|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
1-467 |
0e+00 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 705.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 1 MNQQDIEQVVKAVLLKM--KDSSQPADTVHGMGVFASLDDAVAAAKVAQQGL--KRVAMRQQVIQAIREAGEKHARELAE 76
Cdd:PRK15398 1 MNQQDIEQVVKAVLAEMlsSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYqqKSLAMRQRIIDAIREALLPHAEELAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 77 LAVTETGMGRVEDKFAKNVAQARGTPGVECLTPQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSV 156
Cdd:PRK15398 81 LAVEETGMGRVEDKIAKNVAAAEKTPGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 157 VFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYPGIGLLVVTGGEAVVEAARKhTNKRLIAAG 236
Cdd:PRK15398 161 VFSPHPGAKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMK-SGKKAIGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 237 AGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADELMRLMEDQQAVKLTAAQAEQLQPLLLKNider 316
Cdd:PRK15398 240 AGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKN---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 317 gKGTVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHHTAAM 396
Cdd:PRK15398 316 -GGTVNKKWVGKDAAKILEAAGINVPKDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNRHTAIM 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263436 397 HSRNIDNMNQMANAIDTSIFVKNGPCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV 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: 626.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 31 GVFASLDDAVAAAKVAQQGLKR--VAMRQQVIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTPGVECLT 108
Cdd:cd07121 1 GVFATVDDAVAAAKAAQKQYRKctLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 109 PQVLTGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANL 188
Cdd:cd07121 81 TTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 189 LVTVANPDIDTAQRLFKYPGIGLLVVTGGEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNII 268
Cdd:cd07121 161 VVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG-KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 269 CADEKVLIVVDSVADELMRLMEDQQAVKLTAAQAEQLQPLLLKNIDErgkGTVSRDWVGRDAGKIAAAIGLQVPAQTRLL 348
Cdd:cd07121 240 CIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNKG---ATPNKKWVGKDASKILKAAGIEVPADIRLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 349 FVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIAGLGL 428
Cdd:cd07121 317 IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGLGV 396
|
410 420 430
....*....|....*....|....*....|...
gi 647263436 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 ... |
51-461 |
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: 543.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 51 KRVAMRQQVIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTPGVEC--LTPQVLTGD-NGLTLIENAPWG 127
Cdd:cd07081 18 KSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKdeKTCGVLTGDeNGGTLIIAEPIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 128 VVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYP 207
Cdd:cd07081 98 VVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 208 GIGLLVVTGGEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADELMR 287
Cdd:cd07081 178 GIGLLLATGGPAVVKAAYSSG-KPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 288 LMEDQQAVKLTAAQAEQLQPLLLKNIDergkgtVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVETS--ATHPFAVTELMM 365
Cdd:cd07081 257 LFEGQGAYKLTAEELQQVQPVILKNGD------VNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTslAEHEPFAHEKLS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 366 PVLPVVRVANVDEA--IALAVTLEGGCHHTAAMHSRN---IDNMNQMANAIDTSIFVKNGPC-IAGLGLGGE--GWTTMT 437
Cdd:cd07081 331 PVLAMYRAANFADAdaKALALKLEGGCGHTSAMYSDNikaIENMNQFANAMKTSRFVKNGPCsQGGLGDLYNfrGWPSMT 410
|
410 420
....*....|....*....|....*....
gi 647263436 438 IT--TPTGEGVTS---ARTFVRLRRCVLV 461
Cdd:cd07081 411 LGcgTWGGNSVSEnvgPKHLVNLKTVALR 439
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
51-460 |
2.59e-136 |
|
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: 398.13 E-value: 2.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 51 KRVAMRQQVIQAIREAGEKHARELAELAVTETG-------------MGRVEDKFAKNVAQARGTPGVECLTPQVLTGDNG 117
Cdd:cd07077 13 NHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITASVGHIQDVLLPDNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 118 LTLIENAPWGVVASVTPSTNPAAtVINNAISLIAAGNSVVFAPHPAAKkVSQRAITLLNQAVVAAGGPANLLVTVANPDI 197
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHGPKILVLYVPHPSD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 198 DTAQRLFKYPGIGLLVVTGGEAVVEAARKHTN-KRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNiICADEKVLI 276
Cdd:cd07077 171 ELAEELLSHPKIDLIVATGGRDAVDAAVKHSPhIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQN-ACASEQNLY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 277 VVDSVADELMRLMEDQQAVkltaaqaeqlqplllknidergkgtvsrdwvgrdagkiaaaIGLQVPAQTRLLFVETSATH 356
Cdd:cd07077 250 VVDDVLDPLYEEFKLKLVV-----------------------------------------EGLKVPQETKPLSKETTPSF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 357 PFAVTELMMPVLPVVRVANVDEA--IALAVTLEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIA--GLGLGGEG 432
Cdd:cd07077 289 DDEALESMTPLECQFRVLDVISAveNAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKgrGAFAGKGV 368
|
410 420
....*....|....*....|....*....
gi 647263436 433 WTTMTITTPTGEG-VTSARTFVRLRRCVL 460
Cdd:cd07077 369 ERIVTSGMNNIFGaGVGHDALRPLKRLVR 397
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
52-427 |
7.44e-98 |
|
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: 300.95 E-value: 7.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 52 RVAMR-------QQV---IQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTpgVECLTPQVLTG------D 115
Cdd:cd07122 9 RKAQRefatfsqEQVdkiVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYV--YNDIKDMKTVGvieedeE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 116 NGLTLIEnAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANP 195
Cdd:cd07122 87 KGIVEIA-EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 196 DIDTAQRLFKYPGIGLLVVTGGEAVVEAARKhTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVL 275
Cdd:cd07122 166 SIELTQELMKHPDVDLILATGGPGMVKAAYS-SGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 IVVDSVADELMRLMEDQQAVKLTAAQAEQLQPLLLKNidergKGTVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVET--- 352
Cdd:cd07122 245 IVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDD-----GGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEEtgv 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 353 SATHPFAVtELMMPVLPVVRVANVDEAIALAVTL--EGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGP-CIAGLG 427
Cdd:cd07122 320 GPEEPLSR-EKLSPVLAFYRAEDFEEALEKARELleYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTPsSLGGIG 396
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
66-421 |
2.54e-71 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 242.01 E-value: 2.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 66 AGEKHARELAELAVTETGMGRVEDKFAKN-VA--------QARGTPGVecltpqvLTGDNGLTLIENA-PWGVVASVTPS 135
Cdd:PRK13805 46 AALDARIPLAKMAVEETGRGVVEDKVIKNhFAseyiynsyKDEKTVGV-------IEEDDEFGIIEIAePVGVIAGITPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 136 TNPAATVINNAisLIAA--GNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYPGIGLLV 213
Cdd:PRK13805 119 TNPTSTAIFKA--LIALktRNPIIFSFHPRAQKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALIL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 214 VTGGEAVVEAARKhTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADELMRLMEDQQ 293
Cdd:PRK13805 197 ATGGPGMVKAAYS-SGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 294 AVKLTAAQAEQLQPLLLKNIDergkGTVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVETSAT---HPFAVtELMMPVLPV 370
Cdd:PRK13805 276 AYFLNKKELKKLEKFIFGKEN----GALNADIVGQSAYKIAEMAGFKVPEDTKILIAEVKGVgesEPLSH-EKLSPVLAM 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 647263436 371 VRVANVDEAIALAVTL--EGGCHHTAAMHSRNIDNMNQMANAIDTS-IFVkNGP 421
Cdd:PRK13805 351 YKAKDFEDAVEKAEKLveFGGLGHTAVIYTNDDELIKEFGLRMKACrILV-NTP 403
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
51-427 |
4.13e-67 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 222.82 E-value: 4.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 51 KRVAMRQQ----VIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQARGTpgVECL----TPQVLTGDNGLTLIE 122
Cdd:TIGR02518 23 KLANMTQEqidkIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIV--YDSIkdmkTIGILSEDKEKKVIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 123 NA-PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQ 201
Cdd:TIGR02518 101 IAvPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCITVPTIEGTN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 202 RLFKYPGIGLLVVTGGEAVVEAARKhTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSV 281
Cdd:TIGR02518 181 ELMKNKDTSLILATGGEAMVKAAYS-SGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQSIIVEECN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 282 ADELMRLMEDQQAVKLTAAQAEQLQPLLLKNidergKGTVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVE---TSATHPF 358
Cdd:TIGR02518 260 KDAVVEELKKQGGYFLTAEEAEKLGKFILRP-----NGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEqngVGNKNPY 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263436 359 AvTELMMPVLPVVRVANVDEAIALAVTL--EGGCHHTAAMHSRNIDNMNQMANAIDTS-IFVKNGPCIAGLG 427
Cdd:TIGR02518 335 S-REKLTTILAFYTEENWHEACELSIELlqNEGAGHTLIIHSENKDIVREFALKKPVSrMLVNTGGSLGGIG 405
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
53-460 |
3.27e-60 |
|
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: 201.30 E-value: 3.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETG--MGRVEDKFAKNVAQARGTPGVECL---TPQVLTGDNGLTLIENAPWG 127
Cdd:cd06534 15 PAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKlggPELPSPDPGGEAYVRREPLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 128 VVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLnqavVAAGGPANLLVTVANPDIDTAQRLFKYP 207
Cdd:cd06534 95 VVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVPGGGDEVGAALLSHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 208 GIGLLVVTGGEAVVEAARKH---TNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADE 284
Cdd:cd06534 171 RVDKISFTGSTAVGKAIMKAaaeNLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 285 LMrlmedqqavkltaaqaEQLQPlllknidergkgtvsrdwvgrdagkiaaaiglqvpaqtrlLFVETSATHPFAVTELM 364
Cdd:cd06534 251 FV----------------EKLVT----------------------------------------VLVDVDPDMPIAQEEIF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 365 MPVLPVVRVANVDEAIALAVtlEGGCHHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCI--------AGLGLGGEGWTTm 436
Cdd:cd06534 275 GPVLPVIRFKDEEEAIALAN--DTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgvgpeapfGGVKNSGIGREG- 351
|
410 420
....*....|....*....|....
