGGGRPAgldkgfyvEPTLFADVDNDMR--IAQEEIFGPVLVVIPYDDDDEAVRIA 386
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
37-430 |
4.01e-17 |
|
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: 83.40 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQ---GLKSVAMRQLAITALrEAGEKHARELAELAVTETGMGRVEDKFakNVAQARG---------TPGV 104
Cdd:cd07105 3 DQAVEAAAAAFPawsKTPPSERRDILLKAA-DLLESRRDEFIEAMMEETGATAAWAGF--NVDLAAGmlreaasliTQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 105 ECLSPQVLTGDNGLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGG 184
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKE--PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHW----LIGRVFHEAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 185 PANLL--VTVA---NPDIETAqrLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQ 255
Cdd:cd07105 154 PKGVLnvVTHSpedAPEVVEA--LIAHPAVRKVNFTGstrvGRIIAETAAKHLKPVLLELG-GKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 256 SVVKGASFDNNIIC-ADEKVlIVVDSVADELMRLMESqhAVKLTTAQAEQLQPVLLKNIDERGKGTVS------------ 322
Cdd:cd07105 231 AALFGAFLNSGQICmSTERI-IVHESIADEFVEKLKA--AAEKLFAGPVVLGSLVSAAAADRVKELVDdalskgaklvvg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 323 -RDWVGRDAGKIAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNI 401
Cdd:cd07105 308 gLADESPSGTSMPPTILDNVTPDMDIYSEES-----FG------PVVSIIRVKDEEEAVRIANDSEYGL--SAAVFTRDL 374
|
410 420 430
....*....|....*....|....*....|..
gi 489128223 402 DNMNRMANAIDTSIFVKNGPCI---AGLGLGG 430
Cdd:cd07105 375 ARALAVAKRIESGAVHINGMTVhdePTLPHGG 406
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
36-413 |
6.31e-17 |
|
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: 82.58 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLKSVAMRQLAiTALREAG---EKHARELAELAVTETGMGR----VEDKFAKNVAQARGTpgvECLS 108
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERA-AILRKAAeilEERRDEIADWLIRESGSTRpkaaFEVGAAIAILREAAG---LPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 109 PQVLT----GDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkvsQRAIT---LLNQAVVA 181
Cdd:cd07104 78 PEGEIlpsdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDS------RTPVTgglLIAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANLL-VTVANPDiETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQS 256
Cdd:cd07104 152 AGLPKGVLnVVPGGGS-EIGDALVEHPRVRMISFTGstavGRHIGELAGRHLKKVALELG-GNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 257 VVKGASFDNNIICADEKVLIVVDSVADELmrlmesqhaVKLTTAQAEQLqPVLlkniDERGKGTV-----SRDWVGRDAG 331
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEF---------VEKLVAKAKAL-PVG----DPRDPDTVigpliNERQVDRVHA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 332 KIAAAiglnVPEQTRLL--------------FVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMH 397
Cdd:cd07104 296 IVEDA----VAAGARLLtggtyeglfyqptvLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGL--SAAVF 369
|
410
....*....|....*.
gi 489128223 398 SRNIDNMNRMANAIDT 413
Cdd:cd07104 370 TRDLERAMAFAERLET 385
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-423 |
1.55e-15 |
|
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: 78.54 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 24 VSAVQEMGVFASLDDAVAAAKLAQQGLKSVA--MRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG- 100
Cdd:cd07131 27 VVGTFPLSTASDVDAAVEAAREAFPEWRKVPapRRAEYLFRAAELLKKRKEELARLVTREMG---------KPLAEGRGd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 101 -TPGVECLspQVLTGD--------------NGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAK 165
Cdd:cd07131 98 vQEAIDMA--QYAAGEgrrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 166 KVSQRaitlLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNKRLIAAGAGNPP 241
Cdd:cd07131 176 ACALK----LVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGstevGERIGETCARP-NKRVALEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 242 VVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAEQ--LQPVllknIDERGK 318
Cdd:cd07131 251 IIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLkRFVERAKRLRVGDGLDEEtdMGPL----INEAQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 319 GTVSRdWVgrDAGKIAAAIGLNVPEQ-TRLLFVETSATHPFAVT-----------ELMMPVLPVVRVANVDEAIELAVKL 386
Cdd:cd07131 327 EKVLN-YN--EIGKEEGATLLLGGERlTGGGYEKGYFVEPTVFTdvtpdmriaqeEIFGPVVALIEVSSLEEAIEIANDT 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 489128223 387 EGGChhTAAMHSRNIDNMNRMANAIDTSIFVKNGPCI 423
Cdd:cd07131 404 EYGL--SSAIYTEDVNKAFRARRDLEAGITYVNAPTI 438
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
34-430 |
2.19e-15 |
|
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: 78.04 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG--LKSVAMRQLAItaLREAGE---KHARELAELAVTETGmgrvedkfaKNVAQARG-------- 100
Cdd:cd07109 19 ADVDRAVQAARRAFESgwLRLSPAERGRL--LLRIARlirEHADELARLESLDTG---------KPLTQARAdveaaary 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 101 ----TPGVECLSPQVL-TGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVfaphpaAKKVSQRAITLL 175
Cdd:cd07109 88 feyyGGAADKLHGETIpLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVV------VKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 176 NQAVVA--AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETAD 249
Cdd:cd07109 162 RLAELAeeAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGsvetGIAVMRAAAENVVPVTLELG-GKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 250 LARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAE-QLQPVLLKNIDERGKGTVSRdwvG 327
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLeRLVERFRALRVGPGLEDpDLGPLISAKQLDRVEGFVAR---A 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 328 RDAGKIAAAIGLNVPEQTR-------LLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRN 400
Cdd:cd07109 318 RARGARIVAGGRIAEGAPAggyfvapTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL--VAGVWTRD 395
|
410 420 430
....*....|....*....|....*....|...
gi 489128223 401 IDNMNRMANAIDT-SIFVKNGPCIAGLGL--GG 430
Cdd:cd07109 396 GDRALRVARRLRAgQVFVNNYGAGGGIELpfGG 428
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-423 |
4.26e-15 |
|
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: 76.98 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 38 DAVAAAKLAQQGLKSVAMRQLAITALR--EAGEKHARELAELAVTETGmgrveDKFAKNVAQARGTPGV------ECLSP 109
Cdd:cd07150 25 RAIAAAYDAFPAWAATTPSERERILLKaaEIMERRADDLIDLLIDEGG-----STYGKAWFETTFTPELlraaagECRRV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 110 --QVLTGD-NGL-TLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSqraiTLLNQAVVAAGGP 185
Cdd:cd07150 100 rgETLPSDsPGTvSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG----LKIAEIMEEAGLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 186 ANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGA 261
Cdd:cd07150 176 KGVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIAEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAAAFGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 262 SFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKL------TTAQAEQLQPVLLKNIDERGKGTVSRDWV----GRDA 330
Cdd:cd07150 255 FMHQGQICMSASRIIVEEPVYDEFVkKFVARASKLKVgdprdpDTVIGPLISPRQVERIKRQVEDAVAKGAKlltgGKYD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 331 GKI-AAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMAN 409
Cdd:cd07150 335 GNFyQPTVLTDVTPDMRIFREET-----FG------PVTSVIPAKDAEEALELANDTEYGL--SAAILTNDLQRAFKLAE 401
|
410
....*....|....
