|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
25-546 |
0e+00 |
|
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: 990.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 25 VKNEPILGFNEGSPERAELQKALDDLKGKTEEIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVA 104
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 105 ARREWDLKPIQDRAQVLFKAADIISGPKRAEILAKTMIGQGKTVVQAEIDAAAELIDFFRFNAKHAVELESQQPLDSD-G 183
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPaG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 184 STNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFG 263
Cdd:cd07123 161 VWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 264 DTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSA 343
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 344 CSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLNVIAGGHCNDKKGYFVE 423
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 424 PTIIESTDPQEAIMAEEIFGPVLSVYVYPENDYLEVLHLIDNTSPYALTGAVFALDKNVVNEAAKALRNAAGNYYVNDKS 503
Cdd:cd07123 400 PTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1367454336 504 TGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVVKATHVP 546
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
26-556 |
0e+00 |
|
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: 869.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 26 KNEPILGFNEGSPERAELQKALDDLKGKTEEIPCVVGDEHVWTKDIR-YQLSPFNHSHKLAKFCYADKELLNKAILASVA 104
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNERiPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 105 ARREWDLKPIQDRAQVLFKAADIISGPKRAEILAKTMIGQGKTVVQAEIDAAAELIDFFRFNAKHAVELESQQPLDSDGS 184
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 185 TNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGD 264
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 265 TITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSAC 344
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 345 SRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSP-KLNVIAGGHCNDKKGYFVE 423
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQSFDKIVKYIEDAKKDPeALTILYGGKYDDSQGYFVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 424 PTIIESTDPQEAIMAEEIFGPVLSVYVYPENDYLEVLHLIDNTSPYALTGAVFALDKNVVNEAAKALRNAAGNYYVNDKS 503
Cdd:TIGR01236 400 PTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1367454336 504 TGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVVKATHVPLREWKYPYMG 556
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-544 |
0e+00 |
|
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: 674.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 40 RAELQKALDDLKG-KTEEIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRA 118
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 119 QVLFKAADIISGPKRAEILAKTMIGqGKTVVQaEIDAAAELIDFFRFNAKHAVELESQQPLDSD--GSTNTMLYRGLeGF 196
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEVVPypGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 197 IAAVAPFNFT-AIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGI 275
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 276 NFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWP 355
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 356 QIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHCNDKKGYFVEPTIIESTDPQEA 435
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAEQEAKVLSYIEHGKNEGQL--VLGGKRLEGEGYFVAPTVVEEVPPKAR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 436 IMAEEIFGPVLSVYVYPENDYLEVLHLIDNTsPYALTGAVFALDKNVVNEAAKALrnAAGNYYVNDKSTGSIVAQQPFGG 515
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANST-PYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGVQPFGG 471
|
490 500
....*....|....*....|....*....
gi 1367454336 516 ARASGTNDKPGGPHYVLRWTSPQVVKATH 544
Cdd:cd07083 472 FKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
53-544 |
1.49e-130 |
|
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: 389.49 E-value: 1.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 53 KTEEIPCVVGDEHVWTKDIRYQ--LSPFNhSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISg 130
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 131 pKRAEILAKTM-IGQGKTVVQAEIDAAaELIDFFRFNAKHAVELE-SQQPLDSDGSTNTMLYRGLeGFIAAVAPFNFTAI 208
Cdd:COG1012 80 -ERREELAALLtLETGKPLAEARGEVD-RAADFLRYYAGEARRLYgETIPSDAPGTRAYVRREPL-GVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 209 GGNLAGTPAL-MGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRL 287
Cdd:COG1012 157 LAAWKLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 288 WKQVAQNLdvyknfPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQ 367
Cdd:COG1012 237 AAAAAENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 368 LKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSpKLNVIAGGHC-NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVL 446
Cdd:COG1012 311 LKVGDP-LDPGTDMGPLISEAQLERVLAYIEDAVAE-GAELLTGGRRpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 447 SVYVYpeNDYLEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSiVAQQPFGGARASGTNDKpG 526
Cdd:COG1012 389 SVIPF--DDEEEAIALA-NDTEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-G 461
|
490
....*....|....*...
gi 1367454336 527 GPHYVLRWTSPQVVKATH 544
Cdd:COG1012 462 GREGLEEYTETKTVTIRL 479
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
26-540 |
2.92e-125 |
|
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: 376.95 E-value: 2.92e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 26 KNEPILGFNEGSpERAELQKALDDLKGKT-EEIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVA 104
Cdd:cd07124 2 RNEPFTDFADEE-NRAAFRAALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 105 ARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAEIDAAaELIDFFRFNAKHAVELESQQPLDSDGS 184
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLR-RRRFELAAWMVLEVGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 185 TNTMLYRGLeGFIAAVAPFNF-TAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFG 263
Cdd:cd07124 159 DNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 264 DTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSA 343
Cdd:cd07124 238 DYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 344 CSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHC--NDKKGYF 421
Cdd:cd07124 318 CSRVIVHESVYDEFLERLVERTKALKVGDP-EDPEVYMGPVIDKGARDRIRRYIEIGKSEGRL--LLGGEVleLAAEGYF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 422 VEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHlIDNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVND 501
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKA--KDFDEALE-IANDTEYGLTGGVFSRSPEHLERARREFE--VGNLYANR 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 1367454336 502 KSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVV 540
Cdd:cd07124 470 KITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTV 508
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
96-540 |
3.50e-120 |
|
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: 361.14 E-value: 3.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 96 NKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQAEIDAAaELIDFFRFNAKHAVELE 174
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLE--ERREELAALEtLETGKPIEEALGEVA-RAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 175 SQQPLDSDGSTNTMLYRGLEGFIAAVAPFNFT-AIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQ 253
Cdd:cd07078 78 GEVIPSPDPGELAIVRREPLGVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 254 FVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECGGKNFHFVHKSADVQSVVTGTIRSA 333
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 334 FEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKsSPKLNVIAGGH 413
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDP-DTDMGPLISAAQLDRVLAYIEDAK-AEGAKLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 414 CND-KKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRn 492
Cdd:cd07078 310 RLEgGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEE--EAIELA-NDTEYGLAAGVFTRDLERALRVAERLE- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1367454336 493 aAGNYYVNDKSTGsIVAQQPFGGARASGTNdKPGGPHYVLRWTSPQVV 540
Cdd:cd07078 386 -AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
75-540 |
2.52e-116 |
|
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: 352.22 E-value: 2.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNHShKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQAEI 153
Cdd:pfam00171 12 INPATGE-VIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELEtLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 154 DAAaELIDFFRFNAKHAVELESQqPLDSDGSTNTMLYRGLEGFIAAVAPFNFTA--IGGNLAgtPALM-GNVVLWKPSD- 229
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPLllPAWKIA--PALAaGNTVVLKPSEl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 230 TAMSAsYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECG 309
Cdd:pfam00171 165 TPLTA-LLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 310 GKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKS 389
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 390 FARIKKWLDHAKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHlIDNTSPY 469
Cdd:pfam00171 317 LERVLKYVEDAKEE-GAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRF--KDEEEAIE-IANDTEY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367454336 470 ALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVAqQPFGGARASGTNDKpGGPHYVLRWTSPQVV 540
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
26-532 |
2.80e-110 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 338.45 E-value: 2.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 26 KNEPILGFNEgsPE-RAELQKALDDLKGKT-EEIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASV 103
Cdd:PRK03137 6 KHEPFTDFSV--EEnVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 104 AARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAEIDAAaELIDFFRFNAKHAVELESQQPLDS-D 182
Cdd:PRK03137 84 EAFETWKKWSPEDRARILLRAAAIIR-RRKHEFSAWLVKEAGKPWAEADADTA-EAIDFLEYYARQMLKLADGKPVESrP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 183 GSTNTMLYRGLeGFIAAVAPFNF-TAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPV 261
Cdd:PRK03137 162 GEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 262 FGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKC 341
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 342 SACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwsTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHCNDKKGYF 421
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQASFDKIMSYIEIGKEEGRL--VLGGEGDDSKGYF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 422 VEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHlIDNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVND 501
Cdd:PRK03137 397 IQPTIFADVDPKARIMQEEIFGPVVA--FIKAKDFDHALE-IANNTEYGLTGAVISNNREHLEKARREFH--VGNLYFNR 471
|
490 500 510
....*....|....*....|....*....|.
