|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
1-464 |
0e+00 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 708.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 1 MDEKLIESIVREVAKNINIIESGNSSCNT--LGVFDSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSV 78
Cdd:PRK15398 1 MNQQDIEQVVKAVLAEMLSSQTVSPPAAVgeMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 79 MTVEESKMGRVEDKINKNTLAIERCTGVEDLKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSV 158
Cdd:PRK15398 81 LAVEETGMGRVEDKIAKNVAAAEKTPGVEDLTTEALTGDNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 159 VFSPHPSAVKVSNWLVGKINEAIIEAGGERNLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTIGAGA 238
Cdd:PRK15398 161 VFSPHPGAKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 239 GNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFDYLMFNMEKNNAFKISkKEDMVKLEKGVINEDGSV 318
Cdd:PRK15398 241 GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLT-AEQAEKLQKVVLKNGGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 319 NKKFIGKNAKYILDTLGIECPYDPRLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCRHTAAMHSKHI 398
Cdd:PRK15398 320 NKKWVGKDAAKILEAAGINVPKDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNRHTAIMHSRNV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518847611 399 DRLTIAPKRLQTTIFVKNAPSYAGIGLGGEGYTSFTLASSTGDGITSTVTFTRKRRCVLKNGLFVR 464
Cdd:PRK15398 400 DNLNKMARAIQTSIFVKNGPSYAGLGLGGEGFTTFTIATPTGEGVTSARTFTRRRRCVLVDGFRIR 465
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
31-457 |
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: 650.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 31 GVFDSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEESKMGRVEDKINKNTLAIERCTGVEDLK 110
Cdd:cd07121 1 GVFATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTPGTEDLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 111 TGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGGERNL 190
Cdd:cd07121 81 TTAWSGDNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 191 VVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPC 270
Cdd:cd07121 161 VVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 271 IAEKEVLAVDSIFDYLMFNMEKNNAFKISKKEDMVKLEKGVINEDGSV-NKKFIGKNAKYILDTLGIECPYDPRLIIMET 349
Cdd:cd07121 241 IAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNKGATpNKKWVGKDASKILKAAGIEVPADIRLIIVET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 350 HKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCRHTAAMHSKHIDRLTIAPKRLQTTIFVKNAPSYAGIGLGGEG 429
Cdd:cd07121 321 DKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNRHTAIIHSKNVENLTKMARAMQTTIFVKNGPSYAGLGVGGEG 400
|
410 420
....*....|....*....|....*...
gi 518847611 430 YTSFTLASSTGDGITSTVTFTRKRRCVL 457
Cdd:cd07121 401 YTTFTIAGPTGEGLTSARTFTRRRRCVL 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
36-458 |
4.08e-116 |
|
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: 347.72 E-value: 4.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 36 MKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEESKMGRVEDKINKNTLAIERCTGVE-DLKT-GA 113
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYkDEKTcGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 114 LTGDD-GLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGGERNLVV 192
Cdd:cd07081 81 LTGDEnGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 193 TISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIA 272
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 273 EKEVLAVDSIFDYLMFNMEKNNAFKISKKEdmVKLEKGVINEDGSVNKKFIGKNAKYILDTLGIECPYDPRLIIMETHK- 351
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEE--LQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 352 -EHPFAVKELMMPVLPLIRCKDFDEALD--LAVKLEDGCRHTAAMHS---KHIDRLTIAPKRLQTTIFVKNAP-SYAGIG 424
Cdd:cd07081 319 aEHEPFAHEKLSPVLAMYRAANFADADAkaLALKLEGGCGHTSAMYSdniKAIENMNQFANAMKTSRFVKNGPcSQGGLG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 518847611 425 LGGE--GYTSFTLASST--GDGITSTV---TFTRKRRCVLK 458
Cdd:cd07081 399 DLYNfrGWPSMTLGCGTwgGNSVSENVgpkHLVNLKTVALR 439
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
36-445 |
6.04e-90 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 280.53 E-value: 6.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 36 MKEAIEYASIAQKKFLCSSlSER-----KKITDSIRNKLRPLIKemsvMTVEESKMGRVEDKINKNTLAierCTGV---- 106
Cdd:cd07122 1 VDELVERARKAQREFATFS-QEQvdkivEAVAWAAADAAEELAK----MAVEETGMGVVEDKVIKNHFA---SEYVyndi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 107 EDLKT-GALTGDDGLSLIEF-SPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEA 184
Cdd:cd07122 73 KDMKTvGVIEEDEEKGIVEIaEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 185 GGERNLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASL 264
Cdd:cd07122 153 GAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 265 DNNMPCIAEKEVLAVDSIFDYLMFNMEKNNAFKISKKEdMVKLEKGVINEDGSVNKKFIGKNAKYILDTLGIECPYDPRL 344
Cdd:cd07122 233 DNGTICASEQSVIVDDEIYDEVRAELKRRGAYFLNEEE-KEKLEKALFDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 345 IIMETH---KEHPFAvKELMMPVLPLIRCKDFDEALDLAVKLED--GCRHTAAMHSK---HIDRLTIAPK--RlqttIFV 414
Cdd:cd07122 312 LVAEETgvgPEEPLS-REKLSPVLAFYRAEDFEEALEKARELLEygGAGHTAVIHSNdeeVIEEFALRMPvsR----ILV 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 518847611 415 kNAPSyagiGLGGEGYT------SFTLASST-GDGITS 445
Cdd:cd07122 387 -NTPS----SLGGIGDTynglapSLTLGCGSwGGNSTS 419
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
75-435 |
6.24e-70 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 237.78 E-value: 6.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 75 EMSVMTVEESKMGRVEDKINKNTLAIERCT-GVEDLKT-GALTGDDGLSLIEFS-PFGVIGAITPVTNPTETIICNSINM 151
Cdd:PRK13805 53 PLAKMAVEETGRGVVEDKVIKNHFASEYIYnSYKDEKTvGVIEEDDEFGIIEIAePVGVIAGITPTTNPTSTAIFKALIA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 152 LSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGGERNLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGK 231
Cdd:PRK13805 133 LKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 232 KTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFDYLMFNMEKNNAFkISKKEDMVKLEKGV 311
Cdd:PRK13805 213 PALGVGAGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHGAY-FLNKKELKKLEKFI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 312 IN-EDGSVNKKFIGKNAKYILDTLGIECPYDPRLIIME---THKEHPFAVKELmMPVLPLIRCKDFDEALDLAVKL-EDG 386
Cdd:PRK13805 292 FGkENGALNADIVGQSAYKIAEMAGFKVPEDTKILIAEvkgVGESEPLSHEKL-SPVLAMYKAKDFEDAVEKAEKLvEFG 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 518847611 387 CR-HTAAMHSKHIDRLTIAPKRLQTT-IFVkNAPSyagiGLGGEG--YT----SFTL 435
Cdd:PRK13805 371 GLgHTAVIYTNDDELIKEFGLRMKACrILV-NTPS----SQGGIGdlYNklapSLTL 422
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
41-457 |
1.10e-68 |
|
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: 224.41 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 41 EYASIAQKKFLCSSLSERKKITDSIRNKL---RPLIKEMSVMTVEE----------SKMGRVEDKINKNTLAIERCTGVE 107
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALydtRQRLASEAVSERGAyirslianwiAMMGCSESKLYKNIDTERGITASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 108 DLKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTeTIICNSINMLSAGNSVVFSPHPSAvKVSNWLVGKINEAIIEAGGE 187
Cdd:cd07077 81 GHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSA-PFTNRALALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 188 RNLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKS--GKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLD 265
Cdd:cd07077 159 KILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 266 NNMpCIAEKEVLAVDSIFDYLMfnmeknnafkiskkeDMVKLEKGVInedgsvnkkfigknakyildtlGIECPYDPRLI 345
Cdd:cd07077 239 QNA-CASEQNLYVVDDVLDPLY---------------EEFKLKLVVE----------------------GLKVPQETKPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 346 IMETHKEHPFAVKELMMPVLPLIRCKDFDEALD--LAVKLEDGCRHTAAMHSKHIDRLTIAPKRLQTTIFVKNAPS--YA 421
Cdd:cd07077 281 SKETTPSFDDEALESMTPLECQFRVLDVISAVEnaWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSkkGR 360
|
410 420 430
....*....|....*....|....*....|....*..
gi 518847611 422 GIGLGGEGYTSFTLASSTGDGI-TSTVTFTRKRRCVL 457
Cdd:cd07077 361 GAFAGKGVERIVTSGMNNIFGAgVGHDALRPLKRLVR 397
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
40-453 |
3.29e-56 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 193.93 E-value: 3.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 40 IEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEESKMGRVEDKINKNTLAIERC-TGVEDLKT-GALTGD 117
Cdd:TIGR02518 14 IRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVyDSIKDMKTiGILSED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 118 DGLSLIEFS-PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGGERNLVVTISK 196
Cdd:TIGR02518 94 KEKKVIEIAvPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCITV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 197 ASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEV 276
Cdd:TIGR02518 174 PTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQSI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 277 LAVDSIFDYLMFNMEKNNAFKISkKEDMVKLEKGVINEDGSVNKKFIGKNAKYILDTLGIECPYDPRLIIMETH---KEH 353
Cdd:TIGR02518 254 IVEECNKDAVVEELKKQGGYFLT-AEEAEKLGKFILRPNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQNgvgNKN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 354 PFAvKELMMPVLPLIRCKDFDEALDLAVKL--EDGCRHTAAMHSKHIDRLT-IAPKRLQTTIFVKNAPSYAGIGLGGEGY 430
Cdd:TIGR02518 333 PYS-REKLTTILAFYTEENWHEACELSIELlqNEGAGHTLIIHSENKDIVReFALKKPVSRMLVNTGGSLGGIGATTNLV 411
|
410 420
....*....|....*....|....*....