gi 489128223 410 AIDTSIFVKNGPCI 423
Cdd:cd07150 402 RLESGMVHINDPTI 415
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
34-420 |
6.03e-15 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 76.79 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLK--SVAMRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVE---- 105
Cdd:cd07085 38 EEVDAAVAAAKAAFPAWSatPVLKRQQVMFKFRQLLEENLDELARLITLEHG---------KTLADARGdvLRGLEvvef 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 -CLSPQVLTGDNgltlIENA-----------PWGVVASVTPSTNPAAtvinnaISL------IAAGNSVVFAPHPAAKKV 167
Cdd:cd07085 109 aCSIPHLLKGEY----LENVargidtysyrqPLGVVAGITPFNFPAM------IPLwmfpmaIACGNTFVLKPSERVPGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 168 SQRAITLLNQAVVAAGgpanlLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNKRLIA-AGAGNPPV 242
Cdd:cd07085 179 AMRLAELLQEAGLPDG-----VLNVVHGGKEAVNALLDHPDIKAVSFVGstpvGEYIYERAAAN-GKRVQAlGGAKNHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 243 VVdETADLARAAQSVVkGASFDnniiCADEK-----VLIVVDSVADELMRLMeSQHAVKLTTAQAEQ----LQPVllknI 313
Cdd:cd07085 253 VM-PDADLEQTANALV-GAAFG----AAGQRcmalsVAVAVGDEADEWIPKL-VERAKKLKVGAGDDpgadMGPV----I 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 314 DERGKGTVsRDWVGR--DAGkiAAAI----GLNVPEQTRLLFV------ETSATHPFAVTELMMPVLPVVRVANVDEAIE 381
Cdd:cd07085 322 SPAAKERI-EGLIESgvEEG--AKLVldgrGVKVPGYENGNFVgptildNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIA 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 489128223 382 LAvkleggchhtaamhsrnidNMNRMANAidTSIFVKNG 420
Cdd:cd07085 399 II-------------------NANPYGNG--AAIFTRSG 416
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
125-406 |
7.18e-15 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 76.51 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTVANPDIETAQRLF 204
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEA----GLPAGVVNFVPGSGSEVGDYLV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 205 KYPGIGLLVVTGGEAV----------VDAARKHTnKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKV 274
Cdd:PRK03137 247 DHPKTRFITFTGSREVglriyeraakVQPGQIWL-KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 275 LIVVDSVADELM-RLMESQHAVKL-TTAQAEQLQPVL-------LKNIDERGKGTvSRDWVG--RDAGK---IAAAIGLN 340
Cdd:PRK03137 326 AIVHEDVYDEVLeKVVELTKELTVgNPEDNAYMGPVInqasfdkIMSYIEIGKEE-GRLVLGgeGDDSKgyfIQPTIFAD 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489128223 341 VPEQTRLlfvetsathpfAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNR 406
Cdd:PRK03137 405 VDPKARI-----------MQEEIFGPVVAFIKAKDFDHALEIANNTEYGL--TGAVISNNREHLEK 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
34-413 |
8.64e-15 |
|
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: 76.21 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSV--AMRQLAITALREAGEKHARELAELAVTETG----------MGRVEDKFAKNVAQARGT 101
Cdd:cd07092 19 ADVDAAVAAAHAAFPSWRRTtpAERSKALLKLADAIEENAEELAALESRNTGkplhlvrddeLPGAVDNFRFFAGAARTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 PGVeclspqvLTGD---NGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKkvsqrAITLLNQA 178
Cdd:cd07092 99 EGP-------AAGEylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP-----LTTLLLAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 179 VVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTnKRLIAAGAGNPPVVVDETADLARAA 254
Cdd:cd07092 167 LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGsvrtGKKVARAAADTL-KRVHLELGGKAPVIVFDDADLDAAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 255 QSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAE--QLQPVLLKNIDERGKGTVSrdwvgRDAG 331
Cdd:cd07092 246 AGIATAGYYNAGQDCTAACRVYVHESVYDEFVaALVEAVSAIRVGDPDDEdtEMGPLNSAAQRERVAGFVE-----RAPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 332 KIAAAIGLNVPEQTRLLFVETSATHPF-----AVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNR 406
Cdd:cd07092 321 HARVLTGGRRAEGPGYFYEPTVVAGVAqddeiVQEEIFGPVVTVQPFDDEDEAIELANDVEYGL--ASSVWTRDVGRAMR 398
|
....*..
gi 489128223 407 MANAIDT 413
Cdd:cd07092 399 LSARLDF 405
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
21-403 |
7.51e-14 |
|
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: 73.14 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 21 SQPVSAVQEMGVfASLDDAVAAAKLA-QQG--LKSVAMRQLAItaLREAGEKHARELAELAVTET-------GMGRVEDK 90
Cdd:cd07118 7 GVVVARYAEGTV-EDVDAAVAAARKAfDKGpwPRMSGAERAAV--LLKVADLIRARRERLALIETlesgkpiSQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 91 FAKNV-----AQARGTPGvecLSPQVLtGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAK 165
Cdd:cd07118 84 GAADLwryaaSLARTLHG---DSYNNL-GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKP---SE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 166 KVSQRAItLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPP 241
Cdd:cd07118 157 FTSGTTL-MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGstrvGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 242 VVVDEtADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAEQLQPVLLknIDERGKGT 320
Cdd:cd07118 236 IVFAD-ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVaAVVARSRKVRVGDPLDPETKVGAI--INEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 321 VsRDWV--GRDAGKIAAAIGLNVPEQTRL-----LFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhT 393
Cdd:cd07118 313 I-TDYVdaGRAEGATLLLGGERLASAAGLfyqptIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL--S 389
|
410
....*....|
gi 489128223 394 AAMHSRNIDN 403
Cdd:cd07118 390 AGVWSKDIDT 399
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
19-406 |
9.43e-14 |
|
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: 73.05 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 19 DSSQPVSAVQEMGVfASLDDAVAAAKLAQQGL-KSVAMRQLAItaLREAG---EKHARELAELAVTETG------MGRVE 88
Cdd:cd07097 23 DTSDVVGKYARASA-EDADAAIAAAAAAFPAWrRTSPEARADI--LDKAGdelEARKEELARLLTREEGktlpeaRGEVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 89 ------DKFAknvAQARGTPGVECLSpqvlTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhp 162
Cdd:cd07097 100 ragqifRYYA---GEALRLSGETLPS----TRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 163 aAKKVSQRAITLLNqAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAG 238
Cdd:cd07097 171 -AELTPASAWALVE-ILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGstavGRRIAAAAAARGARVQLEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 239 NPpVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADE-LMRLMESQHAVKLTTAQAEQLQ--PVLLKNIDE 315
Cdd:cd07097 249 NP-LVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRfVEALVERTKALKVGDALDEGVDigPVVSERQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 316 RGKGTVSrdwVGRDAGKIAAAIGLNVPEQTR------LLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGG 389
Cdd:cd07097 328 KDLRYIE---IARSEGAKLVYGGERLKRPDEgyylapALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFG 404
|
410
....*....|....*..
gi 489128223 390 chHTAAMHSRNIDNMNR 406
Cdd:cd07097 405 --LSAGIVTTSLKHATH 419
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
34-402 |
1.05e-13 |
|
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: 73.00 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETGMGRVE---------DKFAKNVAQARGTP 102
Cdd:cd07083 55 AEAEAALEAAWAAFKTwkDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEaiddvaeaiDFIRYYARAALRLR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 103 GVECLSPQVLTGDNGLTLIenaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaa 182
Cdd:cd07083 135 YPAVEVVPYPGEDNESFYV---GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEA---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 183 GGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGG---------EAVVDAARKHTNKRLIAAGAGNPPVVVDETADLARA 253
Cdd:cd07083 208 GFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSletgkkiyeAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQHAvKLTTAQAEQLQPVLLKNIDERGKGTVSRdWV--GRDAG 331
Cdd:cd07083 288 VEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAE-RLSVGPPEENGTDLGPVIDAEQEAKVLS-YIehGKNEG 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489128223 332 KIAAaiGLNVPEQ-----TRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHHTAAMHSRNID 402
Cdd:cd07083 366 QLVL--GGKRLEGegyfvAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKRE 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-415 |
1.39e-13 |
|
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: 72.38 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 26 AVQEMGVFASLDDAVAAAKLAQQGLKSV--AMRQLAITALREAGEKHARELAELAVTETG---------MGRVEDKFAKN 94
Cdd:cd07110 11 GEIPAATAEDVDAAVRAARRAFPRWKKTtgAERAKYLRAIAEGVRERREELAELEARDNGkpldeaawdVDDVAGCFEYY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 95 VAQARG-TPGVECLSPQVLTGDNGLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRait 173
Cdd:cd07110 91 ADLAEQlDAKAERAVPLPSEDFKARVRRE--PVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELE--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 174 lLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKhTNKRLIAAGAGNPPVVVDETAD 249
Cdd:cd07110 166 -LAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGstatGSQVMQAAAQ-DIKPVSLELGGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 250 LARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAE--QLQPVLLKNIDERGKGTVSRdwv 326
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLeRLATAAEAIRVGDPLEEgvRLGPLVSQAQYEKVLSFIAR--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 GRDAGkIAAAIGLNVPEQTR-------LLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSR 399
Cdd:cd07110 321 GKEEG-ARLLCGGRRPAHLEkgyfiapTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL--AAAVISR 397
|
410
....*....|....*.
gi 489128223 400 NIDNMNRMANAIDTSI 415
Cdd:cd07110 398 DAERCDRVAEALEAGI 413
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
36-421 |
2.24e-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: 71.72 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLK--SVAMRQLAITALREAGEKHARELAELAVTETG------MGRVE------DKFAKNVAQArgt 101
Cdd:cd07100 1 IEAALDRAHAAFLAWRktSFAERAALLRKLADLLRERKDELARLITLEMGkpiaeaRAEVEkcawicRYYAENAEAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 pgvecLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAKKVSQRAItLLNQAVVA 181
Cdd:cd07100 78 -----LADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKH---ASNVPGCAL-AIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANLLVTVaNPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSV 257
Cdd:cd07100 149 AGFPEGVFQNL-LIDSDQVEAIIADPRVRGVTLTGseraGRAVAAEAGKNLKKSVLELG-GSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 258 VKGaSFDNN---IICAdeKVLIVVDSVADELM-RLMESQHAVKL--------------TTAQAEQLQPVLLKNIDERGKG 319
Cdd:cd07100 227 VKG-RLQNAgqsCIAA--KRFIVHEDVYDEFLeKFVEAMAALKVgdpmdedtdlgplaRKDLRDELHEQVEEAVAAGATL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 320 TVSRDWVGRDAGKIAAAIGLNVPEQTRlLFVEtsathpfavtELMMPVLPVVRVANVDEAIELAvkleggcHHT-----A 394
Cdd:cd07100 304 LLGGKRPDGPGAFYPPTVLTDVTPGMP-AYDE----------ELFGPVAAVIKVKDEEEAIALA-------NDSpfglgG 365
|
410 420
....*....|....*....|....*...