gi 647263436 437 tittptgeGVTSARTFVRLRRCVL 460
Cdd:cd06534 352 --------GPYGLEEYTRTKTVVI 367
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
56-421 |
4.92e-29 |
|
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: 118.46 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG----MGRVE-----DKFAKNVAQARGTPGVECLTPqvltGDNGLTLIENAPW 126
Cdd:cd07078 22 RAAILRKLADLLEERREELAALETLETGkpieEALGEvaraaDTFRYYAGLARRLHGEVIPSP----DPGELAIVRREPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 127 GVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQavvaAGGPANlLVTVANPDIDTA-QRLFK 205
Cdd:cd07078 98 GVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE----AGLPPG-VLNVVTGDGDEVgAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 206 YPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSV 281
Cdd:cd07078 173 HPRVDKISFTGstavGKAIMRAAAEN-LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 282 ADELM-RLMEDQQAVK--------------LTAAQAEQLQPLLLKNIDERGKGTVSRDWVGRDAG-KIAAAIGLQVPAQT 345
Cdd:cd07078 252 YDEFVeRLVERVKALKvgnpldpdtdmgplISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGyFVPPTVLTDVDPDM 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 346 RLLFVETsathpFAvtelmmPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGP 421
Cdd:cd07078 332 PIAQEEI-----FG------PVLPVIPFKDEEEAIELANDTEYGL--AAGVFTRDLERALRVAERLEAGTVWINDY 394
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
56-433 |
1.26e-28 |
|
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: 117.63 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVEC----------LTPQVLTGDNG-LTLIE 122
Cdd:pfam00171 53 RAAILRKAADLLEERKDELAELETLENG---------KPLAEARGevDRAIDVlryyaglarrLDGETLPSDPGrLAYTR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 123 NAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANLLVTVANPDIDTAQR 202
Cdd:pfam00171 124 REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTAL----LLAELFEEAGLPAGVLNVVTGSGAEVGEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTG----GEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVV 278
Cdd:pfam00171 200 LVEHPDVRKVSFTGstavGRHIAEAAAQNL-KRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADELM-RLMEDQQAVKLTAAQAEQLQ--PLllknIDERGKGTVsRDWV--GRDAGKIAAAIGLQVPAQTRL----LF 349
Cdd:pfam00171 279 ESIYDEFVeKLVEAAKKLKVGDPLDPDTDmgPL----ISKAQLERV-LKYVedAKEEGAKLLTGGEAGLDNGYFveptVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 350 VETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGchHTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIAGL--- 426
Cdd:pfam00171 354 ANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG--LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdgl 431
|
410
....*....|....*
gi 647263436 427 --------GLGGEGW 433
Cdd:pfam00171 432 pfggfkqsGFGREGG 446
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
56-425 |
3.54e-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: 113.68 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVECL--------------TPQVLTGDNGLT 119
Cdd:COG1012 67 RAAILLRAADLLEERREELAALLTLETG---------KPLAEARGevDRAADFLryyagearrlygetIPSDAPGTRAYV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 120 LIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAkkvsQRAITLLNQAVVAAGGPANLLVTVANPDIDT 199
Cdd:COG1012 138 RRE--PLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQT----PLSALLLAELLEEAGLPAGVLNVVTGDGSEV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 200 AQRLFKYPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVL 275
Cdd:COG1012 212 GAALVAHPDVDKISFTGstavGRRIAAAAAEN-LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 IVVDSVADELM-RLMEDQQAVKL--TAAQAEQLQPLllknIDERGKGTVsRDWV--GRDAGKIAAAIGLQVPAQTRL--- 347
Cdd:COG1012 291 LVHESIYDEFVeRLVAAAKALKVgdPLDPGTDMGPL----ISEAQLERV-LAYIedAVAEGAELLTGGRRPDGEGGYfve 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 348 --LFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIAG 425
Cdd:COG1012 366 ptVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGL--AASVFTRDLARARRVARRLEAGMVWINDGTTGA 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
68-383 |
8.65e-21 |
|
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: 94.35 E-value: 8.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 68 EKHARELAELAVTETG---------MGRVEDKFAKNVAQARGTPGvECL-TPQVLTGDNGLTLIENAPWGVVASVTPSTN 137
Cdd:cd07146 54 EARREEFARLITLESGlclkdtryeVGRAADVLRFAAAEALRDDG-ESFsCDLTANGKARKIFTLREPLGVVLAITPFNH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 138 PAATVINNAISLIAAGNSVVFAPHPaakKVSQRAItLLNQAVVAAGGPANLL-VTVANPDiDTAQRLFKYPGIGLLVVTG 216
Cdd:cd07146 133 PLNQVAHKIAPAIAANNRIVLKPSE---KTPLSAI-YLADLLYEAGLPPDMLsVVTGEPG-EIGDELITHPDVDLVTFTG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 217 GEAVVEA-ARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADELMRLMEDQQAV 295
Cdd:cd07146 208 GVAVGKAiAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 296 KLTA---------------AQAEQLQPLLLKNIDeRGKGTVSRDwvGRDAGKIAAAIGLQVPAQTRLLFVETsathpFAv 360
Cdd:cd07146 288 LVVGdpmdpatdmgtvideEAAIQIENRVEEAIA-QGARVLLGN--QRQGALYAPTVLDHVPPDAELVTEET-----FG- 358
|
330 340
....*....|....*....|...
gi 647263436 361 telmmPVLPVVRVANVDEAIALA 383
Cdd:cd07146 359 -----PVAPVIRVKDLDEAIAIS 376
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
56-411 |
2.10e-20 |
|
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: 93.18 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGM----GRVE--------DKFAKNVAQARG-TPGVEcltpQVLTGDNGLTLIE 122
Cdd:cd07145 45 RYKILMKVAELIERRKEELAKLLTIEVGKpikqSRVEvertirlfKLAAEEAKVLRGeTIPVD----AYEYNERRIAFTV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 123 NAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGpanLLVTVANPDIdTAQR 202
Cdd:cd07145 121 REPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGV---INVVTGYGSE-VGDE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTGGEAVVE--AAR-KHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGaSFDN-NIICADEKVLIVV 278
Cdd:cd07145 197 IVTNPKVNMISFTGSTAVGLliASKaGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRG-RFENaGQVCNAVKRILVE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADE-LMRLMEDQQAVKL--------------TAAQAEQLQPLLLKNIDERGKGTVSrdwVGRDAGKIAAAIGLQVPA 343
Cdd:cd07145 276 EEVYDKfLKLLVEKVKKLKVgdpldestdlgpliSPEAVERMENLVNDAVEKGGKILYG---GKRDEGSFFPPTVLENDT 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 344 QTRLLFVEtsathpfavtELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAI 411
Cdd:cd07145 353 PDMIVMKE----------EVFGPVLPIAKVKDDEEAVEIANSTEYGLQ--ASVFTNDINRALKVAREL 408
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
53-413 |
4.48e-20 |
|
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: 92.28 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETGMGRVE------------DKFAKN---VAQARGTPGVECLTPQVLTgdng 117
Cdd:cd07099 39 VEGRAQRLLRWKRALADHADELAELLHAETGKPRADaglevllaleaiDWAARNaprVLAPRKVPTGLLMPNKKAT---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 118 ltlIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANLLvTVANPDI 197
Cdd:cd07099 115 ---VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE----LLAEAWAAAGPPQGVL-QVVTGDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 198 DTAQRLFKYpGIGLLVVTGGEAvveaarkhTNKRLIAAGA-----------GNPPVVVDETADLPRAAEAIVRGASFDNN 266
Cdd:cd07099 187 ATGAALIDA-GVDKVAFTGSVA--------TGRKVMAAAAerlipvvlelgGKDPMIVLADADLERAAAAAVWGAMVNAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 267 IICADEKVLIVVDSVADELmrlmedqqaVKLTAAQAEQLQPlllkNIDERGKG------------TVSR---DWVgrDAG 331
Cdd:cd07099 258 QTCISVERVYVHESVYDEF---------VARLVAKARALRP----GADDIGDAdigpmttarqldIVRRhvdDAV--AKG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 332 KIAAAIGLqvPAQTRLLFVE----TSATHPFAVT--ELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMN 405
Cdd:cd07099 323 AKALTGGA--RSNGGGPFYEptvlTDVPHDMDVMreETFGPVLPVMPVADEDEAIALANDSRYGL--SASVFSRDLARAE 398
|
....*...
gi 647263436 406 QMANAIDT 413
Cdd:cd07099 399 AIARRLEA 406
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
56-432 |
7.21e-20 |
|
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: 91.94 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG----MGRVEDKFAKN-----VAQARGTPGvecltpQVLTGD--NGLTLIENA 124
Cdd:cd07088 59 RAAYLRKLADLIRENADELAKLIVEEQGktlsLARVEVEFTADyidymAEWARRIEG------EIIPSDrpNENIFIFKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHpaakKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLF 204
Cdd:cd07088 133 PIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS----EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVrGASFDNN-IICADEKVLIVVD 279
Cdd:cd07088 209 AHPKVGMISLTGsteaGQKIMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAIV-DSRIINCgQVCTCAERVYVHE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 280 SVADELM-RLMEDQQAVKL--TAAQAEQLQPLLLKNIDERGKGTVSRdwvGRDAGKIAAAIGLQVPAQTRLLFVETSATH 356
Cdd:cd07088 287 DIYDEFMeKLVEKMKAVKVgdPFDAATDMGPLVNEAALDKVEEMVER---AVEAGATLLTGGKRPEGEKGYFYEPTVLTN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 357 PFAVTELMM-----PVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAI---DTSIFVKNGPCIAGL-- 426
Cdd:cd07088 364 VRQDMEIVQeeifgPVLPVVKFSSLDEAIELANDSEYGL--TSYIYTENLNTAMRATNELefgETYINRENFEAMQGFha 441
|
410
....*....|.
gi 647263436 427 -----GLGGEG 432
Cdd:cd07088 442 gwkksGLGGAD 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
56-414 |
2.60e-19 |
|
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: 90.18 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAG---EKHARELAELAVTETGMGRVE---------DKFAKNVAQARGTPGVECLTPQVLTGDNGLTLIEN 123
Cdd:cd07094 42 PHERMAILERAAdllKKRAEEFAKIIACEGGKPIKDarvevdraiDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 APWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRaitlLNQAVVAAGGPANLLVTVANPDIDTAQRL 203
Cdd:cd07094 122 EPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALE----LAKILVEAGVPEGVLQVVTGEREVLGDAF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 204 FKYPGIGLLVVTGGEAVVEAARKHTN-KRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVA 282
Cdd:cd07094 198 AADERVAMLSFTGSAAVGEALRANAGgKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 283 DELMRLMEdQQAVKLTAAQAEQLQPLLLKNIDErGKGTVSRDWVGRDAGKIAAAIGLQVPAQTrlLFVETSATHP----- 357
Cdd:cd07094 278 DEFIEAFV-AAVKKLKVGDPLDEDTDVGPLISE-EAAERVERWVEEAVEAGARLLCGGERDGA--LFKPTVLEDVprdtk 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 647263436 358 FAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAIDTS 414
Cdd:cd07094 354 LSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ--AGIFTRDLNVAFKAAEKLEVG 408
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
54-411 |
1.14e-17 |
|
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: 84.96 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGT--PGV--------ECLTPQ----VLTGDNGLT 119
Cdd:cd07112 48 AERKAVLLRLADLIEAHRDELALLETLDMG---------KPISDALAVdvPSAantfrwyaEAIDKVygevAPTGPDALA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 120 LIENAPWGVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPhpaAKKVSQRAITLLNQAVvAAGGPANLLVTVANPD 196
Cdd:cd07112 119 LITREPLGVVGAVVPWNFPllmAAWKIAPAL---AAGNSVVLKP---AEQSPLTALRLAELAL-EAGLPAGVLNVVPGFG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 197 IDTAQRLFKYPGIGLLVVTGGEAV----VEAARKHTNKRL-IAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICAD 271
Cdd:cd07112 192 HTAGEALGLHMDVDALAFTGSTEVgrrfLEYSGQSNLKRVwLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 272 EKVLIVVDSVADELMRLMedqqavkltAAQAEQLQ---PLLLKN-----IDERGKGTVsRDWV--GRDAGKIAAAIGLQV 341
Cdd:cd07112 272 GSRLLVHESIKDEFLEKV---------VAAAREWKpgdPLDPATrmgalVSEAHFDKV-LGYIesGKAEGARLVAGGKRV 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 342 PAQTRLLFVE------TSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAI 411
Cdd:cd07112 342 LTETGGFFVEptvfdgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLA--ASVWTSDLSRAHRVARRL 415
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
56-413 |
6.84e-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: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGMGR----VEDKFAKNVAQARGTpgvECLTPQVLT----GDNGLTLIENAPWG 127
Cdd:cd07104 24 RAAILRKAAEILEERRDEIADWLIRESGSTRpkaaFEVGAAIAILREAAG---LPRRPEGEIlpsdVPGKESMVRRVPLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 128 VVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkvsQRAIT---LLNQAVVAAGGPANLL-VTVANPDiDTAQRL 203
Cdd:cd07104 101 VVGVISPFNFPLILAMRSVAPALALGNAVVLKPDS------RTPVTgglLIAEIFEEAGLPKGVLnVVPGGGS-EIGDAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 204 FKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVD 279
Cdd:cd07104 174 VEHPRVRMISFTGstavGRHIGELAGRHLKKVALELG-GNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 280 SVADELmrlmedqqaVKLTAAQAEQLqplllKNIDERGKGTV-----SRDWVGRDAGKIAAAI--GLQV----PAQTRLL 348
Cdd:cd07104 253 SVYDEF---------VEKLVAKAKAL-----PVGDPRDPDTVigpliNERQVDRVHAIVEDAVaaGARLltggTYEGLFY 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647263436 349 ----FVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07104 319 qptvLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGL--SAAVFTRDLERAMAFAERLET 385
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
68-430 |
1.20e-16 |
|
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: 81.85 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 68 EKHARELAELAVTETGMGRVEDKFakNVAQARG---------TPGVECLTPQVLTGDNGLTLIEnaPWGVVASVTPSTNP 138
Cdd:cd07105 36 ESRRDEFIEAMMEETGATAAWAGF--NVDLAAGmlreaasliTQIIGGSIPSDKPGTLAMVVKE--PVGVVLGIAPWNAP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 139 AATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANLLVTVANPDIDTAQR---LFKYPGIGLLVVT 215