gi 518847611 431 TSFTL------ASSTGDGITSTVTFTRKR 453
Cdd:TIGR02518 412 PAFTLgcgavgGSSTSDNITPENLINIRR 440
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
41-457 |
2.85e-37 |
|
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: 140.06 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 41 EYASIAQKKFLCSSLSERK----KITDSIRNKLRPLIKEMS-----VMTVEESKMGRVEDKINKNTLAIERCTGVEDLkt 111
Cdd:cd06534 1 AAARAAFKAWAALPPAERAailrKIADLLEERREELAALETletgkPIEEALGEVARAIDTFRYAAGLADKLGGPELP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 112 gaLTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAvKVSNWLVGKIneaIIEAGGERNLV 191
Cdd:cd06534 79 --SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELT-PLTALALAEL---LQEAGLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 192 VTISKASVEEVDYLMESPKVNALCITGGMP----IVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNN 267
Cdd:cd06534 153 NVVPGGGDEVGAALLSHPRVDKISFTGSTAvgkaIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 268 MPCIAEKEVLAVDSIFDylmfnmeknnafkiskkedmvklekgvinedgsvnkKFIGKnakyiLDTLGIECPYDPRLiim 347
Cdd:cd06534 233 QICTAASRLLVHESIYD------------------------------------EFVEK-----LVTVLVDVDPDMPI--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 348 etHKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGcrHTAAMHSKHIDRLTIAPKRLQTTIFVKNAPSyagIGLGG 427
Cdd:cd06534 269 --AQEEIFG------PVLPVIRFKDEEEAIALANDTEYG--LTAGVFTRDLNRALRVAERLRAGTVYINDSS---IGVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 518847611 428 EGYTSFTLASSTG--DGITSTVTFTRKRRCVL 457
Cdd:cd06534 336 EAPFGGVKNSGIGreGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-429 |
4.85e-22 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 98.19 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 37 KEAIEYASIAQKKFLCSSLSER----KKITDSIRNKLRPLIKemsVMTVEESKmgrvedKINKNTLAIERCTGV-----E 107
Cdd:cd07145 24 REAIEVAEKAKDVMSNLPAYKRykilMKVAELIERRKEELAK---LLTIEVGK------PIKQSRVEVERTIRLfklaaE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 108 DLKT---------GALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPhPSAVKVSNWLVGKIn 178
Cdd:cd07145 95 EAKVlrgetipvdAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP-SSNTPLTAIELAKI- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 179 eaIIEAGGERNLVVTISKASVEEVDYLMESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQA 254
Cdd:cd07145 173 --LEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 255 AADIVAGASLDNNMPCIAEKEVLAVDSIFD-YLMFNMEKNNAFKIS----KKEDMVKL--EKGVINEDGSVNKKfIGKNA 327
Cdd:cd07145 251 VSIAVRGRFENAGQVCNAVKRILVEEEVYDkFLKLLVEKVKKLKVGdpldESTDLGPLisPEAVERMENLVNDA-VEKGG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 328 KYILDTLGIECPYDPRLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCRhtAAMHSKHIDR-LTIAPK 406
Cdd:cd07145 330 KILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ--ASVFTNDINRaLKVARE 407
|
410 420 430
....*....|....*....|....*....|...
gi 518847611 407 RLQTTIFVKNAPS-------YAGI---GLGGEG 429
Cdd:cd07145 408 LEAGGVVINDSTRfrwdnlpFGGFkksGIGREG 440
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
38-433 |
6.33e-19 |
|
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: 88.80 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 38 EAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEEskMGRVEDKINKNTL-AIERCTGVEDL------K 110
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLE--TGKPIEEALGEVArAADTFRYYAGLarrlhgE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 111 TGALTGDDGLSLIEFSPFGVIGAITPVTNPTEtIICNSINM-LSAGNSVVFSPHPSAVkVSNWLVGKIneaIIEAGGERN 189
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLL-LAAWKLAPaLAAGNTVVLKPSELTP-LTALLLAEL---LAEAGLPPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 190 LVVTISKASVEEVDYLMESPKVNALCITGGMP----IVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLD 265
Cdd:cd07078 155 VLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 266 NNMPCIAEKEVLAVDSIFDYLMFNM-EKNNAFK--------------ISKK---------EDMVKlEKGVINEDGSVNKk 321
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLvERVKALKvgnpldpdtdmgplISAAqldrvlayiEDAKA-EGAKLLCGGKRLE- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 322 fiGKNAKYILDTLGIECPYDprliiMETHKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRL 401
Cdd:cd07078 313 --GGKGYFVPPTVLTDVDPD-----MPIAQEEIFG------PVLPVIPFKDEEEAIELANDTEYGL--AAGVFTRDLERA 377
|
410 420 430
....*....|....*....|....*....|....*
gi 518847611 402 TIAPKRLQT-TIFVKNAPSYAGIGL--GGEGYTSF 433
Cdd:cd07078 378 LRVAERLEAgTVWINDYSVGAEPSApfGGVKQSGI 412
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
38-419 |
1.90e-18 |
|
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: 87.63 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 38 EAIEYASIAQKKFL-CSSLSER----KKITDSIRNKLRPLIKemsVMTVEESK-----MGRVE---DKINKNTLAIERCT 104
Cdd:cd07082 42 EAAETAYDAGRGWWpTMPLEERidclHKFADLLKENKEEVAN---LLMWEIGKtlkdaLKEVDrtiDYIRDTIEELKRLD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 105 GvEDLKTGALTGDDG-LSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVkvsnwLVG-KINEAII 182
Cdd:cd07082 119 G-DSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGV-----LLGiPLAEAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 183 EAGGERNLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKK---TIGAGAGNPpVIVDETADIEQAAADIV 259
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMkrlVLELGGKDP-AIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 260 AGASLDNNMPCIAEKEVLAVDSIFDYLM-----------FNMEKNNAFKI-----SKKEDMVK------LEKG--VINED 315
Cdd:cd07082 272 KGALSYSGQRCTAIKRVLVHESVADELVellkeevaklkVGMPWDNGVDItplidPKSADFVEgliddaVAKGatVLNGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 316 GsvnkkFIGKNakYILDTLgiecpYDPRLIIMETHKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCRhtAAMHS 395
Cdd:cd07082 352 G-----REGGN--LIYPTL-----LDPVTPDMRLAWEEPFG------PVLPIIRVNDIEEAIELANKSNYGLQ--ASIFT 411
|
410 420
....*....|....*....|....*
gi 518847611 396 KHIDRLTIAPKRLQT-TIFVKNAPS 419
Cdd:cd07082 412 KDINKARKLADALEVgTVNINSKCQ 436
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
37-380 |
5.58e-16 |
|
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: 79.88 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 37 KEAIEYASIAQKKFLCSSLSER----KKITDSIRNKLRPLIKemsVMTVEESK-----MGRVEDKINKNTLAIERCtgvE 107
Cdd:pfam00171 32 DAAIAAARAAFPAWRKTPAAERaailRKAADLLEERKDELAE---LETLENGKplaeaRGEVDRAIDVLRYYAGLA---R 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 108 DLKTGALTGDDG-LSLIEFSPFGVIGAITPVTNPTeTIICNSINM-LSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAG 185
Cdd:pfam00171 106 RLDGETLPSDPGrLAYTRREPLGVVGAITPWNFPL-LLPAWKIAPaLAAGNTVVLKPSELTPLTALLLA----ELFEEAG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 186 GERNLVVTISKASVEEVDYLMESPKVNALCITGGMP----IVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAG 261
Cdd:pfam00171 181 LPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 262 ASLDNNMPCIAEKEVLAVDSIFDylmfnmeknnAFKISKKEDMVKLEKGVINEDGS-----VNKKFIGKNAKYILDTL-- 334
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESIYD----------EFVEKLVEAAKKLKVGDPLDPDTdmgplISKAQLERVLKYVEDAKee 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518847611 335 GIECP------------YDPRLII-----METHKEHPFAvkelmmPVLPLIRCKDFDEALDLA 380
Cdd:pfam00171 331 GAKLLtggeagldngyfVEPTVLAnvtpdMRIAQEEIFG------PVLSVIRFKDEEEAIEIA 387
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
116-434 |
5.82e-16 |
|
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: 79.78 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 116 GDDGLSLIEFSPFGVIGAITPVTNPTeTIICNSINM-LSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAG---GERNlV 191
Cdd:COG1012 130 APGTRAYVRREPLGVVGAITPWNFPL-ALAAWKLAPaLAAGNTVVLKPAEQTPLSALLLA----ELLEEAGlpaGVLN-V 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 192 VTISKASVeeVDYLMESPKVNALCITGGMP----IVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNN 267
Cdd:COG1012 204 VTGDGSEV--GAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 268 MPCIAEKEVLAVDSIFDYLMfnmeknNAFkiskKEDMVKLEKGVINEDGS-----VNKKFIGKNAKYILDTL--GIECPY 340