gi 489128223 395 AMHSRNIDNMNRMANAIDT-SIFVkNGP 421
Cdd:cd07100 366 SVFTTDLERAERVARRLEAgMVFI-NGM 392
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-413 |
3.56e-13 |
|
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: 71.17 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSVAMRQLAiTALREAG---EKHARELAELAVTETGMGRVEDKFAKNVA-----QARGTPgve 105
Cdd:cd07152 13 ADVDRAAARAAAAQRAWAATPPRERA-AVLRRAAdllEEHADEIADWIVRESGSIRPKAGFEVGAAigelhEAAGLP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 cLSPQ--VLTGDNG-LTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkvsQRAIT---LLNQAV 179
Cdd:cd07152 89 -TQPQgeILPSAPGrLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDP------RTPVSggvVIARLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 180 VAAGGPANLLvTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPPVVVDEtADLARAAQ 255
Cdd:cd07152 162 EEAGLPAGVL-HVLPGGADAGEALVEDPNVAMISFTGstavGRKVGEAAGRHLKKVSLELGGKNALIVLDD-ADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 256 SVVKGASFDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLTTAQAEQLQPVLLKNIDERGKGTVSR---DWVgrDAGK 332
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKL-AAKAKHLPVGDPATGQVALGPLINARQLDRVHAivdDSV--AAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 333 IAAAIGlnvpEQTRLLFVETSATH-----PFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRM 407
Cdd:cd07152 317 RLEAGG----TYDGLFYRPTVLSGvkpgmPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGL--SAGIISRDVGRAMAL 390
|
....*.
gi 489128223 408 ANAIDT 413
Cdd:cd07152 391 ADRLRT 396
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-413 |
7.88e-13 |
|
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: 70.02 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQ--GLKSVAMRQLAITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQA---RGT--PGVECLSP 109
Cdd:cd07098 21 DEAIAAARAAQRewAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCekiRWTlkHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 110 QVLTGdNGLTL-----IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFaphpaakKVSQRA-------ITLLNQ 177
Cdd:cd07098 101 ESRPG-GLLMFykrarVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV-------KVSEQVawssgffLSIIRE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 178 AVVAAGGPANlLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARA 253
Cdd:cd07098 173 CLAACGHDPD-LVQLVTCLPETAEALTSHPVIDHITFIGsppvGKKVMAAAAESLTPVVLELG-GKDPAIVLDDADLDQI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGAsFDN---NiiCADEKVLIVVDSVADELMRLMEsqhavklTTAQAEQLQPVLLKNID----------ERGKGT 320
Cdd:cd07098 251 ASIIMRGT-FQSsgqN--CIGIERVIVHEKIYDKLLEILT-------DRVQALRQGPPLDGDVDvgamisparfDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 321 VsRDWVGRDAGKIAAAIGLNVPEQ------TRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTA 394
Cdd:cd07098 321 V-ADAVEKGARLLAGGKRYPHPEYpqghyfPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL--GA 397
|
410
....*....|....*....
gi 489128223 395 AMHSRNIDNMNRMANAIDT 413
Cdd:cd07098 398 SVFGKDIKRARRIASQLET 416
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
34-415 |
8.44e-13 |
|
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: 69.89 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSVAMRQLAITA----LREAG---EKHARELAELAVTETG---------MGRVEDKFAKNVAQ 97
Cdd:cd07114 16 ASAADVDRAVAAARAAFEGGAWRKLTPTErgklLRRLAdliEANAEELAELETRDNGkliretraqVRYLAEWYRYYAGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 98 ARGTPGveclspQVLTGDNG--LTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKkvsqrAITL- 174
Cdd:cd07114 96 ADKIEG------AVIPVDKGdyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP-----ASTLe 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 175 LNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAGA---GNPPVVVDETADLA 251
Cdd:cd07114 165 LAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLelgGKSPNIVFDDADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 252 RAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAE--QLQPVLLKNIDERGKGTVSRdwvGR 328
Cdd:cd07114 245 AAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVeRLVARARAIRVGDPLDPetQMGPLATERQLEKVERYVAR---AR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 329 DAGKIAAAIG--LNVPEQTRLLFVE------TSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRN 400
Cdd:cd07114 322 EEGARVLTGGerPSGADLGAGYFFEptiladVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL--AAGIWTRD 399
|
410
....*....|....*
gi 489128223 401 IDNMNRMANAIDTSI 415
Cdd:cd07114 400 LARAHRVARAIEAGT 414
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
37-411 |
1.92e-12 |
|
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: 68.91 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQGLKSVA------MRQLAITALREAGEKHARELAELAVTETGMGRVEDKFAKNVAQ---------ARGT 101
Cdd:cd07120 19 AEAEAAIAAARRAFDETDwahdprLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAIselryyaglARTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 PG-VECLSPQVLTgdngltLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVV 180
Cdd:cd07120 99 AGrMIEPEPGSFS------LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 181 AAGGPANLlvtVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTnKRLIAAGAGNPPVVVDETADLARAAQS 256
Cdd:cd07120 173 LPAGVVNL---FTESGSEGAAHLVASPDVDVISFTGstatGRAIMAAAAPTL-KRLGLELGGKTPCIVFDDADLDAALPK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 257 VVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTA--QAEQLQPVLLKNIDERGKGTVSRdwvGRDAGKI 333
Cdd:cd07120 249 LERALTIFAGQFCMAGSRVLVQRSIADEVRdRLAARLAAVKVGPGldPASDMGPLIDRANVDRVDRMVER---AIAAGAE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 334 AAAIGLNVPEQT------RLLFVETSATHPFAV-TELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNR 406
Cdd:cd07120 326 VVLRGGPVTEGLakgaflRPTLLEVDDPDADIVqEEIFGPVLTLETFDDEAEAVALANDTDYGL--AASVWTRDLARAMR 403
|
....*
gi 489128223 407 MANAI 411
Cdd:cd07120 404 VARAI 408
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
37-383 |
3.09e-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: 68.07 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARgtpgvE 105
Cdd:cd07095 3 DAAVAAARAAFPGwaALSLEERAAILRRFAELLKANKEELARLISRETGkplweaqteVAAMAGKIDISIKAYH-----E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 CLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAAtVINNAI--SLIAaGNSVVFAPHPAAKKVSQRAITLLNQAVVAAG 183
Cdd:cd07095 78 RTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGH-LPNGHIvpALLA-GNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 184 gpanlLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARK----HTNKRLIAAGAGNPPVVVDETADLARAAQSVVK 259
Cdd:cd07095 156 -----VLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRqfagRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 260 GASFDNNIICADEKVLIVVDS-VADELM-RLMESQHAVK--------------LTTAQAEQLqpVLLKNIDERGKGTVSR 323
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGaVGDAFLeRLVEAAKRLRigapdaeppfmgplIIAAAAARY--LLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 324 DWVGRDAGKiaaaiGLNVPEqtrLLFVETSATHPFAvtELMMPVLPVVRVANVDEAIELA 383
Cdd:cd07095 309 AMERLVAGT-----AFLSPG---IIDVTDAADVPDE--EIFGPLLQVYRYDDFDEAIALA 358
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
34-413 |
3.45e-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: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSVAMRQLAiTALREAGEK---HARELAELAVTETG------MG------RVEDKFAKNVAQA 98
Cdd:cd07107 19 ADVDRAVAAARAAFPEWRATTPLERA-RMLRELATRlreHAEELALIDALDCGnpvsamLGdvmvaaALLDYFAGLVTEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 99 RGTpgveclspQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhPAakkvsQRAITLLNQA 178
Cdd:cd07107 98 KGE--------TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP-PE-----QAPLSALRLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 179 VVAAGG-PANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPPVVVDEtADLARA 253
Cdd:cd07107 164 ELAREVlPPGVFNILPGDGATAGAALVRHPDVKRIALIGsvptGRAIMRAAAEGIKHVTLELGGKNALIVFPD-ADPEAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFD-NNIICADEKVLIVVDSVADELMRLMESQ---HAVKLTTAQAEQLQPVllknIDERgkgtvSRDWVGR- 328
Cdd:cd07107 243 ADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERvaaIKVGDPTDPATTMGPL----VSRQ-----QYDRVMHy 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 329 -DAGKIAAA---IGLNVPEQTRL---------LFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAA 395
Cdd:cd07107 314 iDSAKREGArlvTGGGRPEGPALeggfyveptVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGL--TAA 391
|
410
....*....|....*...
gi 489128223 396 MHSRNIDNMNRMANAIDT 413
Cdd:cd07107 392 IWTNDISQAHRTARRVEA 409
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
37-412 |
3.73e-12 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 67.98 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETGMGRVEDK-------------FAKNVAQARGT 101
Cdd:cd07093 22 DAAVAAAKEAFPGWsrMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtrdipraaanfrfFADYILQLDGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 pgveclspQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkVSQRAITLLNQAVVA 181
Cdd:cd07093 102 --------SYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE----WTPLTAWLLAELANE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNKRLIAAGAGNPPVVVDETADLARAAQSV 257
Cdd:cd07093 170 AGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGetatGRTIMRAAAPN-LKPVSLELGGKNPNIVFADADLDRAVDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 258 VkGASFDNN-IICADEKVLIVVDSVADE-LMRLME--SQHAVKLTTAQAEQLQPVLLKNIDERGKGTVSRdwvGRDAG-K 332
Cdd:cd07093 249 V-RSSFSNNgEVCLAGSRILVQRSIYDEfLERFVEraKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL---ARAEGaT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 333 IAAaiGLNVPEQTRL---------LFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDN 403
Cdd:cd07093 325 ILT--GGGRPELPDLeggyfveptVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGL--AAYVWTRDLGR 400
|
....*....
