|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
1-514 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 998.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 1 MVVEFKNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLVINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFK 80
Cdd:PRK03137 1 MVVPYKHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 81 AANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDR 160
Cdd:PRK03137 81 AALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 161 EGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKE 240
Cdd:PRK03137 161 PGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 241 IGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKC 320
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 321 SACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPT 400
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 401 IISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGY 480
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
490 500 510
....*....|....*....|....*....|....
gi 616190054 481 HPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:PRK03137 481 HPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-514 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 875.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 5 FKNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLVINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANE 84
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 85 AYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaQGKPVLDREGEH 164
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL-RGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 165 NKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 245 LVDHKDTHFVTFTGSRATGTRIYERSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACS 324
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 325 RAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDD--SKGYFVEPTI 401
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPeVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLElaAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 402 ISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYH 481
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQ 479
|
490 500 510
....*....|....*....|....*....|...
gi 616190054 482 PFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:cd07124 480 PFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-514 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 731.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 5 FKNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLVINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANE 84
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 85 AYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDREGEH 164
Cdd:TIGR01237 81 AFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 165 NKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:TIGR01237 161 NQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 245 LVDHKDTHFVTFTGSRATGTRIYERSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACS 324
Cdd:TIGR01237 241 LVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 325 RAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPTIIS 403
Cdd:TIGR01237 321 RAVVHEKVYDEVVERFVEITESLKVGPPDSaDVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 404 GLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPF 483
Cdd:TIGR01237 401 DVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500 510
....*....|....*....|....*....|.
gi 616190054 484 GGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
35-512 |
0e+00 |
|
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: 562.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 35 QDIPLVINGEKIF--KDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRK 112
Cdd:COG1012 4 PEYPLFIGGEWVAaaSGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 113 AEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTT 192
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 193 LAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAv 272
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 273 vqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNT 352
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 353 VD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGT-DDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDF 429
Cdd:COG1012 317 LDpGTDMGPLISEAQLERVLAYIEDAVAEGaELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 430 DEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAvVGYHPFGGFKMSGTDAKtGSPDYLLHFLEQKV 509
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
...
gi 616190054 510 VSE 512
Cdd:COG1012 475 VTI 477
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
49-510 |
0e+00 |
|
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: 538.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 49 DDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWD 128
Cdd:pfam00171 6 SETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 129 EAVGDAAEGIDFIEYYARSMMDLaQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAE 208
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRL-DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMG 288
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA------QNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDpDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:pfam00171 318 ERVLKYVEDAKEEGaKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616190054 447 VITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGyHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADG-LPFGGFKQSGF-GREGGPYGLEEYTEVKTV 459
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-514 |
4.94e-174 |
|
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: 499.80 E-value: 4.94e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 22 FKKALKDVEKELGQDIPLVINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELM 101
Cdd:cd07083 4 MREALRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 102 LRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaQGKPVLDRE--GEHNKYFYKSIGTGVTIP 179
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRL-RYPAVEVVPypGEDNESFYVGLGAGVVIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 180 PWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGS 259
Cdd:cd07083 163 PWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 260 RATGTRIYERSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEK 339
Cdd:cd07083 243 LETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLER 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 340 SIKLTKELTLGNTVDN-TYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFG 418
Cdd:cd07083 323 LLKRAERLSVGPPEENgTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 419 PV--VGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAKTG 496
Cdd:cd07083 403 PVlsVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
490
....*....|....*...
gi 616190054 497 SPDYLLHFLEQKVVSEMF 514
Cdd:cd07083 483 GPHYLRRFLEMKAVAERF 500
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
76-510 |
7.65e-156 |
|
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: 450.89 E-value: 7.65e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 76 EDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGK 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 156 PVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVP 235
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 236 GDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGF 315
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA------ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 316 SGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDS- 392
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDpDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 393 KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrg 472
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN-- 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 616190054 473 CTSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07078 393 DYSVGAEPSaPFGGVKQSGI-GREGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
21-512 |
5.68e-151 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 441.63 E-value: 5.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 21 MFKKALKDVEKELGQDIPLvINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAEL 100
Cdd:cd07125 18 ALADALKAFDEKEWEAIPI-INGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 101 MLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPP 180
Cdd:cd07125 97 LEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 181 WNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSR 260
Cdd:cd07125 177 WNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGST 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 261 ATGTRIyeRSAVVQEGQNFLKrVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKS 340
Cdd:cd07125 257 ETAKLI--NRALAERDGPILP-LIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEML 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 341 IKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPTIISGLKSKDriMQEEIFGP 419
Cdd:cd07125 334 KGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNGYFVAPGIIEIVGIFD--LTTEVFGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 420 VVGFV--KVNDFDEAIEVANDTDYGLTGAVIT-NNRE--HWIKAVNefdVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAK 494
Cdd:cd07125 412 ILHVIrfKAEDLDEAIEDINATGYGLTLGIHSrDEREieYWRERVE---AGNLYINRNITGAIVGRQPFGGWGLSGTGPK 488
|
490
....*....|....*...
gi 616190054 495 TGSPDYLLHFLEQKVVSE 512
Cdd:cd07125 489 AGGPNYLLRFGNEKTVSL 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
40-494 |
1.36e-141 |
|
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: 415.88 E-value: 1.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 40 VINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIM 119
Cdd:cd07097 4 YIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 120 VYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAG 199
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 200 NTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNF 279
Cdd:cd07097 164 NTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA------AR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 280 LKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYM 358
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDeGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 359 GPVINKKQFDKIKNYIEIGKEEG-KLEQGGG--TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEV 435
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGaKLVYGGErlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616190054 436 ANDTDYGLTGAVITNNrehwIKAVNEF----DVGNLYLNRgcTSAVVGYH-PFGGFKMSGTDAK 494
Cdd:cd07097 398 ANDTEFGLSAGIVTTS----LKHATHFkrrvEAGVVMVNL--PTAGVDYHvPFGGRKGSSYGPR 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
54-510 |
3.33e-140 |
|
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: 412.51 E-value: 3.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPADTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD 133
Cdd:cd07131 18 SRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 AAEGIDFIEYYA---RSMmdlaQGkPVLDRE--GEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAE 208
Cdd:cd07131 98 VQEAIDMAQYAAgegRRL----FG-ETVPSElpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMG 288
Cdd:cd07131 173 DTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVALEMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:cd07131 247 GKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDeETDMGPLINEAQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEG-KLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:cd07131 327 EKVLNYNEIGKEEGaTLLLGGerltGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYG 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616190054 443 LTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVgyH-PFGGFKMSGTDAKTGSPDYLLHFLEQKVV 510
Cdd:cd07131 407 LSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV--HlPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-514 |
4.94e-138 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 408.51 E-value: 4.94e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFSV-QENVNMFKKALKDVEKELgQDIPLVINGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANE 84
Cdd:cd07123 2 VNEPVLSYAPgSPERAKLQEALAELKSLT-VEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 85 AYKSWKTWSANDRAELMLRVSAII--RRRKAEIAAIMVYEaGKPWDEAVGDAA-EGIDFIEYYARSMMDLAQGKPVLDRE 161
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLsgKYRYELNAATMLGQ-GKNVWQAEIDAAcELIDFLRFNVKYAEELYAQQPLSSPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 162 GEHNKYFYKSI-GTGVTIPPWNFPfAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKE 240
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 241 IGDYLVDHKDTHFVTFTGSRATGTRIYERSAV-VQEGQNFlKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQK 319
Cdd:cd07123 239 VGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEnLDRYRTY-PRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 320 CSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLE--QGGGTDDSKGYF 396
Cdd:cd07123 318 CSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEiiAGGKCDDSVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 397 VEPTIISGLKSKDRIMQEEIFGPVVGfVKV---NDFDEAIEVANDT-DYGLTGAVITNNRehwiKAVNE------FDVGN 466
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLT-VYVypdSDFEETLELVDTTsPYALTGAIFAQDR----KAIREatdalrNAAGN 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 616190054 467 LYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:cd07123 473 FYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETF 520
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
40-497 |
3.89e-132 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 391.93 E-value: 3.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 40 VINGEKIFKDDK-IKSINPADTsQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07086 2 VIGGEWVGSGGEtFTSRNPANG-EPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVGDAAEGIDfIEYYA----RSMmdlaQGKPVL-DREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTL 193
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMID-ICDYAvglsRML----YGLTIPsERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 194 APVVAGNTVLLKPAEDTPYIAYKLMEILEEA----GLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYER 269
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 270 savVQEgqnFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTL 349
Cdd:cd07086 235 ---VAR---RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 350 GNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGG--TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:cd07086 309 GDPLDeGTLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 426 VNDFDEAIEVANDTDYGLTGAVIT---NNREHWIKAvNEFDVGNLYLNRGCTSAVVGYhPFGGFKMSGTDAKTGS 497
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTedlREAFRWLGP-KGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGS 461
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-510 |
1.28e-131 |
|
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: 390.47 E-value: 1.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07088 2 INGEFVpsSSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVGDAAEGIDFIEYYARSMM----DLAQGkpvlDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAgTTLA 194
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARriegEIIPS----DRPNENIFIFKVPIGVVAGILPWNFPFFLIA-RKLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 195 P-VVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvv 273
Cdd:cd07088 156 PaLVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 274 qegQNfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN-T 352
Cdd:cd07088 234 ---EN-ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDpF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 353 VDNTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDS-KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07088 310 DAATDMGPLVNEAALDKVEEMVERAVEAGaTLLTGGKRPEGeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHpfGGFKMSGT---DAKTGspdyLLHFLEQ 507
Cdd:cd07088 390 EAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLggaDGKHG----LEEYLQT 463
|
...
gi 616190054 508 KVV 510
Cdd:cd07088 464 KVV 466
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
55-511 |
6.40e-130 |
|
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: 385.25 E-value: 6.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07103 2 INPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYA----RSmmdlaQGKPVLDREGEHNKYFYK-SIGTGVTIPPWNFPFAiMAGTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07103 81 DYAASFLEWFAeearRI-----YGRTIPSPAPGKRILVIKqPVGVVAAITPWNFPAA-MITRKIAPALAaGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMG 288
Cdd:cd07103 155 ETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:cd07103 229 GNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDeGTDMGPLINERAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07103 309 EKVEALVEDAVAKGaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 447 VITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGyhPFGGFKMSGTdAKTGSPDYLLHFLEQKVVS 511
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDAEA--PFGGVKESGL-GREGGKEGLEEYLETKYVS 450
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
6-514 |
1.85e-126 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 379.51 E-value: 1.85e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFS-VQENVNMFKKALKDVEKELgQDIPLVINGEKIFKDD-KIKSINPADTSQVIANASKATKQDVEDAFKAAN 83
Cdd:TIGR01236 1 ANEPVLPFRpGSPERDLLRKSLKELKSSS-LEIPLVIGGEEVYDSNeRIPQVNPHNHQAVLAKATNATEEDAMKAVEAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 84 EAYKSWKTWSANDRAELMLRVSAII--RRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVlDRE 161
Cdd:TIGR01236 80 DAKKDWSNLPFYDRAAIFLKAADLLsgPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPI-SAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 162 GEHNKYFYKSI-GTGVTIPPWNFpFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKE 240
Cdd:TIGR01236 159 GEWNRTEYRPLeGFVYAISPFNF-TAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 241 IGDYLVDHKDTHFVTFTGSRATGTRIYERSAV-VQEGQNFlKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQK 319
Cdd:TIGR01236 238 VSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQnLDRYHNF-PRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 320 CSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGK---EEGKLEQGGGTDDSKGY 395
Cdd:TIGR01236 317 CSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDfRGFMGAVIDEQSFDKIVKYIEDAKkdpEALTILYGGKYDDSQGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 396 FVEPTIISGLKSKDRIMQEEIFGPVVGFVKVND--FDEAIEVA-NDTDYGLTGAVITNNREHWIKAVN--EFDVGNLYLN 470
Cdd:TIGR01236 397 FVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDdkYKEILDLVdSTSQYGLTGAVFAKDRKAILEADKklRFAAGNFYIN 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 616190054 471 RGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSEMF 514
Cdd:TIGR01236 477 DKCTGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETF 520
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-510 |
3.05e-122 |
|
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: 365.73 E-value: 3.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV-G 132
Cdd:cd07093 1 NFNPA-TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 133 DAAEGIDFIEYYArsmmDLAQGKP--VLDREGEHNKY-FYKSIGTGVTIPPWNFPFAIMagtT--LAPVVA-GNTVLLKP 206
Cdd:cd07093 80 DIPRAAANFRFFA----DYILQLDgeSYPQDGGALNYvLRQPVGVAGLITPWNLPLMLL---TwkIAPALAfGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 207 AEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnfLKRVIAE 286
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN------LKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 287 MGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TYMGPVINKK 365
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPdTEVGPLISKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 366 QFDKIKNYIEIGKEEG-KLEQGGGTDDS----KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:cd07093 307 HLEKVLGYVELARAEGaTILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 441 YGLTGAVITNNREHWIKAVNEFDVGNLYLN----RGCTSavvgyhPFGGFKMSGTDAKTGspDYLLHF-LEQKVV 510
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDLRT------PFGGVKASGIGREGG--DYSLEFyTELKNV 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
39-490 |
6.56e-122 |
|
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: 365.76 E-value: 6.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEkiFKD----DKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYK--SWKTWSANDRAELMLRVSAIIRRRK 112
Cdd:cd07091 6 LFINNE--FVDsvsgKTFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 113 AEIAAIMVYEAGKPWDE-AVGDAAEGIDFIEYYArSMMDLAQGKpVLDREGEHNKYFYKS-IGTGVTIPPWNFPFaIMAG 190
Cdd:cd07091 83 DELAALESLDNGKPLEEsAKGDVALSIKCLRYYA-GWADKIQGK-TIPIDGNFLAYTRREpIGVCGQIIPWNFPL-LMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 191 TTLAP-VVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYER 269
Cdd:cd07091 160 WKLAPaLAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 270 SAvvqegQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTL 349
Cdd:cd07091 240 AA-----KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 350 GNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVN 427
Cdd:cd07091 315 GDPFDpDTFQGPQVSKAQFDKILSYIESGKKEGaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616190054 428 DFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgcTSAVVGYH-PFGGFKMSG 490
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-510 |
9.62e-121 |
|
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: 362.25 E-value: 9.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV 131
Cdd:cd07114 1 SINPA-TGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 132 GDAAEGIDFIEYYArSMMDLAQGK--PVlDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07114 80 AQVRYLAEWYRYYA-GLADKIEGAviPV-DKGDYLNFTRREPLGVVAAITPWNSPLLLLA-KKLAPALAaGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegQNFlKRVIAEMG 288
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-----ENL-APVTLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:cd07114 231 GKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDpETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEG-KLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:cd07114 311 EKVERYVARAREEGaRVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616190054 443 LTGAVITNN--REHwiKAVNEFDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07114 391 LAAGIWTRDlaRAH--RVARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIGRENGI-EAIREYTQTKSV 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
80-510 |
1.22e-117 |
|
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: 350.76 E-value: 1.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 80 KAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLD 159
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 160 REGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPK 239
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 240 EIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQK 319
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAA------ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 320 CSACSRAIVHKDVYDEVLEKsikltkeltlgntvdntymgpvinkkqfdkiknyieigkeegkleqgggtddskgyFVep 399
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEK--------------------------------------------------------LV-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 400 TIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVG 479
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|.