gi 1367454336 502 KSTGSIVAQQPFGGARASGTNDKPGGPHYVL 532
Cdd:PRK03137 472 GCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
26-540 |
1.34e-102 |
|
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: 318.73 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 26 KNEPILGFNEgSPERAELQKALDDLK---GKTeeIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILAS 102
Cdd:TIGR01237 2 KHEPFTDFAD-EENRQAFFKALATVKeqlGKT--YPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 103 VAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAEIDAAaELIDFFRFNAKHAVELESQQP-LDS 181
Cdd:TIGR01237 79 AKAFEAWKKTDPEERAAILFKAAAIVR-RRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPvNSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 182 DGSTNTMLYRGLeGFIAAVAPFNFT-AIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGP 260
Cdd:TIGR01237 157 EGETNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 261 VFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQK 340
Cdd:TIGR01237 236 EVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 341 CSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHCNDKKGY 420
Cdd:TIGR01237 316 CSAGSRAVVHEKVYDEVVERFVEITESLKVGPP-DSADVYVGPVIDQKSFNKIMEYIEIGKAEGRL--VSGGCGDDSKGY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 421 FVEPTIIESTDPQEAIMAEEIFGPVlsVYVYPENDYLEVLHLIDNTSpYALTGAVFALDKNVVNEAAKALRnaAGNYYVN 500
Cdd:TIGR01237 393 FIGPTIFADVDRKARLAQEEIFGPV--VAFIRASDFDEALEIANNTE-YGLTGGVISNNRDHINRAKAEFE--VGNLYFN 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1367454336 501 DKSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVV 540
Cdd:TIGR01237 468 RNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTV 507
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
33-533 |
1.44e-91 |
|
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: 290.25 E-value: 1.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 33 FNEGSPERAELQKALDDLKGKT-EEIPCVVGDEHVW--TKDIRyqlSPFNHSHKLAKFCYADKELLNKAILASVAARREW 109
Cdd:cd07125 9 IFDLEVPLEALADALKAFDEKEwEAIPIINGEETETgeGAPVI---DPADHERTIGEVSLADAEDVDAALAIAAAAFAGW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 110 DLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQAeIDAAAELIDFFRFNAKHAVELESQQPLDS-DGSTNTM 188
Cdd:cd07125 86 SATPVEERAEILEKAADLLEA-NRGELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGpTGELNGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 189 LYRGLeGFIAAVAPFNF---TAIGGNLAgtpALM-GNVVLWKPS-DTAMSASYAVyNVLRDSGLPPNIIQFVPADGPVFG 263
Cdd:cd07125 164 ELHGR-GVFVCISPWNFplaIFTGQIAA---ALAaGNTVIAKPAeQTPLIAARAV-ELLHEAGVPRDVLQLVPGDGEEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 264 DTITSSEHLAGINFTGSVPTFKRLWKQVAQN--LDVyknfPRVAgECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKC 341
Cdd:cd07125 239 EALVAHPRIDGVIFTGSTETAKLINRALAERdgPIL----PLIA-ETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 342 SACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHCNDKKGYF 421
Cdd:cd07125 314 SALRLLYLQEEIAERFIEMLKGAMASLKVGDP-WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWL--IAPAPLDDGNGYF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 422 VEPTIIE---STDPQeaimaEEIFGPVLSVYVYPENDYLEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYY 498
Cdd:cd07125 391 VAPGIIEivgIFDLT-----TEVFGPILHVIRFKAEDLDEAIEDI-NATGYGLTLGIHSRDEREIEYWRERVE--AGNLY 462
|
490 500 510
....*....|....*....|....*....|....*
gi 1367454336 499 VNDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLR 533
Cdd:cd07125 463 INRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLR 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
101-540 |
2.56e-86 |
|
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: 271.80 E-value: 2.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 101 ASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQAEIDAAaELIDFFRFNAKHAVELE-SQQP 178
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLE--ERREELAALEtLETGKPIEEALGEVA-RAIDTFRYAAGLADKLGgPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 179 LDSDGSTNTMLYRGLeGFIAAVAPFNF-TAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPA 257
Cdd:cd06534 79 SPDPGGEAYVRREPL-GVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 258 DGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYG 337
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 338 GQKCSACSRMYVPDSLWPQIKQGLLdihkqlkvgdpvedwstffsaviddksfarikkwldhaksspklnviagghcndk 417
Cdd:cd06534 232 GQICTAASRLLVHESIYDEFVEKLV------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 418 kgyfvepTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNY 497
Cdd:cd06534 257 -------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEE--EAIALA-NDTEYGLTAGVFTRDLNRALRVAERLR--AGTV 324
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1367454336 498 YVNDKSTGSiVAQQPFGGARASGTNDKpGGPHYVLRWTSPQVV 540
Cdd:cd06534 325 YINDSSIGV-GPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
26-540 |
2.50e-69 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 241.26 E-value: 2.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 26 KNEPILGFNEGSpERAELQKALDDLKGKTEEIPCVVGDehvwTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVAA 105
Cdd:PRK11904 523 KNSKGLNLNDRS-ELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAA 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 106 RREWDLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVvqaeIDAAAEL---IDFFRFNAKHAVELESQ-QPL-D 180
Cdd:PRK11904 598 FPAWSRTPVEERAAILERAADLLEA-NRAELIALCVREAGKTL----QDAIAEVreaVDFCRYYAAQARRLFGApEKLpG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 181 SDGSTNTMLYRGLeGFIAAVAPFNFT-AI-GGNLAGtpALM-GNVVLWKPSD-TAMSASYAVyNVLRDSGLPPNIIQFVP 256
Cdd:PRK11904 673 PTGESNELRLHGR-GVFVCISPWNFPlAIfLGQVAA--ALAaGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLP 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 257 ADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQnldvyKNFPRVA--GECGGKNFHFVHKSADVQSVVTGTIRSAF 334
Cdd:PRK11904 749 GDGATVGAALTADPRIAGVAFTGSTETARIINRTLAA-----RDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAF 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 335 EYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHC 414
Cdd:PRK11904 824 RSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDP-RLLSTDVGPVIDAEAKANLDAHIERMKREARL--LAQLPL 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 415 ND--KKGYFVEPTIIESTDPQEaiMAEEIFGPVLSVYVYPENDYLEVLHLIDNTSpYALTGAVFALDKNVVNEAAKALRn 492
Cdd:PRK11904 901 PAgtENGHFVAPTAFEIDSISQ--LEREVFGPILHVIRYKASDLDKVIDAINATG-YGLTLGIHSRIEETADRIADRVR- 976
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1367454336 493 aAGNYYVNDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVV 540
Cdd:PRK11904 977 -VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
67-545 |
6.86e-68 |
|
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: 227.13 E-value: 6.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 67 WTK--DIRYQLSPFNHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMI-G 143
Cdd:cd07097 9 WVAggDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELARLLTrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 144 QGKTVVQA--EIDAAaelIDFFRFNAKHAVEL--ESQQPLDSDgsTNTMLYRGLEGFIAAVAPFNF-TAIGG-NLAgtPA 217
Cdd:cd07097 87 EGKTLPEArgEVTRA---GQIFRYYAGEALRLsgETLPSTRPG--VEVETTREPLGVVGLITPWNFpIAIPAwKIA--PA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 218 LM-GNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQnld 296
Cdd:cd07097 160 LAyGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAA--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 297 vykNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVED 376
Cdd:cd07097 237 ---RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 377 wSTFFSAVIDDKSFARIKKWLDHAKSSPKlNVIAGGHC--NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeN 454
Cdd:cd07097 314 -GVDIGPVVSERQLEKDLRYIEIARSEGA-KLVYGGERlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRV--R 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 455 DYLEVLHlIDNTSPYALTGAVFALDknvVNEAAKALRNA-AGNYYVNDKSTGsiVAQQ-PFGGARASGTNDKPGGPHYVL 532
Cdd:cd07097 390 DYDEALA-IANDTEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALE 463
|
490
....*....|...