gi 489128223 404 MNRMANAID 412
Cdd:cd07093 401 AHRVARRLE 409
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
34-413 |
3.93e-12 |
|
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: 68.10 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQ--GLKSVAMRQLAITALREAGEKHARELAELAVTETGMGR------VEDkfAKNVAQARGTPGVE 105
Cdd:cd07101 18 ADVEAAFARARAAQRawAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARrhafeeVLD--VAIVARYYARRAER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 106 CLSPQ-------VLTGdnglTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVfaphpaAKKVSQRAITLL--N 176
Cdd:cd07101 96 LLKPRrrrgaipVLTR----TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV------LKPDSQTALTALwaV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 177 QAVVAAGGPANLLVTVANPDIETAQRLFKypGIGLLVVTGGEAVVDAARKHTNKRLIAAGA---GNPPVVVDETADLARA 253
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLelgGKNPMIVLEDADLDKA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDNNIICADEKVLIVVDSVADE-LMRLMESQHAVKLTTA-----------QAEQLQPVLLKNIDERGKG-T 320
Cdd:cd07101 244 AAGAVRACFSNAGQLCVSIERIYVHESVYDEfVRRFVARTRALRLGAAldygpdmgsliSQAQLDRVTAHVDDAVAKGaT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 321 VsrdwvgRDAGKIAAAIGLNVPEQTRLLFVETSAThpFAVTELMMPVLPVVRVANVDEAIELAVKLEGGCHhtAAMHSRN 400
Cdd:cd07101 324 V------LAGGRARPDLGPYFYEPTVLTGVTEDME--LFAEETFGPVVSIYRVADDDEAIELANDTDYGLN--ASVWTRD 393
|
410
....*....|...
gi 489128223 401 IDNMNRMANAIDT 413
Cdd:cd07101 394 GARGRRIAARLRA 406
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
34-430 |
3.96e-12 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 67.77 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSVAMRQLA--ITALREAGEKHARELAELAVTETG-----MGRVEDKFAKNVAQARGTPGVEC 106
Cdd:cd07108 19 ADVDRAVAAAKAAFPEWAATPARERGklLARIADALEARSEELARLLALETGnalrtQARPEAAVLADLFRYFGGLAGEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 107 LSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFaphpaakKVSQRA--ITLLNQAVVAAGG 184
Cdd:cd07108 99 KGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL-------KAAEDAplAVLLLAEILAQVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 185 PANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAG---AGNPPVVVDETADLARAAQSVVKGA 261
Cdd:cd07108 172 PAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSlelGGKSPMIVFPDADLDDAVDGAIAGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 262 SFD-NNIICADEKVLIVVDSVADE-LMRLMESQHAVKLTTAQAEQLQPVLLknIDERGKGTVSrDWV--GRDAGKIAAAI 337
Cdd:cd07108 252 RFTrQGQSCTAGSRLFVHEDIYDAfLEKLVAKLSKLKIGDPLDEATDIGAI--ISEKQFAKVC-GYIdlGLSTSGATVLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 338 GLNVPEQTRL---------LFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMA 408
Cdd:cd07108 329 GGPLPGEGPLadgffvqptIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL--AAYVWTRDLGRALRAA 406
|
410 420
....*....|....*....|....*
gi 489128223 409 NAIDTSiFV---KNGPCIAGLGLGG 430
Cdd:cd07108 407 HALEAG-WVqvnQGGGQQPGQSYGG 430
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-411 |
7.41e-12 |
|
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: 67.08 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 30 MGVFASLDDAVAAAKLAQQGLKSV--AMRQLAITALREAGEKHARELAELAVTETGMgRVEDKFAKNVAQARGT-----P 102
Cdd:cd07115 15 QASAEDVDAAVAAARAAFEAWSAMdpAERGRILWRLAELILANADELARLESLDTGK-PIRAARRLDVPRAADTfryyaG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 103 GVECLSPQVLTGDNG-LTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvva 181
Cdd:cd07115 94 WADKIEGEVIPVRGPfLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 aGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV---VDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQSVV 258
Cdd:cd07115 171 -GFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVgrkIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 259 KGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKL------TTA-----QAEQLQPVLlkNIDERGKGTVSRDWV 326
Cdd:cd07115 250 TGIFYNQGQMCTAGSRLLVHESIYDEFLeRFTSLARSLRPgdpldpKTQmgplvSQAQFDRVL--DYVDVGREEGARLLT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 GrdaGKIAAAIGLNVPEQtrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNR 406
Cdd:cd07115 328 G---GKRPGARGFFVEPT---IFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGL--AAGVWTRDLGRAHR 399
|
....*
gi 489128223 407 MANAI 411
Cdd:cd07115 400 VAAAL 404
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
33-304 |
8.08e-12 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 66.81 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 33 FASLDDAVAAAKLAQQGLK-----SVAMRQLAITALREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGT------ 101
Cdd:PRK13968 25 WAGADDIENALQLAAAGFRdwretNIDYRAQKLRDIGKALRARSEEMAQMITREMG---------KPINQARAEvaksan 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 -------PGVECLSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitL 174
Cdd:PRK13968 96 lcdwyaeHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ----L 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 175 LNQAVVAAGGPANLLVTVaNPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPPVVVDEtADL 250
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWL-NADNDGVSQMINDSRIAAVTVTGsvraGAAIGAQAGAALKKCVLELGGSDPFIVLND-ADL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489128223 251 ARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAEQ 304
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTeRFVAAAAALKMGDPRDEE 304
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-431 |
1.16e-11 |
|
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: 66.43 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 22 QPVSAVQEMGVfASLDDAVAAAKLAQQGLKSV-------AMRQLAitalrEAGEKHARELAELAVTETGmgrvedkfaKN 94
Cdd:cd07086 24 EPIARVFPASP-EDVEAAVAAAREAFKEWRKVpaprrgeIVRQIG-----EALRKKKEALGRLVSLEMG---------KI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 95 VAQARG--TPGVEC------LSPQVltgdNGLT---------LIENA-PWGVVASVTPSTNPAAtVI--NNAISLIaAGN 154
Cdd:cd07086 89 LPEGLGevQEMIDIcdyavgLSRML----YGLTipserpghrLMEQWnPLGVVGVITAFNFPVA-VPgwNAAIALV-CGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 155 SVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANlLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHtNK 230
Cdd:cd07086 163 TVVWKPSETTPLTAIAVTKILAEVLEKNGLPPG-VVNLVTGGGDGGELLVHDPRVPLVSFTGstevGRRVGETVARR-FG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 231 RLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKL------------ 297
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLeRLVKAYKQVRIgdpldegtlvgp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 298 --TTAQAEQLQPVLLKNIDERGKGTVSRDWVGRDAGK--IAAAIGLNVPEQTRLLFVETsathpFAvtelmmPVLPVVRV 373
Cdd:cd07086 321 liNQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGnyVEPTIVTGVTDDARIVQEET-----FA------PILYVIKF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489128223 374 ANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRM--ANAIDTSIFVKNGPCI---AGLGLGGE 431
Cdd:cd07086 390 DSLEEAIAINNDVPQGL--SSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgaeIGGAFGGE 450
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
125-381 |
2.89e-11 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 65.44 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAggpanlLVTVANPDIETAQRLF 204
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS------YVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 205 KYPgIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDS 280
Cdd:PTZ00381 183 KEP-FDHIFFTGsprvGKLVMQAAAENLTPCTLELG-GKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 281 VADELmrLMESQHAVK----------------LTTAQAEQLQPVLlknidERGKGTVsrdWVGRDAGK----IAAAIGLN 340
Cdd:PTZ00381 261 IKDKF--IEALKEAIKeffgedpkksedysriVNEFHTKRLAELI-----KDHGGKV---VYGGEVDIenkyVAPTIIVN 330
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489128223 341 VpeqtrllfvetSATHPFAVTELMMPVLPVVRVANVDEAIE 381
Cdd:PTZ00381 331 P-----------DLDSPLMQEEIFGPILPILTYENIDEVLE 360
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
33-412 |
3.00e-11 |
|
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: 65.31 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 33 FASLDDAVAAAKLAQQGLKsvAMRQLAI----TALREAGEKHAR---ELAELAVTETGM----GRVEDKFAKNVAQ---- 97
Cdd:cd07149 17 VASEEDVEKAIAAAKEGAK--EMKSLPAyeraEILERAAQLLEErreEFARTIALEAGKpikdARKEVDRAIETLRlsae 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 98 -AR----------GTPGVEclspqvltGDNGLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKK 166
Cdd:cd07149 95 eAKrlagetipfdASPGGE--------GRIGFTIRE--PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 167 VSQraitLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDA-ARKHTNKRLIAAGAGNPPVVVD 245
Cdd:cd07149 165 SAL----KLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAiARKAGLKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 246 ETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQ-HAVKLTTAQAEQ--LQPVllknIDERGKGTVS 322
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAAtKKLVVGDPLDEDtdVGPM----ISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 323 RdWV--------------GRDAGKIAAAIGLNVPEQTRLlfvetsathpfAVTELMMPVLPVVRVANVDEAIELAVKLEG 388
Cdd:cd07149 317 E-WVeeaveggarlltggKRDGAILEPTVLTDVPPDMKV-----------VCEEVFAPVVSLNPFDTLDEAIAMANDSPY 384
|
410 420
....*....|....*....|....