gi 616190054 480 YhPFGGFKMSGTDAKtGSPDYLLHFLEQKVV 510
Cdd:cd06534 337 A-PFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
55-511 |
2.04e-117 |
|
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: 352.99 E-value: 2.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07106 2 INPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARsmMDLAQgKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTtLAP-VVAGNTVLLKPAEDTPYI 213
Cdd:cd07106 81 GGAVAWLRYTAS--LDLPD-EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWK-IAPaLLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 214 AYKLMEILEEAgLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAI 293
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGG-DELGPALTSHPDIRKISFTGSTATGKKVMASAA------KTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 294 VVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN-TVDNTYMGPVINKKQFDKIKN 372
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDgLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 373 YIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNN 451
Cdd:cd07106 309 LVEDAKAKGaKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616190054 452 REHWIKAVNEFDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVS 511
Cdd:cd07106 389 LERAEAVARRLEAGTVWIN---THGALDPDaPFGGHKQSGIGVEFG-IEGLKEYTQTQVIN 445
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
54-490 |
3.56e-116 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 350.38 E-value: 3.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKS-WKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVG 132
Cdd:cd07109 1 VFDPS-TGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 133 DAAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPfAIMAGTTLAPVVA-GNTVLLKPAEDTP 211
Cdd:cd07109 80 DVEAAARYFEYYG-GAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYP-LQITGRSVAPALAaGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 212 YIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIyERSAvvqeGQNFlKRVIAEMGGKD 291
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAV-MRAA----AENV-VPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 292 AIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIK 371
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 372 NYIEIGKEEGKLEQGGGT----DDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:cd07109 312 GFVARARARGARIVAGGRiaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 616190054 448 ITNN--REHWIkaVNEFDVGNLYLNRGCTSAVVGYhPFGGFKMSG 490
Cdd:cd07109 392 WTRDgdRALRV--ARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSG 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
41-490 |
1.65e-115 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 349.11 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07138 3 IDGAWVapAGTETIDVINPA-TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVGDAAE-GIDFIEYYARSMMDLA----QGKPVLDREgehnkyfykSIGTGVTIPPWNFPFAIMAGTTL 193
Cdd:cd07138 82 ITLEMGAPITLARAAQVGlGIGHLRAAADALKDFEfeerRGNSLVVRE---------PIGVCGLITPWNWPLNQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 194 APVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVV 273
Cdd:cd07138 153 PALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 274 qegqnfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTV 353
Cdd:cd07138 233 ------VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 354 D-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGG-GTDD--SKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVND 428
Cdd:cd07138 307 DpATTLGPLASAAQFDRVQGYIQKGIEEGaRLVAGGpGRPEglERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616190054 429 FDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVgyhPFGGFKMSG 490
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA---PFGGYKQSG 445
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
74-490 |
3.61e-114 |
|
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: 344.13 E-value: 3.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 74 DVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAQ 153
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILRE-AAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 154 GKpVL--DREGEHNKYFYKSIGT-GVtIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTPY-IAYKLMEILEEAGLPK 228
Cdd:cd07104 80 GE-ILpsDVPGKESMVRRVPLGVvGV-ISPFNFPL-ILAMRSVAPALAlGNAVVLKPDSRTPVtGGLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 229 GVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnfLKRVIAEMGGKDAIVVDENIDTDMAAEAI 308
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRH------LKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 309 VTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQG 386
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDpDTVIGPLINERQVDRVHAIVEDAVAAGaRLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 387 GGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGN 466
Cdd:cd07104 311 GTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420
....*....|....*....|....*
gi 616190054 467 LYLNrgCTSAVVGYH-PFGGFKMSG 490
Cdd:cd07104 388 VHIN--DQTVNDEPHvPFGGVKASG 410
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
31-490 |
4.24e-113 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 343.62 E-value: 4.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 31 KELGQDIPLVINGE--KIFKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKT-WSANDRAELMLRVSAI 107
Cdd:cd07144 2 KSYDQPTGLFINNEfvKSSDGETIKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 108 IRRRKAEIAAIMVYEAGKPWDE-AVGDAAEGIDFIEYYARSMmDLAQGKPVldrEGEHNKYFY---KSIGTGVTIPPWNF 183
Cdd:cd07144 81 VEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWA-DKIQGKTI---PTSPNKLAYtlhEPYGVCGQIIPWNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 184 PFAiMAGTTLAPVVA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRAT 262
Cdd:cd07144 157 PLA-MAAWKLAPALAaGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 263 GTRIYERSAvvqegQNfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIK 342
Cdd:cd07144 236 GRLVMKAAA-----QN-LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 343 LTKE-LTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGG---GTDDSKGYFVEPTIISGLKSKDRIMQEEI 416
Cdd:cd07144 310 HVKQnYKVGSPFDdDTVVGPQVSKTQYDRVLSYIEKGKKEGaKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616190054 417 FGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVvgYHPFGGFKMSG 490
Cdd:cd07144 390 FGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
54-490 |
1.61e-112 |
|
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: 340.96 E-value: 1.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVG- 132
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 133 DAAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTP 211
Cdd:cd07115 80 DVPRAADTFRYYA-GWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPL-MFAAWKVAPALAaGNTVVLKPAELTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 212 YIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnfLKRVIAEMGGKD 291
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGN------LKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 292 AIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKI 370
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDpKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 371 KNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVIT 449
Cdd:cd07115 312 LDYVDVGREEGaRLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 616190054 450 NN--REH-----------WIKAVNEFDVGNlylnrgctsavvgyhPFGGFKMSG 490
Cdd:cd07115 392 RDlgRAHrvaaalkagtvWINTYNRFDPGS---------------PFGGYKQSG 430
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
55-510 |
5.49e-112 |
|
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: 339.60 E-value: 5.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWkTWS--ANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKP------ 126
Cdd:cd07089 2 INPA-TEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWStdAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtara 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 127 --WD---EAVGDAAEGIDFIEY---YARSMMDLAQGKPVLDREgehnkyfykSIGTGVTIPPWNFPFAIMAGTTLAPVVA 198
Cdd:cd07089 80 mqVDgpiGHLRYFADLADSFPWefdLPVPALRGGPGRRVVRRE---------PVGVVAAITPWNFPFFLNLAKLAPALAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 199 GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqn 278
Cdd:cd07089 151 GNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 279 fLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTY 357
Cdd:cd07089 226 -LKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADpGTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 358 MGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDS--KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIE 434
Cdd:cd07089 305 MGPLISAAQRDRVEGYIARGRDEGaRLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVR 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 435 VANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVvgYHPFGGFKMSGTDAKTGsPDYLLHFLEQKVV 510
Cdd:cd07089 385 IANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLGRENG-IEGLEEFLETKSI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
50-507 |
2.60e-111 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 338.04 E-value: 2.60e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 50 DKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWkTWSANDRAE---LMLRVSAIIRRRKAEIAAIMVYEAGKP 126
Cdd:cd07112 2 ETFATINPA-TGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAErkaVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 127 WDEAV-GDAAEGIDFIEYYARSMmDLAQGK--PV-------LDREgehnkyfykSIGTGVTIPPWNFPfAIMAGTTLAPV 196
Cdd:cd07112 80 ISDALaVDVPSAANTFRWYAEAI-DKVYGEvaPTgpdalalITRE---------PLGVVGAVVPWNFP-LLMAAWKIAPA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 197 VA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSavvqe 275
Cdd:cd07112 149 LAaGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYS----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 276 GQNFLKRVIAEMGGKDA-IVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD 354
Cdd:cd07112 224 GQSNLKRVWLECGGKSPnIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 355 -NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTD--DSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07112 304 pATRMGALVSEAHFDKVLGYIESGKAEGaRLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGtdaktGSPDYLLHFLEQ 507
Cdd:cd07112 384 EAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG-----NGRDKSLHALDK 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
56-490 |
5.09e-111 |
|
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: 336.99 E-value: 5.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 56 NPADTSqVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAA 135
Cdd:cd07150 5 NPADGS-VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 136 EGIDFIEYyARSMMDLAQGKpVL--DREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYI 213
Cdd:cd07150 84 FTPELLRA-AAGECRRVRGE-TLpsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 214 AYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVvqegqnFLKRVIAEMGGKDAI 293
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR------HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 294 VVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKN 372
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDpDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 373 YIEIGKEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNN 451
Cdd:cd07150 316 QVEDAVAKGaKLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 616190054 452 REHWIKAVNEFDVGNLYLNrgCTSAVVGYH-PFGGFKMSG 490
Cdd:cd07150 393 LQRAFKLAERLESGMVHIN--DPTILDEAHvPFGGVKASG 430
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
55-512 |
2.91e-109 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 332.78 E-value: 2.91e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARSMMDLAQGKPV---LDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDT 210
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERavpLPSEDFKARVRREPVGVVGLITPWNFPL-LMAAWKVAPALAaGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 211 PYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnfLKRVIAEMGGK 290
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD------IKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 291 DAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNT-VDNTYMGPVINKKQFDK 369
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 370 IKNYIEIGKEEG-KLEQGGGTDD--SKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 447 VITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGsPDYLLHFLEQKVVSE 512
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIGRELG-EWGLDNYLEVKQITR 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
55-491 |
4.50e-109 |
|
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: 331.87 E-value: 4.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPADtSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07149 4 ISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARSMMDLA-QGKPVLDREGEHNK--YFYKS-IGTGVTIPPWNFPFAIMA---GTTLApvvAGNTVLLKPA 207
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAgETIPFDASPGGEGRigFTIREpIGVVAAITPFNFPLNLVAhkvGPAIA---AGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 208 EDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqnfLKRVIAEM 287
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 288 GGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQ 366
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDeDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 367 FDKIKNYIEIGKEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:cd07149 312 AERIEEWVEEAVEGGaRLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 616190054 446 AVITNNREHWIKAVNEFDVGNLYLNRGcTSAVVGYHPFGGFKMSGT 491
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMINDS-STFRVDHMPYGGVKESGT 433
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
49-510 |
7.20e-109 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 332.23 E-value: 7.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 49 DDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAY--KSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKP 126
Cdd:cd07139 13 SETIDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 127 -WDEAVGDAAEGIDFIEYYArsmmDLAQGKPVLDR----EGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTtLAP-VVAGN 200
Cdd:cd07139 92 iSWSRRAQGPGPAALLRYYA----ALARDFPFEERrpgsGGGHVLVRREPVGVVAAIVPWNAPLFLAALK-IAPaLAAGC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 201 TVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFL 280
Cdd:cd07139 167 TVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG------ERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 281 KRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMG 359
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDpATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 360 PVINKKQFDKIKNYIEIGKEEG-KLEQGGG--TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGaRLVTGGGrpAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 437 NDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgctSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGI-GREGGPEGLDAYLETKSI 469
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
55-508 |
3.19e-108 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 330.81 E-value: 3.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPADTSqVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVG 132
Cdd:cd07119 18 INPANGE-VIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 133 DAAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTLAP-VVAGNTVLLKPAEDTP 211
Cdd:cd07119 97 DIDDVANCFRYYA-GLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPL-LQAAWKLAPaLAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 212 YIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKD 291
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA------GNVKKVALELGGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 292 AIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKI 370
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDaDTEMGPLVSAEHREKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 371 KNYIEIGKEEG-KLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:cd07119 329 LSYIQLGKEEGaRLVCGGkrptGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616190054 446 AVITNNREHWIKAVNEFDVGNLYLNRgctsavvgYH------PFGGFKMSGTDAKTGsPDYLLHFLEQK 508
Cdd:cd07119 409 AVWTKDIARANRVARRLRAGTVWIND--------YHpyfaeaPWGGYKQSGIGRELG-PTGLEEYQETK 468
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
55-490 |
1.24e-106 |
|
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: 325.80 E-value: 1.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07090 2 IEPA-TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARSMMDLAqgkpvldreGEH-----NKYFY---KSIGTGVTIPPWNFPFAImAGTTLAPVVA-GNTVLLK 205