Cdd:cd07105 112 VILGTRAIAYPLAAGNTVVLKASELSPRTHW----LIGRVFHEAGLPKGVLNVVTHSPEDAPEVveaLIAHPAVRKVNFT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 216 G----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIIC-ADEKVlIVVDSVADELMRLME 290
Cdd:cd07105 188 GstrvGRIIAETAAKHLKPVLLELG-GKAPAIVLEDADLDAAANAALFGAFLNSGQICmSTERI-IVHESIADEFVEKLK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 291 DqQAVKLTAAqAEQLQPLLLKNIDERGKGTVSrDWVGRDAGKIAAAIGLQVPAQTRL--LFVE-TSATHPFAVTELMMPV 367
Cdd:cd07105 266 A-AAEKLFAG-PVVLGSLVSAAAADRVKELVD-DALSKGAKLVVGGLADESPSGTSMppTILDnVTPDMDIYSEESFGPV 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 368 LPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGPCI---AGLGLGG 430
Cdd:cd07105 343 VSIIRVKDEEEAVRIANDSEYGL--SAAVFTRDLARALAVAKRIESGAVHINGMTVhdePTLPHGG 406
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
53-383 |
1.66e-16 |
|
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: 81.52 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETGMGRV----------EDKFAKNVAQARGTPGVECLTPQVLTGDNGLTLIE 122
Cdd:cd07089 41 AEERARCLRQLHEALEARKEELRALLVAEVGAPVMtaramqvdgpIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVVR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 123 NAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQR 202
Cdd:cd07089 121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP----DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTGGEAV---VEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVD 279
Cdd:cd07089 197 LTTDPRVDMVSFTGSTAVgrrIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 280 SVADELMrlmedqQAVKLTAAQ---------AEQLQPLLLKNIDERGKGTVSRdwvGRDAGKIAAAIGLQVP-------- 342
Cdd:cd07089 277 SRYDEVV------EALAAAFEAlpvgdpadpGTVMGPLISAAQRDRVEGYIAR---GRDEGARLVTGGGRPAgldkgfyv 347
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 647263436 343 AQTRLLFVETSAThpFAVTELMMPVLPVVRVANVDEAIALA 383
Cdd:cd07089 348 EPTLFADVDNDMR--IAQEEIFGPVLVVIPYDDDDEAVRIA 386
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
53-413 |
1.71e-16 |
|
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: 81.46 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETG------MGRVE---DKFAKNVAQARGTPGVECLTPQVLTGDNGLTLIEN 123
Cdd:cd07082 60 LEERIDCLHKFADLLKENKEEVANLLMWEIGktlkdaLKEVDrtiDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 APWGVVASVTPSTNPaatvINNAISLIA----AGNSVVFAPhpaAKKVSQRAITLLnQAVVAAGGPANLLVTVANPDIDT 199
Cdd:cd07082 140 EPLGVVLAIGPFNYP----LNLTVSKLIpaliMGNTVVFKP---ATQGVLLGIPLA-EAFHDAGFPKGVVNVVTGRGREI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 200 AQRLFKYPGIGLLVVTGGEAVVEA-ARKHTNKRLIAA-GAGNPPVVVDEtADLPRAAEAIVRGA-SFdNNIICADEKVLI 276
Cdd:cd07082 212 GDPLVTHGRIDVISFTGSTEVGNRlKKQHPMKRLVLElGGKDPAIVLPD-ADLELAAKEIVKGAlSY-SGQRCTAIKRVL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 277 VVDSVADELMRLMEDQQAvKLTAAQAEQ----LQPL-----------LLKNIDERGkGTVSRDWVGRDAGKIAAAIGLQV 341
Cdd:cd07082 290 VHESVADELVELLKEEVA-KLKVGMPWDngvdITPLidpksadfvegLIDDAVAKG-ATVLNGGGREGGNLIYPTLLDPV 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263436 342 PAQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07082 368 TPDMRLAWEE-----PFG------PVLPIIRVNDIEEAIELANKSNYGLQ--ASIFTKDINKARKLADALEV 426
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
56-413 |
1.90e-15 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 78.06 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGTPGV-------------ECLTPQVLTGDNGLTL-I 121
Cdd:cd07102 42 RKAIVTRAVELLAANTDEIAEELTWQMG---------RPIAQAGGEIRGmlerarymisiaeEALADIRVPEKDGFERyI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 122 ENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRaitlLNQAVVAAGGPANLLVtVANPDIDTAQ 201
Cdd:cd07102 113 RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER----FAAAFAEAGLPEGVFQ-VLHLSHETSA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 202 RLFKYPGIGLLVVTGGEAVVEAARKHTNKRLIAAG---AGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVV 278
Cdd:cd07102 188 ALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADE-LMRLMEDQQAVKL-----------TAAQAEQLQPLLLKNIDERGKGtvsrdwvGRDAgkIAAAIGLQVPAQTR 346
Cdd:cd07102 268 ESIYDAfVEAFVAVVKGYKLgdpldpsttlgPVVSARAADFVRAQIADAIAKG-------ARAL--IDGALFPEDKAGGA 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263436 347 LLF--VETSATHPFAV--TELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07102 339 YLAptVLTNVDHSMRVmrEETFGPVVGIMKVKSDAEAIALMNDSEYGL--TASVWTKDIARAEALGEQLET 407
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
113-421 |
2.68e-15 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 77.87 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 113 TGDNGLTLIENAPWGVVASVTPSTNPaatvINNAISLIA----AGNSVVFAPHpaakkvSQRAITLLN--QAVVAAGGPA 186
Cdd:PLN00412 146 NERNKYCLTSKIPLGVVLAIPPFNYP----VNLAVSKIApaliAGNAVVLKPP------TQGAVAALHmvHCFHLAGFPK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 187 NLLVTVANPDIDTAQRLFKYPGIGLLVVTGGEAVVEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNN 266
Cdd:PLN00412 216 GLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 267 IICADEKVLIVVDSVADELMRLMEDQQAvKLTAAQAE---QLQPLLLKN---------IDERGKGTVSRDWVGRDAGKIA 334
Cdd:PLN00412 296 QRCTAVKVVLVMESVADALVEKVNAKVA-KLTVGPPEddcDITPVVSESsanfieglvMDAKEKGATFCQEWKREGNLIW 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 335 AAIGLQVPAQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIalavtleggcHHTAA--------MHSRNIDNMNQ 406
Cdd:PLN00412 375 PLLLDNVRPDMRIAWEE-----PFG------PVLPVIRINSVEEGI----------HHCNAsnfglqgcVFTRDINKAIL 433
|
330
....*....|....*
gi 647263436 407 MANAIDTSIFVKNGP 421
Cdd:PLN00412 434 ISDAMETGTVQINSA 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
53-420 |
4.53e-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: 77.17 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVE-----CLTPQVLTGDNgltlIENA- 124
Cdd:cd07085 59 VLKRQQVMFKFRQLLEENLDELARLITLEHG---------KTLADARGdvLRGLEvvefaCSIPHLLKGEY----LENVa 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 ----------PWGVVASVTPSTNPAatvinnAISL------IAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGgpanl 188
Cdd:cd07085 126 rgidtysyrqPLGVVAGITPFNFPA------MIPLwmfpmaIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDG----- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 189 LVTVANPDIDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVrGASFD 264
Cdd:cd07085 195 VLNVVHGGKEAVNALLDHPDIKAVSFVGstpvGEYIYERAAAN-GKRVQALGGAKNHAVVMPDADLEQTANALV-GAAFG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 265 nniiCADEK-----VLIVVDSVADELM-RLMEDQQAVKLTAAQAE--QLQPLllknIDERGKGTVsRDWVGR--DAGkiA 334
Cdd:cd07085 273 ----AAGQRcmalsVAVAVGDEADEWIpKLVERAKKLKVGAGDDPgaDMGPV----ISPAAKERI-EGLIESgvEEG--A 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 335 AAI----GLQVPAQTRLLFV------ETSATHPFAVTELMMPVLPVVRVANVDEAIALAvtleggchhtaamhsrnidNM 404
Cdd:cd07085 342 KLVldgrGVKVPGYENGNFVgptildNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII-------------------NA 402
|
410
....*....|....*.
gi 647263436 405 NQMANAidTSIFVKNG 420
Cdd:cd07085 403 NPYGNG--AAIFTRSG 416
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
54-419 |
7.39e-15 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 76.47 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETG-------------MGRVEDKFAKNVAQARGTpgvecLTPqvlTGDNGLTL 120
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGkpirhslrddipgAARAIRWYAEAIDKVYGE-----VAT---TSSHELAM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAKKVSQRAITLLNQAvVAAGGPANLLVTVANPDIDTA 200
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP---SEKSPLSAIRLAGLA-KEAGLPDGVLNVVTGFGHEAG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 201 QRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRL-IAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVL 275
Cdd:PRK09847 229 QALSRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVwLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 IVVDSVADELMRLMEdQQAVKLTAAQAEQLQPLLLKNIDE-------------RGKGTVSRDwvGRDAGkIAAAIGLQVp 342
Cdd:PRK09847 309 LLEESIADEFLALLK-QQAQNWQPGHPLDPATTMGTLIDCahadsvhsfiregESKGQLLLD--GRNAG-LAAAIGPTI- 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 343 aqtrllFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT-SIFVKN 419
Cdd:PRK09847 384 ------FVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGL--GAAVWTRDLSRAHRMSRRLKAgSVFVNN 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
115-400 |
9.54e-15 |
|
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: 76.11 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 115 DNGLTLIenaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSqraiTLLNQAVVAAGGPANLLVTVAN 194
Cdd:cd07124 159 DNRYVYR---PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIA----AKLVEILEEAGLPPGVVNFLPG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 195 PDIDTAQRLFKYPGIGLLVVTGGEAV-----VEAARKHTN----KRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDN 265
Cdd:cd07124 232 PGEEVGDYLVEHPDVRFIAFTGSREVglriyERAAKVQPGqkwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 266 NIICADEKVLIVVDSVADELM-RLMEDQQAVKL-TAAQAE-QLQPLLLKNIDERGKGTVSrdwVGRDAGKIAAaiGLQVP 342
Cdd:cd07124 312 GQKCSACSRVIVHESVYDEFLeRLVERTKALKVgDPEDPEvYMGPVIDKGARDRIRRYIE---IGKSEGRLLL--GGEVL 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263436 343 A-QTRLLFVETS------ATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRN 400
Cdd:cd07124 387 ElAAEGYFVQPTifadvpPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGL--TGGVFSRS 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
54-430 |
1.78e-14 |
|
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: 75.35 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGTpgVECLT---------------PQVLTGDNGL 118
Cdd:cd07109 42 AERGRLLLRIARLIREHADELARLESLDTG---------KPLTQARAD--VEAAAryfeyyggaadklhgETIPLGPGYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 119 TLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVfaphpaAKKVSQRAITLLNQAVVA--AGGPANLLVTVANPD 196
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVV------VKPAEDAPLTALRLAELAeeAGLPAGALNVVTGLG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 197 IDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADE 272
Cdd:cd07109 185 AEAGAALVAHPGVDHISFTGsvetGIAVMRAAAENVVPVTLELG-GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 273 KVLIVVDSVADELM-RLMEDQQAVKLTAAQAE-QLQPLLLKNIDERGKGTVSRdwvGRDAGKIAAAIGLQVPAQTR---- 346
Cdd:cd07109 264 SRLLVHRSIYDEVLeRLVERFRALRVGPGLEDpDLGPLISAKQLDRVEGFVAR---ARARGARIVAGGRIAEGAPAggyf 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 347 ---LLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT-SIFVKNGPC 422
Cdd:cd07109 341 vapTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGL--VAGVWTRDGDRALRVARRLRAgQVFVNNYGA 418
|
410
....*....|
gi 647263436 423 IAGLGL--GG 430
Cdd:cd07109 419 GGGIELpfGG 428
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
50-408 |
1.81e-14 |
|
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: 75.31 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 50 LKRVAMRQQVIQAIREAGEKHARELAELAVTETGMGRVE---------DKFAKNVAQARGTPGVECLTPQVLTGDNGLTL 120
Cdd:cd07083 73 DWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEaiddvaeaiDFIRYYARAALRLRYPAVEVVPYPGEDNESFY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IenaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTVANPDIDTA 200
Cdd:cd07083 153 V---GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEA----GFPPGVVQFLPGVGEEVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 201 QRLFKYPGIGLLVVTGGEAVVE---------AARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICAD 271
Cdd:cd07083 226 AYLTEHERIRGINFTGSLETGKkiyeaaarlAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 272 EKVLIVVDSVADELM-RLMEdqQAVKLTAAQAEQLQPLLLKNIDERGKGTVSRdWV--GRDAGKIAAaiGLQVPAQ---- 344
Cdd:cd07083 306 ASRLILTQGAYEPVLeRLLK--RAERLSVGPPEENGTDLGPVIDAEQEAKVLS-YIehGKNEGQLVL--GGKRLEGegyf 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263436 345 -TRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHHTAAMHSRNIDNMNQMA 408
Cdd:cd07083 381 vAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEAR 445
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
53-421 |
2.70e-14 |
|
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: 74.42 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETG------MGRVE------DKFAKNVAQArgtpgvecLTPQVLTGDNGLTL 120
Cdd:cd07100 20 FAERAALLRKLADLLRERKDELARLITLEMGkpiaeaRAEVEkcawicRYYAENAEAF--------LADEPIETDAGKAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAKKVSQRAItLLNQAVVAAGGPANLLVTVaNPDIDTA 200
Cdd:cd07100 92 VRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKH---ASNVPGCAL-AIEELFREAGFPEGVFQNL-LIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 201 QRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGaSFDNN---IICAdeK 273
Cdd:cd07100 167 EAIIADPRVRGVTLTGseraGRAVAAEAGKNLKKSVLELG-GSDPFIVLDDADLDKAVKTAVKG-RLQNAgqsCIAA--K 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 274 VLIVVDSVADELMRLMEDQ-QAVKL--------------TAAQAEQLQPLLLKNIDERGKGTVSrdwvgrdaGKIAAAIG 338
Cdd:cd07100 243 RFIVHEDVYDEFLEKFVEAmAALKVgdpmdedtdlgplaRKDLRDELHEQVEEAVAAGATLLLG--------GKRPDGPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 339 LQVPAqTRLLFVETSAthPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT-SIFV 417
Cdd:cd07100 315 AFYPP-TVLTDVTPGM--PAYDEELFGPVAAVIKVKDEEEAIALANDSPFGL--GGSVFTTDLERAERVARRLEAgMVFI 389
|
....