Cdd:COG1012 282 QRCTAASRLLVHESIYDEFV------ERL----VAAAKALKVGDPLDPGTdmgplISEAQLERVLAYIEDAVaeGAELLT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 341 DPRL------------II------METHKEHPFAvkelmmPVLPLIRCKDFDEALDLAvkleDGCRH--TAAMHSKHIDR 400
Cdd:COG1012 352 GGRRpdgeggyfveptVLadvtpdMRIAREEIFG------PVLSVIPFDDEEEAIALA----NDTEYglAASVFTRDLAR 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 518847611 401 LTIAPKRLQT-TIFVKNAPSYA------------GIG--LGGEGYTSFT 434
Cdd:COG1012 422 ARRVARRLEAgMVWINDGTTGAvpqapfggvkqsGIGreGGREGLEEYT 470
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
34-380 |
5.88e-16 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 79.99 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 34 DSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSV-MTVEESK-----MGRVEDKINkntlaIERCTGVE 107
Cdd:cd07097 37 EDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARlLTREEGKtlpeaRGEVTRAGQ-----IFRYYAGE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 108 DLKTGALT---GDDGLSL-IEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHpSAVKVSNWlvgKINEAIIE 183
Cdd:cd07097 112 ALRLSGETlpsTRPGVEVeTTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPA-ELTPASAW---ALVEILEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 184 AG---GERNLVVtiskASVEEV-DYLMESPKVNALCITGGMPIvikGLKSGKKTIGAGA-------GNPPVIVDETADIE 252
Cdd:cd07097 188 AGlpaGVFNLVM----GSGSEVgQALVEHPDVDAVSFTGSTAV---GRRIAAAAAARGArvqlemgGKNPLVVLDDADLD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 253 QAAADIVAGASLDNNMPCIAEKEVLAVDSIFDylmfnmeknnAFKISKKEDMVKLEKGVINEDGS-----VNKKFIGKNA 327
Cdd:cd07097 261 LAVECAVQGAFFSTGQRCTASSRLIVTEGIHD----------RFVEALVERTKALKVGDALDEGVdigpvVSERQLEKDL 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518847611 328 KYI---------LDTLG--IECP----YDPRLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLA 380
Cdd:cd07097 331 RYIeiarsegakLVYGGerLKRPdegyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
127-400 |
9.82e-16 |
|
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: 79.19 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVkvsnWLVGKINEAIIEAG---GernlVVTISKASVEEV- 202
Cdd:cd07124 166 PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP----VIAAKLVEILEEAGlppG----VVNFLPGPGEEVg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 203 DYLMESPKVNALCITG----GMPI------VIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIA 272
Cdd:cd07124 238 DYLVEHPDVRFIAFTGsrevGLRIyeraakVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 273 EKEVLAVDSIFDYLMFNM-EKNNAFKISKKEDMVKLEKGVINEdGSVNK--KFI--GKNAKYIL-----DTLGIECPYDP 342
Cdd:cd07124 318 CSRVIVHESVYDEFLERLvERTKALKVGDPEDPEVYMGPVIDK-GARDRirRYIeiGKSEGRLLlggevLELAAEGYFVQ 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518847611 343 RLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSK---HIDR 400
Cdd:cd07124 397 PTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGL--TGGVFSRspeHLER 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
127-380 |
6.61e-15 |
|
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: 76.63 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAGGERNLVVTISKASVEEVDYLM 206
Cdd:cd07146 120 PLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLA----DLLYEAGLPPDMLSVVTGEPGEIGDELI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 207 ESPKVNALCITGGMPI--VIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSI-- 282
Cdd:cd07146 196 THPDVDLVTFTGGVAVgkAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVad 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 283 -FDYLMfnMEKNNAFKISKKEDMVKLEKGVINE------DGSVNKKfIGKNAKYILDTLGIECPYDPrlIIME-THKEHP 354
Cdd:cd07146 276 eFVDLL--VEKSAALVVGDPMDPATDMGTVIDEeaaiqiENRVEEA-IAQGARVLLGNQRQGALYAP--TVLDhVPPDAE 350
|
250 260
....*....|....*....|....*.
gi 518847611 355 FAVKELMMPVLPLIRCKDFDEALDLA 380
Cdd:cd07146 351 LVTEETFGPVAPVIRVKDLDEAIAIS 376
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
127-429 |
2.34e-14 |
|
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: 74.78 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFspHPSAVKVSNWLvgKINEAIIEAGGERNLVVTISKASVEEVDYLM 206
Cdd:cd07094 123 PVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL--KPASKTPLSAL--ELAKILVEAGVPEGVLQVVTGEREVLGDAFA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 207 ESPKVNALCITGGMPI--VIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFD 284
Cdd:cd07094 199 ADERVAMLSFTGSAAVgeALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 285 ylMFNMEKNNAFKISK----------------KEDMVKLEKGVinedgsvnKKFIGKNAKYILD----------TLGIEC 338
Cdd:cd07094 279 --EFIEAFVAAVKKLKvgdpldedtdvgplisEEAAERVERWV--------EEAVEAGARLLCGgerdgalfkpTVLEDV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 339 PYDPRLIIMEThkehpFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCRhtAAMHSKHIDRLTIAPKRLQ--------T 410
Cdd:cd07094 349 PRDTKLSTEET-----FG------PVVPIIRYDDFEEAIRIANSTDYGLQ--AGIFTRDLNVAFKAAEKLEvggvmvndS 415
|
330 340
....*....|....*....|..
gi 518847611 411 TIFVKNAPSYAGI---GLGGEG 429
Cdd:cd07094 416 SAFRTDWMPFGGVkesGVGREG 437
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
127-404 |
4.45e-14 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 74.20 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSnwlvGKINEAIIEAGGERNlVVTISKASVEEV-DYL 205
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIA----AKFVEVLEEAGLPAG-VVNFVPGSGSEVgDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 206 MESPKVNALCITG----GMPI------VIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKE 275
Cdd:PRK03137 246 VDHPKTRFITFTGsrevGLRIyeraakVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 276 VLAVDSIFDYLMFN-MEKNNAFKISKKEDMVKLekG-VINEdGSVNKKF----IGKN-AKYIL-----DTLG------IE 337
Cdd:PRK03137 326 AIVHEDVYDEVLEKvVELTKELTVGNPEDNAYM--GpVINQ-ASFDKIMsyieIGKEeGRLVLggegdDSKGyfiqptIF 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518847611 338 CPYDPRLIIMEthkehpfavKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIA 404
Cdd:PRK03137 403 ADVDPKARIMQ---------EEIFGPVVAFIKAKDFDHALEIANNTEYGL--TGAVISNNREHLEKA 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
123-284 |
1.07e-13 |
|
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: 72.64 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 123 IEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAGGERNL--VVT----ISK 196
Cdd:cd07099 115 VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLA----EAWAAAGPPQGVlqVVTgdgaTGA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 197 ASVEEVdylmespkVNALCITGGMPivikglkSGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGASLD 265
Cdd:cd07099 191 ALIDAG--------VDKVAFTGSVA-------TGRKVMAAAAerlipvvlelgGKDPMIVLADADLERAAAAAVWGAMVN 255
|
170
....*....|....*....
gi 518847611 266 NNMPCIAEKEVLAVDSIFD 284
Cdd:cd07099 256 AGQTCISVERVYVHESVYD 274
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
34-411 |
2.13e-13 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 71.95 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 34 DSMKEAIEYASIAQKKFLCSSLSERKKItdsIRNKLRPLIKEMSVM----------TVEESKMGRV---EDKINKNTLAI 100
Cdd:cd07098 18 EDVDEAIAAARAAQREWAKTSFAERRKV---LRSLLKYILENQEEIcrvacrdtgkTMVDASLGEIlvtCEKIRWTLKHG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 101 ERCTGVEDLKTGALTGDDGlSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEA 180
Cdd:cd07098 95 EKALRPESRPGGLLMFYKR-ARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 181 IIEAGGERNLVVTISkASVEEVDYLMESPKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETA 249
Cdd:cd07098 174 LAACGHDPDLVQLVT-CLPETAEALTSHPVIDHITFIGSPPV-------GKKVMAAAAesltpvvlelgGKDPAIVLDDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 250 DIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFDYL----------------------MFNMEKNNAFkiSKKEDMVK- 306
Cdd:cd07098 246 DLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLleiltdrvqalrqgppldgdvdVGAMISPARF--DRLEELVAd 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 307 -LEKGV-INEDGSVNKKFIGKNAKYILDTLGIECpyDPRLIIMEThkehpfavkELMMPVLPLIRCKDFDEALDLAVKLE 384
Cdd:cd07098 324 aVEKGArLLAGGKRYPHPEYPQGHYFPPTLLVDV--TPDMKIAQE---------EVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420
....*....|....*....|....*..