Cdd:cd07090 81 DSSADCLEYYAGLAPTLS---------GEHvplpgGSFAYtrrEPLGVCAGIGAWNYPIQI-ASWKSAPALAcGNAMVYK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 206 PAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIA 285
Cdd:cd07090 151 PSPFTPLTALLLAEILTEAGLPDGVFNVVQGG-GETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 286 EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TYMGPVINK 364
Cdd:cd07090 224 ELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEdTQMGALISE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 365 KQFDKIKNYIEIGKEEG-KLEQGG----GTDDSK-GYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:cd07090 304 EHLEKVLGYIESAKQEGaKVLCGGervvPEDGLEnGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRAND 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 439 TDYGLTGAVITNN--REHwiKAVNEFDVGNLYLNR-GCTSAVVgyhPFGGFKMSG 490
Cdd:cd07090 384 TTYGLAAGVFTRDlqRAH--RVIAQLQAGTCWINTyNISPVEV---PFGGYKQSG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
55-511 |
2.38e-106 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 325.08 E-value: 2.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPW-DEAVGD 133
Cdd:cd07108 2 INPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 AAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYI 213
Cdd:cd07108 81 AAVLADLFRYFG-GLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 214 AYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqnflKRVIA---EMGGK 290
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvslELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 291 DAIVVDENIDTDMAAEAIVTSA-FGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TYMGPVINKKQFD 368
Cdd:cd07108 230 SPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEaTDIGAIISEKQFA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 369 KIKNYIEIGKE--EGKLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:cd07108 310 KVCGYIDLGLStsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616190054 443 LTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAV-VGYhpfGGFKMSGTdAKTGSPDYLL-HFLEQKVVS 511
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPgQSY---GGFKQSGL-GREASLEGMLeHFTQKKTVN 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
55-510 |
1.15e-105 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 324.30 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYK---SWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEA- 130
Cdd:cd07141 27 INPA-TGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 131 VGDAAEGIDFIEYYArSMMDLAQGK--PVldrEGEHNKYFYKS-IGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKP 206
Cdd:cd07141 106 LVDLPGAIKVLRYYA-GWADKIHGKtiPM---DGDFFTYTRHEpVGVCGQIIPWNFPL-LMAAWKLAPALAcGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 207 AEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSavvqeGQNFLKRVIAE 286
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA-----GKSNLKRVTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 287 MGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKK 365
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDpKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 366 QFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLT 444
Cdd:cd07141 336 QFKKILELIESGKKEGaKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 445 GAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07141 416 AAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGE-YGLQEYTEVKTV 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
54-510 |
2.00e-105 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 322.79 E-value: 2.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD 133
Cdd:cd07107 1 VINPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 AAEGIDFIEYYARSMMDLaQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYI 213
Cdd:cd07107 80 VMVAAALLDYFAGLVTEL-KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 214 AYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIyERSAVvqEGqnfLKRVIAEMGGKDAI 293
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAI-MRAAA--EG---IKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 294 VVDENIDTDMAAEAIVTSA-FGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN-TVDNTYMGPVINKKQFDKIK 371
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDpTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 372 NYIEIGKEEG-KLEQGGGTDD----SKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07107 312 HYIDSAKREGaRLVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616190054 447 VITNNREHWIKAVNEFDVGNLYLNRgctsavVGYH----PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWING------SSRHflgaPFGGVKNSGIGREECL-EELLSYTQEKNV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
55-491 |
1.25e-104 |
|
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: 320.43 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD- 133
Cdd:cd07092 2 VDPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 AAEGIDFIEYYA---RSMMDLAQGKPVldrEGeHNKYFYK-SIGTGVTIPPWNFPFAiMAGTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07092 81 LPGAVDNFRFFAgaaRTLEGPAAGEYL---PG-HTSMIRRePIGVVAQIAPWNYPLM-MAAWKIAPALAaGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEaGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYeRSAVVQegqnfLKRVIAEMG 288
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVA-RAAADT-----LKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDeDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAV 447
Cdd:cd07092 309 ERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 616190054 448 ITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGT 491
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVN--THIPLAAEMPHGGFKQSGY 430
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-511 |
1.98e-103 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 332.93 E-value: 1.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLvINGEKifkdDKIKSINPADTSQVIANASKATKQDVEDAFKAANEA 85
Cdd:PRK11904 523 KNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPI-INGEG----EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 86 YKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYA---RSMMdlAQGKPVLDREG 162
Cdd:PRK11904 598 FPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAaqaRRLF--GAPEKLPGPTG 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 163 EHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIG 242
Cdd:PRK11904 676 ESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVG 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 243 DYLVDHKDTHFVTFTGSRATGTRIyERSAVVQEGQnfLKRVIAEMGGKDAIVVD-----ENIDTDmaaeaIVTSAFGFSG 317
Cdd:PRK11904 756 AALTADPRIAGVAFTGSTETARII-NRTLAARDGP--IVPLIAETGGQNAMIVDstalpEQVVDD-----VVTSAFRSAG 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 318 QKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKL----EQGGGTDds 392
Cdd:PRK11904 828 QRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDAEAKANLDAHIERMKREARLlaqlPLPAGTE-- 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 393 KGYFVEPTIISgLKSKDRImQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAV---ITNNREHWIKAVNefdVGNL 467
Cdd:PRK11904 906 NGHFVAPTAFE-IDSISQL-EREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIhsrIEETADRIADRVR---VGNV 980
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 616190054 468 YLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVS 511
Cdd:PRK11904 981 YVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1024
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
39-490 |
8.18e-103 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 316.98 E-value: 8.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIA 116
Cdd:cd07559 3 NFINGEWVapSKGEYFDNYNPV-NGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 117 AIMVYEAGKPWDEAVG-DAAEGIDFIEYYARSMMDLAQGKPVLDrEGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTLAP 195
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEID-EDTLSYHFHEPLGVVGQIIPWNFPL-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 196 VVA-GNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvq 274
Cdd:cd07559 160 ALAaGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 275 egQNFLKrVIAEMGGK-------DAIVVDENIDtDMAAEAIVTSAFGfSGQKCSACSRAIVHKDVYDEVLEKSIKLTKEL 347
Cdd:cd07559 236 --ENLIP-VTLELGGKspniffdDAMDADDDFD-DKAEEGQLGFAFN-QGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 348 TLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGG----TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVV 421
Cdd:cd07559 311 KVGNPLDpETMMGAQVSKDQLEKILSYVDIGKEEGaEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616190054 422 GFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-511 |
9.50e-103 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 333.06 E-value: 9.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLvINGEKIfKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEA 85
Cdd:COG4230 528 RNSAGLDLSDEAVLAALSAALAAAAEKQWQAAPL-IAGEAA-SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAA 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 86 YKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmdlAQGkpvldREGEHN 165
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYA------AQA-----RRLFAA 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 166 KYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYL 245
Cdd:COG4230 675 PTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAAL 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 246 VDHKDTHFVTFTGSRATGTRIyERSAVVQEGQnfLKRVIAEMGGKDAIVVD-----ENIDTDmaaeaIVTSAFGFSGQKC 320
Cdd:COG4230 755 VADPRIAGVAFTGSTETARLI-NRTLAARDGP--IVPLIAETGGQNAMIVDssalpEQVVDD-----VLASAFDSAGQRC 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 321 SACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKL--EQGGGTDDSKGYFV 397
Cdd:COG4230 827 SALRVLCVQEDIADRVLEMLKGAMAELRVGDPADlSTDVGPVIDAEARANLEAHIERMRAEGRLvhQLPLPEECANGTFV 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 398 EPTIISgLKSKDRImQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTS 475
Cdd:COG4230 907 APTLIE-IDSISDL-EREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIG 984
|
490 500 510
....*....|....*....|....*....|....*.
gi 616190054 476 AVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVS 511
Cdd:COG4230 985 AVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVT 1020
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
50-510 |
8.58e-102 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 314.71 E-value: 8.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 50 DKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDE 129
Cdd:PLN02278 40 KTFPVYNPA-TGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 130 AVGDAAEGIDFIEYYA----RSMMDLAQgKPVLDRegehnKYFYKSIGTGVT--IPPWNFPFAIM---AGTTLApvvAGN 200
Cdd:PLN02278 119 AIGEVAYGASFLEYFAeeakRVYGDIIP-SPFPDR-----RLLVLKQPVGVVgaITPWNFPLAMItrkVGPALA---AGC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 201 TVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFL 280
Cdd:PLN02278 190 TVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA------ATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 281 KRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMG 359
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEeGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 360 PVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGaKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616190054 439 TDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGyhPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGL-GREGSKYGIDEYLEIKYV 492
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
37-489 |
9.77e-100 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 308.68 E-value: 9.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 37 IPLVINGEKIF-KDDKIKSI-NPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAE 114
Cdd:cd07085 1 LKLFINGEWVEsKTTEWLDVyNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 115 IAAIMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAQGKPVLDREGEHNKYFYKS-IGTGVTIPPWNFPFAI-MAGTT 192
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKGEYLENVARGIDTYSYRQpLGVVAGITPFNFPAMIpLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 193 LApVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAv 272
Cdd:cd07085 159 MA-IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGG-KEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 273 vqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN- 351
Cdd:cd07085 236 -----ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 352 TVDNTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDD----SKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKV 426
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGaKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 427 NDFDEAIEVANDTDYGlTGAVI-TNNREHWIKAVNEFDVGNLYLNRGCtsAV-VGYHPFGGFKMS 489
Cdd:cd07085 391 DTLDEAIAIINANPYG-NGAAIfTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGS 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
52-490 |
2.98e-98 |
|
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: 304.61 E-value: 2.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKP----- 126
Cdd:cd07151 12 IDVLNPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTrikan 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 127 --WDEAVGDAAEgidfieyyARSMMDLAQGKPVL-DREGEHNKYFYKSIGTGVTIPPWNFPFAiMAGTTLAPVVA-GNTV 202
Cdd:cd07151 91 ieWGAAMAITRE--------AATFPLRMEGRILPsDVPGKENRVYREPLGVVGVISPWNFPLH-LSMRSVAPALAlGNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 203 LLKPAEDTPYIAYKLM-EILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLK 281
Cdd:cd07151 162 VLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG------RHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 282 RVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGP 360
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDpDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 361 VINKKQFDKIKNYIEIGKEEGKLEQGGGtdDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGG--EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 616190054 441 YGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCT--SAVVgyhPFGGFKMSG 490
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVndEPHV---PFGGEKNSG 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
55-510 |
2.77e-97 |
|
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: 301.56 E-value: 2.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVG 132
Cdd:cd07118 2 RSPA-HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 133 DAAEGIDFIEYYARSMMDLaqgkpvldrEGEHnkyfYKSIGTGVT-------------IPPWNFPFAIMAGTTLAPVVAG 199
Cdd:cd07118 81 EIEGAADLWRYAASLARTL---------HGDS----YNNLGDDMLglvlrepigvvgiITPWNFPFLILSQKLPFALAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 200 NTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNF 279
Cdd:cd07118 148 CTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA------RN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 280 LKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYM 358
Cdd:cd07118 222 LKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDpETKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 359 GPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDS-KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07118 302 GAIINEAQLAKITDYVDAGRAEGaTLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 437 NDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgctSAVVGYH--PFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07118 382 NDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVN----TFLDGSPelPFGGFKQSGIGRELGR-YGVEEYTELKTV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
75-490 |
7.89e-97 |
|
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: 299.76 E-value: 7.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 75 VEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQG 154
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 155 KPVlDREGEHNKYFYKSIGTGVTIPPWNFPF---AIMAGTTLApvvAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVV 231
Cdd:cd07100 81 EPI-ETDAGKAYVRYEPLGVVLGIMPWNFPFwqvFRFAAPNLM---AGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 232 NFVPGDPKEIgDYLVDHKDTHFVTFTGSRATGtriyerSAVVQE-GQNfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVT 310
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSERAG------RAVAAEaGKN-LKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 311 SAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGG 388
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDeDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 389 TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLY 468
Cdd:cd07100 309 RPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420
....*....|....*....|..