gi 647263436 418 kNGP 421
Cdd:cd07100 390 -NGM 392
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
114-403 |
3.10e-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: 74.30 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 114 GDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAKKVSQRAItLLNQAVVAAGGPANLLVTVA 193
Cdd:cd07118 108 GDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKP---SEFTSGTTL-MLAELLIEAGLPAGVVNIVT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 194 NPDIDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDEtADLPRAAEAIVRGASFDNNIIC 269
Cdd:cd07118 184 GYGATVGQAMTEHPDVDMVSFTGstrvGKAIAAAAARNLKKVSLELGGKNPQIVFAD-ADLDAAADAVVFGVYFNAGECC 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 270 ADEKVLIVVDSVADELM-RLMEDQQAVKLTAAQAEQLQPLLLknIDERGKGTVsRDWV--GRDAGKIAAAIGLQVPAQTR 346
Cdd:cd07118 263 NSGSRLLVHESIADAFVaAVVARSRKVRVGDPLDPETKVGAI--INEAQLAKI-TDYVdaGRAEGATLLLGGERLASAAG 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263436 347 L-----LFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDN 403
Cdd:cd07118 340 LfyqptIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL--SAGVWSKDIDT 399
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
56-423 |
3.73e-14 |
|
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: 74.31 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVECL-----TPQVLTGDNGLTLIENA---- 124
Cdd:cd07131 61 RAEYLFRAAELLKKRKEELARLVTREMG---------KPLAEGRGdvQEAIDMAqyaagEGRRLFGETVPSELPNKdamt 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 ---PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRaitlLNQAVVAAGGPANLLVTVANPDIDTAQ 201
Cdd:cd07131 132 rrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALK----LVELFAEAGLPPGVVNVVHGRGEEVGE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 202 RLFKYPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIV 277
Cdd:cd07131 208 ALVEHPDVDVVSFTGstevGERIGETCARP-NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 278 VDSVADELM-RLMEDQQAVKLTAAQAEQ--LQPLllknIDERGKGTVSRdWVgrDAGKIAAAIGLQVPAQ-TRLLFVETS 353
Cdd:cd07131 287 HESVYDEFLkRFVERAKRLRVGDGLDEEtdMGPL----INEAQLEKVLN-YN--EIGKEEGATLLLGGERlTGGGYEKGY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 354 ATHPFAVT-----------ELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGPC 422
Cdd:cd07131 360 FVEPTVFTdvtpdmriaqeEIFGPVVALIEVSSLEEAIEIANDTEYGL--SSAIYTEDVNKAFRARRDLEAGITYVNAPT 437
|
.
gi 647263436 423 I 423
Cdd:cd07131 438 I 438
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
54-383 |
5.18e-14 |
|
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: 73.90 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGMGR---VEDKFAKNVAQARGTPGVECLTPQVLTGD---NGLTLIENAPWG 127
Cdd:cd07092 41 AERSKALLKLADAIEENAEELAALESRNTGKPLhlvRDDELPGAVDNFRFFAGAARTLEGPAAGEylpGHTSMIRREPIG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 128 VVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKkvsqrAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYP 207
Cdd:cd07092 121 VVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP-----LTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 208 GIGLLVVTG----GEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVAD 283
Cdd:cd07092 196 RVRMVSLTGsvrtGKKVARAAADTL-KRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 284 ELM-RLMEDQQAVKLTAAQAE--QLQPLLLKNIDERGKGTVSRdwVGRDA-----GKIAAAIGLQVPAqTRLLFVETSAT 355
Cdd:cd07092 275 EFVaALVEAVSAIRVGDPDDEdtEMGPLNSAAQRERVAGFVER--APAHArvltgGRRAEGPGYFYEP-TVVAGVAQDDE 351
|
330 340
....*....|....*....|....*...
gi 647263436 356 hpFAVTELMMPVLPVVRVANVDEAIALA 383
Cdd:cd07092 352 --IVQEEIFGPVVTVQPFDDEDEAIELA 377
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-423 |
9.10e-14 |
|
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: 73.13 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrveDKFAKNVAQARGTPGV------EC--LTPQVLTGD-NGL-TLIENAP 125
Cdd:cd07150 45 RERILLKAAEIMERRADDLIDLLIDEGG-----STYGKAWFETTFTPELlraaagECrrVRGETLPSDsPGTvSMSVRRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 126 WGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSqraiTLLNQAVVAAGGPANLLVTVANPDIDTAQRLFK 205
Cdd:cd07150 120 LGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG----LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 206 YPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSV 281
Cdd:cd07150 196 DPRVRMVTFTGstavGREIAEKAGRHLKKITLELG-GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 282 ADELmrlmedqqaVKLTAAQAEQlqpllLKNIDERGKGTVsrdwVG-----RDAGKIAAAIGLQVPAQTRLLFVETSATH 356
Cdd:cd07150 275 YDEF---------VKKFVARASK-----LKVGDPRDPDTV----IGplispRQVERIKRQVEDAVAKGAKLLTGGKYDGN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 357 PFA------VTELMM--------PVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGPC 422
Cdd:cd07150 337 FYQptvltdVTPDMRifreetfgPVTSVIPAKDAEEALELANDTEYGL--SAAILTNDLQRAFKLAERLESGMVHINDPT 414
|
.
gi 647263436 423 I 423
Cdd:cd07150 415 I 415
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-411 |
1.52e-13 |
|
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: 72.38 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQ---------ARGTPGvECLTPQvlTGDNGLTLIEna 124
Cdd:cd07120 42 RLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAIselryyaglARTEAG-RMIEPE--PGSFSLVLRE-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLlvtVANPDIDTAQRLF 204
Cdd:cd07120 117 PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIPSLPAGVVNL---FTESGSEGAAHLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:cd07120 194 ASPDVDVISFTGstatGRAIMAAAAPTL-KRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELM-RLMEDQQAVKL--TAAQAEQLQPLllknIDERGKGTVSRdWVGRDAGKIAAAI--------GLQVPAQTRLLF 349
Cdd:cd07120 273 IADEVRdRLAARLAAVKVgpGLDPASDMGPL----IDRANVDRVDR-MVERAIAAGAEVVlrggpvteGLAKGAFLRPTL 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 350 VETSATHPFAV-TELMMPVLPVVRVANVDEAIALAvtleggcHHT-----AAMHSRNIDNMNQMANAI 411
Cdd:cd07120 348 LEVDDPDADIVqEEIFGPVLTLETFDDEAEAVALA-------NDTdyglaASVWTRDLARAMRVARAI 408
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
54-415 |
2.13e-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: 72.00 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARG-TPGVECLTPQVLTGDNGLTLIEn 123
Cdd:cd07110 41 AERAKYLRAIAEGVRERREELAELEARDNGkpldeaawdVDDVAGCFEYYADLAEQlDAKAERAVPLPSEDFKARVRRE- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 aPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRaitlLNQAVVAAGGPANLLVTVANPDIDTAQRL 203
Cdd:cd07110 120 -PVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELE----LAEIAAEAGLPPGVLNVVTGTGDEAGAPL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 204 FKYPGIGLLVVTG----GEAVVEAARKhTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVD 279
Cdd:cd07110 195 AAHPGIDKISFTGstatGSQVMQAAAQ-DIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 280 SVADELM-RLMEDQQAVKLTAAQAE--QLQPLLLKNIDERGKGTVSRdwvGRDAGkIAAAIGLQVPAQTR-------LLF 349
Cdd:cd07110 274 SIADAFLeRLATAAEAIRVGDPLEEgvRLGPLVSQAQYEKVLSFIAR---GKEEG-ARLLCGGRRPAHLEkgyfiapTVF 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 350 VETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSI 415
Cdd:cd07110 350 ADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL--AAAVISRDAERCDRVAEALEAGI 413
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
125-401 |
5.64e-13 |
|
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: 70.74 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaAKKVSQRAITLLNqAVVAAGGPANLLVTVANPDIDTAQRLF 204
Cdd:cd07097 135 PLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP---AELTPASAWALVE-ILEEAGLPAGVFNLVMGSGSEVGQALV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNpPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:cd07097 211 EHPDVDAVSFTGstavGRRIAAAAAARGARVQLEMGGKN-PLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADE-LMRLMEDQQAVKLTAAQAEQLQ--PLLLKNIDERGKGTVSrdwVGRDAGKIAAAIGLQVPAQTR------LLFVE 351
Cdd:cd07097 290 IHDRfVEALVERTKALKVGDALDEGVDigPVVSERQLEKDLRYIE---IARSEGAKLVYGGERLKRPDEgyylapALFAG 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 647263436 352 TSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGchHTAAMHSRNI 401
Cdd:cd07097 367 VTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFG--LSAGIVTTSL 414
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
53-383 |
6.59e-13 |
|
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: 70.38 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 53 VAMRQQVIQAIREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARgtpgvECLTPQVLTGDNGLTLIEN 123
Cdd:cd07095 21 LEERAAILRRFAELLKANKEELARLISRETGkplweaqteVAAMAGKIDISIKAYH-----ERTGERATPMAQGRAVLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 APWGVVASVTPSTNPAAtVINNAI--SLIAaGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGgpanlLVTVANPDIDTAQ 201
Cdd:cd07095 96 RPHGVMAVFGPFNFPGH-LPNGHIvpALLA-GNTVVFKPSELTPAVAELMVELWEEAGLPPG-----VLNLVQGGRETGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 202 RLFKYPGIGLLVVTGGEAVVEAARK----HTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIV 277
Cdd:cd07095 169 ALAAHEGIDGLLFTGSAATGLLLHRqfagRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 278 VDS-VADELM-RLMEDQQAVK--------------LTAAQAEQLqpLLLKNIDERGKGTVSRDWVGRDAGKiaaaiGLQV 341
Cdd:cd07095 249 PDGaVGDAFLeRLVEAAKRLRigapdaeppfmgplIIAAAAARY--LLAQQDLLALGGEPLLAMERLVAGT-----AFLS 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 647263436 342 PAqtrLLFVETSATHPFAvtELMMPVLPVVRVANVDEAIALA 383
Cdd:cd07095 322 PG---IIDVTDAADVPDE--EIFGPLLQVYRYDDFDEAIALA 358
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-413 |
1.04e-12 |
|
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: 69.63 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVA-----QARGTPgvecLTPQ--VLTGDNG-LTLIENAPWG 127
Cdd:cd07152 37 RAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAigelhEAAGLP----TQPQgeILPSAPGrLSLARRVPLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 128 VVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkvsQRAIT---LLNQAVVAAGGPANLLvTVANPDIDTAQRLF 204
Cdd:cd07152 113 VVGVISPFNFPLILAMRSVAPALALGNAVVLKPDP------RTPVSggvVIARLFEEAGLPAGVL-HVLPGGADAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDEtADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:cd07152 186 EDPNVAMISFTGstavGRKVGEAAGRHLKKVSLELGGKNALIVLDD-ADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELMRLMEDqQAVKLT----AAQAEQLQPLllknIDErgkgtvsrdwvgRDAGKIAAAIGLQVPAQTRllfVETSATH 356
Cdd:cd07152 265 VADAYTAKLAA-KAKHLPvgdpATGQVALGPL----INA------------RQLDRVHAIVDDSVAAGAR---LEAGGTY 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647263436 357 P---FAVT--------------ELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07152 325 DglfYRPTvlsgvkpgmpafdeEIFGPVAPVTVFDSDEEAVALANDTEYGL--SAGIISRDVGRAMALADRLRT 396
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
52-304 |
1.20e-12 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 69.50 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 52 RVAMRQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARGT-------------PGVECLTPQVLTGDNGL 118
Cdd:PRK13968 49 NIDYRAQKLRDIGKALRARSEEMAQMITREMG---------KPINQARAEvaksanlcdwyaeHGPAMLKAEPTLVENQQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 119 TLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANLLVTVaNPDID 198
Cdd:PRK13968 120 AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ----LIAQVFKDAGIPQGVYGWL-NADND 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 199 TAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDEtADLPRAAEAIVRGASFDNNIICADEKV 274
Cdd:PRK13968 195 GVSQMINDSRIAAVTVTGsvraGAAIGAQAGAALKKCVLELGGSDPFIVLND-ADLELAVKAAVAGRYQNTGQVCAAAKR 273
|
250 260 270
....*....|....*....|....*....|.