gi 1367454336 533 RWTSpqvVKATHV 545
Cdd:cd07097 464 FYTT---IKTVYV 473
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
39-540 |
1.00e-63 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 225.97 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 39 ERAELQKALDDLKGKTEEI-PCVVGDEHvwTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDR 117
Cdd:COG4230 540 VLAALSAALAAAAEKQWQAaPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 118 AQVLFKAADIISGpKRAEILAKTMIGQGKTVVqaeiDAAAEL---IDFFRFNAKHAVELESqqpldsdgstNTMLYRGLe 194
Cdd:COG4230 618 AAILERAADLLEA-HRAELMALLVREAGKTLP----DAIAEVreaVDFCRYYAAQARRLFA----------APTVLRGR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 195 GFIAAVAPFNFTaiggnLAG-----TPALM-GNVVLWKPSD-TAMSASYAVyNVLRDSGLPPNIIQFVPADGPVFGDTIT 267
Cdd:COG4230 682 GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 268 SSEHLAGINFTGSVPTFKRLWKQVAQNLDvyKNFPRVAgECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRM 347
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDG--PIVPLIA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 348 YVPDSLWPQIK---QGLLDihkQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKL--NVIAGGHCNdkKGYFV 422
Cdd:COG4230 833 CVQEDIADRVLemlKGAMA---ELRVGDP-ADLSTDVGPVIDAEARANLEAHIERMRAEGRLvhQLPLPEECA--NGTFV 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 423 EPTIIESTDPQEaiMAEEIFGPVLSVYVYPENDYLEVLHLIDNTSpYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDK 502
Cdd:COG4230 907 APTLIEIDSISD--LEREVFGPVLHVVRYKADELDKVIDAINATG-YGLTLGVHSRIDETIDRVAARAR--VGNVYVNRN 981
|
490 500 510
....*....|....*....|....*....|....*...
gi 1367454336 503 STGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVV 540
Cdd:COG4230 982 IIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
41-537 |
2.36e-62 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 222.05 E-value: 2.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 41 AELQKALDDLKGKTEEIPCVVGDEHVwTKDIRYQLSPFNHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQV 120
Cdd:PRK11905 539 AALDEALNAFAAKTWHAAPLLAGGDV-DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAI 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 121 LFKAADIISGpKRAEILAKTMIGQGKTVVqaeiDAAAEL---IDFFRFNAKHAVELESQQPLdsdgstntmlyRGLeGFI 197
Cdd:PRK11905 618 LERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGPGH-----------KPL-GPV 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 198 AAVAPFNFT-AI-GGNLAGtpALM-GNVVLWKPSD-TAMSASYAVyNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLA 273
Cdd:PRK11905 681 VCISPWNFPlAIfTGQIAA--ALVaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPGDGRTVGAALVADPRIA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 274 GINFTGSVPTFKRLWKQVAQNLDvyKNFPRVAgECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSL 353
Cdd:PRK11905 758 GVMFTGSTEVARLIQRTLAKRSG--PPVPLIA-ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDV 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 354 WPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKL--NVIAGGHCNdkKGYFVEPTIIESTD 431
Cdd:PRK11905 835 ADRVLTMLKGAMDELRIGDP-WRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLvhQLPLPAETE--KGTFVAPTLIEIDS 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 432 PQEaiMAEEIFGPVLSVYVYPENDyLEvlHLID--NTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVA 509
Cdd:PRK11905 912 ISD--LEREVFGPVLHVVRFKADE-LD--RVIDdiNATGYGLTFGLHSRIDETIAHVTSRIR--AGNIYVNRNIIGAVVG 984
|
490 500
....*....|....*....|....*...
gi 1367454336 510 QQPFGGARASGTNDKPGGPHYVLRWTSP 537
Cdd:PRK11905 985 VQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
76-540 |
5.98e-61 |
|
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: 207.83 E-value: 5.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 76 SPFnHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQA--E 152
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 153 IDAAaelIDFFRFNAKHAVELESQQ-PLD-SDGSTNTMLY--RGLEGFIAAVAPFNFTAiggNLAG---TPALM-GNVVL 224
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFDaSPGGEGRIGFtiREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 225 WKPSD-TAMSAsYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyknFPR 303
Cdd:cd07149 156 LKPASqTPLSA-LKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 304 VAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSA 383
Cdd:cd07149 227 VTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 384 VIDDKSFARIKKWLDHAKSSPKlNVIAGGHCNdkkGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLI 463
Cdd:cd07149 306 MISEAEAERIEEWVEEAVEGGA-RLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLD--EAIAMA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 464 dNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSiVAQQPFGGARASGTNDKpgGPHYVLR-WTSPQVV 540
Cdd:cd07149 380 -NDSPYGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGTGRE--GPRYAIEeMTEIKLV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
75-536 |
2.57e-60 |
|
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: 206.81 E-value: 2.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNHSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQAEI 153
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 154 DAAaELIDFFRFNAK-----HAVELESQQPlDSDgstnTMLYRGLEGFIAAVAPFNF-TAIGGNLAGtPALM-GNVVLWK 226
Cdd:cd07131 97 DVQ-EAIDMAQYAAGegrrlFGETVPSELP-NKD----AMTRRQPIGVVALITPWNFpVAIPSWKIF-PALVcGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 227 PSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAG 306
Cdd:cd07131 170 PAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------RPNKRVAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 307 ECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVID 386
Cdd:cd07131 244 EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE-ETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 387 DKSFARIKKWLDHAKSSpKLNVIAGGHCNDK----KGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYvypENDYLEVLHL 462
Cdd:cd07131 323 EAQLEKVLNYNEIGKEE-GATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALI---EVSSLEEAIE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 463 IDNTSPYALTGAVFALDknvVNEAAKALRNA-AGNYYVNDKSTGSIVaQQPFGGARASGTNDKPGGP---HYVLRWTS 536
Cdd:cd07131 399 IANDTEYGLSSAIYTED---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTtalDAFTEWKA 472
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
75-540 |
4.91e-60 |
|
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: 205.96 E-value: 4.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNHShKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQA-- 151
Cdd:cd07088 18 LNPATGE-VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLiVEEQGKTLSLArv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 152 EIDAAAeliDFFRFNAKHAVELESQ-QPLDSDGStNTMLYRGLEGFIAAVAPFNFTA--IGGNLAgtPALM-GNVVLWKP 227
Cdd:cd07088 95 EVEFTA---DYIDYMAEWARRIEGEiIPSDRPNE-NIFIFKVPIGVVAGILPWNFPFflIARKLA--PALVtGNTIVIKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 228 SDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknfPRVAGE 307
Cdd:cd07088 169 SEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 308 CGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDD 387
Cdd:cd07088 243 LGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 388 KSFARIKKWLDHAKSSPKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLIdNTS 467
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELA-NDS 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 468 PYALTGAVFALDKNVVNEAAKALRnaAGNYYVNdksTGSIVAQQPF-GGARASGTNDKpGGPHYVLRWTSPQVV 540
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELE--FGETYIN---RENFEAMQGFhAGWKKSGLGGA-DGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
90-540 |
1.73e-59 |
|
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: 203.91 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIIS--GPKRAEILAKTmigQGKTVVQA--EIDAAAeliDFFRF 165
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEanAEELARLLTLE---QGKPLAEAqfEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQplDSDGSTNTMLYRGLeGFIAAVAPFNFTAIggnLAG---TPALM-GNVVLWKPSdtamsaSYAVYNV 241
Cdd:cd07106 90 TASLDLPDEVIE--DDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPS------PFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 242 LR-----DSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyKnfpRVAGECGGKNFHFV 316
Cdd:cd07106 158 LKlgelaQEVLPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTL---K---RVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 317 HKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKW 396
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 397 LDHAKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVF 476
Cdd:cd07106 310 VEDAKAK-GAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDED--EVIARA-NDSEYGLGASVW 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 477 ALDknvVNEAAK-ALRNAAGNYYVNdkSTGSIVAQQPFGGARASGTndkpG---GPHYVLRWTSPQVV 540
Cdd:cd07106 386 SSD---LERAEAvARRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGLKEYTQTQVI 444
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-538 |
2.77e-58 |
|
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: 202.06 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 21 AAVEVKNEpilgfNEGSPERAELQKALDdlkgKTEEIPCVVGDEHVWTKDIRYQLSPFNHSHKLAKFCYADKELLNKAIL 100
Cdd:TIGR01238 11 LGIDLDNE-----SELKPLEAQIHAWAD----KTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 101 ASVAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAeIDAAAELIDFFRFNAKHAVELESQQPLD 180