gi 616190054 469 LNRGCTSAVvgYHPFGGFKMSG 490
Cdd:cd07100 389 INGMVKSDP--RLPFGGVKRSG 408
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
52-490 |
2.37e-96 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 300.26 E-value: 2.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEA- 130
Cdd:PRK13252 24 FEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 131 VGDAAEGIDFIEYYArsmmDLAqgkPVLdrEGEH-----NKYFY---KSIGTGVTIPPWNFPFAImAGTTLAP-VVAGNT 201
Cdd:PRK13252 103 VVDIVTGADVLEYYA----GLA---PAL--EGEQiplrgGSFVYtrrEPLGVCAGIGAWNYPIQI-ACWKSAPaLAAGNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 202 VLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLK 281
Cdd:PRK13252 173 MIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA------ASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 282 RVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGP 360
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDpATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 361 VINKKQFDKIKNYIEIGKEEG-KLEQGGG--TDDS--KGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEV 435
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGaRLLCGGErlTEGGfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIAR 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 616190054 436 ANDTDYGLTGAVITN--NREHwiKAVNEFDVGNLYLNR-GCTSAVVgyhPFGGFKMSG 490
Cdd:PRK13252 406 ANDTEYGLAAGVFTAdlSRAH--RVIHQLEAGICWINTwGESPAEM---PVGGYKQSG 458
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-512 |
5.94e-96 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 315.65 E-value: 5.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLVINGEKifKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEA 85
Cdd:PRK11905 525 RNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGGDV--DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 86 YKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDRegehn 165
Cdd:PRK11905 603 FPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPL----- 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 166 kyfyksiGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYL 245
Cdd:PRK11905 678 -------GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAAL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 246 VDHKDTHFVTFTGSRATGTRIYersavvqegQNFLKRV------IAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQK 319
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQ---------RTLAKRSgppvplIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQR 821
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 320 CSA----CsraiVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKL--EQGGGTDDS 392
Cdd:PRK11905 822 CSAlrvlC----LQEDVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETE 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 393 KGYFVEPTII--SGLkskdRIMQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITnnR-----EHWIKAVNefd 463
Cdd:PRK11905 898 KGTFVAPTLIeiDSI----SDLEREVFGPVLHVVrfKADELDRVIDDINATGYGLTFGLHS--RidetiAHVTSRIR--- 968
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 616190054 464 VGNLYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFLEQKVVSE 512
Cdd:PRK11905 969 AGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPI 1017
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-490 |
1.39e-95 |
|
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: 297.95 E-value: 1.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGE-KIFKDDKIKSINPADtSQVIANASKATKQDVEDAFKAANEAYKSW-KTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07082 6 INGEwKESSGKTIEVYSPID-GEVIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaQGKPVLDREGEHNK----YFYKS-IGTGVTIPPWNFPFAImAGTTL 193
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGDSLPGDWFPGTKgkiaQVRREpLGVVLAIGPFNYPLNL-TVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 194 AP-VVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAV 272
Cdd:cd07082 163 IPaLIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 273 vqegqnflKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNT 352
Cdd:cd07082 243 --------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 353 VDN-TYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDdsKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07082 315 WDNgVDITPLIDPKSADFVEGLIDDAVAKGaTVLNGGGRE--GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCtSAVVGYHPFGGFKMSG 490
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC-QRGPDHFPFLGRKDSG 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
35-510 |
1.41e-95 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 298.29 E-value: 1.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 35 QDIPLVINGE--KIFKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYK-SW-KTWSANDRAELMLRVSAIIRR 110
Cdd:cd07143 5 QPTGLFINGEfvDSVHGGTVKVYNPS-TGKLITKIAEATEADVDIAVEVAHAAFEtDWgLKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 111 RKAEIAAIMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAQGKpVLDREGEHNKY-FYKSIGTGVTIPPWNFPFaIM 188
Cdd:cd07143 84 NLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYG-GWADKIHGQ-VIETDIKKLTYtRHEPIGVCGQIIPWNFPL-LM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 189 AGTTLAPVVA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIY 267
Cdd:cd07143 161 CAWKIAPALAaGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 268 ERSAvvqegQNFLKRVIAEMGGKDAIVVDENIDTDmaaEAIVTSAFGF---SGQKCSACSRAIVHKDVYDEVLEKSIKLT 344
Cdd:cd07143 241 EAAA-----KSNLKKVTLELGGKSPNIVFDDADLE---SAVVWTAYGIffnHGQVCCAGSRIYVQEGIYDKFVKRFKEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 345 KELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVG 422
Cdd:cd07143 313 KKLKVGDPFAeDTFQGPQVSQIQYERIMSYIESGKAEGaTVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 423 FVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpdYLL 502
Cdd:cd07143 393 VIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIGRELGE--YAL 468
|
....*....
gi 616190054 503 H-FLEQKVV 510
Cdd:cd07143 469 EnYTQIKAV 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
52-511 |
1.04e-94 |
|
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: 295.03 E-value: 1.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEA- 130
Cdd:cd07145 1 IEVRNPA-NGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 131 --VGDAAEGIDFIEYYARSMmdlaQGK--PVLDREGEHNKYFY---KSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTV 202
Cdd:cd07145 80 veVERTIRLFKLAAEEAKVL----RGEtiPVDAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFA-HKIAPAIAvGNSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 203 LLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKR 282
Cdd:cd07145 155 VVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 283 VIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPV 361
Cdd:cd07145 229 VALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDeSTDLGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 362 INKKQFDKIKNYIEIGKEEG-KLEQGGGTDDskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:cd07145 309 ISPEAVERMENLVNDAVEKGgKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616190054 441 YGLTGAVITNNREHWIKAVNEFDVGNLYLNrGCTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVVS 511
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGI-GREGVRYTMLEMTEEKTIV 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
39-512 |
1.61e-94 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 296.26 E-value: 1.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYK--SWKTWSAND---RAELMLRVSAIIRRR 111
Cdd:PLN02467 10 LFIGGEWRepVLGKRIPVVNPA-TEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTgavRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 112 KAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmDLA------QGKPV-LDREGEHNKYFYKSIGTGVTIPPWNFP 184
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYA----DLAealdakQKAPVsLPMETFKGYVLKEPLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 185 FaIMAGTTLAPVVA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATG 263
Cdd:PLN02467 165 L-LMATWKVAPALAaGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 264 TRIYerSAVVQEgqnfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKL 343
Cdd:PLN02467 244 RKIM--TAAAQM----VKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 344 TKELTLGNT-VDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGT---DDSKGYFVEPTIISGLKSKDRIMQEEIFGP 419
Cdd:PLN02467 318 AKNIKISDPlEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpeHLKKGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 420 VVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGsPD 499
Cdd:PLN02467 398 VLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELG-EW 474
|
490
....*....|...
gi 616190054 500 YLLHFLEQKVVSE 512
Cdd:PLN02467 475 GLENYLSVKQVTK 487
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
49-510 |
1.89e-94 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 295.12 E-value: 1.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 49 DDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKS-WKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPW 127
Cdd:cd07113 14 EKRLDITNPA-TEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 128 DEAVG-DAAEGIDFIEYYARSMMDLAqGK---PVL-DREGEhnKY----FYKSIGTGVTIPPWNFPFAIMAGTTLAPVVA 198
Cdd:cd07113 93 HLSRAfEVGQSANFLRYFAGWATKIN-GEtlaPSIpSMQGE--RYtaftRREPVGVVAGIVPWNFSVMIAVWKIGAALAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 199 GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIyERSAVvqegqN 278
Cdd:cd07113 170 GCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGK-GAVGAQLISHPDVAKVSFTGSVATGKKI-GRQAA-----S 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 279 FLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TY 357
Cdd:cd07113 243 DLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDEsVM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 358 MGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07113 323 FGPLANQPHFDKVCSYLDDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 437 NDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGC--TSAVvgyhPFGGFKMSGTDAKTGSpDYLLHFLEQKVV 510
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTflDPAV----PFGGMKQSGIGREFGS-AFIDDYTELKSV 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
39-510 |
5.87e-94 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 294.02 E-value: 5.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEkiFKDDK----IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYK--SWKTWSANDRAELMLRVSAIIRRRK 112
Cdd:cd07142 6 LFINGQ--FVDAAsgktFPTIDPR-NGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 113 AEIAAIMVYEAGKPWDEA-VGDAAEGIDFIEYYArSMMDLAQGKpVLDREGEHNKY-FYKSIGTGVTIPPWNFPFaIMAG 190
Cdd:cd07142 83 DELAALETWDNGKPYEQArYAEVPLAARLFRYYA-GWADKIHGM-TLPADGPHHVYtLHEPIGVVGQIIPWNFPL-LMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 191 TTLAPVVA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYER 269
Cdd:cd07142 160 WKVGPALAcGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 270 SAvvqegQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTL 349
Cdd:cd07142 240 AA-----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 350 GNTVDNTY-MGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVN 427
Cdd:cd07142 315 GDPFRKGVeQGPQVDKEQFEKILSYIEHGKEEGaTLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 428 DFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFLEQ 507
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGI-YALNNYLQV 471
|
...
gi 616190054 508 KVV 510
Cdd:cd07142 472 KAV 474
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
55-490 |
7.78e-93 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 291.04 E-value: 7.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD- 133
Cdd:PRK13473 22 YNPA-TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 ---AAEGIDFIEYYARSMMDLAQGKPVldreGEHNKYFYK-SIGTGVTIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAE 208
Cdd:PRK13473 101 ipaIVDVFRFFAGAARCLEGKAAGEYL----EGHTSMIRRdPVGVVASIAPWNYPL-MMAAWKLAPALAaGNTVVLKPSE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnfLKRVIAEMG 288
Cdd:PRK13473 176 ITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS------VKRTHLELG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:PRK13473 249 GKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDeDTELGPLISAAHR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEGKLE--QGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:PRK13473 329 DRVAGFVERAKALGHIRvvTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLAS 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 616190054 446 AVITNN--REHwiKAVNEfdvgnlyLNRGCTSavVGYH-------PFGGFKMSG 490
Cdd:PRK13473 409 SVWTRDvgRAH--RVSAR-------LQYGCTW--VNTHfmlvsemPHGGQKQSG 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
39-495 |
4.53e-92 |
|
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: 288.97 E-value: 4.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGE--KIFKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIA 116
Cdd:cd07117 3 LFINGEwvKGSSGETIDSYNPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 117 AIMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTLAP 195
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFA-GVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPF-LMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 196 VVA-GNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvq 274
Cdd:cd07117 160 ALAaGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 275 egqnflKRVIA---EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN 351
Cdd:cd07117 236 ------KKLIPatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 352 TVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:cd07117 310 PLDpDTQMGAQVNKDQLDKILSYVDIAKEEGaKILTGGhrltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 426 VNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKT 495
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIGRET 457
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
101-501 |
2.15e-91 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 285.09 E-value: 2.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 101 MLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYA----RSMMDLAQGkpvlDREGEHNKYFYKSIGTGV 176
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAewarRYEGEIIQS----DRPGENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 177 TIPPWNFPFAIMAgTTLAP-VVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVT 255
Cdd:PRK10090 77 GILPWNFPFFLIA-RKMAPaLLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 256 FTGSRATGTRIYERSAvvqegQNFLKrVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDE 335
Cdd:PRK10090 156 MTGSVSAGEKIMAAAA-----KNITK-VCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 336 VLEKSIKLTKELTLGNTVDNTY--MGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIM 412
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPAERNDiaMGPLINAAALERVEQKVARAVEEGaRVALGGKAVEGKGYYYPPTLLLDVRQEMSIM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 413 QEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHpfGGFKMS--- 489
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSgig 387
|
410
....*....|..
gi 616190054 490 GTDAKTGSPDYL 501
Cdd:PRK10090 388 GADGKHGLHEYL 399
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-498 |
1.95e-90 |
|
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: 283.80 E-value: 1.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 62 QVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFI 141
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 142 eYYARSMMDLAQGKPVLDREGEHNKYFYKSIGT-GVtIPPWNFPFaIMAGTTLAPVVA-GNTVLLKPAEDTPYIA-YKLM 218
Cdd:cd07152 82 -HEAAGLPTQPQGEILPSAPGRLSLARRVPLGVvGV-ISPFNFPL-ILAMRSVAPALAlGNAVVLKPDPRTPVSGgVVIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 219 EILEEAGLPKGVVNFVPGDPkEIGDYLVDHKDTHFVTFTGSRATGTRIYErsavvQEGQNfLKRVIAEMGGKDAIVVDEN 298
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGE-----AAGRH-LKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 299 IDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTV-DNTYMGPVINKKQFDKIKNYIEIG 377
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPAtGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 378 KEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWI 456
Cdd:cd07152 312 VAAGaRLEAGGTYD---GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616190054 457 KAVNEFDVGNLYLNRGcTSAVVGYHPFGGFKMSGTDAKTGSP 498
Cdd:cd07152 389 ALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-512 |
3.33e-89 |
|
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: 280.73 E-value: 3.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 60 TSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGK----PWDEaVGDAA 135
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEE-VLDVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 136 EGIdfiEYYARSMMDL------AQGKPVLDREGEHnkyfYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAED 209
Cdd:cd07101 84 IVA---RYYARRAERLlkprrrRGAIPVLTRTTVN----RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 210 TPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDthFVTFTGSRATGTRIYERSAvvqegqnflKRVI---AE 286
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAG---------RRLIgcsLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 287 MGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTY-MGPVINKK 365
Cdd:cd07101 226 LGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPdMGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 366 QFDKIKNYIEIGKEEGKLEQGGGTD--DSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07101 306 QLDRVTAHVDDAVAKGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 444 TGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVSE 512
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG-AEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
55-483 |
9.05e-88 |
|
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: 277.20 E-value: 9.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPADTSqVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPwdeaVGDA 134
Cdd:cd07102 1 ISPIDGS-VIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP----IAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARSMMDLAQGK----PVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDT 210
Cdd:cd07102 76 GGEIRGMLERARYMISIAEEAladiRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 211 PYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIyERSAvvqeGQNFLKrVIAEMGGK 290
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLS-HETSAALIADPRIDHVSFTGSVAGGRAI-QRAA----AGRFIK-VGLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 291 DAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDK 369
Cdd:cd07102 229 DPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDpSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 370 IKNYIEIGKEEG-KLEQGGGT---DDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:cd07102 309 VRAQIADAIAKGaRALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 616190054 446 AVITNNREHWIKAVNEFDVGNLYLNR------------------GCTSAVVGYHPF 483
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNRcdyldpalawtgvkdsgrGVTLSRLGYDQL 444
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-506 |
1.63e-87 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 277.95 E-value: 1.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 6 KNEPGYDFSVQENVNMFKKALKDVEKELGQDIPLVinGEKIFKDDKIKSI-NPADTSQVIANASKATKQDVEDAFKAANE 84
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKTWQAAPII--GHSYKADGEAQPVtNPADRRDIVGQVFHANLAHVQAAIDSAQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 85 AYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDlaqgkpVLDREGeh 164
Cdd:TIGR01238 86 AFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRD------VLGEFS-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 165 nkyfYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDY 244
Cdd:TIGR01238 158 ----VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 245 LVDHKDTHFVTFTGSRATGTRIYERSAVVQEGQNFLkrvIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACS 324
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPL---IAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 325 RAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDS----KGYFVEP 399
Cdd:TIGR01238 311 VLCVQEDVADRVLTMIQGAMQELKVGVPHLlTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSracqHGTFVAP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 400 TIISgLKSKDRiMQEEIFGPVVGFV--KVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAV 477
Cdd:TIGR01238 391 TLFE-LDDIAE-LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAV 468
|
490 500
....*....|....*....|....*....