gi 647263436 275 LIVVDSVADELM-RLMEDQQAVKLTAAQAEQ 304
Cdd:PRK13968 274 FIIEEGIASAFTeRFVAAAAALKMGDPRDEE 304
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
125-431 |
1.54e-12 |
|
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: 69.13 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAAtVI--NNAISLIaAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANlLVTVANPDIDTAQR 202
Cdd:cd07086 133 PLGVVGVITAFNFPVA-VPgwNAAIALV-CGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPG-VVNLVTGGGDGGEL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVV 278
Cdd:cd07086 210 LVHDPRVPLVSFTGstevGRRVGETVARR-FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVH 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADELMRlmedqqavKLTAAqAEQLQ---PLLLKN-----IDERGkgtVSRDWVGRDAGKIAAAIGL----QVPAQTR 346
Cdd:cd07086 289 ESVYDEFLE--------RLVKA-YKQVRigdPLDEGTlvgplINQAA---VEKYLNAIEIAKSQGGTVLtggkRIDGGEP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 347 LLFVE----TSATHPFAV--TELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQM--ANAIDTSIFVK 418
Cdd:cd07086 357 GNYVEptivTGVTDDARIvqEETFAPILYVIKFDSLEEAIAINNDVPQGL--SSSIFTEDLREAFRWlgPKGSDCGIVNV 434
|
330
....*....|....*.
gi 647263436 419 NGPCI---AGLGLGGE 431
Cdd:cd07086 435 NIPTSgaeIGGAFGGE 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
42-383 |
1.56e-12 |
|
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: 69.09 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 42 AAKVAQQGLKRVAM--RQQVIQAIREAGEKHARELAELAVTETG----MGRVEDKFAknVAQARGTPGVEcLTPQVLT-G 114
Cdd:cd07106 27 AAKAAFPGWSATPLeeRRAALLAIADAIEANAEELARLLTLEQGkplaEAQFEVGGA--VAWLRYTASLD-LPDEVIEdD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 115 DNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVvaaggPANLLVTVAN 194
Cdd:cd07106 104 DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVL-----PPGVLNVVSG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 195 PDiDTAQRLFKYPGIGLLVVTG----GEAVVEAARKhTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICA 270
Cdd:cd07106 179 GD-ELGPALTSHPDIRKISFTGstatGKKVMASAAK-TLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 271 DEKVLIVVDSVADELMRLMEDQ-------------------------QAVK--LTAAQAEQLQPLLLKNIDErGKG---- 319
Cdd:cd07106 257 AIKRLYVHESIYDEFCEALVALakaavvgdgldpgttlgpvqnkmqyDKVKelVEDAKAKGAKVLAGGEPLD-GPGyfip 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263436 320 -TVSRDwvgrdagkiaaaiglqVPAQTRLLFVEtsathPFAvtelmmPVLPVVRVANVDEAIALA 383
Cdd:cd07106 336 pTIVDD----------------PPEGSRIVDEE-----QFG------PVLPVLKYSDEDEVIARA 373
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
125-406 |
3.04e-12 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 68.42 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTVANPDIDTAQRLF 204
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEA----GLPAGVVNFVPGSGSEVGDYLV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTGGEAV-----VEAARKHTN----KRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVL 275
Cdd:PRK03137 247 DHPKTRFITFTGSREVglriyERAAKVQPGqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 IVVDSVADELM-RLMEDQQAVKL-TAAQAEQLQPLL-------LKNIDERGKGTvSRDWVG--RDAGK---IAAAIGLQV 341
Cdd:PRK03137 327 IVHEDVYDEVLeKVVELTKELTVgNPEDNAYMGPVInqasfdkIMSYIEIGKEE-GRLVLGgeGDDSKgyfIQPTIFADV 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263436 342 PAQTRLlfvetsathpfAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQ 406
Cdd:PRK03137 406 DPKARI-----------MQEEIFGPVVAFIKAKDFDHALEIANNTEYGL--TGAVISNNREHLEK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
54-413 |
3.73e-12 |
|
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: 68.10 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGMGRVEDKFAKNVAQA---RGT--PGVECLTPQVLTGdNGLTL-----IEN 123
Cdd:cd07098 40 AERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCekiRWTlkHGEKALRPESRPG-GLLMFykrarVEY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 APWGVVASVTPSTNPAATVINNAISLIAAGNSVVFaphpaakKVSQRA-------ITLLNQAVVAAGGPANlLVTVANPD 196
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV-------KVSEQVawssgffLSIIRECLAACGHDPD-LVQLVTCL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 197 IDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGAsFDN---NiiC 269
Cdd:cd07098 191 PETAEALTSHPVIDHITFIGsppvGKKVMAAAAESLTPVVLELG-GKDPAIVLDDADLDQIASIIMRGT-FQSsgqN--C 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 270 ADEKVLIVVDSVADELMRLMEDQqavkltaAQAEQLQPLLLKNID----------ERGKGTVsRDWVGRDAGKIAAAIGL 339
Cdd:cd07098 267 IGIERVIVHEKIYDKLLEILTDR-------VQALRQGPPLDGDVDvgamisparfDRLEELV-ADAVEKGARLLAGGKRY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 340 QVPAQ------TRLLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07098 339 PHPEYpqghyfPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL--GASVFGKDIKRARRIASQLET 416
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
125-411 |
1.58e-11 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 65.91 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaaKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLF 204
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKP----SEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:PRK10090 147 GNPKVAMVSMTGsvsaGEKIMAAAAKNITKVCLELG-GKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELM-RLMEDQQAVKL-TAAQAEQLQ--PLL----LKNIDERGKGTVSRDWVGRDAGKIAAAIGLQVPAQtrlLFVET 352
Cdd:PRK10090 226 IYDQFVnRLGEAMQAVQFgNPAERNDIAmgPLInaaaLERVEQKVARAVEEGARVALGGKAVEGKGYYYPPT---LLLDV 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 647263436 353 SATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAI 411
Cdd:PRK10090 303 RQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGL--TSSIYTQNLNVAMKAIKGL 359
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
125-380 |
3.70e-11 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 65.05 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAggpanlLVTVANPDIDTAQRLF 204
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS------YVRVIEGGVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPgIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:PTZ00381 183 KEP-FDHIFFTGsprvGKLVMQAAAENLTPCTLELG-GKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELMRLM---------EDQQAVK-----LTAAQAEQLQPLLlknidERGKGTVsrdWVGRDAGK----IAAAIGLQVp 342
Cdd:PTZ00381 261 IKDKFIEALkeaikeffgEDPKKSEdysriVNEFHTKRLAELI-----KDHGGKV---VYGGEVDIenkyVAPTIIVNP- 331
|
250 260 270
....*....|....*....|....*....|....*...
gi 647263436 343 aqtrllfvetSATHPFAVTELMMPVLPVVRVANVDEAI 380
Cdd:PTZ00381 332 ----------DLDSPLMQEEIFGPILPILTYENIDEVL 359
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
125-381 |
5.77e-11 |
|
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: 64.17 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVV-----FAPHPAAkkvsqraitlLNQAVVAAGGPANLlVTVANPDIDT 199
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAIlkpseLTPHTSA----------VIAKIIREAFDEDE-VAVFEGDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 200 AQRLFKYPgIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVL 275
Cdd:cd07134 169 AQALLELP-FDHIFFTGspavGKIVMAAAAKHLASVTLELG-GKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 IVVDSVADELMRLMEDQQAVKLTAAQAEQLQPLLLKNIDERGKGTVSR---DWVGRDAgKIAAaiGLQVPAQTRL----L 348
Cdd:cd07134 247 FVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGlldDAVAKGA-KVEF--GGQFDAAQRYiaptV 323
|
250 260 270
....*....|....*....|....*....|...
gi 647263436 349 FVETSATHPFAVTELMMPVLPVVRVANVDEAIA 381
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIE 356
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
125-381 |
6.91e-11 |
|
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: 64.08 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAKKVSQRaitLLNQAVVAAggpanlLVTVANPDIDTAQ 201
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSelaPATSALLAK---LIPKYFDPE------AVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 202 RLFKYPgIGLLVVTGGEA----VVEAARKHtnkrLIAA----GaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEK 273
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAvgkiVMEAAAKH----LTPVtlelG-GKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 274 VLIVVDSVADELMRLMedQQAVK----------------LTAAQAEQLQPLLlknidergkgtvsrdwvgrDAGKIaaAI 337
Cdd:cd07087 245 YVLVHESIKDELIEEL--KKAIKefygedpkespdygriINERHFDRLASLL-------------------DDGKV--VI 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 647263436 338 GLQVPAQTRL----LFVETSATHPFAVTELMMPVLPVVRVANVDEAIA 381
Cdd:cd07087 302 GGQVDKEERYiaptILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIE 349
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
125-413 |
8.89e-11 |
|
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: 63.87 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVfaphpaAKKVSQRAITLL--NQAVVAAGGPANLLVTVANPDIDTAQR 202
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV------LKPDSQTALTALwaVELLIEAGLPRDLWQVVTGPGSEVGGA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKypGIGLLVVTGGEAVVEAARKHTNKRLIAAGA---GNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVD 279
Cdd:cd07101 192 IVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLelgGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 280 SVADE-LMRLMEDQQAVKLTAAQA--EQLQPLllknIDERGKGTVSR---DWVGRDA-----GKIAAAIGLQVPAQTRLL 348
Cdd:cd07101 270 SVYDEfVRRFVARTRALRLGAALDygPDMGSL----ISQAQLDRVTAhvdDAVAKGAtvlagGRARPDLGPYFYEPTVLT 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647263436 349 FVETSAThpFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07101 346 GVTEDME--LFAEETFGPVVSIYRVADDDEAIELANDTDYGLN--ASVWTRDGARGRRIAARLRA 406
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
52-411 |
1.85e-10 |
|
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: 62.84 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 52 RVAMRQQVIQAIREAGEKHARELAELAVTETGMgRVEDKFAKNVAQARGT-----PGVECLTPQVLTGDNG-LTLIENAP 125
Cdd:cd07115 39 DPAERGRILWRLAELILANADELARLESLDTGK-PIRAARRLDVPRAADTfryyaGWADKIEGEVIPVRGPfLNYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 126 WGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTVANPDIDTAQRLFK 205
Cdd:cd07115 118 VGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEA----GFPAGVLNVVTGFGEVAGAALVE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 206 YPGIGLLVVTGGEAV----VEAArKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSV 281
Cdd:cd07115 194 HPDVDKITFTGSTAVgrkiMQGA-AGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 282 ADELM-RLMEDQQAVKL--TAAQAEQLQPLllknIDERGKGTVSrDWVGRDA---------GKIAAAIGLQVPAQtrlLF 349
Cdd:cd07115 273 YDEFLeRFTSLARSLRPgdPLDPKTQMGPL----VSQAQFDRVL-DYVDVGReegarlltgGKRPGARGFFVEPT---IF 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647263436 350 VETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAI 411
Cdd:cd07115 345 AAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGL--AAGVWTRDLGRAHRVAAAL 404
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
125-412 |
1.93e-10 |
|
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: 62.61 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANLLVTVANPDIDTAQRLF 204
Cdd:cd07149 123 PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSAL----KLAELLLEAGLPKGALNVVTGSGETVGDALV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTGGEAVVEA-ARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVAD 283
Cdd:cd07149 199 TDPRVRMISFTGSPAVGEAiARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 284 ELMRLMEDQ-QAVKLTAAQAEQ--LQPLllknIDERGKGTVSRdWV--------------GRDAGKIAAAIGLQVPAQTR 346
Cdd:cd07149 279 EFLERFVAAtKKLVVGDPLDEDtdVGPM----ISEAEAERIEE-WVeeaveggarlltggKRDGAILEPTVLTDVPPDMK 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 347 LlfvetsathpfAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAID 412
Cdd:cd07149 354 V-----------VCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ--AGVFTNDLQKALKAARELE 406
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
56-412 |
7.13e-10 |
|
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: 60.72 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARGTPGvecltpQVLTGD------NGLTL 120
Cdd:cd07147 45 RAAILLHCVARLEERFEELAETIVLEAGkpikdargeVARAIDTFRIAAEEATRIYG------EVLPLDisargeGRQGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaakkVSQRAIT--LLNQAVVAAGGPANLlVTVANPDID 198
Cdd:cd07147 119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP------ASRTPLSalILGEVLAETGLPKGA-FSVLPCSRD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 199 TAQRLFKYPGIGLLVVTGGEAV-----VEAARKHTNKRLiaagAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEK 273
Cdd:cd07147 192 DADLLVTDERIKLLSFTGSPAVgwdlkARAGKKKVVLEL----GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 274 VLIVVDSVADELMRLMedqqavkltAAQAEQLqplllKNIDERGKGT-----VSRDWVGRDAGKIAAAiglqVPAQTRLL 348
Cdd:cd07147 268 RVLVHRSVYDEFKSRL---------VARVKAL-----KTGDPKDDATdvgpmISESEAERVEGWVNEA----VDAGAKLL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 349 --------------FVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHhtAAMHSRNIDNMNQMANAID 412