Cdd:TIGR01238 82 SAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEFSVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 181 SDGStntmlyrglegfIAAVAPFNFT-AIGGNLAGTPALMGNVVLWKPSD-TAMSASYAVyNVLRDSGLPPNIIQFVPAD 258
Cdd:TIGR01238 160 SRGV------------FVCISPWNFPlAIFTGQISAALAAGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQLLPGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 259 GPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyKNFPRVAgECGGKNFHFVHKSADVQSVVTGTIRSAFEYGG 338
Cdd:TIGR01238 227 GADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 339 QKCSA----CSRMYVPDSLWPQIkQGLLDihkQLKVGDPVEdWSTFFSAVIDDKSFARIKKWLDHAKSSPK--LNVIAGG 412
Cdd:TIGR01238 304 QRCSAlrvlCVQEDVADRVLTMI-QGAMQ---ELKVGVPHL-LTTDVGPVIDAEAKQNLLAHIEHMSQTQKkiAQLTLDD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 413 HCNDKKGYFVEPTIIESTDPQEaiMAEEIFGPVLSVYVYPENDYLEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRn 492
Cdd:TIGR01238 379 SRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKARELDQIVDQI-NQTGYGLTMGVHSRIETTYRWIEKHAR- 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1367454336 493 aAGNYYVNDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQ 538
Cdd:TIGR01238 455 -VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
76-520 |
3.16e-58 |
|
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: 200.74 E-value: 3.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 76 SPFNHSHkLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--E 152
Cdd:cd07094 5 NPYDGEV-IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIaCEGGKPIKDArvE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 153 IDAAaelIDFFRFNAKHAVELESQQ-PLD-SDGSTNTMLYRGLE--GFIAAVAPFNFTAiggNLAG---TPAL-MGNVVL 224
Cdd:cd07094 82 VDRA---IDTLRLAAEEAERIRGEEiPLDaTQGSDNRLAWTIREpvGVVLAITPFNFPL---NLVAhklAPAIaTGCPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 225 WKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyknFPRV 304
Cdd:cd07094 156 LKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GKRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 305 AGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAV 384
Cdd:cd07094 228 ALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDE-DTDVGPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 385 IDDKSFARIKKWLDHA-KSSPKLnvIAGGHcndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLI 463
Cdd:cd07094 307 ISEEAAERVERWVEEAvEAGARL--LCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRY--DDFEEAIRIA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367454336 464 DNTsPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDkSTGSIVAQQPFGGARASG 520
Cdd:cd07094 380 NST-DYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
90-536 |
3.82e-58 |
|
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: 200.63 E-value: 3.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQA--EIDAAAELIdffRFN 166
Cdd:cd07150 18 GSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEgGSTYGKAwfETTFTPELL---RAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 167 AK--HAVELESQQPlDSDGsTNTMLYRGLEGFIAAVAPFNF-TAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYNVLR 243
Cdd:cd07150 93 AGecRRVRGETLPS-DSPG-TVSMSVRRPLGVVAGITPFNYpLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 244 DSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFVHKSADVQ 323
Cdd:cd07150 171 EAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSS 403
Cdd:cd07150 245 YAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDP-RDPDTVIGPLISPRQVERIKRQVEDAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 PKlNVIAGGHCNdkkGYFVEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHLiDNTSPYALTGAVFALDknvV 483
Cdd:cd07150 324 GA-KLLTGGKYD---GNFYQPTVLTDVTPDMRIFREETFGPVTS--VIPAKDAEEALEL-ANDTEYGLSAAILTND---L 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1367454336 484 NEAAK-ALRNAAGNYYVNDkSTGSIVAQQPFGGARASGTNdKPGGPHYV-----LRWTS 536
Cdd:cd07150 394 QRAFKlAERLESGMVHIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
77-520 |
1.26e-57 |
|
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: 199.20 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 77 PFNHSHkLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EI 153
Cdd:cd07103 4 PATGEV-IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLtLEQGKPLAEArgEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 154 DAAAeliDFFRFNAKHAVELESQQ-PLDSDGSTNTMLYRGLeGFIAAVAPFNFTA------IGGNLAGtpalmGNVVLWK 226
Cdd:cd07103 81 DYAA---SFLEWFAEEARRIYGRTiPSPAPGKRILVIKQPV-GVVAAITPWNFPAamitrkIAPALAA-----GCTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 227 PS-DTAMSAsYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyKnfpRVA 305
Cdd:cd07103 152 PAeETPLSA-LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV---K---RVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 306 GECGGkNFHF-VHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAV 384
Cdd:cd07103 225 LELGG-NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDE-GTDMGPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 385 IDDKSFARIKKWLDHAKSspK-LNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLI 463
Cdd:cd07103 303 INERAVEKVEALVEDAVA--KgAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTED--EVIARA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 464 dNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNdksTGSI-VAQQPFGGARASG 520
Cdd:cd07103 379 -NDTPYGLAAYVFTRDLARAWRVAEALE--AGMVGIN---TGLIsDAEAPFGGVKESG 430
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
84-520 |
2.83e-56 |
|
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: 196.25 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-------IGQGKTVVQAEIDAA 156
Cdd:cd07086 26 IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGRLVslemgkiLPEGLGEVQEMIDIC 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 157 aeliDFF-----RFNAK--------HAVeLESQQPLdsdgstntmlyrgleGFIAAVAPFNF-TAIGG-NLAgtPALM-G 220
Cdd:cd07086 104 ----DYAvglsrMLYGLtipserpgHRL-MEQWNPL---------------GVVGVITAFNFpVAVPGwNAA--IALVcG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 221 NVVLWKPSDTAMSASYAVY----NVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTfkrlWKQVAQNld 296
Cdd:cd07086 162 NTVVWKPSETTPLTAIAVTkilaEVLEKNGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEV----GRRVGET-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 297 VYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVED 376
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 377 wSTFFSAVIDDKSFARIKKWLDHAKSSpKLNVIAGGHC--NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLsvYVYPEN 454
Cdd:cd07086 315 -GTLVGPLINQAAVEKYLNAIEIAKSQ-GGTVLTGGKRidGGEPGNYVEPTIVTGVTDDARIVQEETFAPIL--YVIKFD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1367454336 455 DYLEVLHlIDNTSPYALTGAVFALDknvVNEAAKALRNA---AGNYYVNdksTGSIVA--QQPFGGARASG 520
Cdd:cd07086 391 SLEEAIA-INNDVPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVN---IPTSGAeiGGAFGGEKETG 454
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
90-521 |
2.90e-56 |
|
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: 195.64 E-value: 2.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EIDAAAELidfFRFN 166
Cdd:cd07145 18 LSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLtIEVGKPIKQSrvEVERTIRL---FKLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 167 AKHAVELESQQ-PLDS-DGSTNTMLYRGLE--GFIAAVAPFNFTA------IGGNLAgtpalMGNVVLWKPSDTAMSASY 236
Cdd:cd07145 93 AEEAKVLRGETiPVDAyEYNERRIAFTVREpiGVVGAITPFNFPAnlfahkIAPAIA-----VGNSVVVKPSSNTPLTAI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 237 AVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFV 316
Cdd:cd07145 168 ELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG------GTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 317 HKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKW 396
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDE-STDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 397 LDHAKSspklnviAGGHC----NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHlIDNTSPYALT 472
Cdd:cd07145 321 VNDAVE-------KGGKIlyggKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLP--IAKVKDDEEAVE-IANSTEYGLQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 473 GAVFALDKNvvneaaKALRNA----AGNYYVNDKST---GSIvaqqPFGGARASGT 521
Cdd:cd07145 391 ASVFTNDIN------RALKVAreleAGGVVINDSTRfrwDNL----PFGGFKKSGI 436
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
95-520 |
7.11e-56 |
|
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: 193.90 E-value: 7.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 95 LNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQA--EIDAAAELIdffrfnaKHAV 171
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAafEVGAAIAIL-------REAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 172 ELESQ-----QPLDSDGSTNtMLYRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPS-DTAMSASYAVYNVLRD 244
Cdd:cd07104 73 GLPRRpegeiLPSDVPGKES-MVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFVHKSADVQS 324
Cdd:cd07104 152 AGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSp 404
Cdd:cd07104 226 AVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERQVDRVHAIVEDAVAA- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KLNVIAGGHCNdkkGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLIdNTSPYALTGAVFALDknvVN 484