gi 616190054 478 VGYHPFGGFKMSGTDAKTGSPDYLLHFLE 506
Cdd:TIGR01238 469 VGVQPFGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
55-510 |
2.67e-87 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 276.02 E-value: 2.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07099 1 RNPA-TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARsmmdlaQGKPVLDRE--GEHNKYFYKSIGT-----GVT--IPPWNFPFAIMAGTTLAPVVAGNTVLLK 205
Cdd:cd07099 80 LLALEAIDWAAR------NAPRVLAPRkvPTGLLMPNKKATVeyrpyGVVgvISPWNYPLLTPMGDIIPALAAGNAVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 206 PAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKdTHFVTFTGSRATGTRIYERSAvvqegQNFLKrVIA 285
Cdd:cd07099 154 PSEVTPLVGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDAG-VDKVAFTGSVATGRKVMAAAA-----ERLIP-VVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 286 EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN-TVDNTYMGPVINK 364
Cdd:cd07099 226 ELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGAdDIGDADIGPMTTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 365 KQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07099 306 RQLDIVRRHVDDAVAKGaKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 444 TGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07099 386 SASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGG-GRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
55-510 |
1.41e-85 |
|
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: 271.23 E-value: 1.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPADTSqVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:cd07094 4 HNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFI--------EYYARSM-MDLAQGkpvldREGEHNKYFYKSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLL 204
Cdd:cd07094 83 DRAIDTLrlaaeeaeRIRGEEIpLDATQG-----SDNRLAWTIREPVGVVLAITPFNFPLNLVA-HKLAPAIAtGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 205 KPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqnfLKRVI 284
Cdd:cd07094 157 KPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 285 AEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVIN 363
Cdd:cd07094 229 LELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDeDTDVGPLIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 364 KKQFDKIKNYIEIGKEEGKLEQGGGTDDskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07094 309 EEAAERVERWVEEAVEAGARLLCGGERD--GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 444 TGAVITNNREHWIKAVNEFDVGNLYLNRGcTSAVVGYHPFGGFKMSGTdAKTGSPDYLLHFLEQKVV 510
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGV-GREGVPYAMEEMTEEKTV 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
39-510 |
1.58e-84 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 270.15 E-value: 1.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYK--SWKTWSANDRAELMLRVSAIIRRRKAE 114
Cdd:PLN02766 23 LFINGEFVdaASGKTFETRDPR-TGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 115 IAAIMVYEAGKPWdeAVGDAAE---GIDFIEYYARSMmDLAQGKpVLDREGEHNKYFYKS-IGTGVTIPPWNFP---FAI 187
Cdd:PLN02766 102 LAALDTIDAGKLF--ALGKAVDipaAAGLLRYYAGAA-DKIHGE-TLKMSRQLQGYTLKEpIGVVGHIIPWNFPstmFFM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 188 MAGTTLApvvAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIY 267
Cdd:PLN02766 178 KVAPALA---AGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 268 ERSAvvqegQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKEL 347
Cdd:PLN02766 255 QAAA-----TSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 348 TLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:PLN02766 330 VVGDPFDpRARQGPQVDKQQFEKILSYIEHGKREGaTLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 426 VNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpDYLLHFL 505
Cdd:PLN02766 410 FKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFGRDQGM-DALDKYL 486
|
....*
gi 616190054 506 EQKVV 510
Cdd:PLN02766 487 QVKSV 491
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-513 |
1.83e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 270.60 E-value: 1.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 60 TSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGK----PWDEaVGDAA 135
Cdd:PRK09407 41 TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKarrhAFEE-VLDVA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 136 EGIDfieYYARSMMDL-----AQGK-PVLDREGEHnkyfYKSIGT-GVtIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAE 208
Cdd:PRK09407 120 LTAR---YYARRAPKLlaprrRAGAlPVLTKTTEL----RQPKGVvGV-ISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDthFVTFTGSRATGTRIYERSAvvqegqnflKRVI---A 285
Cdd:PRK09407 192 QTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAG---------RRLIgfsL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 286 EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTY-MGPVINK 364
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSAdMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 365 KQFDKIKNYIEIGKEEG-KLEQGGGTDDSKG-YFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYG 442
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGaTVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYG 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616190054 443 LTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYH-PFGGFKMSGTDAKTGsPDYLLHFLEQKVVSEM 513
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGRRHG-AEGLLKYTESQTIATQ 491
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
39-510 |
4.39e-84 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 270.14 E-value: 4.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEkiFKD----DKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRK 112
Cdd:PLN02466 60 LLINGQ--FVDaasgKTFPTLDPR-TGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 113 AEIAAIMVYEAGKPWDEAVG-DAAEGIDFIEYYArSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGT 191
Cdd:PLN02466 137 DELAALETWDNGKPYEQSAKaELPMFARLFRYYA-GWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPL-LMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 192 TLAPVVA-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERS 270
Cdd:PLN02466 215 KVGPALAcGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 271 AvvqegQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSikltKELTLG 350
Cdd:PLN02466 295 A-----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA----KARALK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 351 NTVDNTY-----MGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFV 424
Cdd:PLN02466 366 RVVGDPFkkgveQGPQIDSEQFEKILRYIKSGVESGaTLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 425 KVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSGTDAKTGSpdYLLH- 503
Cdd:PLN02466 446 KFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKGI--YSLNn 521
|
....*..
gi 616190054 504 FLEQKVV 510
Cdd:PLN02466 522 YLQVKAV 528
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
38-505 |
1.83e-83 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 281.86 E-value: 1.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 38 PLVinGEKIFKDDKIKSINPADTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAA 117
Cdd:PRK11809 649 PML--EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMG 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 118 IMVYEAGKPWDEAVGDAAEGIDFIEYYArsmmdlAQGKPVLDREGehnkyfYKSIGTGVTIPPWNFPFAIMAGTTLAPVV 197
Cdd:PRK11809 727 LLVREAGKTFSNAIAEVREAVDFLRYYA------GQVRDDFDNDT------HRPLGPVVCISPWNFPLAIFTGQVAAALA 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 198 AGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVQEGQ 277
Cdd:PRK11809 795 AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQ 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 278 NFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN----TV 353
Cdd:PRK11809 875 GRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNpdrlST 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 354 DntyMGPVINKKQFDKIKNYIEIGKEEG----KLEQGGGTDDSKGYFVEPTIISgLKSKDRiMQEEIFGPVVGFVKV--N 427
Cdd:PRK11809 955 D---IGPVIDAEAKANIERHIQAMRAKGrpvfQAARENSEDWQSGTFVPPTLIE-LDSFDE-LKREVFGPVLHVVRYnrN 1029
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616190054 428 DFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDAKTGSPDYLLHFL 505
Cdd:PRK11809 1030 QLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLL 1107
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
74-490 |
6.93e-83 |
|
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: 263.67 E-value: 6.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 74 DVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYArSMMDLAQ 153
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-SLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 154 GKPV-LDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVN 232
Cdd:cd07105 80 GGSIpSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 233 FVPGDPK---EIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIV 309
Cdd:cd07105 160 VVTHSPEdapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA------KHLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 310 TSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDntymGPVINKKQFDKIKNYIEIGKEEG-KLEQGGG 388
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL----GSLVSAAAADRVKELVDDALSKGaKLVVGGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 389 TDDSK-GYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNL 467
Cdd:cd07105 310 ADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420
....*....|....*....|....*.
gi 616190054 468 YLNrGCT---SAVVgyhPFGGFKMSG 490
Cdd:cd07105 390 HIN-GMTvhdEPTL---PHGGVKSSG 411
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
40-493 |
1.60e-82 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 264.07 E-value: 1.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 40 VINGEKIFKDDKIKSINPADtSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIM 119
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 120 VYEAGKPWDEAVGDAAEGIDfieyyarsMMDLAQG------KPVL--DREGEHNKYFYKSIGTGVTIPPWNFPFAIMA-G 190
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMID--------ICDFAVGlsrqlyGLTIpsERPGHRMMEQWNPLGVVGVITAFNFPVAVWGwN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 191 TTLApVVAGNTVLLKPAEDTPYIA---YKLM-EILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGtri 266
Cdd:cd07130 153 AAIA-LVCGNVVVWKPSPTTPLTAiavTKIVaRVLEKNGLPGAIASLVCGG-ADVGEALVKDPRVPLVSFTGSTAVG--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 267 yerSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKE 346
Cdd:cd07130 228 ---RQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 347 LTLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEE-GKLEQGGGTDDSKGYFVEPTIISGLkSKDRIMQEEIFGPVVGFV 424
Cdd:cd07130 305 VRIGDPLDdGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616190054 425 KVNDFDEAIEVANDTDYGLTGAVITNN---REHWIKAVNEfDVGNLYLNRGCTSAVVGyHPFGGFKM------SGTDA 493
Cdd:cd07130 384 KFDTLEEAIAWNNEVPQGLSSSIFTTDlrnAFRWLGPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKEtgggreSGSDA 459
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
39-511 |
5.18e-81 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 260.51 E-value: 5.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEkiFKD----DKIKSINPADTSqVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRK 112
Cdd:cd07140 8 LFINGE--FVDaeggKTYNTINPTDGS-VICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 113 AEIAAIMVYEAGKPWDEAVGD-AAEGIDFIEYYArSMMDLAQGK--PVLDREGEHNKYFYKS--IGTGVTIPPWNFPFAI 187
Cdd:cd07140 85 EELATIESLDSGAVYTLALKThVGMSIQTFRYFA-GWCDKIQGKtiPINQARPNRNLTLTKRepIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 188 MAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIY 267
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 268 ERSAVVQegqnfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKEL 347
Cdd:cd07140 244 KSCAVSN-----LKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 348 TLGNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVK 425
Cdd:cd07140 319 KIGDPLDrSTDHGPQNHKAHLDKLVEYCERGVKEGaTLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 426 VN--DFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGyhPFGGFKMSGTDAKTGSpDYLLH 503
Cdd:cd07140 399 FDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLGE-EALNE 475
|
....*...