gi 489128223 389 GCHhtAAMHSRNIDNMNRMANAID 412
Cdd:cd07149 385 GLQ--AGVFTNDLQKALKAARELE 406
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
34-411 |
1.01e-10 |
|
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: 63.75 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETGM----GRVE-----DkFAKNVA-QARGT 101
Cdd:cd07125 69 EDVDAALAIAAAAFAGwsATPVEERAEILEKAADLLEANRGELIALAAAEAGKtladADAEvreaiD-FCRYYAaQAREL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 PGVECLsPQVLTGDNGLTLienAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQavva 181
Cdd:cd07125 148 FSDPEL-PGPTGELNGLEL---HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHE---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAV------VDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQ 255
Cdd:cd07125 220 AGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETaklinrALAERDGPILPLIAETGGKNAMIVDSTALPEQAVK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 256 SVVKGAsFDNniicADEK-----VLIVVDSVADELMRL----MESQH---AVKLTTaqaeQLQPV-------LLKNIDER 316
Cdd:cd07125 300 DVVQSA-FGS----AGQRcsalrLLYLQEEIAERFIEMlkgaMASLKvgdPWDLST----DVGPLidkpagkLLRAHTEL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 317 GKGtvsrdwvgrdAGKIAAAIGLNVPEQT----RLLFVETSATHPfavTELMMPVLPVVR--VANVDEAIELAVKLEGGC 390
Cdd:cd07125 371 MRG----------EAWLIAPAPLDDGNGYfvapGIIEIVGIFDLT---TEVFGPILHVIRfkAEDLDEAIEDINATGYGL 437
|
410 420
....*....|....*....|.
gi 489128223 391 hhTAAMHSRNIDNMNRMANAI 411
Cdd:cd07125 438 --TLGIHSRDEREIEYWRERV 456
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
36-413 |
1.97e-10 |
|
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: 62.45 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQGLKSVAMRQLAiTALREAGE---KHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVECLS-- 108
Cdd:cd07103 21 ADAAIDAAAAAFKTWRKTTARERA-AILRRWADlirERAEDLARLLTLEQG---------KPLAEARGevDYAASFLEwf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 109 ------------PQVLTGDNGLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAkkvsqrAIt 173
Cdd:cd07103 91 aeearriygrtiPSPAPGKRILVIKQ--PVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAeetPLS------AL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 174 LLNQAVVAAGGPA---NLLVTVANpdiETAQRLFKYPGIGLLVVTGGEAVvdaarkhtNKRLIAAGA-----------GN 239
Cdd:cd07103 162 ALAELAEEAGLPAgvlNVVTGSPA---EIGEALCASPRVRKISFTGSTAV--------GKLLMAQAAdtvkrvslelgGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 240 PPVVVDETADLARAAQSVVkGASFDNN---IICADEkvLIVVDSVADELMRLMesqhavkltTAQAEQLQ---------- 306
Cdd:cd07103 231 APFIVFDDADLDKAVDGAI-ASKFRNAgqtCVCANR--IYVHESIYDEFVEKL---------VERVKKLKvgngldegtd 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 307 --PVllknIDERGKGTVSR---DWVGRDA-----GKIAAAIGL--------NVPEQTRLLFVETsathpFAvtelmmPVL 368
Cdd:cd07103 299 mgPL----INERAVEKVEAlveDAVAKGAkvltgGKRLGLGGYfyeptvltDVTDDMLIMNEET-----FG------PVA 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489128223 369 PVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAIDT 413
Cdd:cd07103 364 PIIPFDTEDEVIARANDTPYGL--AAYVFTRDLARAWRVAEALEA 406
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
125-381 |
2.21e-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: 62.16 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAKKVSQRaitLLNQAVVAAggpanlLVTVANPDIETAQ 201
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSelaPATSALLAK---LIPKYFDPE------AVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 202 RLFKYPgIGLLVVTGGEAVvdaarkhtnKRLIAAGA------------GNPPVVVDETADLARAAQSVVKGASFDNNIIC 269
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAV---------GKIVMEAAakhltpvtlelgGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 270 ADEKVLIVVDSVADELMRLMesQHAVK----------------LTTAQAEQLQPvLLKNIDERGKGTVSRDwvGRdagKI 333
Cdd:cd07087 241 IAPDYVLVHESIKDELIEEL--KKAIKefygedpkespdygriINERHFDRLAS-LLDDGKVVIGGQVDKE--ER---YI 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489128223 334 AAAIGLNVPEQtrllfvetsatHPFAVTELMMPVLPVVRVANVDEAIE 381
Cdd:cd07087 313 APTILDDVSPD-----------SPLMQEEIFGPILPILTYDDLDEAIE 349
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
20-432 |
2.71e-10 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 62.23 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 20 SSQPVSAVQEMGVfASLDDAVAAAKLAQQGLKSVAMRQLAiTALREAGE---KHARELAELAVTETGMGRVEDK------ 90
Cdd:PRK11241 35 NGDKLGSVPKMGA-DETRAAIDAANRALPAWRALTAKERA-NILRRWFNlmmEHQDDLARLMTLEQGKPLAEAKgeisya 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 91 ------FAKNVAQARG--TPGVEclspqvltGDNGLTLIENaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhp 162
Cdd:PRK11241 113 asfiewFAEEGKRIYGdtIPGHQ--------ADKRLIVIKQ-PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 163 aakkVSQRAITLLNQAVVA--AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAG 236
Cdd:PRK11241 182 ----ASQTPFSALALAELAirAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 237 aGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMEsQHAVKLTTAQAEQLQPVLLKNIDER 316
Cdd:PRK11241 258 -GNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQ-QAVSKLHIGDGLEKGVTIGPLIDEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 317 GKGTVSR---DWVGRDA----GKIAAAIGLNVPEQTrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGG 389
Cdd:PRK11241 336 AVAKVEEhiaDALEKGArvvcGGKAHELGGNFFQPT--ILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489128223 390 ChhTAAMHSRNIDNMNRMANAIDTSIFVKNGPCIA----------GLGLGGEG 432
Cdd:PRK11241 414 L--AAYFYARDLSRVFRVGEALEYGIVGINTGIISnevapfggikASGLGREG 464
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
125-411 |
3.32e-10 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 61.68 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaaKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIETAQRLF 204
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKP----SEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 205 KYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDS 280
Cdd:PRK10090 147 GNPKVAMVSMTGsvsaGEKIMAAAAKNITKVCLELG-GKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 281 VADELM-RLMESQHAVKL-TTAQAEQLQ--PVL----LKNIDERGKGTVSRDWVGRDAGKIAAAIGLNVPEQtrlLFVET 352
Cdd:PRK10090 226 IYDQFVnRLGEAMQAVQFgNPAERNDIAmgPLInaaaLERVEQKVARAVEEGARVALGGKAVEGKGYYYPPT---LLLDV 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489128223 353 SATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAI 411
Cdd:PRK10090 303 RQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGL--TSSIYTQNLNVAMKAIKGL 359
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
125-381 |
4.24e-10 |
|
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: 61.47 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVV-----FAPHPAAkkvsqraitlLNQAVVAAGGPANLlVTVANPDIET 199
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAIlkpseLTPHTSA----------VIAKIIREAFDEDE-VAVFEGDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 200 AQRLFKYPgIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVL 275
Cdd:cd07134 169 AQALLELP-FDHIFFTGspavGKIVMAAAAKHLASVTLELG-GKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 276 IVVDSVADELMRLMESQHAVKLTTAQAEQLQPVLLKNIDERGKGTVSR---DWVGRDA-----GK-------IAAAIGLN 340
Cdd:cd07134 247 FVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGlldDAVAKGAkvefgGQfdaaqryIAPTVLTN 326
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489128223 341 VPEQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEAIE 381
Cdd:cd07134 327 VTPDMKIM-----------QEEIFGPVLPIITYEDLDEVIE 356
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
37-430 |
4.72e-10 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 61.67 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 37 DDAVAAAKLAQQGLKSV-------AMRQLAITALREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARG 100
Cdd:PLN02467 48 DAAVEAARKAFKRNKGKdwarttgAVRAKYLRAIAAKITERKSELAKLETLDCGkpldeaawdMDDVAGCFEYYADLAEA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 101 TPGVEClSPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAkkvsqrAITLLNQAVV 180
Cdd:PLN02467 128 LDAKQK-APVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELA------SVTCLELADI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 181 A--AGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAvvdaarkhTNKRLIAAGA-----------GNPPVVVDET 247
Cdd:PLN02467 201 CreVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTA--------TGRKIMTAAAqmvkpvslelgGKSPIIVFDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 248 ADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADE-LMRLMESQHAVKLTTAQAE--QLQPVLLKNIDERGKGTVSrd 324
Cdd:PLN02467 273 VDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEfLEKLVKWAKNIKISDPLEEgcRLGPVVSEGQYEKVLKFIS-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 325 wVGRDAGKIAAAIGLNVPEQTRLLFVEtsATHPFAVT--------ELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAM 396
Cdd:PLN02467 351 -TAKSEGATILCGGKRPEHLKKGFFIE--PTIITDVTtsmqiwreEVFGPVLCVKTFSTEDEAIELANDSHYGL--AGAV 425
|
410 420 430
....*....|....*....|....*....|....*.