gi 518847611 385 DGCrhTAAMHSKHIDRLTIAPKRLQTT 411
Cdd:cd07098 393 YGL--GASVFGKDIKRARRIASQLETG 417
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
126-400 |
9.97e-12 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 66.56 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 126 SPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEaiiEAG---GERNLVVTiskASVEEV 202
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFE---EAGlpkGVLNVVVG---AGSEIG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 203 DYLMESPKVNALCITGGMPI--VIKGLKSG--KKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLA 278
Cdd:cd07151 203 DAFVEHPVPRLISFTGSTPVgrHIGELAGRhlKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 279 VDSIFD-YLMFNMEKNNAFKI---SKKEDMVklekG-VINED--GSVNKKFigKNAKYILDTLGIECPYDPRLiiMETH- 350
Cdd:cd07151 283 HEDVYDeFVEKFVERVKALPYgdpSDPDTVV----GpLINESqvDGLLDKI--EQAVEEGATLLVGGEAEGNV--LEPTv 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518847611 351 -----KEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDR 400
Cdd:cd07151 355 lsdvtNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGL--SGAVFTSDLER 407
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
33-434 |
1.33e-11 |
|
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: 66.12 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 33 FDSMKEAIEYASIAQKKFLCSSLSERKKItdsIRNKLRPLIKEMSVMTVEESK-MGR-VEDKINKNTLAIER----CTGV 106
Cdd:cd07102 17 LEAVRAALERARAAQKGWRAVPLEERKAI---VTRAVELLAANTDEIAEELTWqMGRpIAQAGGEIRGMLERarymISIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 107 ED-LKTGALTGDDGL-SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVkvsnwLVG-KINEAIIE 183
Cdd:cd07102 94 EEaLADIRVPEKDGFeRYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP-----LCGeRFAAAFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 184 AGGERNLV-VTISKASVeeVDYLMESPKVNALCITGGmpiVIKGLK----SGKKTIGAG---AGNPPVIVDETADIEQAA 255
Cdd:cd07102 169 AGLPEGVFqVLHLSHET--SAALIADPRIDHVSFTGS---VAGGRAiqraAAGRFIKVGlelGGKDPAYVRPDADLDAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 256 ADIVAGASLDNNMPCIAEKEVLAVDSIFD-YLMFNMEKNNAFKISKKED-------MVKLEKGVINEdgSVNKKFIGKNA 327
Cdd:cd07102 244 ESLVDGAFFNSGQSCCSIERIYVHESIYDaFVEAFVAVVKGYKLGDPLDpsttlgpVVSARAADFVR--AQIADAIAKGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 328 KYILD--TLGIECP----YDPRLII-----METHKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSK 396
Cdd:cd07102 322 RALIDgaLFPEDKAggayLAPTVLTnvdhsMRVMREETFG------PVVGIMKVKSDAEAIALMNDSEYGL--TASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 518847611 397 HIDRLTIAPKRLQT-TIF---------------VKNapSYAGIGLGGEGYTSFT 434
Cdd:cd07102 394 DIARAEALGEQLETgTVFmnrcdyldpalawtgVKD--SGRGVTLSRLGYDQLT 445
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
122-429 |
8.71e-11 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 63.82 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 122 LIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGgernlVVTISKASVEE 201
Cdd:cd07088 128 FIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAG-----VLNIVTGRGSV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 202 V-DYLMESPKVNALCITGGMPivikglkSGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAgASLDNN-M 268
Cdd:cd07088 203 VgDALVAHPKVGMISLTGSTE-------AGQKIMEAAAenitkvslelgGKAPAIVMKDADLDLAVKAIVD-SRIINCgQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 269 PCIAEKEVLAVDSIFDYLMFNM-EKNNAFKI----SKKEDMVKL--EKGVINEDGSVnKKFIGKNAKyiLDTLGIECP-- 339
Cdd:cd07088 275 VCTCAERVYVHEDIYDEFMEKLvEKMKAVKVgdpfDAATDMGPLvnEAALDKVEEMV-ERAVEAGAT--LLTGGKRPEge 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 340 ----YDPRLII-----METHKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQ- 409
Cdd:cd07088 352 kgyfYEPTVLTnvrqdMEIVQEEIFG------PVLPVVKFSSLDEAIELANDSEYGL--TSYIYTENLNTAMRATNELEf 423
|
330 340
....*....|....*....|....*....
gi 518847611 410 --TTIFVKNAPSYAGI-------GLGGEG 429
Cdd:cd07088 424 geTYINRENFEAMQGFhagwkksGLGGAD 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
99-284 |
1.13e-10 |
|
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: 63.42 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 99 AIERCTGVEDLKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAvKVSNWLVGKI- 177
Cdd:cd07089 95 LADSFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDT-PLSALLLGEIi 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 178 NEAIIEAGgernlVVTISKASVEEV-DYLMESPKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIV 245
Cdd:cd07089 174 AETDLPAG-----VVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAV-------GRRIMAQAAatlkrvllelgGKSANIV 241
|
170 180 190
....*....|....*....|....*....|....*....
gi 518847611 246 DETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFD 284
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYD 280
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
37-380 |
1.62e-10 |
|
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: 62.67 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 37 KEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEM-SVMTVEESK-----MGRVEDKINKNTLAI----ERCTgv 106
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELaRLISRETGKplweaQTEVAAMAGKIDISIkayhERTG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 107 edlkTGALTGDDGLSLIEFSPFGVIGAITPVTNPTEtiICNSINM--LSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEA 184
Cdd:cd07095 81 ----ERATPMAQGRAVLRHRPHGVMAVFGPFNFPGH--LPNGHIVpaLLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 185 GgernlVVTISKASVEEVDYLMESPKVNALCITG-------------GMPIVIKGLKSGkktigagaGNPPVIVDETADI 251
Cdd:cd07095 155 G-----VLNLVQGGRETGEALAAHEGIDGLLFTGsaatglllhrqfaGRPGKILALEMG--------GNNPLVVWDVADI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 252 EQAAADIVAGASLDNNMPCIAEKEVLAVDSifdylmfnmEKNNAFKISKKEDMVKLEKGVINED-----GSVN------- 319
Cdd:cd07095 222 DAAAYLIVQSAFLTAGQRCTCARRLIVPDG---------AVGDAFLERLVEAAKRLRIGAPDAEppfmgPLIIaaaaary 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518847611 320 ----KKFIGKNAKYILD-TLGIECPY--DPRLIIMETHKEHPFAvkELMMPVLPLIRCKDFDEALDLA 380
Cdd:cd07095 293 llaqQDLLALGGEPLLAmERLVAGTAflSPGIIDVTDAADVPDE--EIFGPLLQVYRYDDFDEAIALA 358
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
127-284 |
1.82e-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: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPtetiicnsINM--------LSAGNSVVFSPHP----SAVkvsnwlvgKINEAIIEAGGERNlVVTI 194
Cdd:cd07149 123 PIGVVAAITPFNFP--------LNLvahkvgpaIAAGNAVVLKPASqtplSAL--------KLAELLLEAGLPKG-ALNV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 195 SKASVEEV-DYLMESPKVNALCITGGmPIVIKGL--KSG-KKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPC 270
Cdd:cd07149 186 VTGSGETVgDALVTDPRVRMISFTGS-PAVGEAIarKAGlKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVC 264
|
170
....*....|....