Cdd:cd07104 304 GARLLTGGTYE---GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPF--DDDEEAVELA-NDTEYGLSAAVFTRD---LE 374
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367454336 485 EAAK-ALRNAAGNYYVNDkSTGSIVAQQPFGGARASG 520
Cdd:cd07104 375 RAMAfAERLETGMVHIND-QTVNDEPHVPFGGVKASG 410
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
76-520 |
3.05e-54 |
|
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: 190.15 E-value: 3.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 76 SPFNHShKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQAEID 154
Cdd:cd07147 5 NPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 155 AAaELIDFFRFNAKHAVELE-SQQPLDSdgSTNTMLYRGL-----EGFIAAVAPFNFTAiggNLAG---TPAL-MGNVVL 224
Cdd:cd07147 82 VA-RAIDTFRIAAEEATRIYgEVLPLDI--SARGEGRQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 225 WKPSD-TAMSAsYAVYNVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvyknfpR 303
Cdd:cd07147 156 LKPASrTPLSA-LILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 304 VAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSA 383
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD-ATDVGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 384 VIDDKSFARIKKWLDHAKSSPKlNVIAGGHCndkKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLI 463
Cdd:cd07147 305 MISESEAERVEGWVNEAVDAGA-KLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPY--DDFDEALAAV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 464 dNTSPYALTGAVFALDknvVNEAAKALRN-AAGNYYVNDKSTGSiVAQQPFGGARASG 520
Cdd:cd07147 379 -NDSKFGLQAGVFTRD---LEKALRAWDElEVGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
68-520 |
6.77e-54 |
|
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: 189.83 E-value: 6.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 68 TKDIryqLSPFNHShKLAKFCYADKEllnKAILASVAARR-----EWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMI 142
Cdd:cd07119 14 TRDI---INPANGE-VIATVPEGTAE---DAKRAIAAARRafdsgEWPHLPAQERAALLFRIADKIR-EDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 143 GQGKTVVQAEIDAAaELIDFFRFNAKHAVElESQQPLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GN 221
Cdd:cd07119 86 NTGKTLRESEIDID-DVANCFRYYAGLATK-ETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 222 VVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNF 301
Cdd:cd07119 164 TVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA------GNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 302 PRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFF 381
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGL-DADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 382 SAVIDDKSFARIKKWLDHAKSS-PKL----NVIAGGHCndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDy 456
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEgARLvcggKRPTGDEL--AKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 457 lEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDksTGSIVAQQPFGGARASG 520
Cdd:cd07119 394 -EAIRLA-NDTPYGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
84-520 |
3.52e-53 |
|
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: 187.13 E-value: 3.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQA--EIDAAAELID 161
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIEEArvDIDSSADCLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 162 FFrfnAKHAVELESQQ-PLDSDGSTNTMlyRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSAsYAV 238
Cdd:cd07090 89 YY---AGLAPTLSGEHvPLPGGSFAYTR--REPLGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPfTPLTA-LLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 239 YNVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHK 318
Cdd:cd07090 163 AEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK------HVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 319 SADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIKKWLD 398
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 399 HAKSSpKLNVIAGG-----HCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTsPYALTG 473
Cdd:cd07090 315 SAKQE-GAKVLCGGervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEE--EVIRRANDT-TYGLAA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSivAQQPFGGARASG 520
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQ--AGTCWINTYNISP--VEVPFGGYKQSG 433
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
85-520 |
5.91e-53 |
|
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: 186.60 E-value: 5.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 85 AKFCYADKELLNKAILASVAARR--EW-DLKPIQdRAQVLFKAADIISgpKRAEILAKT-MIGQGKTV--VQAEIDAAAE 158
Cdd:cd07114 11 ARVPEASAADVDRAVAAARAAFEggAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELeTRDNGKLIreTRAQVRYLAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 159 lidFFRFNAKHAVELESQ-QPLDSDGSTNTMLYRGLeGFIAAVAPFN----FTAigGNLAgtPAL-MGNVVLWKPSDTAM 232
Cdd:cd07114 88 ---WYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNspllLLA--KKLA--PALaAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 233 SASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKN 312
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA------ENLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 313 FHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFAR 392
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDP-LDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 393 IKKWLDHAKSSPKlNVIAGG----HCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHlIDNTSP 468
Cdd:cd07114 313 VERYVARAREEGA-RVLTGGerpsGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE--EAIA-LANDSE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 469 YALTGAVFALDknvvneAAKALRNA----AGNYYVNDKSTGSIVAqqPFGGARASG 520
Cdd:cd07114 389 YGLAAGIWTRD------LARAHRVAraieAGTVWVNTYRALSPSS--PFGGFKDSG 436
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
80-520 |
1.20e-52 |
|
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: 186.03 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 80 HSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTV-VQAEIDAAA 157
Cdd:cd07108 6 TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALE--ARSEELARLLaLETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 158 eLIDFFRFNAKHAVELESQQ-PLDSDgstnTMLYRGLE--GFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSDTAMS 233
Cdd:cd07108 84 -LADLFRYFGGLAGELKGETlPFGPD----VLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 234 ASYAVYNVLRDSgLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknFPrVAGECGGKNF 313
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL-----IP-VSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 314 HFVHKSADVQSVVTGTIRSA-FEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFAR 392
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPL-DEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 393 IKKWLDHAKSSPKLNVIAGG----HCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHLIdNTSP 468
Cdd:cd07108 311 VCGYIDLGLSTSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLC--AIPWKDEDEVIAMA-NDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367454336 469 YALTGAVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07108 388 YGLAAYVWTRDLGRALRAAHALE--AGWVQVN--QGGGQQPGQSYGGFKQSG 435
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
84-540 |
3.40e-52 |
|
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: 185.34 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAA-RREWDLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQAEIDAAAELIDF 162
Cdd:cd07113 28 IASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQSANF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 163 FRFNAKHAVELESQQPLDSDGSTNTMLYRGLE-----GFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASY 236
Cdd:cd07113 107 LRYFAGWATKINGETLAPSIPSMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPLTLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 237 AVYNVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFV 316
Cdd:cd07113 187 RVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT------RVTLELGGKNAAAF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 317 HKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKW 396
Cdd:cd07113 260 LKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE-SVMFGPLANQPHFDKVCSY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 397 LDHAKSSPKlNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVF 476
Cdd:cd07113 339 LDDARAEGD-EIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE--ELIQLI-NDTPFGLTASVW 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 477 AldknvvNEAAKALRNA----AGNYYVNDKSTgsIVAQQPFGGARASGTNdKPGGPHYVLRWTSPQVV 540
Cdd:cd07113 415 T------NNLSKALRYIprieAGTVWVNMHTF--LDPAVPFGGMKQSGIG-REFGSAFIDDYTELKSV 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
84-520 |
3.99e-52 |
|
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: 184.56 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQAEIDAAAELIDFF 163
Cdd:cd07115 10 IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAADTF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 164 RFNAKHAVELESQQ-PLDSDGSTNTMlyRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSDTAMSASYAVYNV 241
Cdd:cd07115 89 RYYAGWADKIEGEViPVRGPFLNYTV--REPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRIAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 242 LRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSAD 321
Cdd:cd07115 167 MAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 322 VQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIKKWLDHAK 401