Cdd:cd07147 330 tggkrdgalleptiLEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ--AGVFTRDLEKALRAWDELE 405
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
125-408 |
7.90e-10 |
|
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: 60.71 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAaggPANLlVTVANPDIDTAQRLF 204
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLL---PPED-VTLINGDGKTMQALL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTGGEAVVEAARKHTNK-RLIAAGAGNPPVVVDETADLPRA-AEAIVRGASFDNNIICADEKVLIVVDS-- 280
Cdd:cd07084 176 LHPNPKMVLFTGSSRVAEKLALDAKQaRIYLELAGFNWKVLGPDAQAVDYvAWQCVQDMTACSGQKCTAQSMLFVPENws 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 ---VADELMRLMEdQQAVKLTAAQAEQLQPLL--LKNIDERGKGTVSRDWVGRDAGKIAAAIGLQVPAQTRLLFVETSAT 355
Cdd:cd07084 256 ktpLVEKLKALLA-RRKLEDLLLGPVQTFTTLamIAHMENLLGSVLLFSGKELKNHSIPSIYGACVASALFVPIDEILKT 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 647263436 356 HPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGCHHTAAMHSRNIDNMNQMA 408
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELI 387
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
49-413 |
1.08e-09 |
|
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: 60.47 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 49 GLKRVAMRQQVIQAIREagekHARELAELAVTETG------MG------RVEDKFAKNVAQARGTpgvecltpQVLTGDN 116
Cdd:cd07107 40 PLERARMLRELATRLRE----HAEELALIDALDCGnpvsamLGdvmvaaALLDYFAGLVTELKGE--------TIPVGGR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 117 GLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhPAakkvsQRAITLLNQAVVAAGG-PANLLVTVANP 195
Cdd:cd07107 108 NLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP-PE-----QAPLSALRLAELAREVlPPGVFNILPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 196 DIDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDEtADLPRAAEAIVRGASFD-NNIICA 270
Cdd:cd07107 182 GATAGAALVRHPDVKRIALIGsvptGRAIMRAAAEGIKHVTLELGGKNALIVFPD-ADPEAAADAAVAGMNFTwCGQSCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 271 DEKVLIVVDSVADELMRLMEDQQA---VKLTAAQAEQLQPLL--------LKNIDERGKGTVSRDWVGRDAGKIAAAIGL 339
Cdd:cd07107 261 STSRLFVHESIYDEVLARVVERVAaikVGDPTDPATTMGPLVsrqqydrvMHYIDSAKREGARLVTGGGRPEGPALEGGF 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647263436 340 QVPAQtrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07107 341 YVEPT---VFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGL--TAAIWTNDISQAHRTARRVEA 409
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
125-432 |
1.38e-09 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 59.92 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPhpaakkVSQRAITLLNQAVVA--AGGPANLLVTVANPDIDTAQR 202
Cdd:PRK11241 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP------ASQTPFSALALAELAirAGIPAGVFNVVTGSAGAVGGE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVV 278
Cdd:PRK11241 220 LTSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLELG-GNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADELMRLMedQQAV-KLTAAQAEQLQPLLLKNIDERGKGTVSR---DWVGRDA----GKIAAAIGLQVPAQTrlLFV 350
Cdd:PRK11241 299 DGVYDRFAEKL--QQAVsKLHIGDGLEKGVTIGPLIDEKAVAKVEEhiaDALEKGArvvcGGKAHELGGNFFQPT--ILV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 351 ETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKNGPCIA------ 424
Cdd:PRK11241 375 DVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL--AAYFYARDLSRVFRVGEALEYGIVGINTGIISnevapf 452
|
330
....*....|..
gi 647263436 425 ----GLGLGGEG 432
Cdd:PRK11241 453 ggikASGLGREG 464
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
54-430 |
2.62e-09 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 59.36 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARGTPGVEClTPQVLTGDNGLTLIENA 124
Cdd:PLN02467 72 AVRAKYLRAIAAKITERKSELAKLETLDCGkpldeaawdMDDVAGCFEYYADLAEALDAKQK-APVSLPMETFKGYVLKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAkkvsqrAITLLNQAVVA--AGGPANLLVTVANPDIDTAQR 202
Cdd:PLN02467 151 PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELA------SVTCLELADICreVGLPPGVLNVVTGLGTEAGAP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTGGEAvveaarkhTNKRLIAAGA-----------GNPPVVVDETADLPRAAEAIVRGASFDNNIICAD 271
Cdd:PLN02467 225 LASHPGVDKIAFTGSTA--------TGRKIMTAAAqmvkpvslelgGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 272 EKVLIVVDSVADE-LMRLMEDQQAVKLTAAQAE--QLQPLLLKNIDERGKGTVSrdwVGRDAGKIAAAIGLQVPAQTRLL 348
Cdd:PLN02467 297 TSRLLVHERIASEfLEKLVKWAKNIKISDPLEEgcRLGPVVSEGQYEKVLKFIS---TAKSEGATILCGGKRPEHLKKGF 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 349 FVEtsATHPFAVT--------ELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSIFVKN- 419
Cdd:PLN02467 374 FIE--PTIITDVTtsmqiwreEVFGPVLCVKTFSTEDEAIELANDSHYGL--AGAVISNDLERCERVSEAFQAGIVWINc 449
|
410
....*....|..
gi 647263436 420 -GPCIAGLGLGG 430
Cdd:PLN02467 450 sQPCFCQAPWGG 461
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
56-415 |
2.99e-09 |
|
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: 58.72 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG---------MGRVEDKFAKNVAQARGTPGvecltpQVLTGDNG--LTLIENA 124
Cdd:cd07114 45 RGKLLRRLADLIEANAEELAELETRDNGkliretraqVRYLAEWYRYYAGLADKIEG------AVIPVDKGdyLNFTRRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKkvsqrAITL-LNQAVVAAGGPANLLVTVANPDIDTAQRL 203
Cdd:cd07114 119 PLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP-----ASTLeLAKLAEEAGFPPGVVNVVTGFGPETGEAL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 204 FKYPGIGLLVVTGGEAVVEAARKHTNKRLIAAGA---GNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:cd07114 194 VEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLelgGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELM-RLMEDQQAVKL--TAAQAEQLQPLLLKNIDERGKGTVSRdwvGRDAGKIAAAIG--LQVPAQTRLLFVE---- 351
Cdd:cd07114 274 IYDEFVeRLVARARAIRVgdPLDPETQMGPLATERQLEKVERYVAR---AREEGARVLTGGerPSGADLGAGYFFEptil 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 352 --TSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSI 415
Cdd:cd07114 351 adVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGL--AAGIWTRDLARAHRVARAIEAGT 414
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
113-411 |
5.91e-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: 57.92 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 113 TGDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAvvaaGGPANLLVTV 192
Cdd:cd07143 132 TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 193 ANPDIDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNII 268
Cdd:cd07143 208 SGYGRTCGNAISSHMDIDKVAFTGstlvGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 269 CADEKVLIVVDSVADELMRLMEDQ-QAVKL---------TAAQAEQLQPLLLKNIDERGKGTVSRDWVGrdaGKIAAAIG 338
Cdd:cd07143 288 CCAGSRIYVQEGIYDKFVKRFKEKaKKLKVgdpfaedtfQGPQVSQIQYERIMSYIESGKAEGATVETG---GKRHGNEG 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263436 339 LQVPAQtrlLFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAI 411
Cdd:cd07143 365 YFIEPT---IFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGL--AAAVFTNNINNAIRVANAL 432
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
96-411 |
5.46e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 54.89 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 96 AQARGTPGVECLtPQVLTGDNGLTLienAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLL 175
Cdd:cd07125 142 AQARELFSDPEL-PGPTGELNGLEL---HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 176 NQavvaAGGPANLLVTVANPDIDTAQRLFKYPGIGLLVVTGGEAVVE------AARKHTNKRLIAAGAGNPPVVVDETAD 249
Cdd:cd07125 218 HE----AGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKlinralAERDGPILPLIAETGGKNAMIVDSTAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 250 LPRAAEAIVRGAsFDNniicADEK-----VLIVVDSVADELMRLMEDqqavkltaaQAEQLQ---PLLLKN-----IDEr 316
Cdd:cd07125 294 PEQAVKDVVQSA-FGS----AGQRcsalrLLYLQEEIAERFIEMLKG---------AMASLKvgdPWDLSTdvgplIDK- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 317 gkgtvsrdwvgrDAGKIAAAIGLQVPAQTRLLF------------------VETSATHPfavTELMMPVLPVVR--VANV 376
Cdd:cd07125 359 ------------PAGKLLRAHTELMRGEAWLIApaplddgngyfvapgiieIVGIFDLT---TEVFGPILHVIRfkAEDL 423
|
330 340 350
....*....|....*....|....*....|....*
gi 647263436 377 DEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAI 411
Cdd:cd07125 424 DEAIEDINATGYGL--TLGIHSRDEREIEYWRERV 456
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
121-383 |
6.23e-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: 54.53 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPAnlLVTVANPDIDTA 200
Cdd:cd07135 104 IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAA----LLAELVPKYLDPD--AFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 201 QRLFKYpGIGLLVVTGGEAV----VEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIIC-ADEKVL 275
Cdd:cd07135 178 TALLEQ-KFDKIFYTGSGRVgriiAEAAAKHLTPVTLELG-GKSPVIVTKNADLELAAKRILWGKFGNAGQICvAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 276 I---VVDSVADELMRLMED---QQAVKLTA-------AQAEQLQPLLlknidERGKGTVSrdwVG--RDAGK--IAAAIG 338
Cdd:cd07135 256 VdpsVYDEFVEELKKVLDEfypGGANASPDytrivnpRHFNRLKSLL-----DTTKGKVV---IGgeMDEATrfIPPTIV 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 647263436 339 LQVPAQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEAIALA 383
Cdd:cd07135 328 SDVSWDDSLM-----------SEELFGPVLPIIKVDDLDEAIKVI 361
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-383 |
7.45e-08 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 54.58 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGMGRVEDkfAKNVAQARGTPGVECLTPQVLTGD------NGLTLIENAPWGVV 129
Cdd:PRK09457 61 RQAIVERFAALLEENKEELAEVIARETGKPLWEA--ATEVTAMINKIAISIQAYHERTGEkrsemaDGAAVLRHRPHGVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 130 ASVTPSTNPAAtVINNAI--SLIAaGNSVVFAPHPAAKKVSQRAITLLNQAVVAAgGPANLLVTvanpDIDTAQRLFKYP 207
Cdd:PRK09457 139 AVFGPYNFPGH-LPNGHIvpALLA-GNTVVFKPSELTPWVAELTVKLWQQAGLPA-GVLNLVQG----GRETGKALAAHP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 208 GIGLLVVTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSV-A 282
Cdd:PRK09457 212 DIDGLLFTGsantGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 283 DELM-RLMEDQQAVKLTAAQAEQlQPLLLKNIDERgkgtvsrdwvgrdagkiaAAIGLqVPAQTRLL---------FVET 352
Cdd:PRK09457 292 DAFLaRLVAVAKRLTVGRWDAEP-QPFMGAVISEQ------------------AAQGL-VAAQAQLLalggkslleMTQL 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 647263436 353 SATHPFA------VT--------ELMMPVLPVVRVANVDEAIALA 383
Cdd:PRK09457 352 QAGTGLLtpgiidVTgvaelpdeEYFGPLLQVVRYDDFDEAIRLA 396
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
51-414 |
9.86e-08 |
|
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: 53.96 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 51 KRVAMRQQVIQAIREagekHARELAELAVTETGM----GRVE--------DKFAKNVAQARGTPGVECLTPqvlTGDNGL 118
Cdd:cd07148 45 ERIAILERLADLMEE----RADELALLIAREGGKplvdAKVEvtraidgvELAADELGQLGGREIPMGLTP---ASAGRI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 119 TLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGgpanlLVTVANPDID 198
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEG-----WCQAVPCENA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 199 TAQRLFKYPGIGLLVVTGGEAVVEAARKHtnkrlIAAGA-------GNPPVVVDETADLPRAAEAIVRGASFDNNIICAD 271
Cdd:cd07148 193 VAEKLVTDPRVAFFSFIGSARVGWMLRSK-----LAPGTrcalehgGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 272 EKVLIVVDSVADELMRLMEDqQAVKLTAAQA----EQLQPLLLKNIDERgkgtvSRDWVgRDA----GKI---AAAIGLQ 340
Cdd:cd07148 268 VQRVFVPAEIADDFAQRLAA-AAEKLVVGDPtdpdTEVGPLIRPREVDR-----VEEWV-NEAvaagARLlcgGKRLSDT 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647263436 341 VPAQTRLLFVETSAThpFAVTELMMPVLPVVRVANVDEAIALAVTLEggCHHTAAMHSRNIDNMNQMANAIDTS 414
Cdd:cd07148 341 TYAPTVLLDPPRDAK--VSTQEIFGPVVCVYSYDDLDEAIAQANSLP--VAFQAAVFTKDLDVALKAVRRLDAT 410
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
54-383 |
1.00e-07 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 54.15 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 54 AMRQQVIQAIREAGEKHARELAELAVTETGMGR---VEDKFAKNVAQARGTPG-VECLTPQVlTGD--NGLT-LIENAPW 126
Cdd:PRK13473 61 KERAEALLKLADAIEENADEFARLESLNCGKPLhlaLNDEIPAIVDVFRFFAGaARCLEGKA-AGEylEGHTsMIRRDPV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 127 GVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPHPaakkvsQRAITLLNQAVVAAGG-PANLLVTVANPDIDTAQR 202
Cdd:PRK13473 140 GVVASIAPWNYPlmmAAWKLAPAL---AAGNTVVLKPSE------ITPLTALKLAELAADIlPPGVLNVVTGRGATVGDA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 203 LFKYPGIGLLVVTG----GEAVVEAARKHTnKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVV 278
Cdd:PRK13473 211 LVGHPKVRMVSLTGsiatGKHVLSAAADSV-KRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 279 DSVADELM-RLMEDQQAVKLTAAQAEQ--LQPLLLKNIDERGKGTVSRdwvGRDAGKIAAAIGLQVPAQTRLLF---VET 352
Cdd:PRK13473 290 RGIYDDLVaKLAAAVATLKVGDPDDEDteLGPLISAAHRDRVAGFVER---AKALGHIRVVTGGEAPDGKGYYYeptLLA 366
|
330 340 350
....*....|....*....|....*....|...