gi 518847611 271 IAEKEVLAVDSIFD 284
Cdd:cd07149 265 ISVQRIFVHEDIYD 278
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
127-380 |
6.58e-10 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 61.24 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPH---P-SAVKVSnwlvgkinEAIIEAG---GERNLVVtiskASV 199
Cdd:PLN02278 160 PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSeltPlTALAAA--------ELALQAGippGVLNVVM----GDA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 200 EEV-DYLMESPKVNALCITGGMPIvikglksGKKTI-GAGA----------GNPPVIVDETADIEQAAADIVAGASLDNN 267
Cdd:PLN02278 228 PEIgDALLASPKVRKITFTGSTAV-------GKKLMaGAAAtvkrvslelgGNAPFIVFDDADLDVAVKGALASKFRNSG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 268 MPCIAEKEVLAVDSIFDYLmfnmeknnAFKISKKEDMVK----LEKGV-----INEDgSVNK------KFIGKNAKYILD 332
Cdd:PLN02278 301 QTCVCANRILVQEGIYDKF--------AEAFSKAVQKLVvgdgFEEGVtqgplINEA-AVQKveshvqDAVSKGAKVLLG 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 518847611 333 ----TLGIECpYDPRLII-----METHKEHPFAvkelmmPVLPLIRCKDFDEALDLA 380
Cdd:PLN02278 372 gkrhSLGGTF-YEPTVLGdvtedMLIFREEVFG------PVAPLTRFKTEEEAIAIA 421
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
119-377 |
9.34e-10 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 60.43 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 119 GLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINE-------AIIEAGgernlv 191
Cdd:PTZ00381 101 GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKyldpsyvRVIEGG------ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 192 VTISKASVEE-VDYLM--ESPKVNALCITGG----MPIVikgLKSGKKTigagagnpPVIVDETADIEQAAADIVAGASL 264
Cdd:PTZ00381 175 VEVTTELLKEpFDHIFftGSPRVGKLVMQAAaenlTPCT---LELGGKS--------PVIVDKSCNLKVAARRIAWGKFL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 265 DNNMPCIAEKEVLAVDSIFDYL----------MF--NMEKN-------NAFKISKKEDMVKLEKGVINEDGSVNkkfigK 325
Cdd:PTZ00381 244 NAGQTCVAPDYVLVHRSIKDKFiealkeaikeFFgeDPKKSedysrivNEFHTKRLAELIKDHGGKVVYGGEVD-----I 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518847611 326 NAKYILDTlgiecpydprlIIMETHKEHPFAVKELMMPVLPLIRCKDFDEAL 377
Cdd:PTZ00381 319 ENKYVAPT-----------IIVNPDLDSPLMQEEIFGPILPILTYENIDEVL 359
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
113-416 |
1.35e-09 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 59.91 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 113 ALTGDDGLSLIEFSPFGVIGAITPVTNPTeTIICNSIN-MLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGgernLV 191
Cdd:PRK09847 143 ATTSSHELAMIVREPVGVIAAIVPWNFPL-LLTCWKLGpALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDG----VL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 192 VTISKASVEEVDYLMESPKVNALCITG----GMPIVIKGLKSGKKTI--GAGAGNPPVIVDETADIEQAAADIVAGASLD 265
Cdd:PRK09847 218 NVVTGFGHEAGQALSRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVwlEAGGKSANIVFADCPDLQQAASATAAGIFYN 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 266 NNMPCIAEKEVLAVDSIFD-YLMFNMEKNNAFKISKKEDMVKLEKGVINEDGSVN-KKFI-GKNAKYILDTLGIECPYDP 342
Cdd:PRK09847 298 QGQVCIAGTRLLLEESIADeFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSvHSFIrEGESKGQLLLDGRNAGLAA 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518847611 343 RL---IIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQT-TIFVKN 416
Cdd:PRK09847 378 AIgptIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGL--GAAVWTRDLSRAHRMSRRLKAgSVFVNN 453
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
125-380 |
1.69e-09 |
|
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: 59.90 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 125 FSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSnwlvGKINEAIIEAGGERNLVVTISKASVEEVDY 204
Cdd:cd07083 152 YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVG----YKVFEIFHEAGFPPGVVQFLPGVGEEVGAY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 205 LMESPKVNALCITGGMPIVIK----------GLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEK 274
Cdd:cd07083 228 LTEHERIRGINFTGSLETGKKiyeaaarlapGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAAS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 275 EVLAVDSIFDYLMFNM-EKNNAFKISKKEDMVKLEKGVINEDGSVN-KKFI--GKNAKYILdtLGIECP-----YDPRLI 345
Cdd:cd07083 308 RLILTQGAYEPVLERLlKRAERLSVGPPEENGTDLGPVIDAEQEAKvLSYIehGKNEGQLV--LGGKRLegegyFVAPTV 385
|
250 260 270
....*....|....*....|....*....|....*..
gi 518847611 346 IMETHKEHPFAVKELMMPVLPLIRCK--DFDEALDLA 380
Cdd:cd07083 386 VEEVPPKARIAQEEIFGPVLSVIRYKddDFAEALEVA 422
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
116-414 |
2.40e-09 |
|
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: 59.27 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 116 GDDGLSLIEFSPFGVIGAITPVTNPTeTIICNSINM-LSAGNSVVFSPH--PSAVKVsnwlvgKINEAIIEAG---GERN 189
Cdd:cd07118 108 GDDMLGLVLREPIGVVGIITPWNFPF-LILSQKLPFaLAAGCTVVVKPSefTSGTTL------MLAELLIEAGlpaGVVN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 190 lVVTISKASVEEVdyLMESPKVNALCITGGMPIvikglksGKKTIGAGAGN-----------PPVIVDETADIEQAAADI 258
Cdd:cd07118 181 -IVTGYGATVGQA--MTEHPDVDMVSFTGSTRV-------GKAIAAAAARNlkkvslelggkNPQIVFADADLDAAADAV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 259 VAGASLDNNMPCIAEKEVLAVDSIFDylmfnmeknnAFKISKKEDMVKLEKG-----------VINEDG-SVNKKFI--G 324
Cdd:cd07118 251 VFGVYFNAGECCNSGSRLLVHESIAD----------AFVAAVVARSRKVRVGdpldpetkvgaIINEAQlAKITDYVdaG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 325 KNAKYILDTLGIECPYDPRLIIMET-----HKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHID 399
Cdd:cd07118 321 RAEGATLLLGGERLASAAGLFYQPTiftdvTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL--SAGVWSKDID 398
|
330
....*....|....*.
gi 518847611 400 RLTIAPKRLQT-TIFV 414
Cdd:cd07118 399 TALTVARRIRAgTVWV 414
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
121-284 |
2.67e-09 |
|
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: 58.88 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLvGKINEAIIEAGgernlVVTISKASVE 200
Cdd:cd07092 112 SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLL-AELAAEVLPPG-----VVNVVCGGGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 201 EV-DYLMESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKE 275
Cdd:cd07092 186 SAgDALVAHPRVRMVSLTGsvrtGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACR 265
|
....*....
gi 518847611 276 VLAVDSIFD 284
Cdd:cd07092 266 VYVHESVYD 274
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
36-284 |
4.35e-09 |
|
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: 58.24 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 36 MKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMS-VMTVEeskMGrvedKINKNTLA-IERC---------T 104
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELArLITLE---MG----KPIAEARAeVEKCawicryyaeN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 105 GVEDLKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNwlvgKINEAIIEA 184
Cdd:cd07100 74 AEAFLADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCAL----AIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 185 GGERNLVVTIsKASVEEVDYLMESPKVNALCITGGMP---IV--IKGlKSGKKTI---GagaGNPPVIVDETADIEQAAA 256
Cdd:cd07100 150 GFPEGVFQNL-LIDSDQVEAIIADPRVRGVTLTGSERagrAVaaEAG-KNLKKSVlelG---GSDPFIVLDDADLDKAVK 224
|
250 260
....*....|....*....|....*...
gi 518847611 257 DIVAGASLDNNMPCIAEKEVLAVDSIFD 284
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYD 252
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
127-429 |
5.77e-09 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 57.99 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGgernlVVTISKASVEEV-DYL 205
Cdd:PRK11241 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAG-----VFNVVTGSAGAVgGEL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 206 MESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDS 281
Cdd:PRK11241 221 TSNPLVRKLSFTGsteiGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 282 IFDylmfnmeknnAFKISKKEDMVKLEKGVINEDGS-----VNKKFIGKNAKYILDTL-------------GIECPYDPR 343
Cdd:PRK11241 301 VYD----------RFAEKLQQAVSKLHIGDGLEKGVtigplIDEKAVAKVEEHIADALekgarvvcggkahELGGNFFQP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 344 LIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQ-------TTIFVKN 416
Cdd:PRK11241 371 TILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGL--AAYFYARDLSRVFRVGEALEygivginTGIISNE 448
|
330
....*....|....*.
gi 518847611 417 APSYAGI---GLGGEG 429
Cdd:PRK11241 449 VAPFGGIkasGLGREG 464
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
34-284 |
6.73e-09 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 57.95 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 34 DSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEEskMGRvedKINKNTLAIERCTGVED----- 108
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITRE--MGK---PINQARAEVAKSANLCDwyaeh 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 109 ----LKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSaVKVSNWLVGKI-NEAIIE 183
Cdd:PRK13968 104 gpamLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN-VMGCAQLIAQVfKDAGIP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 184 AGgernlVVTISKASVEEVDYLMESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIV 259
Cdd:PRK13968 183 QG-----VYGWLNADNDGVSQMINDSRIAAVTVTGsvraGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260
....*....|....*....|....*
gi 518847611 260 AGASLDNNMPCIAEKEVLAVDSIFD 284
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIAS 282
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
126-400 |
7.69e-09 |
|
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: 57.72 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 126 SPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNwlvgKINEAIIEAG---GERNLVVtiskASVEEV 202
Cdd:cd07150 118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL----KIAEIMEEAGlpkGVFNVVT----GGGAEV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 203 -DYLMESPKVNALCITG----GMPIVIKGLKSGKK-TIGAGaGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEV 276
Cdd:cd07150 190 gDELVDDPRVRMVTFTGstavGREIAEKAGRHLKKiTLELG-GKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 277 LAVDSIFDYLMfnmeKNNAFKISKKEDMVKLEKGV-----INE------DGSVNKKfIGKNAKyILDTLGIECPY----- 340
Cdd:cd07150 269 IVEEPVYDEFV----KKFVARASKLKVGDPRDPDTvigplISPrqveriKRQVEDA-VAKGAK-LLTGGKYDGNFyqptv 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518847611 341 ----DPRLIIMEThkehpfavkELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDR 400
Cdd:cd07150 343 ltdvTPDMRIFRE---------ETFGPVTSVIPAKDAEEALELANDTEYGL--SAAILTNDLQR 395
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
126-284 |
2.62e-08 |
|
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: 55.78 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 126 SPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAGGERNL--VVT-----ISKAS 198
Cdd:cd07101 117 RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAV----ELLIEAGLPRDLwqVVTgpgseVGGAI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 199 VEEVDYLMespkvnalcITGGMPI-VIKGLKSGKKTIGAGA---GNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEK 274
Cdd:cd07101 193 VDNADYVM---------FTGSTATgRVVAERAGRRLIGCSLelgGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
170
....*....|
gi 518847611 275 EVLAVDSIFD 284
Cdd:cd07101 264 RIYVHESVYD 273
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
34-377 |
4.67e-08 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 55.15 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 34 DSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMSVMTVEE----SKMGRVEDKINKNTLAIERCTGVEDL 109
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEiakpAKDAVTEVVRSGDLISYTAEEGVRIL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 110 KTGAL--------TGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPhPSAVKVSNWLvgkINEAI 181
Cdd:PLN00412 133 GEGKFlvsdsfpgNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP-PTQGAVAALH---MVHCF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 182 IEAGGERNLVVTISKASVEEVDYLMESPKVNALCITGGMpiviKGLKSGKKtigAG--------AGNPPVIVDETADIEQ 253
Cdd:PLN00412 209 HLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD----TGIAISKK---AGmvplqmelGGKDACIVLEDADLDL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 254 AAADIVAGASLDNNMPCIAEKEVLAVDSIFDYLmfnMEKNNAfkiskkeDMVKLEKGVINEDGSVNKKFIGKNAKYI--- 330
Cdd:PLN00412 282 AAANIIKGGFSYSGQRCTAVKVVLVMESVADAL---VEKVNA-------KVAKLTVGPPEDDCDITPVVSESSANFIegl 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518847611 331 -LD------TLGIECPYDPRLII----------METHKEHPFAvkelmmPVLPLIRCKDFDEAL 377
Cdd:PLN00412 352 vMDakekgaTFCQEWKREGNLIWpllldnvrpdMRIAWEEPFG------PVLPVIRINSVEEGI 409
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
120-284 |
4.67e-08 |
|
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: 55.23 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 120 LSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEaiiEAG---GERNLVVTisk 196
Cdd:cd07104 91 ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFE---EAGlpkGVLNVVPG--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 197 aSVEEV-DYLMESPKVNALCITGGMPIvikglksGKKtIGAGA------------GNPPVIVDETADIEQAAADIVAGAS 263
Cdd:cd07104 165 -GGSEIgDALVEHPRVRMISFTGSTAV-------GRH-IGELAgrhlkkvalelgGNNPLIVLDDADLDLAVSAAAFGAF 235
|
170 180
....*....|....*....|.