gi 616190054 504 FLEQKVVS 511
Cdd:cd07140 476 YLKTKTVT 483
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
60-490 |
2.17e-80 |
|
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: 257.94 E-value: 2.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 60 TSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGID 139
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 140 FIEYYAR-------SMMDL---AQGKpvlDREGEHNKYfykSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPAE 208
Cdd:cd07147 88 TFRIAAEeatriygEVLPLdisARGE---GRQGLVRRF---PIGPVSAITPFNFPLNLVA-HKVAPAIAaGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 209 DTPYIAYKLMEILEEAGLPKGVVNFVPGdPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSavvqeGQnflKRVIAEMG 288
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARA-----GK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINKKQF 367
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDdATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 368 DKIKNYIEIGKEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGA 446
Cdd:cd07147 312 ERVEGWVNEAVDAGaKLLTGGKRD---GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 616190054 447 VITNNREHWIKAVNEFDVGNLYLNRgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSG 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
54-508 |
2.18e-80 |
|
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: 258.04 E-value: 2.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKSwKTWSAND--RAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV 131
Cdd:cd07120 1 SIDPA-TGEVIGTYADGGVAEAEAAIAAARRAFDE-TDWAHDPrlRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 132 GDAAEGIDFIEYYA---RSMmdlaQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLKPA 207
Cdd:cd07120 79 FEISGAISELRYYAglaRTE----AGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLV-RSLAPALAaGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 208 EDTPYIAYKLMEILEEA-GLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqNFLKRVIAE 286
Cdd:cd07120 154 GQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA------PTLKRLGLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 287 MGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTY-MGPVINKK 365
Cdd:cd07120 228 LGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASdMGPLIDRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 366 QFDKIKNYIEIGKEEGK--LEQGGGTDD--SKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDY 441
Cdd:cd07120 308 NVDRVDRMVERAIAAGAevVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616190054 442 GLTGAVITNNREHWIKAVNEFDVGNLYLNrgcTSAVVGYH-PFGGFKMSGTdAKTGSPDYLLHFLEQK 508
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWIN---DWNKLFAEaEEGGYRQSGL-GRLHGVAALEDFIEYK 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
41-490 |
3.48e-80 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 258.15 E-value: 3.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKI--FKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07116 5 IGGEWVapVKGEYFDNITPV-TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVG-DAAEGIDFIEYYARSMMdlAQGKPVLDREGEHNKY-FYKSIGTGVTIPPWNFPFaIMAGTTLAPV 196
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCIR--AQEGSISEIDENTVAYhFHEPLGVVGQIIPWNFPL-LMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 197 VA-GNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqe 275
Cdd:cd07116 161 LAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 276 gQNFLKrVIAEMGGKD-----AIVVDENID-TDMAAEAIVTSAFGfSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTL 349
Cdd:cd07116 236 -ENIIP-VTLELGGKSpniffADVMDADDAfFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 350 GNTVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGG-----TDDSKGYFVEPTIISGlKSKDRIMQEEIFGPVVGF 423
Cdd:cd07116 313 GNPLDtETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGernelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 424 VKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgCTSAVVGYHPFGGFKMSG 490
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
60-496 |
7.09e-80 |
|
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: 256.52 E-value: 7.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 60 TSQVIANASKATKQDVEDAFKAANeAYKSwkTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEA---VGDAAE 136
Cdd:cd07146 8 TGEVVGTVPAGTEEALREALALAA-SYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTryeVGRAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 137 GIDFIEYYAR-------SMMDLAQGKP---VLDREgehnkyfykSIGTGVTIPPWNFPFAIMAgTTLAPVVA-GNTVLLK 205
Cdd:cd07146 85 VLRFAAAEALrddgesfSCDLTANGKArkiFTLRE---------PLGVVLAITPFNHPLNQVA-HKIAPAIAaNNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 206 PAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqegqnfLKRVIA 285
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 286 EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGPVINK 364
Cdd:cd07146 227 ELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDpATDMGTVIDE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 365 KQFDKIKNYIEIGKEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL 443
Cdd:cd07146 307 EAAIQIENRVEEAIAQGaRVLLGNQRQ---GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 444 TGAVITNNREHWIKAVNEFDVGNLYLNRGctsavVGYH----PFGGFKMSGTDAKTG 496
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVNVNEV-----PGFRselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-508 |
3.15e-79 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 255.78 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKIFKDDK--IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:cd07111 26 INGKWVKPENRksFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAV-GDAAEGIDFIEYYArsmmDLAQgkpVLDREGEHnkyfYKSIGTGVTIPPWNFPFAIMAgTTLAPVV 197
Cdd:cd07111 105 ESLDNGKPIRESRdCDIPLVARHFYHHA----GWAQ---LLDTELAG----WKPVGVVGQIVPWNFPLLMLA-WKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 198 A-GNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPkEIGDYLVDHKDTHFVTFTGSRATGTRIyeRSAVVQEG 276
Cdd:cd07111 173 AmGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRAL--RRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 277 qnflKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-N 355
Cdd:cd07111 250 ----KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDkA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 356 TYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIE 434
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGaDVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 435 VANDTDYGLTGAVITNNREH-------------WIKAVNEFDvgnlylnrgctSAVvgyhPFGGFKMSGTdAKTGSPDYL 501
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLalevalslkagvvWINGHNLFD-----------AAA----GFGGYRESGF-GREGGKEGL 469
|
....*..
gi 616190054 502 LHFLEQK 508
Cdd:cd07111 470 YEYLRPS 476
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
74-490 |
7.42e-78 |
|
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: 250.65 E-value: 7.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 74 DVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFI--------EYYA 145
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIdisikayhERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 146 RSMMDLAQGKPVLDregehnkyfYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAG 225
Cdd:cd07095 81 ERATPMAQGRAVLR---------HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 226 LPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYErsavvQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAA 305
Cdd:cd07095 152 LPPGVLNLVQGG-RETGEALAAHEGIDGLLFTGSAATGLLLHR-----QFAGRPGKILALEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 306 EAIVTSAFGFSGQKCSACSRAIVHKD-VYDEVLEKSIKLTKELTLGN-TVDNTYMGPVINKKQFDKIKNYIEIGKEEG-- 381
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGApDAEPPFMGPLIIAAAAARYLLAQQDLLALGge 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 382 ---KLEQGggtdDSKGYFVEPTIISGLKSKDRiMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKA 458
Cdd:cd07095 306 pllAMERL----VAGTAFLSPGIIDVTDAADV-PDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERF 380
|
410 420 430
....*....|....*....|....*....|..
gi 616190054 459 VNEFDVGNLYLNRGCTSAvVGYHPFGGFKMSG 490
Cdd:cd07095 381 LARIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
39-490 |
1.42e-73 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 241.02 E-value: 1.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGEKIF-KDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAA 117
Cdd:PRK09457 3 LWINGDWIAgQGEAFESRNPV-SGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 118 IMVYEAGKPWDEAVGDAAEGIDFIE-----YYAR---SMMDLAQGKPVLdRegehnkyfYKSIGTGVTIPPWNFPFAIMA 189
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAisiqaYHERtgeKRSEMADGAAVL-R--------HRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 190 GTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYER 269
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGG-RETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 270 SAvvqeGQNflKRVIA-EMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVY-DEVLEKSIKLTKEL 347
Cdd:PRK09457 232 FA----GQP--EKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 348 TLGNTVDNT--YMGPVINKKQFDKI----KNYIEIG----KEEGKLEQGGGtddskgyFVEPTIISGLKSKDRImQEEIF 417
Cdd:PRK09457 306 TVGRWDAEPqpFMGAVISEQAAQGLvaaqAQLLALGgkslLEMTQLQAGTG-------LLTPGIIDVTGVAELP-DEEYF 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616190054 418 GPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAvVGYHPFGGFKMSG 490
Cdd:PRK09457 378 GPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-501 |
3.17e-68 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 227.10 E-value: 3.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKIFKD--DKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAI 118
Cdd:PRK11241 15 INGEWLDANngEVIDVTNPA-NGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 119 MVYEAGKPWDEAVGDAAEGIDFIEYYARSMMDLaQGKPVLDREGEHNKYFYKS-IGTGVTIPPWNFPFAIM---AGTTLA 194
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRI-YGDTIPGHQADKRLIVIKQpIGVTAAITPWNFPAAMItrkAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 195 pvvAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvq 274
Cdd:PRK11241 173 ---AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 275 egqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTV- 353
Cdd:PRK11241 247 ---KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLe 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 354 DNTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEA 432
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGaRVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616190054 433 IEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGyhPFGGFKMSG---TDAKTGSPDYL 501
Cdd:PRK11241 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGlgrEGSKYGIEDYL 473
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
39-507 |
8.03e-66 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 220.92 E-value: 8.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 39 LVINGE--KIFKDDKIKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKS--WKTWSANDRAELMLRVSAIIRRRKAE 114
Cdd:PRK09847 22 LFINGEytAAAENETFETVDPV-TQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 115 IAAIMVYEAGKPWDEAVGDAAEG-IDFIEYYARSMmDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFaIMAGTTL 193
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGaARAIRWYAEAI-DKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL-LLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 194 AP-VVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIyersaV 272
Cdd:PRK09847 179 GPaLAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL-----L 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 273 VQEGQNFLKRVIAEMGGKDA-IVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN 351
Cdd:PRK09847 254 KDAGDSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 352 TVD-NTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYfVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:PRK09847 334 PLDpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 431 EAIEVANDTDYGLTGAVITNN--REH----WIKA----VNEFDVGNLYLnrgctsavvgyhPFGGFKMSGTdaktgSPDY 500
Cdd:PRK09847 413 QALQLANDSQYGLGAAVWTRDlsRAHrmsrRLKAgsvfVNNYNDGDMTV------------PFGGYKQSGN-----GRDK 475
|
....*..
gi 616190054 501 LLHFLEQ 507
Cdd:PRK09847 476 SLHALEK 482
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-490 |
5.14e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 217.68 E-value: 5.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV 131
Cdd:PRK09406 3 IATINPA-TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 132 GDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYF--YKSIGTGVTIPPWNFP------FAimagttlAP-VVAGNTV 202
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEPADAAAVGASRAYvrYQPLGVVLAVMPWNFPlwqvvrFA-------APaLMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 203 LLKPAEDTPYIAYKLMEILEEAGLPKGVVN--FVPGDPKEigDYLVDHKdTHFVTFTGSRATGtriyerSAVVQEGQNFL 280
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFQtlLVGSGAVE--AILRDPR-VAAATLTGSEPAG------RAVAAIAGDEI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 281 KRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMG 359
Cdd:PRK09406 226 KKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDpDTDVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 360 PVINKKQFDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:PRK09406 306 PLATEQGRDEVEKQVDDAVAAGaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 616190054 439 TDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrGCTSAVVGYhPFGGFKMSG 490
Cdd:PRK09406 386 TTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSG 435
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
55-490 |
5.53e-61 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 208.07 E-value: 5.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 55 INPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDA 134
Cdd:PLN00412 36 TNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 135 AEGIDFIEYYARS-MMDLAQGKPVLDRE---GEHNKYFYKS---IGTGVTIPPWNFPFAiMAGTTLAP-VVAGNTVLLKP 206
Cdd:PLN00412 115 VRSGDLISYTAEEgVRILGEGKFLVSDSfpgNERNKYCLTSkipLGVVLAIPPFNYPVN-LAVSKIAPaLIAGNAVVLKP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 207 AEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRaTGTRIYERSAVVQegqnflkrVIAE 286
Cdd:PLN00412 194 PTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAISKKAGMVP--------LQME 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 287 MGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQ 366
Cdd:PLN00412 265 LGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 367 FDKIKNYIEIGKEEG-KLEQGGGTDdskGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:PLN00412 345 ANFIEGLVMDAKEKGaTFCQEWKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQG 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 616190054 446 AVITNNREHWIKAVNEFDVGNLYLN----RGctsavVGYHPFGGFKMSG 490
Cdd:PLN00412 422 CVFTRDINKAILISDAMETGTVQINsapaRG-----PDHFPFQGLKDSG 465
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
56-512 |
5.71e-61 |
|
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: 207.15 E-value: 5.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 56 NPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPW-DEAVGD- 133
Cdd:cd07098 2 DPA-TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMvDASLGEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 --AAEGIDFIeyyarsmmdLAQGKPVL---DREGEHNKyFYKS-------IGTGVTIPPWNFPFAIMAGTTLAPVVAGNT 201
Cdd:cd07098 81 lvTCEKIRWT---------LKHGEKALrpeSRPGGLLM-FYKRarveyepLGVVGAIVSWNYPFHNLLGPIIAALFAGNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 202 VLLKPAEDT-----PYIAYkLMEILEEAGLPKGVVNFVPGDPkEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAvvqeg 276
Cdd:cd07098 151 IVVKVSEQVawssgFFLSI-IRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAA----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 277 qNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNT 356
Cdd:cd07098 224 -ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 357 Y-MGPVINKKQFDKIKNYIEIGKEEG-KLEQGG----GTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFD 430
Cdd:cd07098 303 VdVGAMISPARFDRLEELVADAVEKGaRLLAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 431 EAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDaKTGSPDYLLHFLEQKVV 510
Cdd:cd07098 383 EAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSV 461
|
..
gi 616190054 511 SE 512
Cdd:cd07098 462 TE 463
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
54-490 |
3.25e-60 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 205.10 E-value: 3.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 54 SINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD 133
Cdd:PRK13968 11 SVNPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 134 AAEGIDFIEYYARSMMDLAQGKPVLdREGEHNKYFYKSIGTGVTIPPWNFP-FAIMAGTtlAPVV-AGNTVLLKPAEDTP 211
Cdd:PRK13968 90 VAKSANLCDWYAEHGPAMLKAEPTL-VENQQAVIEYRPLGTILAIMPWNFPlWQVMRGA--VPILlAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 212 YIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHfVTFTGSRATGTRIYERSAVVqegqnfLKRVIAEMGGKD 291
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAA-VTVTGSVRAGAAIGAQAGAA------LKKCVLELGGSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 292 AIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN-TVDNTYMGPVINKKQFDKI 370
Cdd:PRK13968 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDpRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 371 KNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVIT 449
Cdd:PRK13968 320 HHQVEATLAEGaRLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 616190054 450 NNREHWIKAVNEFDVGNLYLNRGCTS-AVVGyhpFGGFKMSG 490
Cdd:PRK13968 400 TDETQARQMAARLECGGVFINGYCASdARVA---FGGVKKSG 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
27-470 |
7.64e-55 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 194.19 E-value: 7.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 27 KDVEKELGQDIPLVINGEKIFKDDK--IKSINPAdTSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRV 104
Cdd:PLN02419 104 QSTQPQMPPRVPNLIGGSFVESQSSsfIDVINPA-TQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 105 SAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYyARSMMDLAQGKPVLDREGEHNKYFYKS-IGTGVTIPPWNF 183
Cdd:PLN02419 183 QELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH-ACGMATLQMGEYLPNVSNGVDTYSIREpLGVCAGICPFNF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 184 PFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIgDYLVDHKDTHFVTFTGSRATG 263
Cdd:PLN02419 262 PAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 264 TRIYERSAVvqEGqnflKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVY---DEVLEKS 340
Cdd:PLN02419 341 MHIYARAAA--KG----KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 341 IKLtkELTLGNTVDNTyMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTD-----DSKGYFVEPTIISGLKSKDRIMQEE 415
Cdd:PLN02419 415 KAL--KVTCGSEPDAD-LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDivvpgYEKGNFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 416 IFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLN 470
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
173-496 |
1.06e-54 |
|
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: 189.74 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 173 GTGVTIPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGdYLVDH 248
Cdd:cd07135 110 GVVLIIGPWNYPVL----LALSPLVgaiaAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETT-ALLEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 249 KDTHfVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIV 328
Cdd:cd07135 184 KFDK-IFYTGSGRVGRIIAEAAA------KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 329 HKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEIGKeeGKLEQGGGTDDSKgYFVEPTIISGLKSK 408
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--GKVVIGGEMDEAT-RFIPPTIVSDVSWD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 409 DRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNR---EHWIKAVNEFD--VGNLYLNRGCTSAvvgyhPF 483
Cdd:cd07135 334 DSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKseiDHILTRTRSGGvvINDTLIHVGVDNA-----PF 408
|
330
....*....|...