gi 489128223 397 HSRNIDNMNRMANAIDTSIFVKN--GPCIAGLGLGG 430
Cdd:PLN02467 426 ISNDLERCERVSEAFQAGIVWINcsQPCFCQAPWGG 461
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
34-383 |
9.94e-10 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 60.31 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSV--AMRQLAITALREAGEKHARELAELAVTETGMGR---VEDKFAKNVAQARGTPG-VECL 107
Cdd:PRK13473 39 AQVDAAVAAADAAFPEWSQTtpKERAEALLKLADAIEENADEFARLESLNCGKPLhlaLNDEIPAIVDVFRFFAGaARCL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 108 SPQVlTGD--NGLT-LIENAPWGVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPHPaakkvsQRAITLLNQAVVA 181
Cdd:PRK13473 119 EGKA-AGEylEGHTsMIRRDPVGVVASIAPWNYPlmmAAWKLAPAL---AAGNTVVLKPSE------ITPLTALKLAELA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGG-PANLLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTnKRLIAAGAGNPPVVVDETADLARAAQS 256
Cdd:PRK13473 189 ADIlPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGsiatGKHVLSAAADSV-KRTHLELGGKAPVIVFDDADLDAVVEG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 257 VVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKLTTAQAEQ--LQPVLLKNIDERGKGTVSRdwvGRDAGKI 333
Cdd:PRK13473 268 IRTFGYYNAGQDCTAACRIYAQRGIYDDLVaKLAAAVATLKVGDPDDEDteLGPLISAAHRDRVAGFVER---AKALGHI 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489128223 334 AAAIGLNVPEQTRLLF---VETSATHPFAVT--ELMMPVLPVVRVANVDEAIELA 383
Cdd:PRK13473 345 RVVTGGEAPDGKGYYYeptLLAGARQDDEIVqrEVFGPVVSVTPFDDEDQAVRWA 399
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
125-408 |
3.45e-09 |
|
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: 58.79 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAaggPANLlVTVANPDIETAQRLF 204
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLL---PPED-VTLINGDGKTMQALL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 205 KYPGIGLLVVTGGEAVVDAARKHTNK-RLIAAGAGNPPVVVDETAD-LARAAQSVVKGASFDNNIICADEKVLIVVDS-- 280
Cdd:cd07084 176 LHPNPKMVLFTGSSRVAEKLALDAKQaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENws 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 281 ---VADELMRLMESQhAVKLTTAQAEQlQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIGLNVPEQTRLLFV---ETSA 354
Cdd:cd07084 256 ktpLVEKLKALLARR-KLEDLLLGPVQ-TFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGACVASALFVpidEILK 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489128223 355 THPFAVTELMMPVLPVVRVANVDEA--IELAVKLEGgcHHTAAMHSRNIDNMNRMA 408
Cdd:cd07084 334 TYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHG--SLTAAIYSNDPIFLQELI 387
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
113-411 |
7.69e-09 |
|
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: 57.54 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 113 TGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTV 192
Cdd:cd07143 132 TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 193 ANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNII 268
Cdd:cd07143 208 SGYGRTCGNAISSHMDIDKVAFTGstlvGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 269 CADEKVLIVVDSVADE-LMRLMESQHAVKL---------TTAQAEQLQPVLLKNIDERGKGTVSRDWVGrdaGKIAAAIG 338
Cdd:cd07143 288 CCAGSRIYVQEGIYDKfVKRFKEKAKKLKVgdpfaedtfQGPQVSQIQYERIMSYIESGKAEGATVETG---GKRHGNEG 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489128223 339 LNVpEQTrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAI 411
Cdd:cd07143 365 YFI-EPT--IFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGL--AAAVFTNNINNAIRVANAL 432
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-412 |
1.14e-08 |
|
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: 57.26 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLK--SVAMRQLAITALREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARGTP 102
Cdd:cd07147 21 DDIEEAIAAAVKAFRPMRalPAHRRAAILLHCVARLEERFEELAETIVLEAGkpikdargeVARAIDTFRIAAEEATRIY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 103 GvECL----SPQvltGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaakkVSQRAIT--LLN 176
Cdd:cd07147 101 G-EVLpldiSAR---GEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP------ASRTPLSalILG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 177 QAVVAAGGPANLL--VTVANPDietAQRLFKYPGIGLLVVTGGEAVVDAARKHT-NKRLIAAGAGNPPVVVDETADLARA 253
Cdd:cd07147 171 EVLAETGLPKGAFsvLPCSRDD---ADLLVTDERIKLLSFTGSPAVGWDLKARAgKKKVVLELGGNAAVIVDSDADLDFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMeSQHAVKLTT----AQAEQLQPVllknIDERGKGTVSrDWV--- 326
Cdd:cd07147 248 AQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRL-VARVKALKTgdpkDDATDVGPM----ISESEAERVE-GWVnea 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 327 -----------GRDAGKIAAAIGLNVPEQTRLlfvetSATHPFAvtelmmPVLPVVRVANVDEAIELAVKLEGGCHhtAA 395
Cdd:cd07147 322 vdagaklltggKRDGALLEPTILEDVPPDMEV-----NCEEVFG------PVVTVEPYDDFDEALAAVNDSKFGLQ--AG 388
|
410
....*....|....*..
gi 489128223 396 MHSRNIDNMNRMANAID 412
Cdd:cd07147 389 VFTRDLEKALRAWDELE 405
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
121-383 |
4.53e-08 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 55.30 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPAnlLVTVANPDIETA 200
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAA----LLAELVPKYLDPD--AFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 201 QRLFKYpGIGLLVVTGGEAVvdaarkhtnKRLIAAGA------------GNPPVVVDETADLARAAQSVVKGASFDNNII 268
Cdd:cd07135 178 TALLEQ-KFDKIFYTGSGRV---------GRIIAEAAakhltpvtlelgGKSPVIVTKNADLELAAKRILWGKFGNAGQI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 269 CADEKVLIVVDSVADELMRLMESQ----------------HAVklTTAQAEQLQPVLlknidERGKGTVSrdwVG--RDA 330
Cdd:cd07135 248 CVAPDYVLVDPSVYDEFVEELKKVldefypgganaspdytRIV--NPRHFNRLKSLL-----DTTKGKVV---IGgeMDE 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489128223 331 GK--IAAAIGLNVpeqtrllfvetSATHPFAVTELMMPVLPVVRVANVDEAIELA 383
Cdd:cd07135 318 ATrfIPPTIVSDV-----------SWDDSLMSEELFGPVLPIIKVDDLDEAIKVI 361
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
118-413 |
2.77e-07 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 52.84 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 118 LTLIENAPWGVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPHpaakkvSQRAITLLNQA-VVAAGGPANLLVTVA 193
Cdd:cd07117 129 LSIVLREPIGVVGQIIPWNFPflmAAWKLAPAL---AAGNTVVIKPS------STTSLSLLELAkIIQDVLPKGVVNIVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 194 NPDIETAQRLFKYPGIGLLVVTGGEAVVDAARKHTNKRLIAAG---AGNPPVVVDETADLARAAQSVVKGASFDNNIICA 270
Cdd:cd07117 200 GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATlelGGKSANIIFDDANWDKALEGAQLGILFNQGQVCC 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 271 DEKVLIVVDSVADELM-RLMESQHAVKL------TTAQAEQLQPVLLKNID---ERGKGTVSRDWVGRDAGKIAAAIGLN 340
Cdd:cd07117 280 AGSRIFVQEGIYDEFVaKLKEKFENVKVgnpldpDTQMGAQVNKDQLDKILsyvDIAKEEGAKILTGGHRLTENGLDKGF 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489128223 341 VPEQTrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAIDT 413
Cdd:cd07117 360 FIEPT--LIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGL--GGGVFTKDINRALRVARAVET 428
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
25-400 |
4.37e-07 |
|
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: 52.22 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 25 SAVQEMGVFASLDDAVAAAKL-AQQGLKSVAMRQLAITALREAGEKHARELAEL--AV--TETGMGRVEDKFAKNVAQAR 99
Cdd:TIGR01238 82 SAQQAFPTWNATPAKERAAKLdRLADLLELHMPELMALCVREAGKTIHNAIAEVreAVdfCRYYAKQVRDVLGEFSVESR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 100 GTpgVECLSPqvltgdngltlienapWGVvasvtpstnPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAV 179
Cdd:TIGR01238 162 GV--FVCISP----------------WNF---------PLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 180 VAAGgpANLLVTVANPDIETAqrLFKYPGIGLLVVTGGEAVVDAARKHTNKR------LIAAGAGNPPVVVDETADLARA 253
Cdd:TIGR01238 215 FPAG--TIQLLPGRGADVGAA--LTSDPRIAGVAFTGSTEVAQLINQTLAQRedapvpLIAETGGQNAMIVDSTALPEQV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 254 AQSVVKGASFDNNIICADEKVLIVVDSVADELMRLMESQHAvKLTTAQAEQLQPVLLKNIDERGKGTVSR--DWVGRDAG 331