gi 518847611 264 LDNNMPCIAEKEVLAVDSIFD 284
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYD 256
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-377 |
5.47e-08 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 54.94 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 34 DSMKEAIEYASIAQKKFLCSSLSERKKITDSIRNKLRPLIKEMS-VMTVEESK--------MGRVEDKINknTLAIE--R 102
Cdd:cd07147 21 DDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAeTIVLEAGKpikdargeVARAIDTFR--IAAEEatR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 103 CTG-VEDLKTGAlTGDDGLSLIEFSPFGVIGAITPVTNPTeTIICNSIN-MLSAGNSVVFSPhPSAVKVSNWLVGkinEA 180
Cdd:cd07147 99 IYGeVLPLDISA-RGEGRQGLVRRFPIGPVSAITPFNFPL-NLVAHKVApAIAAGCPFVLKP-ASRTPLSALILG---EV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 181 IIEAGGERNlVVTISKASVEEVDYLMESPKVNALCITGGmPIVIKGLKS--GKKTIGAG-AGNPPVIVDETADIEQAAAD 257
Cdd:cd07147 173 LAETGLPKG-AFSVLPCSRDDADLLVTDERIKLLSFTGS-PAVGWDLKAraGKKKVVLElGGNAAVIVDSDADLDFAAQR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 258 IVAGASLDNNMPCIAEKEVLAVDSIFDYLMFNM-EKNNAFKISKKEDMVKLEKGVINED------GSVNKKfIGKNAKyI 330
Cdd:cd07147 251 IIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLvARVKALKTGDPKDDATDVGPMISESeaerveGWVNEA-VDAGAK-L 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 518847611 331 LDTLGIECPYDPRLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEAL 377
Cdd:cd07147 329 LTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEAL 375
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
121-378 |
5.93e-08 |
|
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: 54.84 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVF-----SPHPSAV---KVSNWLVGKInEAIIEAGGErnlvv 192
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLkpselAPATSALlakLIPKYFDPEA-VAVVEGGVE----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 193 tISKASVEE-VDYLMespkvnalcITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVA 260
Cdd:cd07087 168 -VATALLAEpFDHIF---------FTGSPAV-------GKIVMEAAAkhltpvtlelgGKSPCIVDKDANLEVAARRIAW 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 261 GASLDNNMPCIAEKEVLAVDSIFDYLMFNMEKN-NAF---KISKKED---MVK----------LEKGVINEDGSVNKKfi 323
Cdd:cd07087 231 GKFLNAGQTCIAPDYVLVHESIKDELIEELKKAiKEFygeDPKESPDygrIINerhfdrlaslLDDGKVVIGGQVDKE-- 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518847611 324 gknAKYILDTlgiecpydprlIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALD 378
Cdd:cd07087 309 ---ERYIAPT-----------ILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIE 349
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
117-434 |
9.66e-08 |
|
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: 54.07 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 117 DDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAvKVSNWLVGKINEAIIEAGgernlVVTISK 196
Cdd:cd07106 104 DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT-PLCTLKLGELAQEVLPPG-----VLNVVS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 197 ASVEEVDYLMESPKVNALCITGGMPIVIKGLKSGKKTI-------GagaGNPPVIVDETADIEQAAADIVAGASLDNNMP 269
Cdd:cd07106 178 GGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLkrvtlelG---GNDAAIVLPDVDIDAVAPKLFWGAFINSGQV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 270 CIAEKEVLAVDSIFDYLMfnmeknnafkiskkEDMVKLEKGVINEDGSVNKKFIG--------------------KNAK- 328
Cdd:cd07106 255 CAAIKRLYVHESIYDEFC--------------EALVALAKAAVVGDGLDPGTTLGpvqnkmqydkvkelvedakaKGAKv 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 329 ------------YILDTLGIECPYDPRLIimethKEHPFAvkelmmPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSK 396
Cdd:cd07106 321 laggepldgpgyFIPPTIVDDPPEGSRIV-----DEEQFG------PVLPVLKYSDEDEVIARANDSEYGL--GASVWSS 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518847611 397 HIDRL-TIApKRLQT-TIFVK-------NAP------SyaGIG--LGGEGYTSFT 434
Cdd:cd07106 388 DLERAeAVA-RRLEAgTVWINthgaldpDAPfgghkqS--GIGveFGIEGLKEYT 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
127-262 |
1.04e-07 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 54.11 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAGGERNL--VVT-----ISKASV 199
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAV----ELLYEAGLPRDLwqVVTgpgpvVGTALV 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518847611 200 EEVDYLMespkvnalcITGGMPI--VIkGLKSGKKTIGAGA---GNPPVIVDETADIEQAAADIVAGA 262
Cdd:PRK09407 230 DNADYLM---------FTGSTATgrVL-AEQAGRRLIGFSLelgGKNPMIVLDDADLDKAAAGAVRAC 287
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
127-380 |
1.75e-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: 53.20 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPtetiicnsINM--------LSAGNSVVFSPHP----SAVKVSnwlvgkinEAIIEAG---GERNLV 191
Cdd:cd07103 117 PVGVVAAITPWNFP--------AAMitrkiapaLAAGCTVVLKPAEetplSALALA--------ELAEEAGlpaGVLNVV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 192 VTiSKASVeeVDYLMESPKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETADIEQAAADIV- 259
Cdd:cd07103 181 TG-SPAEI--GEALCASPRVRKISFTGSTAV-------GKLLMAQAAdtvkrvslelgGNAPFIVFDDADLDKAVDGAIa 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 260 -----AGASldnnmpCIAEKEVLAVDSIFDylmfnmeknnAF--KISKKEDMVK----LEKGV-----INEDGsVNK--K 321
Cdd:cd07103 251 skfrnAGQT------CVCANRIYVHESIYD----------EFveKLVERVKKLKvgngLDEGTdmgplINERA-VEKveA 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518847611 322 FI----GKNAKYILDTLGIECP---YDPRLII-----METHKEHPFAvkelmmPVLPLIRCKDFDEALDLA 380
Cdd:cd07103 314 LVedavAKGAKVLTGGKRLGLGgyfYEPTVLTdvtddMLIMNEETFG------PVAPIIPFDTEDEVIARA 378
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
121-284 |
2.49e-07 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 52.99 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHP----SAVKVSnwlvgkinEAIIEA--GGERNlVVTI 194
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEitplTALKLA--------ELAADIlpPGVLN-VVTG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 195 SKASVEevDYLMESPKVNALCITGGMPivikglkSGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGAS 263
Cdd:PRK13473 203 RGATVG--DALVGHPKVRMVSLTGSIA-------TGKHVLSAAAdsvkrthlelgGKAPVIVFDDADLDAVVEGIRTFGY 273
|
170 180
....*....|....*....|.