gi 616190054 484 GGFKMSGTDAKTG 496
Cdd:cd07135 409 GGVGDSGYGAYHG 421
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
76-490 |
2.48e-54 |
|
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: 188.50 E-value: 2.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 76 EDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVgdAAEgIDF----IEYYARSMMDL 151
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAY--LTE-IAVvlgeIDHALKHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 152 AQGKPV---LDREGEHNKYFYKSIGTGVTIPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYIAyKLMEILEEA 224
Cdd:cd07087 78 MKPRRVsvpLLLQPAKAYVIPEPLGVVLIIGPWNYPLQ----LALAPLIgaiaAGNTVVLKPSELAPATS-ALLAKLIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 225 GLPKGVVNFVPGDPKEIGDyLVDHK-DthFVTFTGSRATGTRIYERSAvvqegQNfLKRVIAEMGGKDAIVVDENIDTDM 303
Cdd:cd07087 153 YFDPEAVAVVEGGVEVATA-LLAEPfD--HIFFTGSPAVGKIVMEAAA-----KH-LTPVTLELGGKSPCIVDKDANLEV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 304 AAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEigkeEGKL 383
Cdd:cd07087 224 AARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD----DGKV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 384 EQGGGTDDSKGYfVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFD 463
Cdd:cd07087 300 VIGGQVDKEERY-IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETS 378
|
410 420
....*....|....*....|....*..
gi 616190054 464 VGNLYLNRGCTSAVVGYHPFGGFKMSG 490
Cdd:cd07087 379 SGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
52-497 |
1.06e-52 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.19 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPADtSQVIANASKATKQDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV 131
Cdd:PLN02315 36 VSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 132 GDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTP 211
Cdd:PLN02315 115 GEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 212 YIAYKLM----EILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGtriyerSAVVQEGQNFLKRVIAEM 287
Cdd:PLN02315 195 LITIAMTklvaEVLEKNNLPGAIFTSFCGG-AEIGEAIAKDTRIPLVSFTGSSKVG------LMVQQTVNARFGKCLLEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 288 GGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDN-TYMGPVINKKQ 366
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKgTLLGPLHTPES 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 367 FDKIKNYIEIGKEEG-KLEQGGGTDDSKGYFVEPTIISGLKSKDrIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTG 445
Cdd:PLN02315 348 KKNFEKGIEIIKSQGgKILTGGSAIESEGNFVQPTIVEISPDAD-VVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 446 AVITNNRE---HWIKAVNEfDVGNLYLNRGCTSAVVGyHPFGGFKMSGTDAKTGS 497
Cdd:PLN02315 427 SIFTRNPEtifKWIGPLGS-DCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS 479
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
52-490 |
8.68e-51 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 179.92 E-value: 8.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 52 IKSINPADTSqVIANASKATKQDVEDAFKAANEAYKSWKTW-SANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEA 130
Cdd:cd07148 1 LEVVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 131 VGDAAEGIDFIEYYARSM---------MDLAQGKpvldrEGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNT 201
Cdd:cd07148 80 KVEVTRAIDGVELAADELgqlggreipMGLTPAS-----AGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 202 VLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIyeRSAVVQEgqnflK 281
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWML--RSKLAPG-----T 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 282 RVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVD-NTYMGP 360
Cdd:cd07148 227 RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDpDTEVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 361 VINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFvEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTD 440
Cdd:cd07148 307 LIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLP 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 616190054 441 YGLTGAVITNNREHWIKAVNEFDVGNLYLNRGcTSAVVGYHPFGGFKMSG 490
Cdd:cd07148 386 VAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSG 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
175-490 |
3.22e-48 |
|
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: 172.69 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 175 GVT--IPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDpKEIGDYLVDH 248
Cdd:cd07136 102 GVVliIAPWNYPFQL----ALAPLIgaiaAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGG-VEENQELLDQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 249 K-DTHFvtFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAI 327
Cdd:cd07136 176 KfDYIF--FTGSVRVGKIVMEAAA------KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 328 VHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIeigkEEGKLEQGGGTDDsKGYFVEPTIISGLKS 407
Cdd:cd07136 248 VHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLL----DNGKIVFGGNTDR-ETLYIEPTILDNVTW 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 408 KDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNlylnrGCTSAVVgYH------ 481
Cdd:cd07136 323 DDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGG-----GCINDTI-MHlanpyl 396
|
....*....
gi 616190054 482 PFGGFKMSG 490
Cdd:cd07136 397 PFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
78-490 |
4.40e-48 |
|
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: 172.03 E-value: 4.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 78 AFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAvgDAAE---GIDFIEYYARSMMDLAQG 154
Cdd:cd07134 3 VFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEV--DLTEilpVLSEINHAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 155 KPV---LDREGEHNKYFYKSIGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEEAGLP 227
Cdd:cd07134 81 KRVrtpLLLFGTKSKIRYEPKGVCLIISPWNYPF----NLAFGPLVsaiaAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 228 KGVVNFVpGDPkEIGDYL----VDHkdthfVTFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDM 303
Cdd:cd07134 157 DEVAVFE-GDA-EVAQALlelpFDH-----IFFTGSPAVGKIVMAAAA------KHLASVTLELGGKSPTIVDETADLKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 304 AAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELtLGNTV---DNTYMGPVINKKQFDKIKNYIEIGKEE 380
Cdd:cd07134 224 AAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKF-YGKDAarkASPDLARIVNDRHFDRLKGLLDDAVAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 381 G-KLEQGGGTDDSKGYfVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAV 459
Cdd:cd07134 303 GaKVEFGGQFDAAQRY-IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVL 381
|
410 420 430
....*....|....*....|....*....|.
gi 616190054 460 NEFDVGNLYLNRGCTSAVVGYHPFGGFKMSG 490
Cdd:cd07134 382 ARTSSGGVVVNDVVLHFLNPNLPFGGVNNSG 412
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-493 |
3.24e-43 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 158.92 E-value: 3.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 76 EDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV--------GDAAEGIDFI------ 141
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlseillvkNEIKYAISNLpewmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 142 EYYARSMMDLaqgkpvLDRegehnKYFYKS-IGTGVTIPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYIAyK 216
Cdd:cd07132 81 EPVKKNLATL------LDD-----VYIYKEpLGVVLIIGAWNYPLQL----TLVPLVgaiaAGNCVVIKPSEVSPATA-K 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 217 LMEILeeagLPK-------GVVNfvpGDPKEIGDyLVDHKDTHfVTFTGSRATGTRIYERSAVvqegqnFLKRVIAEMGG 289
Cdd:cd07132 145 LLAEL----IPKyldkecyPVVL---GGVEETTE-LLKQRFDY-IFYTGSTSVGKIVMQAAAK------HLTPVTLELGG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 290 KDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDK 369
Cdd:cd07132 210 KSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 370 IKNYIEigkeEGKLEQGGGTDDSKGYfVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVIT 449
Cdd:cd07132 290 LKKLLS----GGKVAIGGQTDEKERY-IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFS 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 616190054 450 NNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMSGTDA 493
Cdd:cd07132 365 NNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGA 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
175-490 |
4.99e-39 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 148.25 E-value: 4.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 175 GVT--IPPWNFPFAimagTTLAPVV----AGNTVLLKPAEDTPYIAyKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDH 248
Cdd:PTZ00381 111 GVVlvIGAWNYPLN----LTLIPLAgaiaAGNTVVLKPSELSPHTS-KLMAKLLTKYLDPSYVRVIEGGVEVTTELLKEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 249 KDTHFvtFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIV 328
Cdd:PTZ00381 186 FDHIF--FTGSPRVGKLVMQAAA------ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 329 HKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEIGKeeGKLEQGGGTDDSKGYfVEPTIISGLKSK 408
Cdd:PTZ00381 258 HRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHG--GKVVYGGEVDIENKY-VAPTIIVNPDLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 409 DRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRgCTSAVVGYH-PFGGFK 487
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIND-CVFHLLNPNlPFGGVG 413
|
...
gi 616190054 488 MSG 490
Cdd:PTZ00381 414 NSG 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
172-496 |
1.87e-35 |
|
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: 137.16 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 172 IGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEiGDYLVD 247
Cdd:cd07137 102 LGVVLVISAWNFPF----LLSLEPVIgaiaAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPE-TTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 248 HK-DTHFvtFTGSRATGtRIyersaVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGF-SGQKCSACSR 325
Cdd:cd07137 176 QKwDKIF--FTGSPRVG-RI-----IMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 326 AIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYfVEPTIISGL 405
Cdd:cd07137 248 VLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLY-IEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 406 KSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGG 485
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
330
....*....|.
gi 616190054 486 FKMSGTDAKTG 496
Cdd:cd07137 407 VGESGFGAYHG 417
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
75-499 |
1.04e-33 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 132.75 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 75 VEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAvGDAAEGIDFIEYYArsmmDLAQG 154
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLRARA----FVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 155 KPVLDREGEH-------NKYFYKsIGTGVT--IPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAG 225
Cdd:cd07084 76 YRIPHEPGNHlgqglkqQSHGYR-WPYGPVlvIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 226 -LPKGVVNFVPGDpKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVqegqnflkRVIAEMGGKDAIVVDENIDT-DM 303
Cdd:cd07084 155 lLPPEDVTLINGD-GKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--------RIYLELAGFNWKVLGPDAQAvDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 304 AAEAIVTSAFGFSGQKCSACSRAIVHKdvyDEVLEKSIKLTKELTLGNTVDNTYMGPVInkkQFDKIKNYIEIGKEEG-- 381
Cdd:cd07084 226 VAWQCVQDMTACSGQKCTAQSMLFVPE---NWSKTPLVEKLKALLARRKLEDLLLGPVQ---TFTTLAMIAHMENLLGsv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 382 -----KLEQGGGTDDSKGYFVEPTI---ISGLKSKDRIMQEEIFGPVVGFVKVNDFDEA--IEVANDTDYGLTGAVITNN 451
Cdd:cd07084 300 llfsgKELKNHSIPSIYGACVASALfvpIDEILKTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSND 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 616190054 452 REHWIKAVNEFDV-GNLY-LNRGCTSAVVGYHPFGGFKMSGTDAKTGSPD 499
Cdd:cd07084 380 PIFLQELIGNLWVaGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
58-454 |
1.13e-33 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 133.55 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 58 ADTSQVIANASKATKqDVEDAFKAANE-AYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVgDAAE 136
Cdd:cd07128 22 AVTGEVVARVSSEGL-DFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAATGATRRDSWI-DIDG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 137 GIDFIEYYA---RSMMD----LAQGKPV-LDREGehnKYFYKSI-----GTGVTIPPWNFPFAIMAGTtLAP-VVAGNTV 202
Cdd:cd07128 100 GIGTLFAYAslgRRELPnahfLVEGDVEpLSKDG---TFVGQHIltprrGVAVHINAFNFPVWGMLEK-FAPaLLAGVPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 203 LLKPAEDTPYIAYKLMEILEEAG-LPKGVVNFVPGDPKEIGDYLvDHKDThfVTFTGSRATGTRIYERSAVVQEGQnflk 281
Cdd:cd07128 176 IVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHL-GEQDV--VAFTGSAATAAKLRAHPNIVARSI---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 282 RVIAEMG-------GKDAIVVDENID---TDMAAEAIVTSafgfsGQKCSACSRAIVHKDVYDEVLEKSIKLTKELTLGN 351
Cdd:cd07128 249 RFNAEADslnaailGPDATPGTPEFDlfvKEVAREMTVKA-----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 352 -TVDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGG-------GTDDSKGYFVEPTIisgLKSKD-----RIMQEEIFG 418
Cdd:cd07128 324 pRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGpdrfevvGADAEKGAFFPPTL---LLCDDpdaatAVHDVEAFG 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 616190054 419 PVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREH 454
Cdd:cd07128 401 PVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAF 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
165-438 |
8.83e-33 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 129.91 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 165 NKYFYKSIG-TGVtIPPWNFPFAImagtTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEEAGLPKgVVNFVPGDPk 239
Cdd:cd07133 95 AEVEYQPLGvVGI-IVPWNYPLYL----ALGPLIaalaAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGA- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 240 EIG--------DYLVdhkdthfvtFTGSRATGtRIYERSAvvqeGQNfLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTS 311
Cdd:cd07133 168 DVAaafsslpfDHLL---------FTGSTAVG-RHVMRAA----AEN-LTPVTLELGGKSPAIIAPDADLAKAAERIAFG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 312 AFGFSGQKCSACSRAIVHKDVYDEVLEKSIKLTKELtLGNTVDNTYMGPVINKKQFDKIKNYIEIGKEEG-KLEQ--GGG 388
Cdd:cd07133 233 KLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTSIINERHYARLQGLLEDARAKGaRVIElnPAG 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 616190054 389 TDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVAND 438
Cdd:cd07133 312 EDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINA 361
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
172-490 |
2.46e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 120.60 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 172 IGTGVTIPPWNFPFaimaGTTLAPVV----AGNTVLLKPAEDTPYIAYKLMEILEeAGLPKGVVNFVPGDPkEIGDYLVD 247
Cdd:PLN02203 109 LGVVLIFSSWNFPI----GLSLEPLIgaiaAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEGGP-AVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 248 HK-DTHFvtFTGSRATGtRIYERSAVvqegqNFLKRVIAEMGGKDAIVVD---ENIDTDMAAEAIVTSAFGF-SGQKCSA 322
Cdd:PLN02203 183 HKwDKIF--FTGSPRVG-RIIMTAAA-----KHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 323 CSRAIVHKDVYDEVLEKSIKLTKELTLGNTVDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDsKGYFVEPTII 402
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDE-KKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 403 SGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNrgctSAVVGYH- 481
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN----DAIIQYAc 409
|
330
....*....|..