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 402 SSPKlNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHlIDNTSPYALTGAVFALDKN 481
Cdd:cd07115 320 EEGA-RLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALR-IANGTEYGLAAGVWTRDLG 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 1367454336 482 VVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07115 396 RAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
90-521 |
7.44e-52 |
|
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: 183.54 E-value: 7.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQA---EIDAAAElidFFRF 165
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIE--ARADELALLeSLDTGKPITLArtrDIPRAAA---NFRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNF--------TAiggnlagtPAL-MGNVVLWKPSD-TAMSAS 235
Cdd:cd07093 91 FADYILQLDGES-YPQDGGALNYVLRQPVGVAGLITPWNLplmlltwkIA--------PALaFGNTVVLKPSEwTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 236 YAVyNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHF 315
Cdd:cd07093 162 LLA-ELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA------PNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 316 VHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKK 395
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 396 WLDHAKSSPKlNVIAGGHC----NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHLIdNTSPYAL 471
Cdd:cd07093 314 YVELARAEGA-TILTGGGRpelpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVT--VIPFDDEEEAIELA-NDTPYGL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367454336 472 TGAVFALDKNVVNEAAKALRnaAGNYYVN-----DKSTgsivaqqPFGGARASGT 521
Cdd:cd07093 390 AAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
98-521 |
7.83e-52 |
|
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: 183.73 E-value: 7.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 98 AILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQ--AEIDAAAELIDFFrfnAKHAVELE 174
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIdALDCGNPVSAmlGDVMVAAALLDYF---AGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 175 SQQPLDSDGSTNTMLYRGLeGFIAAVAPFN----FTAigGNLAgTPALMGNVVLWKPSDTAMSASYAVYNVLRDSgLPPN 250
Cdd:cd07107 99 GETIPVGGRNLHYTLREPY-GVVARIVAFNhplmFAA--AKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 251 IIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQSVVTGTI 330
Cdd:cd07107 174 VFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALIVFPDADPEAAADAAV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 331 RSA-FEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKLNVI 409
Cdd:cd07107 248 AGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQQYDRVMHYIDSAKREGARLVT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 410 AGGHCNDK---KGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFAldknvvNEA 486
Cdd:cd07107 327 GGGRPEGPaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEA--EMVAQA-NGVEYGLTAAIWT------NDI 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1367454336 487 AKALRNA----AGNYYVNDKSTGSIVAqqPFGGARASGT 521
Cdd:cd07107 398 SQAHRTArrveAGYVWINGSSRHFLGA--PFGGVKNSGI 434
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
90-520 |
1.26e-51 |
|
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: 183.21 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAIlasVAARR---EWDLK-PIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQAEIDAAAELIDFFR 164
Cdd:cd07089 16 AGAADVDAAI---AAARRafdTGDWStDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 165 FNAKHAVELESQQPLDsDGSTNTMLYRGL---E--GFIAAVAPFNFtAIGGNLAGT-PAL-MGNVVLWKPS-DTAMSAsY 236
Cdd:cd07089 91 YFADLADSFPWEFDLP-VPALRGGPGRRVvrrEpvGVVAAITPWNF-PFFLNLAKLaPALaAGNTVVLKPApDTPLSA-L 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 237 AVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFV 316
Cdd:cd07089 168 LLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK------RVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 317 HKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIKKW 396
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 397 LDHAKSSPKLNVIAGGH--CNDkKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylevlHLID--NTSPYALT 472
Cdd:cd07089 321 IARGRDEGARLVTGGGRpaGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDD-----EAVRiaNDSDYGLS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367454336 473 GAVFALDknvvneAAKALRNA----AGNYYVNDKSTGSIVAqqPFGGARASG 520
Cdd:cd07089 395 GGVWSAD------VDRAYRVArrirTGSVGINGGGGYGPDA--PFGGYKQSG 438
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
83-520 |
3.38e-51 |
|
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: 182.41 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 83 KLAKFCYADKELLNKAILASVAARREWDLKPI--QDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQ-AEIDAAaEL 159
Cdd:cd07091 31 VICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIER-DRDELAALESLDNGKPLEEsAKGDVA-LS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 160 IDFFRFNAKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNF----TA--IGgnlagtPAL-MGNVVLWKPSD-TA 231
Cdd:cd07091 109 IKCLRYYAGWADKIQGKT-IPIDGNFLAYTRREPIGVCGQIIPWNFpllmLAwkLA------PALaAGNTVVLKPAEqTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 232 MSASYaVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGK 311
Cdd:cd07091 182 LSALY-LAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKS-----NLKKVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 312 NFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFA 391
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP-FDPDTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 392 RIKKWLDHAKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTSpYAL 471
Cdd:cd07091 335 KILSYIESGKKE-GATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED--EVIERANDTE-YGL 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1367454336 472 TGAVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07091 411 AAGVFTKDINKALRVSRALK--AGTVWVN--TYNVFDAAVPFGGFKQSG 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
101-520 |
4.29e-51 |
|
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: 181.65 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 101 ASVAARRE------WDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQAEIDAAAELIDFFRFNA------ 167
Cdd:cd07112 28 RAVAAARRafesgvWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSAANTFRWYAeaidkv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 168 --------KHAVELESQQPLdsdgstntmlyrgleGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPS-DTAMSAsya 237
Cdd:cd07112 106 ygevaptgPDALALITREPL---------------GVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAeQSPLTA--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 238 vynvLR------DSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGK 311
Cdd:cd07112 168 ----LRlaelalEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQS-----NLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 312 NFHFV-HKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSF 390
Cdd:cd07112 239 SPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 391 ARIKKWLDHAKSSpKLNVIAGG--HCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSP 468
Cdd:cd07112 318 DKVLGYIESGKAE-GARLVAGGkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE--EAVALA-NDSV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1367454336 469 YALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIvaQQPFGGARASG 520
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
75-520 |
6.89e-51 |
|
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: 181.00 E-value: 6.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPfNHSHKLAKFCYADKELLNKAIlasVAARRE-----WDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTV 148
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAV---AAARKAfdkgpWPRMSGAERAAVLLKVADLIR--ARRERLALIeTLESGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 149 VQA--EIDAAAELidfFRFNAKHAVEL--ESQQPLDSDgsTNTMLYRGLEGFIAAVAPFNFtaiggnlagtPALM----- 219
Cdd:cd07118 76 SQArgEIEGAADL---WRYAASLARTLhgDSYNNLGDD--MLGLVLREPIGVVGIITPWNF----------PFLIlsqkl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 220 ------GNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQ 293
Cdd:cd07118 141 pfalaaGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 294 NLDvyknfpRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDP 373
Cdd:cd07118 221 NLK------KVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 374 VEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPE 453
Cdd:cd07118 295 LDP-ETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDT 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367454336 454 NDylEVLHLIDNTsPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSivAQQPFGGARASG 520
Cdd:cd07118 374 VD--EAIALANDT-VYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGS--PELPFGGFKQSG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
76-540 |
4.43e-50 |
|
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: 178.66 E-value: 4.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 76 SPFNhSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQA--EI 153
Cdd:cd07101 2 APFT-GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 154 DAAAELIDFFRFNAKHAVELESQQPLDSDGSTNTMLYRGLeGFIAAVAPFNF---TAIGGNLagtPALM-GNVVLWKP-S 228