gi 518847611 264 LDNNMPCIAEKEVLAVDSIFD 284
Cdd:PRK13473 274 YNAGQDCTAACRIYAQRGIYD 294
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
121-379 |
3.50e-07 |
|
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: 52.51 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVV-----FSPHPSAVkvsnwlvgkINEAIIEAGGERnlVVTIS 195
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVlkpseLTPNTSKV---------IAKIIEETFDEE--YVAVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 196 KASVEEVDYLMESpKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGASL 264
Cdd:cd07136 163 EGGVEENQELLDQ-KFDYIFFTGSVRV-------GKIVMEAAAkhltpvtlelgGKSPCIVDEDANLKLAAKRIVWGKFL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 265 DNNMPCIAEKEVLAVDSIFDYLMFNMEK--NNAF--KISKKEDMVKL--EK------GVINEDgsvnKKFIGKNAKYilD 332
Cdd:cd07136 235 NAGQTCVAPDYVLVHESVKEKFIKELKEeiKKFYgeDPLESPDYGRIinEKhfdrlaGLLDNG----KIVFGGNTDR--E 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 518847611 333 TLGIEcpydPRLIImETHKEHPFAVKELMMPVLPLIRCKDFDEALDL 379
Cdd:cd07136 309 TLYIE----PTILD-NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEI 350
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
115-284 |
3.52e-07 |
|
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: 52.19 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 115 TGDDGLSLIEFSPFGVIGAITPVTNPtetII--CNSINM-LSAGNSVVFSPHPSAVKVSnWLVGkinEAIIEAG---GER 188
Cdd:cd07105 86 DKPGTLAMVVKEPVGVVLGIAPWNAP---VIlgTRAIAYpLAAGNTVVLKASELSPRTH-WLIG---RVFHEAGlpkGVL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 189 NLVVTISKASVEEVDYLMESPKVNALCITGGMPIvikglksGKKtIGAGA------------GNPPVIVDETADIEQAAA 256
Cdd:cd07105 159 NVVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRV-------GRI-IAETAakhlkpvllelgGKAPAIVLEDADLDAAAN 230
|
170 180
....*....|....*....|....*...
gi 518847611 257 DIVAGASLDNNMPCIAEKEVLAVDSIFD 284
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIAD 258
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
127-284 |
3.81e-07 |
|
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: 52.17 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTeTIICNSIN-MLSAGNSVVF--SPHPSAVKVsnwlvgKINEAIIEAG---GERNlVVTISKASVE 200
Cdd:cd07114 119 PLGVVAAITPWNSPL-LLLAKKLApALAAGNTVVLkpSEHTPASTL------ELAKLAEEAGfppGVVN-VVTGFGPETG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 201 EVdyLMESPKVNALCITGGmpivikgLKSGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGASLDNNMP 269
Cdd:cd07114 191 EA--LVEHPLVAKIAFTGG-------TETGRHIARAAAenlapvtlelgGKSPNIVFDDADLDAAVNGVVAGIFAAAGQT 261
|
170
....*....|....*
gi 518847611 270 CIAEKEVLAVDSIFD 284
Cdd:cd07114 262 CVAGSRLLVQRSIYD 276
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
107-380 |
4.73e-07 |
|
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: 51.84 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 107 EDLKTGALTGDDGLSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSnwlvgKINEAIIEAGG 186
Cdd:cd07135 88 EKVKDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTA-----ALLAELVPKYL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 187 ERNLVVTISKAsVEEVDYLMESpKVNALCITGgmpivikglkSGK--KTIGAGA------------GNPPVIVDETADIE 252
Cdd:cd07135 163 DPDAFQVVQGG-VPETTALLEQ-KFDKIFYTG----------SGRvgRIIAEAAakhltpvtlelgGKSPVIVTKNADLE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 253 QAAADIVAGASLDNNMPCIAEKEVLAVDSIFDYLMFNMEKN-NAF---KISKKEDMVKLekgvINE----------DGSV 318
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVlDEFypgGANASPDYTRI----VNPrhfnrlksllDTTK 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518847611 319 NKKFIGKNAkyILDTLGIecpydPRLIIMETHKEHPFAVKELMMPVLPLIRCKDFDEALDLA 380
Cdd:cd07135 307 GKVVIGGEM--DEATRFI-----PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVI 361
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
127-442 |
1.38e-06 |
|
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: 50.42 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIIEAGgernlVVTISKASVEEV-DYL 205
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPG-----VVNVVHGRGEEVgEAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 206 MESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDS 281
Cdd:cd07131 210 VEHPDVDVVSFTGstevGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 282 IFDYL--MFnMEKNNAFKISKKEDMVKLEKGVINEDGsVNKKF----IGKN--AKYILDTLGIE-------CPYDPRLII 346
Cdd:cd07131 290 VYDEFlkRF-VERAKRLRVGDGLDEETDMGPLINEAQ-LEKVLnyneIGKEegATLLLGGERLTgggyekgYFVEPTVFT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 347 METHKEHpFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQTTIFVKNAPSyagigLG 426
Cdd:cd07131 368 DVTPDMR-IAQEEIFGPVVALIEVSSLEEAIEIANDTEYGL--SSAIYTEDVNKAFRARRDLEAGITYVNAPT-----IG 439
|
330
....*....|....*.
gi 518847611 427 GEGYTSFTLASSTGDG 442
Cdd:cd07131 440 AEVHLPFGGVKKSGNG 455
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
121-378 |
1.70e-06 |
|
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: 50.30 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVV-----FSPHPSAVkvsnwlVGKIneaIIEAGGERNlvVTIS 195
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAIlkpseLTPHTSAV------IAKI---IREAFDEDE--VAVF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 196 KASVEEVDYLMESPkVNALCITGGmPIVikglksGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGASL 264
Cdd:cd07134 163 EGDAEVAQALLELP-FDHIFFTGS-PAV------GKIVMAAAAkhlasvtlelgGKSPTIVDETADLKKAAKKIAWGKFL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 265 DNNMPCIAEkevlavdsifDYLMFNMEKNNAFKISKKEDMVK-LEKGVINEDGS-----VNKKF-----------IGKNA 327
Cdd:cd07134 235 NAGQTCIAP----------DYVFVHESVKDAFVEHLKAEIEKfYGKDAARKASPdlariVNDRHfdrlkgllddaVAKGA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518847611 328 K------------YILDTLGIECPydPRLIIMEthkehpfavKELMMPVLPLIRCKDFDEALD 378
Cdd:cd07134 305 KvefggqfdaaqrYIAPTVLTNVT--PDMKIMQ---------EEIFGPVLPIITYEDLDEVIE 356
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
127-284 |
9.21e-06 |
|
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: 47.82 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPhPSAVKVSNWLVGKI-NEAIIEAGgernlVVTISKASVEEV-DY 204
Cdd:cd07115 117 PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP-AELTPLSALRIAELmAEAGFPAG-----VLNVVTGFGEVAgAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 205 LMESPKVNALCITGGMPIvikglksGKKTIGAGAGN-----------PPVIVDETADIEQAAADIVAGASLDNNMPCIAE 273
Cdd:cd07115 191 LVEHPDVDKITFTGSTAV-------GRKIMQGAAGNlkrvslelggkSANIVFADADLDAAVRAAATGIFYNQGQMCTAG 263
|
170
....*....|.
gi 518847611 274 KEVLAVDSIFD 284
Cdd:cd07115 264 SRLLVHESIYD 274
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
38-432 |
1.84e-05 |
|
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: 47.06 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 38 EAIEYASIAQKKFLCSSLSERKKITdsirNKLRPLIKEMS--VMTVEESKMGrvedKINKNTLAIERCTGVEDLK--TGA 113
Cdd:cd07117 42 RAVKAAQEAFKTWRKTTVAERANIL----NKIADIIDENKelLAMVETLDNG----KPIRETRAVDIPLAADHFRyfAGV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 114 LTGDDG---------LSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPhPSAVKVSNWLVGKINEAIIEA 184
Cdd:cd07117 114 IRAEEGsanmidedtLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKP-SSTTSLSLLELAKIIQDVLPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 185 GgernLVVTISKASVEEVDYLMESPKVNALCITGGMPIVIK-GLKSGKKTIGAG---AGNPPVIVDETADIEQAAADIVA 260
Cdd:cd07117 193 G----VVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDvAIAAAKKLIPATlelGGKSANIIFDDANWDKALEGAQL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 261 GASLDNNMPCIAEKEVLAVDSIFDYLMFNM-EKNNAFKISKKEDMVKLEKGVINEDgSVNKKF----IGKNAKYILDTLG 335
Cdd:cd07117 269 GILFNQGQVCCAGSRIFVQEGIYDEFVAKLkEKFENVKVGNPLDPDTQMGAQVNKD-QLDKILsyvdIAKEEGAKILTGG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 336 ---IECPYD------PRLIIMETHkEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPK 406
Cdd:cd07117 348 hrlTENGLDkgffiePTLIVNVTN-DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGL--GGGVFTKDINRALRVAR 424
|
410 420 430
....*....|....*....|....*....|....*.