gi 647263436 353 SATHPFAVT--ELMMPVLPVVRVANVDEAIALA 383
Cdd:PRK13473 367 GARQDDEIVqrEVFGPVVSVTPFDDEDQAVRWA 399
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
118-413 |
3.48e-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: 52.46 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 118 LTLIENAPWGVVASVTPSTNP---AATVINNAIsliAAGNSVVFAPHpaakkvSQRAITLLNQA-VVAAGGPANLLVTVA 193
Cdd:cd07117 129 LSIVLREPIGVVGQIIPWNFPflmAAWKLAPAL---AAGNTVVIKPS------STTSLSLLELAkIIQDVLPKGVVNIVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 194 NPDIDTAQRLFKYPGIGLLVVTGGEAVVEAARKHTNKRLIAAG---AGNPPVVVDETADLPRAAEAIVRGASFDNNIICA 270
Cdd:cd07117 200 GKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATlelGGKSANIIFDDANWDKALEGAQLGILFNQGQVCC 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 271 DEKVLIVVDSVADELM-RLMEDQQAVKLTAAQAEQLQplLLKNIDERGKGTVsRDWVgrDAGKIAAA---IGLQVPAQTR 346
Cdd:cd07117 280 AGSRIFVQEGIYDEFVaKLKEKFENVKVGNPLDPDTQ--MGAQVNKDQLDKI-LSYV--DIAKEEGAkilTGGHRLTENG 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647263436 347 L---------LFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDT 413
Cdd:cd07117 355 LdkgffieptLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGL--GGGVFTKDINRALRVARAVET 428
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
56-430 |
3.68e-07 |
|
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: 52.36 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG-----MGRVEDKFAKNVAQARGTPGVECLTPQVLTGDNGLTLIENAPWGVVA 130
Cdd:cd07108 43 RGKLLARIADALEARSEELARLLALETGnalrtQARPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 131 SVTPSTNPAATVINNAISLIAAGNSVVFaphpaakKVSQRA--ITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYPG 208
Cdd:cd07108 123 AILPWNAPLMLAALKIAPALVAGNTVVL-------KAAEDAplAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 209 IGLLVVTGGEAVVEAARKHTNKRLIAAG---AGNPPVVVDETADLPRAAEAIVRGASFD-NNIICADEKVLIVVDSVADE 284
Cdd:cd07108 196 VDKVTFTGSTEVGKIIYRAAADRLIPVSlelGGKSPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 285 -LMRLMEDQQAVKLTaaqaeqlQPLLLKN-----IDERGKGTVSrDWV--GRDAGKIAAAIGLQVPAQTRL--------- 347
Cdd:cd07108 276 fLEKLVAKLSKLKIG-------DPLDEATdigaiISEKQFAKVC-GYIdlGLSTSGATVLRGGPLPGEGPLadgffvqpt 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 348 LFVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSiFV---KNGPCIA 424
Cdd:cd07108 348 IFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL--AAYVWTRDLGRALRAAHALEAG-WVqvnQGGGQQP 424
|
....*.
gi 647263436 425 GLGLGG 430
Cdd:cd07108 425 GQSYGG 430
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
56-413 |
5.07e-07 |
|
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: 51.66 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETGmgrvedkfaKNVAQARG--TPGVECL----------TPQVLTGDNG----LT 119
Cdd:cd07103 43 RAAILRRWADLIRERAEDLARLLTLEQG---------KPLAEARGevDYAASFLewfaeearriYGRTIPSPAPgkriLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 120 LIEnaPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAkkvsqrAItLLNQAVVAAGGPA---NLLVTVA 193
Cdd:cd07103 114 IKQ--PVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAeetPLS------AL-ALAELAEEAGLPAgvlNVVTGSP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 194 NpdiDTAQRLFKYPGIGLLVVTGGEAVveaarkhtNKRLIAAGA-----------GNPPVVVDETADLPRAAEAIVrGAS 262
Cdd:cd07103 185 A---EIGEALCASPRVRKISFTGSTAV--------GKLLMAQAAdtvkrvslelgGNAPFIVFDDADLDKAVDGAI-ASK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 263 FDNN---IICADEkvLIVVDSVADELM-RLMEDQQAVKLTAAQAE--QLQPLllknIDERGKGTVSR---DWVGRDA--- 330
Cdd:cd07103 253 FRNAgqtCVCANR--IYVHESIYDEFVeKLVERVKKLKVGNGLDEgtDMGPL----INERAVEKVEAlveDAVAKGAkvl 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 331 --GKIAAAIGL--------QVPAQTRLLFVETsathpFAvtelmmPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRN 400
Cdd:cd07103 327 tgGKRLGLGGYfyeptvltDVTDDMLIMNEET-----FG------PVAPIIPFDTEDEVIARANDTPYGL--AAYVFTRD 393
|
410
....*....|...
gi 647263436 401 IDNMNQMANAIDT 413
Cdd:cd07103 394 LARAWRVAEALEA 406
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
125-290 |
7.20e-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: 51.45 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQavvaAGGPANLLVTVANPDIDTAQRLF 204
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE----AGFPAGTIQLLPGRGADVGAALT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTGGEAVVEAARKHTNKR------LIAAGAGNPPVVVDETAdLPRAAEAIVRGASFDN-NIICADEKVLIV 277
Cdd:TIGR01238 236 SDPRIAGVAFTGSTEVAQLINQTLAQRedapvpLIAETGGQNAMIVDSTA-LPEQVVRDVLRSAFDSaGQRCSALRVLCV 314
|
170
....*....|...
gi 647263436 278 VDSVADELMRLME 290
Cdd:TIGR01238 315 QEDVADRVLTMIQ 327
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
43-284 |
1.53e-06 |
|
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: 50.26 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 43 AKVAQQGLKR--VAMRQQVIQAIREAGEKHARELAELAVTETGMGRVEDK-------------FAKNVAQARGtpgvECL 107
Cdd:cd07093 28 AKEAFPGWSRmsPAERARILHKVADLIEARADELALLESLDTGKPITLARtrdipraaanfrfFADYILQLDG----ESY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 108 TPQvltgDNGLTLIENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPaakkVSQRAITLLNQAVVAAGGPAN 187
Cdd:cd07093 104 PQD----GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE----WTPLTAWLLAELANEAGLPPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 188 LLVTVANPDIDTAQRLFKYPGIGLLVVTG----GEAVVEAARKHtNKRLIAAGAGNPPVVVDETADLPRAAEAIVRgASF 263
Cdd:cd07093 176 VVNVVHGFGPEAGAALVAHPDVDLISFTGetatGRTIMRAAAPN-LKPVSLELGGKNPNIVFADADLDRAVDAAVR-SSF 253
|
250 260
....*....|....*....|..
gi 647263436 264 DNN-IICADEKVLIVVDSVADE 284
Cdd:cd07093 254 SNNgEVCLAGSRILVQRSIYDE 275
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
125-383 |
1.79e-06 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 50.26 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQA--------VVAAGGPanllvTVANPD 196
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAglprdlwqVVTGPGP-----VVGTAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 197 IDTAQrlfkYpgiglLVVTG----GEAVVEAArkhtNKRLIAAGA---GNPPVVVDETADLPRAAEAIVRGAsFDNN-II 268
Cdd:PRK09407 229 VDNAD----Y-----LMFTGstatGRVLAEQA----GRRLIGFSLelgGKNPMIVLDDADLDKAAAGAVRAC-FSNAgQL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 269 CADEKVLIVVDSVADE-LMRLMEDQQAVKLTAA--QAEQLQPLllknIDERGKGTVSR---DWVGRDA-----GKIAAAI 337
Cdd:PRK09407 295 CISIERIYVHESIYDEfVRAFVAAVRAMRLGAGydYSADMGSL----ISEAQLETVSAhvdDAVAKGAtvlagGKARPDL 370
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 647263436 338 GlqvPaqtrlLFVE----TSATHPFAV--TELMMPVLPVVRVANVDEAIALA 383
Cdd:PRK09407 371 G---P-----LFYEptvlTGVTPDMELarEETFGPVVSVYPVADVDEAVERA 414
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
150-383 |
2.61e-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: 49.78 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 150 IAAGNSVVFAPHPAAkkVSQRAITL-LNQAVVAAGGPANLLVTVA--NPDIDTAQRLFKYPGIGLLVVTGGEAVVEAARK 226
Cdd:cd07127 218 LATGNPVIVKPHPAA--ILPLAITVqVAREVLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 227 H-TNKRLIAAGAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIV-------------VDSVADELMR----- 287
Cdd:cd07127 296 NaRQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddgrksFDEVAADLAAaidgl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 288 LMEDQQAVKLTAA-QAeqlqPLLLKNIDE-RGKGTVSRDWVGRDAGKIAAAIglqvpAQTRLLFVETSATHPFAVTELMM 365
Cdd:cd07127 376 LADPARAAALLGAiQS----PDTLARIAEaRQLGEVLLASEAVAHPEFPDAR-----VRTPLLLKLDASDEAAYAEERFG 446
|
250
....*....|....*...