Cdd:TIGR01238 291 VRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQ-ELKVGVPHLLTTDVGPVIDAEAKQNLLAhiEHMSQTQK 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489128223 332 KIAAAIGLNVPEQTRLLFVETSATHPFAVTELMM----PVLPVVRVaNVDEAIELAVKL-EGGCHHTAAMHSRN 400
Cdd:TIGR01238 370 KIAQLTLDDSRACQHGTFVAPTLFELDDIAELSEevfgPVLHVVRY-KARELDQIVDQInQTGYGLTMGVHSRI 442
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
34-383 |
7.71e-07 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 51.50 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQG--LKSVAMRQLAITALREAGEKHARELAELAVTETGMGRVEDkfAKNVAQARGTPGVECLSPQV 111
Cdd:PRK09457 37 AQVDAAVRAARAAFPAwaRLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA--ATEVTAMINKIAISIQAYHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 112 LTGD------NGLTLIENAPWGVVASVTPSTNPAAtVINNAI--SLIAaGNSVVFAPHPAAKKVSQRAITLLNQAVVAAg 183
Cdd:PRK09457 115 RTGEkrsemaDGAAVLRHRPHGVVAVFGPYNFPGH-LPNGHIvpALLA-GNTVVFKPSELTPWVAELTVKLWQQAGLPA- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 184 GPANLLVTvanpDIETAQRLFKYPGIGLLVVTGGEAVVDAARK----HTNKRLIAAGAGNPPVVVDETADLARAAQSVVK 259
Cdd:PRK09457 192 GVLNLVQG----GRETGKALAAHPDIDGLLFTGSANTGYLLHRqfagQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 260 GASFDNNIICADEKVLIVVDSV-ADELM-RLMESQHAVKLTTAQAEQlQPVLLKNIDER-GKGTVS--RDWVGRDAGKIA 334
Cdd:PRK09457 268 SAFISAGQRCTCARRLLVPQGAqGDAFLaRLVAVAKRLTVGRWDAEP-QPFMGAVISEQaAQGLVAaqAQLLALGGKSLL 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489128223 335 AAIGLNvpEQTRLL---FVETSATHPFAVTELMMPVLPVVRVANVDEAIELA 383
Cdd:PRK09457 347 EMTQLQ--AGTGLLtpgIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLA 396
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
125-415 |
1.05e-06 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 50.84 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHpaakkvSQRAITLLNQAVVA--AGGPANLL--VTVANPDIETA 200
Cdd:PLN02278 160 PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPS------ELTPLTALAAAELAlqAGIPPGVLnvVMGDAPEIGDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 201 qrLFKYPGIGLLVVTGGEAV-----VDAARkhTNKRLIAAGAGNPPVVVDETADLARAAQSVVkGASFDN---NIICADE 272
Cdd:PLN02278 234 --LLASPKVRKITFTGSTAVgkklmAGAAA--TVKRVSLELGGNAPFIVFDDADLDVAVKGAL-ASKFRNsgqTCVCANR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 273 kvLIVVDSVADEL-------MRLMESQHAVKLTTAQAEQLQPVLLKNIDERGKGTVSRDWVGRDAGKiAAAIGLNVPEQT 345
Cdd:PLN02278 309 --ILVQEGIYDKFaeafskaVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGK-RHSLGGTFYEPT 385
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 346 RLlfVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAIDTSI 415
Cdd:PLN02278 386 VL--GDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGL--AAYIFTRDLQRAWRVSEALEYGI 451
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
68-430 |
1.13e-06 |
|
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: 50.88 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 68 EKHARELAELAVTETGM----GRVEDKFA----KNVAQARGT-PGVEClsPQVLT--GDNGLTLIENAPWGVVASVTPST 136
Cdd:cd07148 58 EERADELALLIAREGGKplvdAKVEVTRAidgvELAADELGQlGGREI--PMGLTpaSAGRIAFTTREPIGVVVAISAFN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 137 NPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGgpanlLVTVANPDIETAQRLFKYPGIGLLVVTG 216
Cdd:cd07148 136 HPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEG-----WCQAVPCENAVAEKLVTDPRVAFFSFIG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 217 GEAVVDAARKHtnkrlIAAGA-------GNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSVADELMRLM 289
Cdd:cd07148 211 SARVGWMLRSK-----LAPGTrcalehgGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 290 eSQHAVKLTTAQA----EQLQPVLLKNIDERgkgtvSRDWV--GRDAGK-------------IAAAIGLNVPEQTRLlfv 350
Cdd:cd07148 286 -AAAAEKLVVGDPtdpdTEVGPLIRPREVDR-----VEEWVneAVAAGArllcggkrlsdttYAPTVLLDPPRDAKV--- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 351 etsATHpfavtELMMPVLPVVRVANVDEAIELAVKLEggCHHTAAMHSRNIDNMNRMANAIDTSIFVKN----------- 419
Cdd:cd07148 357 ---STQ-----EIFGPVVCVYSYDDLDEAIAQANSLP--VAFQAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvdwmp 426
|
410
....*....|...
gi 489128223 420 --GPCIAGLGLGG 430
Cdd:cd07148 427 faGRRQSGYGTGG 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
39-383 |
1.58e-06 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 50.26 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 39 AVAAAKLAQQGL--KSVAMRQLAITALREAGEKHARELAELAVTETGMGRV----EDKFAKNVAQ--ARGTPGVecLSPQ 110
Cdd:PRK09407 59 AFARARAAQRAWaaTPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRhafeEVLDVALTARyyARRAPKL--LAPR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 111 VLTGdnGLTLIENA-----PWGVVASVTPSTNPAATVINNAISLIAAGNSVVfaphpaAKKVSQRAITLL--NQAVVAAG 183
Cdd:PRK09407 137 RRAG--ALPVLTKTtelrqPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV------LKPDSQTPLTALaaVELLYEAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 184 GPANLLVTVanpdietaqrlfkyPGIGLLVvtgGEAVVDAA------------RK---HTNKRLIAAGA---GNPPVVVD 245
Cdd:PRK09407 209 LPRDLWQVV--------------TGPGPVV---GTALVDNAdylmftgstatgRVlaeQAGRRLIGFSLelgGKNPMIVL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 246 ETADLARAAQSVVKGAsFDNN-IICADEKVLIVVDSVADE-LMRLMESQHAVKLTTA-----------QAEQLQPVLLKN 312
Cdd:PRK09407 272 DDADLDKAAAGAVRAC-FSNAgQLCISIERIYVHESIYDEfVRAFVAAVRAMRLGAGydysadmgsliSEAQLETVSAHV 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489128223 313 IDERGKG-TVsrdWVGrdaGKIAAAIGLNVPEQTRLLFVETSAThpFAVTELMMPVLPVVRVANVDEAIELA 383
Cdd:PRK09407 351 DDAVAKGaTV---LAG---GKARPDLGPLFYEPTVLTGVTPDME--LAREETFGPVVSVYPVADVDEAVERA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
51-382 |
2.54e-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: 49.81 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 51 KSVAMRQLAITALREAGEKHAREL------------AELAVTETGMGRVEDKFA-KNVA-----QARGTPgveclspqvL 112
Cdd:cd07136 17 KDVEFRIEQLKKLKQAIKKYENEIlealkkdlgkseFEAYMTEIGFVLSEINYAiKHLKkwmkpKRVKTP---------L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 113 TGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVvaaggPANLlVTV 192
Cdd:cd07136 88 LNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEY-VAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 193 ANPDIETAQRL----FKYpgiglLVVTGGEAV----VDAARKHtnkrLIAA----GaGNPPVVVDETADLARAAQSVVKG 260
Cdd:cd07136 162 VEGGVEENQELldqkFDY-----IFFTGSVRVgkivMEAAAKH----LTPVtlelG-GKSPCIVDEDANLKLAAKRIVWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 261 aSFDN---NIICADekVLIVVDSVADELMRLMesQHAVKLTTAQAEQLQPVLLKNIDE----RGKGTVsrdwvgrDAGKI 333
Cdd:cd07136 232 -KFLNagqTCVAPD--YVLVHESVKEKFIKEL--KEEIKKFYGEDPLESPDYGRIINEkhfdRLAGLL-------DNGKI 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489128223 334 aaAIGLNVPEQTRL----LFVETSATHPFAVTELMMPVLPVVRVANVDEAIEL 382
Cdd:cd07136 300 --VFGGNTDRETLYieptILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEI 350
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
150-383 |
3.90e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 49.40 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 150 IAAGNSVVFAPHPAAkkVSQRAITL-LNQAVVAAGGPANLLVTVANPDIE--TAQRLFKYPGIGLLVVTGGEAVVDAARK 226
Cdd:cd07127 218 LATGNPVIVKPHPAA--ILPLAITVqVAREVLAEAGFDPNLVTLAADTPEepIAQTLATRPEVRIIDFTGSNAFGDWLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 227 H-TNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIV-------------VDSVADELMR----- 287
Cdd:cd07127 296 NaRQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddgrksFDEVAADLAAaidgl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 288 LMESQHAVKLTTAQaeQLQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIglnvpEQTRLLFVETSATHPFAVTELMMPV 367
Cdd:cd07127 376 LADPARAAALLGAI--QSPDTLARIAEARQLGEVLLASEAVAHPEFPDAR-----VRTPLLLKLDASDEAAYAEERFGPI 448
|
250
....*....|....*.