gi 518847611 407 RLQT--------TIFVKNAP--SYAGIGLGGEGYTS 432
Cdd:cd07117 425 AVETgrvwvntyNQIPAGAPfgGYKKSGIGRETHKS 460
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
127-266 |
3.20e-05 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 46.14 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHP----SAVKVSnwlvgkinEAIIEAG---GERNLVvtisKASV 199
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPftplTALLLA--------EILTEAGlpdGVFNVV----QGGG 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518847611 200 EEVDYLMESPKVNALCITGGMPivikglkSGKKTIGAGA-----------GNPPVIVDETADIEQAaadiVAGASLDN 266
Cdd:cd07090 184 ETGQLLCEHPDVAKVSFTGSVP-------TGKKVMSAAAkgikhvtlelgGKSPLIIFDDADLENA----VNGAMMAN 250
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
120-284 |
3.73e-05 |
|
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: 45.80 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 120 LSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPsavkvsnwLVGKINEAIIEAGGE-----RNLVVTI 194
Cdd:cd07120 110 FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG--------QTAQINAAIIRILAEipslpAGVVNLF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 195 SKASVEEVDYLMESPKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPC 270
Cdd:cd07120 182 TESGSEGAAHLVASPDVDVISFTGstatGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFC 261
|
170
....*....|....
gi 518847611 271 IAEKEVLAVDSIFD 284
Cdd:cd07120 262 MAGSRVLVQRSIAD 275
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
126-409 |
6.17e-05 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 45.11 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 126 SPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPhpSAVKVSNWLV-GKINEAIIEAGGERNLVVtiskASVEEVDY 204
Cdd:PRK10090 70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKP--SEFTPNNAIAfAKIVDEIGLPKGVFNLVL----GRGETVGQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 205 LMES-PKVNALCITGGMPIVIKGLKSGKKTIGAGA----GNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAV 279
Cdd:PRK10090 144 ELAGnPKVAMVSMTGSVSAGEKIMAAAAKNITKVClelgGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 280 DSIFDYLMFNMEKN-NAFKISKKEDMVKLEKG-VINEDG--SVNKKF---IGKNAKYILD---TLGIECPYDPRLIImET 349
Cdd:PRK10090 224 KGIYDQFVNRLGEAmQAVQFGNPAERNDIAMGpLINAAAleRVEQKVaraVEEGARVALGgkaVEGKGYYYPPTLLL-DV 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 350 HKEHPFAVKELMMPVLPLIRCKDFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQ 409
Cdd:PRK10090 303 RQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGL--TSSIYTQNLNVAMKAIKGLK 360
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
120-284 |
1.03e-04 |
|
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: 44.59 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 120 LSLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEaiiEAGGERNLV-VTISKAS 198
Cdd:cd07152 103 LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFE---EAGLPAGVLhVLPGGAD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 199 VEEVdyLMESPKVNALCITGGMPIvikglksGKKtIGAGA------------GNPPVIVDETADIEQAAADIVAGASLDN 266
Cdd:cd07152 180 AGEA--LVEDPNVAMISFTGSTAV-------GRK-VGEAAgrhlkkvslelgGKNALIVLDDADLDLAASNGAWGAFLHQ 249
|
170
....*....|....*...
gi 518847611 267 NMPCIAEKEVLAVDSIFD 284
Cdd:cd07152 250 GQICMAAGRHLVHESVAD 267
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
121-284 |
1.51e-04 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 43.96 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 121 SLIEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSpHPSAV-KVSNWLVGKINEAIIEAGGERNLVvtISKASV 199
Cdd:PRK09406 117 AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK-HASNVpQTALYLADLFRRAGFPDGCFQTLL--VGSGAV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 200 EEVdylMESPKVNALCITGGMPI-----VIKGlKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEK 274
Cdd:PRK09406 194 EAI---LRDPRVAAATLTGSEPAgravaAIAG-DEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAK 269
|
170
....*....|
gi 518847611 275 EVLAVDSIFD 284
Cdd:PRK09406 270 RFIVHADVYD 279
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
123-379 |
1.55e-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: 43.94 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 123 IEFSPFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAVKVSNWLVGKINEAIieaggeRNLVVTISKASVEEV 202
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYL------DTKAIKVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 203 DYLMESpKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETADIEQAAADIVAGA-SLDNNMPC 270
Cdd:cd07137 171 TALLEQ-KWDKIFFTGSPRV-------GRIIMAAAAkhltpvtlelgGKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQAC 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 271 IAEKEVLaVDSIF-----DYLMFNMEK---------NNAFKISKKEDMVKLEKgvINEDGSVNKKFI---GKNAK--YIL 331
Cdd:cd07137 243 IAPDYVL-VEESFaptliDALKNTLEKffgenpkesKDLSRIVNSHHFQRLSR--LLDDPSVADKIVhggERDEKnlYIE 319
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518847611 332 DTLGIECPYDPrlIIMethkehpfaVKELMMPVLPLIRCKDFDEALDL 379
Cdd:cd07137 320 PTILLDPPLDS--SIM---------TEEIFGPLLPIITVKKIEESIEI 356
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
126-284 |
1.64e-04 |
|
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: 43.71 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 126 SPFGVIGAITPVTNPTetiicnsinMLS---------AGNSVV-----FSPhpsavkVSNWLVGKI-NEAIIEAGgernl 190
Cdd:cd07093 116 QPVGVAGLITPWNLPL---------MLLtwkiapalaFGNTVVlkpseWTP------LTAWLLAELaNEAGLPPG----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 191 VVTISKASVEEV-DYLMESPKVNALCITGGMPIvikglksGKKTIGAGA-----------GNPPVIVDETADIEqAAADI 258
Cdd:cd07093 176 VVNVVHGFGPEAgAALVAHPDVDLISFTGETAT-------GRTIMRAAApnlkpvslelgGKNPNIVFADADLD-RAVDA 247
|
170 180
....*....|....*....|....*..
gi 518847611 259 VAGASLDNN-MPCIAEKEVLAVDSIFD 284
Cdd:cd07093 248 AVRSSFSNNgEVCLAGSRILVQRSIYD 274
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
152-262 |
3.63e-04 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 43.02 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 152 LSAGNSVVFSPHPSAVKVSNWLVgkinEAIIEAG---GERNLVvtisKASVEEVDYLMESPKVNALCITG---------- 218
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTV----KLWQQAGlpaGVLNLV----QGGRETGKALAAHPDIDGLLFTGsantgyllhr 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518847611 219 ---GMPIVIKGLKSGkktigagaGNPPVIVDETADIEQAAADIVAGA 262
Cdd:PRK09457 231 qfaGQPEKILALEMG--------GNNPLVIDEVADIDAAVHLIIQSA 269
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| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
127-379 |
8.23e-04 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 41.57 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 127 PFGVIGAITPVTNPTETIICNSINMLSAGNSVVFSPHPSAvKVSNWLVGKINEAIIEAGgernlVVTISKASVEEVDYLM 206
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELA-PASSALLAKLLEQYLDSS-----AVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 207 ESpKVNALCITG----GMPIVIKGLKSGKKTIGAGAGNPPVIVDETADIEQAAADIVAGA-SLDNNMPCIAEKEVLAVDS 281
Cdd:PLN02174 186 EQ-KWDKIFYTGsskiGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKwGCNNGQACISPDYILTTKE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 282 ----IFDYLMFNMEKNNAFKISKKEDMVKLEKG--------VINEDGSVNKKFIG-----KNAKyILDTLGIECPYDpRL 344
Cdd:PLN02174 265 yapkVIDAMKKELETFYGKNPMESKDMSRIVNSthfdrlskLLDEKEVSDKIVYGgekdrENLK-IAPTILLDVPLD-SL 342
|
250 260 270
....*....|....*....|....*....|....*
gi 518847611 345 IIMEthkehpfavkELMMPVLPLIRCKDFDEALDL 379
Cdd:PLN02174 343 IMSE----------EIFGPLLPILTLNNLEESFDV 367
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| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
91-434 |
2.09e-03 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 40.27 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 91 DKINKNTLAIerctgvedlktgaltGDDGLSLIEFSPFGVIGAITPVTNPtetiicnsINM--------LSAGNSVVFSP 162
Cdd:cd07091 120 DKIQGKTIPI---------------DGNFLAYTRREPIGVCGQIIPWNFP--------LLMlawklapaLAAGNTVVLKP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 163 H---P-SAVKVSNWlvgkINEAIIEAGgernlVVTISKASVEEV-DYLMESPKVNALCITG----GMPIVIKGLKSGKK- 232
Cdd:cd07091 177 AeqtPlSALYLAEL----IKEAGFPPG-----VVNIVPGFGPTAgAAISSHMDVDKIAFTGstavGRTIMEAAAKSNLKk 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 233 -TIGAGaGNPPVIVDETADIEQAAADIVAGASLDNNMPCIAEKEVLAVDSIFDYLMFNM-EKNNAFKISKKEDMvKLEKG 310
Cdd:cd07091 248 vTLELG-GKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFkARAEKRVVGDPFDP-DTFQG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518847611 311 VINEDGSVNK--KFI--GKNAK---------------YILDTLGIECPYDprliiMETHKEHPFAvkelmmPVLPLIRCK 371
Cdd:cd07091 326 PQVSKAQFDKilSYIesGKKEGatlltggerhgskgyFIQPTVFTDVKDD-----MKIAKEEIFG------PVVTILKFK 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518847611 372 DFDEALDLAVKLEDGCrhTAAMHSKHIDRLTIAPKRLQT-TIFVK--NAPSYA---------GIG--LGGEGYTSFT 434
Cdd:cd07091 395 TEDEVIERANDTEYGL--AAGVFTKDINKALRVSRALKAgTVWVNtyNVFDAAvpfggfkqsGFGreLGEEGLEEYT 469
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