gi 616190054 482 ---PFGGFKMSG 490
Cdd:PLN02203 410 dslPFGGVGESG 421
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
97-454 |
9.45e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.65 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 97 RAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAAEGIDFIEYYAR---SMMD---LAQGKPVldREGEHNKYFYK 170
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaALGDarlLRDGEAV--QLGKDPAFQGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 171 SI-----GTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAG-LPKGVVNFVPGDPKEIGDY 244
Cdd:PRK11903 143 HVlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 245 LvdhKDTHFVTFTGSRATGTRIYERSAVVQEGQnflkRVIAEMGGKDAIVV--DENIDT---DMAAEAIVTSAFGFSGQK 319
Cdd:PRK11903 223 L---QPFDVVSFTGSAETAAVLRSHPAVVQRSV----RVNVEADSLNSALLgpDAAPGSeafDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 320 CSACSRAIVHKDVYDEVLEK-SIKLTKeLTLGNTVDNTY-MGPVINKKQFDKIKNYIEIGKEEGKLEQGGGT------DD 391
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEAlAARLAK-TTVGNPRNDGVrMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvdaDP 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616190054 392 SKGYFVEPTII--SGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREH 454
Cdd:PRK11903 375 AVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAF 439
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
172-496 |
2.29e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 105.90 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 172 IGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKPAEDTPYIAYKLMEILEEAgLPKGVVNFVPGDPKEIGDYLVDHKDT 251
Cdd:PLN02174 113 LGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKWDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 252 HFvtFTGSRATGTRIYERSAvvqegqNFLKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFGF-SGQKCSACSRAIVHK 330
Cdd:PLN02174 192 IF--YTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYILTTK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 331 DVYDEVLEkSIKLTKELTLG-NTVDNTYMGPVINKKQFDKIKNYIEIGKEEGKLEQgGGTDDSKGYFVEPTIISGLKSKD 409
Cdd:PLN02174 264 EYAPKVID-AMKKELETFYGkNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVY-GGEKDRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 410 RIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGLTGAVITNNREHWIKAVNEFDVGNLYLNRGCTSAVVGYHPFGGFKMS 489
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGES 421
|
....*..
gi 616190054 490 GTDAKTG 496
Cdd:PLN02174 422 GMGAYHG 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
41-451 |
3.84e-21 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 96.41 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 41 INGEKIFK--DDKIKSINPadtsqVIANASKATKQDVEDAFKAAnEAYKSWktwsandrAELMLRVSAIIRRRKAE--IA 116
Cdd:cd07126 20 LNGDKFISvpDTDEDEINE-----FVDSLRQCPKSGLHNPLKNP-ERYLLY--------GDVSHRVAHELRKPEVEdfFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 117 AIMVYEAGKPWDEAVGDAAEGIDFIEYYARSMMD-LAQGKPVL-DREGEHNKYFYKSIGTGVTIPPWNFPFAIMAGTTLA 194
Cdd:cd07126 86 RLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRfLARSFNVPgDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 195 PVVAGNTVLLKPAEDTPYIAYKLMEILEEAGLPKGVVNFVPGDPKEIGDYLVDHKdTHFVTFTGSratgTRIYERSAVVQ 274
Cdd:cd07126 166 ALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEAN-PRMTLFTGS----SKVAERLALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 275 EGqnflkRVIAEMGGKD-AIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSIkltKELTLGNTV 353
Cdd:cd07126 241 HG-----KVKLEDAGFDwKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAGILDKL---KALAEQRKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 354 DNTYMGPVI---NKKQFDKIKNYIEIgkEEGKLEQGGG--TDDSKGYF---VEPTII-----SGLKSKD-RIMQEEIFGP 419
Cdd:cd07126 313 EDLTIGPVLtwtTERILDHVDKLLAI--PGAKVLFGGKplTNHSIPSIygaYEPTAVfvpleEIAIEENfELVTTEVFGP 390
|
410 420 430
....*....|....*....|....*....|....
gi 616190054 420 --VVGFVKVNDFDEAIEVANDTDYGLTGAVITNN 451
Cdd:cd07126 391 fqVVTEYKDEQLPLVLEALERMHAHLTAAVVSND 424
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
75-454 |
1.44e-16 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 81.82 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 75 VEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGDAA--------------EGidf 140
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGrttgqlrlfadlvrEG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 141 ieYYARSMMDLAQ------GKPVLDRegehnkyFYKSIGTGVTIPPWNFPFA--IMAGTTLAPVVAGNTVLLK--PAE-D 209
Cdd:cd07129 78 --SWLDARIDPADpdrqplPRPDLRR-------MLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAHpG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 210 TPYIAYKLM-EILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSRATGTRIYERSAVVQEGqnflKRVIAEMG 288
Cdd:cd07129 149 TSELVARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP----IPFYAELG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMA---AEAIVTSAFGFSGQKCSACSRAIVHKdvyDEVLEKSIKLTKElTLGNTVDNTYMGPVInKK 365
Cdd:cd07129 225 SVNPVFILPGALAERGeaiAQGFVGSLTLGAGQFCTNPGLVLVPA---GPAGDAFIAALAE-ALAAAPAQTMLTPGI-AE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 366 QFDKIKNyiEIGKEEGKLEQGGGTDDSKGYFVEPTIisgLKS------KDRIMQEEIFGPVVGFVKVNDFDEAIEVANDT 439
Cdd:cd07129 300 AYRQGVE--ALAAAPGVRVLAGGAAAEGGNQAAPTL---FKVdaaaflADPALQEEVFGPASLVVRYDDAAELLAVAEAL 374
|
410
....*....|....*
gi 616190054 440 DYGLTGAVITNNREH 454
Cdd:cd07129 375 EGQLTATIHGEEDDL 389
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
74-436 |
7.63e-15 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 77.13 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 74 DVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEAGKPWDEAV---GDAAE--GIDFIEYYARSM 148
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFqagGPHAQdrGLEAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 149 MDLAQGKPVLDREGEHN----KYFYKSIGTGV-------TIPPWN-FPfaimagTTLAPVVAGNTVLLK-------PAED 209
Cdd:cd07127 165 SRIPPTAEWEKPQGKHDplamEKTFTVVPRGValvigcsTFPTWNgYP------GLFASLATGNPVIVKphpaailPLAI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 210 TPYIAyklMEILEEAGLPKGVVNFVPGDPKE-IGDYLVDHKDTHFVTFTGSRATGTRIyERSAvvqeGQnflKRVIAEMG 288
Cdd:cd07127 239 TVQVA---REVLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDFTGSNAFGDWL-EANA----RQ---AQVYTEKA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 289 GKDAIVVDENIDTDMAAEAIVTSAFGFSGQKCSACSRAIVHKD---------VYDEVLEKSIKLTKELTLGNTVDNTYMG 359
Cdd:cd07127 308 GVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGLLADPARAAALLG 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616190054 360 PVINKKQFDKIKNYIEIGKEEGKLEQGGGTDDSKGYFVEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07127 388 AIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
73-463 |
4.09e-12 |
|
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: 68.03 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 73 QDVEDAFKAANEAYKSWKTWSANDRAELMLRVSAIIRRRKAEIAAIMVYEA--GKPWD-----EAVGDAAEGIDFIEYYA 145
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETgmGRVEDkiaknHLAAEKTPGTEDLTTTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 146 RSmmdlaqgkpvldreGEHNKYFYKSIGTGV--TIPPWNFPFAIMAGTTLAPVVAGNTVLLKP---AEDTPYIAYKLM-E 219
Cdd:cd07121 84 WS--------------GDNGLTLVEYAPFGVigAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELInK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 220 ILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSratgtriyerSAVVQEGQNFLKRVIAEMGGKDAIVVDENI 299
Cdd:cd07121 150 AIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGG----------PAVVKAALSSGKKAIGAGAGNPPVVVDETA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 300 DTDMAAEAIVTSAfGFSGQ-KCSACSRAIVHKDVYDEVLEKSIK-----LTKE--LTLGNTVDNTYMGPVINKKQfdkik 371
Cdd:cd07121 220 DIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADYLIAAMQRngayvLNDEqaEQLLEVVLLTNKGATPNKKW----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 372 nyieIGKEEGK-LEQGGGTDDSKgyfvEPTIISGLKSKDRIMQEEIFGPVVGFVKVNDFDEAIEVANDTDYGL--TGAVI 448
Cdd:cd07121 294 ----VGKDASKiLKAAGIEVPAD----IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIH 365
|
410
....*....|....*
gi 616190054 449 TNNREHWIKAVNEFD 463
Cdd:cd07121 366 SKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
75-436 |
2.79e-10 |
|
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: 62.28 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 75 VEDAFKAANEAYKSWKTWSANDRAELM--LRVSAIIRRRKAEIAAIMVYEAGKPWDEAVGD--AAEGIDFIEYYARSMMD 150
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFraAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNhfAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 151 LAQGKPVLD-REGEhnkyfykSIGTGVTIPPWNFPFAIMAGTTLAPVVAGNTVLLKP---AEDTPYIAYKLM-EILEEAG 225
Cdd:cd07081 81 LTGDENGGTlIIAE-------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 226 LPKGVVNFVPGDPKEIGDYLVDHKDTHFVTFTGSratgtriyerSAVVQEGQNFLKRVIAEMGGKDAIVVDENIDTDMAA 305
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATGG----------PAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 306 EAIVTSAFGFSGQKCSACSRAIVHKDVYDEVLEKSikltkeltlgntvdNTYMGPVINKKQFDKIKNYIE---------I 376
Cdd:cd07081 224 QSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLF--------------EGQGAYKLTAEELQQVQPVILkngdvnrdiV 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616190054 377 GKEEGKLEQGGG---TDDSKGYFVEPTIIsglkSKDRIMQEEIFGPVVGFVKVNDFDEAIEVA 436
Cdd:cd07081 290 GQDAYKIAAAAGlkvPQETRILIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
214-462 |
2.12e-08 |
|
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: 56.35 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 214 AYKLM-EILEEAGLPKGVVNFVPGDPKEIGDYLVDHKDTHFVTftgsrATGtriyersavvqeGQNFLKRviAEMGGKDA 292
Cdd:cd07122 141 AAKIMrEAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLIL-----ATG------------GPGMVKA--AYSSGKPA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 293 I---------VVDENIDTDMAAEAIVTS-AFGFsGQKCSACSRAIVHKDVYDEVLEksiKLTKEltlgntvdNTYmgpVI 362
Cdd:cd07122 202 IgvgpgnvpaYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRA---ELKRR--------GAY---FL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 363 NKKQFDKIKNYIE----------IGKEEGKLEQGGG---TDDSKGYFVEPTIIsglkSKDRIMQEEIFGPVVGFVKVNDF 429
Cdd:cd07122 267 NEEEKEKLEKALFddggtlnpdiVGKSAQKIAELAGievPEDTKVLVAEETGV----GPEEPLSREKLSPVLAFYRAEDF 342
|
250 260 270
....*....|....*....|....*....|....*..
gi 616190054 430 DEAIEVAND-TDYGLTG--AVI-TNNREHwikaVNEF 462
Cdd:cd07122 343 EEALEKARElLEYGGAGhtAVIhSNDEEV----IEEF 375
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
116-339 |
3.74e-08 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 55.69 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 116 AAIMVYEAGKPW-DEAVGDAAEGIDFIEYYARSMMDLAQGKPVLDREGEHNKYFYKSIGTGVTIP----------PWNFP 184
Cdd:cd07077 25 IANALYDTRQRLaSEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITASVGHIQDVLLPdngetyvrafPIGVT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 185 FAIMAGT--TLAPVVA------GNTVLLKPAEDTPYIAYKLMEILEEA---GLPKGVVNFVPGDPKEIGDYLVDHKDTHF 253
Cdd:cd07077 105 MHILPSTnpLSGITSAlrgiatRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEELLSHPKIDL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616190054 254 VTFTGSRATGTRIYERSAVvqegqnflKRVIAEMGGKDAIVVDENIDTDMAAEAIVTSAFgFSGQKCSACSRAIVHKDVY 333
Cdd:cd07077 185 IVATGGRDAVDAAVKHSPH--------IPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVDDVL 255
|
....*.
gi 616190054 334 DEVLEK 339
Cdd:cd07077 256 DPLYEE 261
|
|
| |