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPK-GVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 229 DTAMSASYAVyNVLRDSGLPPNIIQFVPADGPVFGDTITssEHLAGINFTGSVPTFKRLWKQVAQNLDVYknfprvAGEC 308
Cdd:cd07101 156 QTALTALWAV-ELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 309 GGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGdPVEDWSTFFSAVIDDK 388
Cdd:cd07101 227 GGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLG-AALDYGPDMGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 389 SFARIKKWLDHAKSSPKlNVIAGGHCNDKKG-YFVEPTIIESTDPQEAIMAEEIFGPVlsVYVYPENDYLEVLHLIdNTS 467
Cdd:cd07101 306 QLDRVTAHVDDAVAKGA-TVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPV--VSIYRVADDDEAIELA-NDT 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 468 PYALTGAVFALDKNVVNEAAKALRnaAGNYYVND---KSTGSIVAqqPFGGARASGTNDKpGGPHYVLRWTSPQVV 540
Cdd:cd07101 382 DYGLNASVWTRDGARGRRIAARLR--AGTVNVNEgyaAAWASIDA--PMGGMKDSGLGRR-HGAEGLLKYTETQTV 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
75-520 |
8.64e-49 |
|
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: 175.57 E-value: 8.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNHShKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAEID 154
Cdd:cd07151 15 LNPYTGE-TLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGSTRIKANIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 155 AAAElIDFFRFNAKHAVELESQ-QPLDSDGSTNtMLYRGLEGFIAAVAPFNFTAiggNLAG---TPAL-MGNVVLWKP-S 228
Cdd:cd07151 93 WGAA-MAITREAATFPLRMEGRiLPSDVPGKEN-RVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNAVVLKPaS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 229 DTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGEC 308
Cdd:cd07151 168 DTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG------RHLKKVALEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 309 GGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDK 388
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 389 SFARIKKWLDHAKSSPKLNVIAGGHcndkKGYFVEPTIIESTDPQEAIMAEEIFGPVlsVYVYPENDYLEVLHLIdNTSP 468
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEA----EGNVLEPTVLSDVTNDMEIAREEIFGPV--APIIKADDEEEALELA-NDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 469 YALTGAVFALDknvVNEAAK-ALRNAAGNYYVNDKStgsiVAQQP---FGGARASG 520
Cdd:cd07151 394 YGLSGAVFTSD---LERGVQfARRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
90-520 |
1.46e-48 |
|
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: 175.00 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM---IGQGKTV---VQAE-----IDAAAE 158
Cdd:cd07138 33 GTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAItleMGAPITLaraAQVGlgighLRAAAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 159 LIDFFRFnakhavelESQQPldsdgstNTMLYRGLEGFIAAVAPFNFTA--IGGNLAgtPALM-GNVVLWKPSDTAMSAS 235
Cdd:cd07138 111 ALKDFEF--------EERRG-------NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 236 YAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyKnfpRVAGECGGKNFHF 315
Cdd:cd07138 174 IILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV---K---RVALELGGKSANI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 316 VHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFAR--- 392
Cdd:cd07138 248 ILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP-RDPATTLGPLASAAQFDRvqg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 393 -IKKWLDH-AKsspklnVIAGG-----HCNdkKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVY-PENDYLEvlhlID 464
Cdd:cd07138 327 yIQKGIEEgAR------LVAGGpgrpeGLE--RGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYdDEDEAIA----IA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 465 NTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDkstGSIVAQQPFGGARASG 520
Cdd:cd07138 395 NDTPYGLAGYVWSADPERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
89-500 |
8.37e-48 |
|
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: 172.43 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 89 YADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGPKR--AEILAKTMigqGKTVVQA--EIDAAAELIDFFR 164
Cdd:cd07102 14 LASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDeiAEELTWQM---GRPIAQAggEIRGMLERARYMI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 165 FNAKHAveLESQQPLDSDGSTNTMLYRGLeGFIAAVAPFN---FTAIGgnlAGTPALM-GNVVLWKPSDTAMSASYAVYN 240
Cdd:cd07102 91 SIAEEA--LADIRVPEKDGFERYIRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVILKHSPQTPLCGERFAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 241 VLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFVHKSA 320
Cdd:cd07102 165 AFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA------GRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 321 DVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHA 400
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 401 KSSPKLNVIAGGHCNDKK--GYFVEPTIIESTDPQEAIMAEEIFGPVLSVY-VypENDYlEVLHLIdNTSPYALTGAVFA 477
Cdd:cd07102 317 IAKGARALIDGALFPEDKagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMkV--KSDA-EAIALM-NDSEYGLTASVWT 392
|
410 420
....*....|....*....|...
gi 1367454336 478 LDKNVVNEAAKALrnAAGNYYVN 500
Cdd:cd07102 393 KDIARAEALGEQL--ETGTVFMN 413
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
98-533 |
1.36e-47 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 178.63 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 98 AILASVAARREWDLKPIQDRAQVLFKAADIIsgpkraEILAKTMIG-----QGKTVVQAeIDAAAELIDFFRFNAkhave 172
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLM------EAQMQTLMGllvreAGKTFSNA-IAEVREAVDFLRYYA----- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 173 leSQQPLDSDGSTntmlYRGLeGFIAAVAPFNFT-AI-GGNLAGTPAlMGNVVLWKPSD-TAMSASYAVyNVLRDSGLPP 249
Cdd:PRK11809 755 --GQVRDDFDNDT----HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 250 NIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVY-KNFPRVAgECGGKNFHFVHKSADVQSVVTG 328
Cdd:PRK11809 826 GVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQgRPIPLIA-ETGGQNAMIVDSSALTEQVVAD 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 329 TIRSAFEYGGQKCSA----CSRMYVPDSLWPQIKQGLldihKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLD--HAKS 402
Cdd:PRK11809 905 VLASAFDSAGQRCSAlrvlCLQDDVADRTLKMLRGAM----AECRMGNP-DRLSTDIGPVIDAEAKANIERHIQamRAKG 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 403 SPKLNVIAGGHCNDKKGYFVEPTIIESTDPQEaiMAEEIFGPVLSVYVYPENDYLEVLHLIdNTSPYALTGAVFA-LDKN 481
Cdd:PRK11809 980 RPVFQAARENSEDWQSGTFVPPTLIELDSFDE--LKREVFGPVLHVVRYNRNQLDELIEQI-NASGYGLTLGVHTrIDET 1056
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 482 V--VNEAAKAlrnaaGNYYVNDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLR 533
Cdd:PRK11809 1057 IaqVTGSAHV-----GNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
90-547 |
1.71e-47 |
|
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: 172.33 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAA-RREWDLK-PIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQAEIDAAAELIDFFRFN 166
Cdd:cd07143 41 ATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTAKRVDVQASADTFRYY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 167 AKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSASYAVyNVLRD 244
Cdd:cd07143 119 GGWADKIHGQV-IETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSElTPLSALYMT-KLIPE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGKNFHFVHKSADVQS 324
Cdd:cd07143 197 AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGGKSPNIVFDDADLES 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSP 404
Cdd:cd07143 272 AVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAE-DTFQGPQVSQIQYERIMSYIESGKAEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KlNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHlIDNTSPYALTGAVFALDKNVVN 484
Cdd:cd07143 351 A-TVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVA--VIKFKTEEEAIK-RANDSTYGLAAAVFTNNINNAI 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1367454336 485 EAAKALRnaAGNYYVNDKSTgsIVAQQPFGGARASGTNDKPGgpHYVLrwTSPQVVKATHVPL 547
Cdd:cd07143 427 RVANALK--AGTVWVNCYNL--LHHQVPFGGYKQSGIGRELG--EYAL--ENYTQIKAVHINL 481
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
98-527 |
2.61e-47 |
|
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: 170.92 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 98 AILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTmIGQ--GK--TVVQAEIDAAAELIDFfRFNAKHavEL 173
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARL-ISRetGKplWEAQTEVAAMAGKIDI-SIKAYH--ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 174 ESQQPLDSDGSTNTMLYRGLeGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSASYAVyNVLRDSGLPPNI 251
Cdd:cd07095 79 TGERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSElTPAVAELMV-ELWEEAGLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 252 IQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYknfprVAGECGGKNFHFVHKSADVQSVVTGTIR 331
Cdd:cd07095 157 LNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 332 SAFEYGGQKCSACSRMYVPDSLWPQ-IKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKK--WLDHAKSS-PKLN 407
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAAAAARYLLaqQDLLALGGePLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 408 VIAGghcnDKKGYFVEPTIIESTDPQEaIMAEEIFGPVLSVYVYpeNDYLEVLHLIDNTsPYALTGAVFALDKNVVNEAA 487
Cdd:cd07095 310 MERL----VAGTAFLSPGIIDVTDAAD-VPDEEIFGPLLQVYRY--DDFDEAIALANAT-RFGLSAGLLSDDEALFERFL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1367454336 488 KALRnaAGNYYVNDKSTGSIVAqQPFGGARASGtNDKPGG 527
Cdd:cd07095 382 ARIR--AGIVNWNRPTTGASST-APFGGVGLSG-NHRPSA 417