gi 647263436 366 PVLPVVRVANVDEAIALA 383
Cdd:cd07127 447 PIAFVVATDSTDHSIELA 464
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
68-412 |
1.32e-05 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 47.44 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 68 EKHARELAELAVTETG----MGRVEDkFAKNVAQARGTPGV------ECLTPQV--LTGDNGLTLIENAPWGVVASVTPS 135
Cdd:cd07113 74 EQHGEELAQLETLCSGksihLSRAFE-VGQSANFLRYFAGWatkingETLAPSIpsMQGERYTAFTRREPVGVVAGIVPW 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 136 TNPAATVINNAISLIAAGNSVVFAPHPAAkkvsqrAITLLNQAVVA--AGGPANLLvTVANPDIDTAQRLFKYPGIGLLV 213
Cdd:cd07113 153 NFSVMIAVWKIGAALATGCTIVIKPSEFT------PLTLLRVAELAkeAGIPDGVL-NVVNGKGAVGAQLISHPDVAKVS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 214 VTG----GEAVVEAARKHTNKRLIAAGAGNPPVVVdETADLPRAAEAIVRGASFDNNIICADEKVLIVVDSVADELMRLM 289
Cdd:cd07113 226 FTGsvatGKKIGRQAASDLTRVTLELGGKNAAAFL-KDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 290 EDQ-QAVKLTAAQAEQLQPLLLKNIDERGKGTVSRDWVGRDAGKIAAaiGLQVPAQTRlLFVETSATHPFAVTELMM--- 365
Cdd:cd07113 305 KQAlSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVR--GGEALAGEG-YFVQPTLVLARSADSRLMree 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 647263436 366 ---PVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAID 412
Cdd:cd07113 382 tfgPVVSFVPYEDEEELIQLINDTPFGL--TASVWTNNLSKALRYIPRIE 429
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
125-382 |
1.73e-05 |
|
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: 47.11 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVvaaggPANLlVTVANPDIDTAQRL- 203
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEY-VAVVEGGVEENQELl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 204 ---FKYpgiglLVVTGGEAV----VEAARKHtnkrLIAA----GaGNPPVVVDETADLPRAAEAIVRGaSFDN---NIIC 269
Cdd:cd07136 174 dqkFDY-----IFFTGSVRVgkivMEAAAKH----LTPVtlelG-GKSPCIVDEDANLKLAAKRIVWG-KFLNagqTCVA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 270 ADekVLIVVDSVADELMRLMEdQQAVKLTAAQAEQlQPLLLKNIDE----RGKGTVsrdwvgrDAGKIaaAIGLQVPAQT 345
Cdd:cd07136 243 PD--YVLVHESVKEKFIKELK-EEIKKFYGEDPLE-SPDYGRIINEkhfdRLAGLL-------DNGKI--VFGGNTDRET 309
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 647263436 346 RL----LFVETSATHPFAVTELMMPVLPVVRVANVDEAIAL 382
Cdd:cd07136 310 LYieptILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEI 350
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
56-415 |
1.83e-05 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 46.99 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 56 RQQVIQAIREAGEKHARELAELAVTETG------MGRVE------DKFAKNVAQARGTpgvecLTPQVLTgdNGLTLIEN 123
Cdd:PLN02278 86 RSKILRRWYDLIIANKEDLAQLMTLEQGkplkeaIGEVAygasflEYFAEEAKRVYGD-----IIPSPFP--DRRLLVLK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 124 APWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHpaakkvSQRAITLLNQAVVA--AGGPANLL--VTVANPDIDT 199
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPS------ELTPLTALAAAELAlqAGIPPGVLnvVMGDAPEIGD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 200 AqrLFKYPGIGLLVVTGGEAV---VEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAEAIVrGASFDN---NIICADEk 273
Cdd:PLN02278 233 A--LLASPKVRKITFTGSTAVgkkLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGAL-ASKFRNsgqTCVCANR- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 274 vLIVVDSVADELmrlmedqqAVKLTAAqAEQLQ------------PLL----LKNIDERGKGTVSRDWVGRDAGKiAAAI 337
Cdd:PLN02278 309 -ILVQEGIYDKF--------AEAFSKA-VQKLVvgdgfeegvtqgPLIneaaVQKVESHVQDAVSKGAKVLLGGK-RHSL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263436 338 GLQVPAQTRLlfVETSATHPFAVTELMMPVLPVVRVANVDEAIALAVTLEGGChhTAAMHSRNIDNMNQMANAIDTSI 415
Cdd:PLN02278 378 GGTFYEPTVL--GDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGL--AAYIFTRDLQRAWRVSEALEYGI 451
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
121-381 |
2.61e-05 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 46.32 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVV-----FAPHPAAkkvsqraitLLNQAVVAAGGPAnlLVTVANP 195
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMikpseFTPRTSA---------LLAELLAEYFDED--EVAVVTG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 196 DIDTAQRLFKYPgIGLLVVTGGEAVveaarkhtnKRLIAAGA------------GNPPVVVDETADLPRAAEAIVRGASF 263
Cdd:cd07133 166 GADVAAAFSSLP-FDHLLFTGSTAV---------GRHVMRAAaenltpvtlelgGKSPAIIAPDADLAKAAERIAFGKLL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 264 DNNIIC-ADEKVLIVVDSVadelmrlmedQQAVKLTAAQAEQLQPLLLKNID----------ERGKGTVSrdwvgrDAGK 332
Cdd:cd07133 236 NAGQTCvAPDYVLVPEDKL----------EEFVAAAKAAVAKMYPTLADNPDytsiinerhyARLQGLLE------DARA 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263436 333 IAAAIgLQVPAQTRLLfvetSATHPFAVT--------------ELMMPVLPVVRVANVDEAIA 381
Cdd:cd07133 300 KGARV-IELNPAGEDF----AATRKLPPTlvlnvtddmrvmqeEIFGPILPILTYDSLDEAID 357
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
148-388 |
6.86e-05 |
|
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: 45.22 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 148 SLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYPGIGLLVVTGGEAVVEAarkh 227
Cdd:cd07129 130 SALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRA---- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 228 tnkrLIAAGAGNP-------------PVVVDETAdLPRAAEAIVRG--ASFDNNI--ICADEKVLIVVDSVADELMRlme 290
Cdd:cd07129 206 ----LFDAAAARPepipfyaelgsvnPVFILPGA-LAERGEAIAQGfvGSLTLGAgqFCTNPGLVLVPAGPAGDAFI--- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 291 dQQAVKLTAAQAEqlQPLLLKNIDERGKGTVSRdWVGRDAGKIAAAIGLQVPAQTR--LLFVETSAT---HPFAVTELMM 365
Cdd:cd07129 278 -AALAEALAAAPA--QTMLTPGIAEAYRQGVEA-LAAAPGVRVLAGGAAAEGGNQAapTLFKVDAAAflaDPALQEEVFG 353
|
250 260
....*....|....*....|...
gi 647263436 366 PVLPVVRVANVDEAIALAVTLEG 388
Cdd:cd07129 354 PASLVVRYDDAAELLAVAEALEG 376
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
115-297 |
1.87e-04 |
|
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: 43.58 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 115 DNGLTLIEN-APWGVVASVTPStNPAATVInnAISL-IAAGNSVVF-----APHpaakkvSQRAI-TLLNQAVVAAGGPA 186
Cdd:cd07079 98 PNGLQIEKVrVPLGVIGIIYES-RPNVTVD--AAALcLKSGNAVILrggseALH------SNRALvEIIQEALEEAGLPE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 187 NLLVTVANPDIDTAQRLFKYPG-IGLLVVTGGEAVVEAARKHTNKRLIAAGAGNPPVVVDETADLPRAAeAIVRGASFDN 265
Cdd:cd07079 169 DAVQLIPDTDREAVQELLKLDDyIDLIIPRGGAGLIRFVVENATIPVIKHGDGNCHVYVDESADLEMAV-RIVVNAKTQR 247
|
170 180 190
....*....|....*....|....*....|....*.
gi 647263436 266 NIIC-ADEKVLI---VVDSVADELMRLMEDQQaVKL 297
Cdd:cd07079 248 PSVCnALETLLVhrdIAEEFLPKLAEALREAG-VEL 282
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
125-383 |
2.18e-04 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 43.57 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNsVVFAPHpaAKKVSQRAItLLNQAVVAAGGPANLLVTVANPDiDTAQRLF 204
Cdd:PRK09406 123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGN-VGLLKH--ASNVPQTAL-YLADLFRRAGFPDGCFQTLLVGS-GAVEAIL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIVVDS 280
Cdd:PRK09406 198 RDPRVAAATLTGsepaGRAVAAIAGDEIKKTVLELG-GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHAD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 281 VADELM-RLMEDQQAVKL--TAAQAEQLQPLllknIDERGKGTVSRdwVGRDAGKIAAAI--GLQVPAQTRLLF---VET 352
Cdd:PRK09406 277 VYDAFAeKFVARMAALRVgdPTDPDTDVGPL----ATEQGRDEVEK--QVDDAVAAGATIlcGGKRPDGPGWFYpptVIT 350
|
250 260 270
....*....|....*....|....*....|...
gi 647263436 353 SATHPFAV--TELMMPVLPVVRVANVDEAIALA 383
Cdd:PRK09406 351 DITPDMRLytEEVFGPVASLYRVADIDEAIEIA 383
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
121-379 |
2.33e-04 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 43.50 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQRAITLLNQAVvaagGPANLLVTVANPDIDTA 200
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYL----DSSAVRVVEGAVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 201 QRLFKYPGIgllVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGASFDNN---------I 267
Cdd:PLN02174 184 LLEQKWDKI---FYTGsskiGRVIMAAAAKHLTPVVLELG-GKSPVVVDSDTDLKVTVRRIIAGKWGCNNgqacispdyI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 268 ICADEKVLIVVDSVADELMRL-----MEDQQAVKL-TAAQAEQLQPLL-LKNIDERGKGTVSRDwvgRDAGKIAAAIGLQ 340
Cdd:PLN02174 260 LTTKEYAPKVIDAMKKELETFygknpMESKDMSRIvNSTHFDRLSKLLdEKEVSDKIVYGGEKD---RENLKIAPTILLD 336
|
250 260 270
....*....|....*....|....*....|....*....
gi 647263436 341 VPAQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEA 379
Cdd:PLN02174 337 VPLDSLIM-----------SEEIFGPLLPILTLNNLEES 364
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
125-296 |
2.34e-04 |
|
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: 43.45 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 125 PWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPHPAAKKVSQraitLLNQAVVAAGGPANlLVTVANPDIDTAQRLF 204
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL----LLAEILTEAGLPDG-VFNVVQGGGETGQLLC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 205 KYPGIGLLVVTG----GEAVVEAAR---KHTNKRLiaagAGNPPVVVDETADLPRAAEAIVRGASFDNNIICADEKVLIV 277
Cdd:cd07090 191 EHPDVAKVSFTGsvptGKKVMSAAAkgiKHVTLEL----GGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFV 266
|
170 180
....*....|....*....|
gi 647263436 278 VDSVADE-LMRLMEDQQAVK 296
Cdd:cd07090 267 QRSIKDEfTERLVERTKKIR 286
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
121-382 |
2.38e-04 |
|
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: 43.55 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 121 IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVVFAPH---PAAKKVSQRAIT--LLNQAV-VAAGGPAnllVTVAN 194
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSelaPATSALLAKLIPeyLDTKAIkVIEGGVP---ETTAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 195 PDidtaQRLFKypgiglLVVTG----GEAVVEAARKHTNKRLIAAGaGNPPVVVDETADLPRAAEAIVRGA-SFDNNIIC 269
Cdd:cd07137 174 LE----QKWDK------IFFTGsprvGRIIMAAAAKHLTPVTLELG-GKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQAC 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 270 ADEKVLIVVDSVADELMRLM---------EDQQAVKLTAAQAEQLQPLLLKNIDERGKgtVSRDWV---GRDAGK--IAA 335
Cdd:cd07137 243 IAPDYVLVEESFAPTLIDALkntlekffgENPKESKDLSRIVNSHHFQRLSRLLDDPS--VADKIVhggERDEKNlyIEP 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 647263436 336 AIGLQVPAQTRLLfvetsathpfaVTELMMPVLPVVRVANVDEAIAL 382
Cdd:cd07137 321 TILLDPPLDSSIM-----------TEEIFGPLLPIITVKKIEESIEI 356
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
168-258 |
6.69e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.90 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263436 168 SQRAI-TLLNQAVVAAGGPANLLVTVANPDIDTAQRLFKYPG-IGLLVVTGGEAVVEAARKHTNKRLIAAGAGNPPVVVD 245
Cdd:PRK00197 155 SNRALvAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRRVVENATVPVIEHGDGICHIYVD 234
|
90
....*....|...
gi 647263436 246 ETADLPRAAEAIV 258
Cdd:PRK00197 235 ESADLDKALKIVL 247
|
|
| |