gi 489128223 368 LPVVRVANVDEAIELA 383
Cdd:cd07127 449 AFVVATDSTDHSIELA 464
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
121-382 |
4.15e-06 |
|
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: 48.95 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAKKVSQRAIT--LLNQAV-VAAGGPAnllvtvan 194
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSelaPATSALLAKLIPeyLDTKAIkVIEGGVP-------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 195 pdiETAQRL-FKYPGIgllVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGA-SFDNNII 268
Cdd:cd07137 169 ---ETTALLeQKWDKI---FFTGsprvGRIIMAAAAKHLTPVTLELG-GKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 269 CADEKVLIVVDSVADELMRLM-------------ESQHAVKLTTAQAEQLQPVLLKniDERGKGTV----SRDwvgRDAG 331
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALkntlekffgenpkESKDLSRIVNSHHFQRLSRLLD--DPSVADKIvhggERD---EKNL 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489128223 332 KIAAAIGLNVPEQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEAIEL 382
Cdd:cd07137 317 YIEPTILLDPPLDSSIM-----------TEEIFGPLLPIITVKKIEESIEI 356
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
34-383 |
8.94e-06 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 47.81 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 34 ASLDDAVAAAKLAQQGLKSVAMRQLAITALREAG--EKHARELAELAVTETGmgrvedkfaKNVAQARGTPGvECLSPQV 111
Cdd:PRK09406 23 DEVDAAIARAHARFRDYRTTTFAQRARWANAAADllEAEADQVAALMTLEMG---------KTLASAKAEAL-KCAKGFR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 112 LTGDNGLTLI--ENA---------------PWGVVASVTPSTNPAATVINNAISLIAAGNsVVFAPHpaAKKVSQRAItL 174
Cdd:PRK09406 93 YYAEHAEALLadEPAdaaavgasrayvryqPLGVVLAVMPWNFPLWQVVRFAAPALMAGN-VGLLKH--ASNVPQTAL-Y 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 175 LNQAVVAAGGPANLLVTVANPDiETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGaGNPPVVVDETADL 250
Cdd:PRK09406 169 LADLFRRAGFPDGCFQTLLVGS-GAVEAILRDPRVAAATLTGsepaGRAVAAIAGDEIKKTVLELG-GSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 251 ARAAQSVVKGASFDNNIICADEKVLIVVDSVADELM-RLMESQHAVKL--TTAQAEQLQPVllknIDERGKGTVSRdwVG 327
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAeKFVARMAALRVgdPTDPDTDVGPL----ATEQGRDEVEK--QV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489128223 328 RDAGKIAAAI--GLNVPEQTRLLF---VETSATHPFAV--TELMMPVLPVVRVANVDEAIELA 383
Cdd:PRK09406 321 DDAVAAGATIlcGGKRPDGPGWFYpptVITDITPDMRLytEEVFGPVASLYRVADIDEAIEIA 383
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
36-290 |
2.16e-05 |
|
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: 46.53 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 36 LDDAVAAAKLAQQ--GLKSVAMRQlaiTALREAGE---KHARELAELAVTETG----MGRVEdkfAKNVAQ-----ARGT 101
Cdd:cd07090 21 VDLAVKSAKAAQKewSATSGMERG---RILRKAADllrERNDEIARLETIDNGkpieEARVD---IDSSADcleyyAGLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 102 PGVECLSPQVLTGDNGLTliENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVA 181
Cdd:cd07090 95 PTLSGEHVPLPGGSFAYT--RREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL----LLAEILTE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 182 AGGPANlLVTVANPDIETAQRLFKYPGIGLLVVTG----GEAVVDAAR---KHTNKRLiaagAGNPPVVVDETADLARAA 254
Cdd:cd07090 169 AGLPDG-VFNVVQGGGETGQLLCEHPDVAKVSFTGsvptGKKVMSAAAkgiKHVTLEL----GGKSPLIIFDDADLENAV 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 489128223 255 QSVVKGASFDNNIICADEKVLIVVDSVADE-LMRLME 290
Cdd:cd07090 244 NGAMMANFLSQGQVCSNGTRVFVQRSIKDEfTERLVE 280
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
121-382 |
4.87e-05 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 45.81 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQ-----AVVAAGGPanllVTVANP 195
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQyldssAVRVVEGA----VTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 196 DIETAQRLFKYPGIGLLvvtgGEAVVDAARKHTNKRLIAAGaGNPPVVVDETADLARAAQSVVKGASFDNN--------- 266
Cdd:PLN02174 184 LLEQKWDKIFYTGSSKI----GRVIMAAAAKHLTPVVLELG-GKSPVVVDSDTDLKVTVRRIIAGKWGCNNgqacispdy 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 267 IICADEKVLIVVDSVADELMRL-----MESQHAVKLTTAQAEQLQPVLL--KNIDERGKGTVSRDwvgRDAGKIAAAIGL 339
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFygknpMESKDMSRIVNSTHFDRLSKLLdeKEVSDKIVYGGEKD---RENLKIAPTILL 335
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489128223 340 NVPEQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEAIEL 382
Cdd:PLN02174 336 DVPLDSLIM-----------SEEIFGPLLPILTLNNLEESFDV 367
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
115-258 |
8.51e-05 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 44.73 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 115 DNGLTLIEN-APWGVVASVTPStNPAATVInnAISL-IAAGNSVVF-----APHpaakkvSQRAI-TLLNQAVVAAGGPA 186
Cdd:cd07079 98 PNGLQIEKVrVPLGVIGIIYES-RPNVTVD--AAALcLKSGNAVILrggseALH------SNRALvEIIQEALEEAGLPE 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489128223 187 NLLVTVANPDIETAQRLFKYPG-IGLLVVTGGEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQSVV 258
Cdd:cd07079 169 DAVQLIPDTDREAVQELLKLDDyIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAVRIVV 241
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
148-388 |
1.15e-04 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 44.45 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 148 SLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPGIGLLVVTGGEAVVDAarkh 227
Cdd:cd07129 130 SALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRA---- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 228 tnkrLIAAGAGNP-------------PVVVDETADLARAAQ-------SVVKGA-SFdnniiCADEKVLIVVDSVADELM 286
Cdd:cd07129 206 ----LFDAAAARPepipfyaelgsvnPVFILPGALAERGEAiaqgfvgSLTLGAgQF-----CTNPGLVLVPAGPAGDAF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 287 RlmesQHAVKLTTAQAEQlqPVLLKNIDE---RGKGTVSRDWVGRDAGKIAAAIGLNVPEQTrlLFVETSAT---HPFAV 360
Cdd:cd07129 277 I----AALAEALAAAPAQ--TMLTPGIAEayrQGVEALAAAPGVRVLAGGAAAEGGNQAAPT--LFKVDAAAflaDPALQ 348
|
250 260
....*....|....*....|....*...
gi 489128223 361 TELMMPVLPVVRVANVDEAIELAVKLEG 388
Cdd:cd07129 349 EEVFGPASLVVRYDDAAELLAVAEALEG 376
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
125-382 |
5.68e-04 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 42.13 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQrAITLLNQAVVAAGGPANLLVTVANPDIETAQRLF 204
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI-AMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 205 KYPGIGLLVVTGGEAVVDAARKHTNKRL---IAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICADEKVLIVVDSV 281
Cdd:PLN02315 233 KDTRIPLVSFTGSSKVGLMVQQTVNARFgkcLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 282 ADELM-RLMESQHAVKLTTAQAEQ-----LQPVLLKNIDERGKGTVSrdwvgRDAGKI-----AAAIGLNVPEQTrllFV 350
Cdd:PLN02315 313 YDDVLeQLLTVYKQVKIGDPLEKGtllgpLHTPESKKNFEKGIEIIK-----SQGGKIltggsAIESEGNFVQPT---IV 384
|
250 260 270
....*....|....*....|....*....|..
gi 489128223 351 ETSATHPFAVTELMMPVLPVVRVANVDEAIEL 382
Cdd:PLN02315 385 EISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
168-258 |
1.54e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 40.82 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 168 SQRAI-TLLNQAVVAAGGPANLLVTVANPDIETAQRLFKYPG-IGLLVVTGGEAVVDAARKHTNKRLIAAGAGNPPVVVD 245
Cdd:PRK00197 155 SNRALvAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVD 234
|
90
....*....|...
gi 489128223 246 ETADLARAAQSVV 258
Cdd:PRK00197 235 ESADLDKALKIVL 247
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
117-411 |
5.36e-03 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 39.03 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 117 GLTLIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaakkVSQRAITLLNQAVVA--AGGPANLLVTVAN 194
Cdd:PLN02766 152 GYTLKE--PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKP------AEQTPLSALFYAHLAklAGVPDGVINVVTG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 195 PDIETAQRLFKYPGIGLLVVTG----GEAVVDAARKHTNKRLIAAGAGNPPVVVDETADLARAAQSVVKGASFDNNIICA 270
Cdd:PLN02766 224 FGPTAGAAIASHMDVDKVSFTGstevGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489128223 271 DEKVLIVVDSVADELM-RLMESQHAVKL------TTAQAEQLQPV----LLKNIdERGKGTVSRDWVGrdaGKIAAAIGL 339
Cdd:PLN02766 304 ASSRVYVQEGIYDEFVkKLVEKAKDWVVgdpfdpRARQGPQVDKQqfekILSYI-EHGKREGATLLTG---GKPCGDKGY 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489128223 340 NVpEQTrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIELAVKLEGGChhTAAMHSRNIDNMNRMANAI 411
Cdd:PLN02766 380 YI-EPT--IFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGL--AAGIVTKDLDVANTVSRSI 446
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