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
90-521 |
2.73e-46 |
|
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: 168.27 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKT---VVQAEIDAAaelIDFFRF 165
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPlhlVRDDELPGA---VDNFRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQPLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSDTAMSASYAVYNVLRD 244
Cdd:cd07092 91 FAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLLAELAAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 sGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQS 324
Cdd:cd07092 171 -VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGKAPVIVFDDADLDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARIKKWLDHAKSSP 404
Cdd:cd07092 244 AVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDP-DDEDTEMGPLNSAAQRERVAGFVERAPAHA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KlnVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVN 484
Cdd:cd07092 323 R--VLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDED--EAIELA-NDVEYGLASSVWTRDVGRAM 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 1367454336 485 EAAKALRnaAGNYYVNDKstGSIVAQQPFGGARASGT 521
Cdd:cd07092 398 RLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
84-520 |
1.50e-45 |
|
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: 166.64 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAA--RREWDLKPIQdRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQAEIDAAAeLI 160
Cdd:cd07109 10 FARIARGGAADVDRAVQAARRAfeSGWLRLSPAE-RGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA-AA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 161 DFFRFNAKHAVELESQQ-PLdSDGSTNTMLYRGLeGFIAAVAPFNFTA-IGGNLAGtPAL-MGNVVLWKPSDTAMSASYA 237
Cdd:cd07109 86 RYFEYYGGAADKLHGETiPL-GPGYFVYTVREPH-GVTGHIIPWNYPLqITGRSVA-PALaAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 238 VYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFVH 317
Cdd:cd07109 163 LAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA------ENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 318 KSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDWStfFSAVIDDKSFARIKKWL 397
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 398 DHAKSSpKLNVIAGGHC---NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVY-PENDYLEvlhlIDNTSPYALTG 473
Cdd:cd07109 315 ARARAR-GARIVAGGRIaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFdDEAEAIA----LANGTDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVaQQPFGGARASG 520
Cdd:cd07109 390 GVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
62-520 |
2.29e-45 |
|
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: 166.21 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 62 GDEHVWTKDIRYQLSPFNHShKLAKFCYADKELLNKAI-LASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT 140
Cdd:cd07082 8 GEWKESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAeTAYDAGRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 141 M---IGQGKTVVQAEIDAAAELIDFFRFNAKhavELEsQQPLDSDGSTNT-----MLYRGLEGFIAAVAPFNFTAiggNL 212
Cdd:cd07082 85 LmweIGKTLKDALKEVDRTIDYIRDTIEELK---RLD-GDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPL---NL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 213 AGT---PAL-MGNVVLWKP-SDTAMSASYAVyNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRL 287
Cdd:cd07082 158 TVSkliPALiMGNTVVFKPaTQGVLLGIPLA-EAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 288 WKQVAQNldvyknfpRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQ 367
Cdd:cd07082 237 KKQHPMK--------RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 368 LKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSpKLNVIAGGHcnDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLS 447
Cdd:cd07082 309 LKVGMPWDN-GVDITPLIDPKSADFVEGLIDDAVAK-GATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 448 VYVYpeNDYLEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKStgsivaQQ-----PFGGARASG 520
Cdd:cd07082 385 IIRV--NDIEEAIELA-NKSNYGLQASIFTKDINKARKLADALE--VGTVNINSKC------QRgpdhfPFLGRKDSG 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
84-520 |
2.60e-45 |
|
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: 166.43 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAARREWDLK-PIQDRAQVLFKAADIISgpKRAEILA--KTMiGQGKTVVQAEIDAAAELI 160
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLDEII 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 161 DFFRF----------------NAKHAVELesQQPLdsdgstntmlyrgleGFIAAVAPFNFT------AIGGNLAGtpal 218
Cdd:cd07144 113 AVIRYyagwadkiqgktiptsPNKLAYTL--HEPY---------------GVCGQIIPWNYPlamaawKLAPALAA---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 219 mGNVVLWKPSD-TAMSASYaVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdv 297
Cdd:cd07144 172 -GNTVVIKPAEnTPLSLLY-FANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 298 yKNfprVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQ-LKVGDPVED 376
Cdd:cd07144 248 -KA---VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 377 wSTFFSAVIDDKSFARIKKWLDHAKSS-PKLNVIAGGHCN-DKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeN 454
Cdd:cd07144 324 -DTVVGPQVSKTQYDRVLSYIEKGKKEgAKLVYGGEKAPEgLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF--K 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1367454336 455 DYLEVLHLIDNTsPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07144 401 TYEEAIKKANDT-TYGLAAAVFTKDIRRAHRVARELE--AGMVWIN--SSNDSDVGVPFGGFKMSG 461
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-548 |
2.72e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 164.28 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 104 AARREWDLKPIQDRAQVLFKAADIISGpKRAEILaktmigqgkTVVQAEI-----DAAAELIDFF---RFNAKHAVELES 175
Cdd:PRK09407 65 AAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYARRAPKLLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 176 QQ------PLdsdgSTNTMLYRGLEGFIAAVAPFNF---TAIGGNLagtPALM-GNVVLWKP-SDTAMSASYAVyNVLRD 244
Cdd:PRK09407 135 PRrragalPV----LTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-ELLYE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPADGPVFGDTITssEHLAGINFTGSVPTFKRLWKQVAQNLDVYknfprvAGECGGKNFHFVHKSADVQS 324
Cdd:PRK09407 207 AGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDADLDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGdPVEDWSTFFSAVIDDKSFARIKKWLDHAKSSP 404
Cdd:PRK09407 279 AAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYDYSADMGSLISEAQLETVSAHVDDAVAKG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KlNVIAGGHCNDKKG-YFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVV 483
Cdd:PRK09407 358 A-TVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD--EAVERA-NDTPYGLNASVWTGDTARG 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1367454336 484 NEAAKALRnaAGNYYVNDKST---GSIVAqqPFGGARASGTNDKpGGPHYVLRWTSPQVVKATHV-PLR 548
Cdd:PRK09407 434 RAIAARIR--AGTVNVNEGYAaawGSVDA--PMGGMKDSGLGRR-HGAEGLLKYTESQTIATQRVlPLA 497
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
95-520 |
1.14e-43 |
|
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: 160.70 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 95 LNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQA--EIDAAAELIDFFrfnAKHAV 171
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 172 ELESQQPLDSDGSTNTMLYRGLeGFIAAVAPFNFT-------AIggnlagtPALM-GNVVLWKPSDTAMSASYAVYNVLR 243
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfAA-------PNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 244 DSGLPPNIIQFVPADGPVFgDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyKnfpRVAGECGGKNFHFVHKSADVQ 323
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNL---K---KSVLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFF----SAVIDDKSFARIKKWLDH 399
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDE-DTDLgplaRKDLRDELHEQVEEAVAA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 400 -AKsspklnVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVY-VYPENDYLEVLhlidNTSPYALTGAVFA 477
Cdd:cd07100 300 gAT------LLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIkVKDEEEAIALA----NDSPFGLGGSVFT 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367454336 478 LDKNVVNEAAKALRnaAGNYYVND--KSTgsivAQQPFGGARASG 520
Cdd:cd07100 370 TDLERAERVARRLE--AGMVFINGmvKSD----PRLPFGGVKRSG 408
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
89-528 |
1.23e-43 |
|
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: 160.92 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 89 YADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAEIDAAAELIDFFrfnak 168
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE-EHADEIADWIVRESGSIRPKAGFEVGAAIGELH----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 169 HAVELESQ---QPLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPS-DTAMSASYAVYNVLR 243
Cdd:cd07152 83 EAAGLPTQpqgEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 244 DSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQ 323
Cdd:cd07152 163 EAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLK------KVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDWSTfFSAVIDDKSFARIKKWLDHAKSS 403
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVA-LGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 PKlNVIAGGHcndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFAldKNVV 483
Cdd:cd07152 315 GA-RLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDE--EAVALA-NDTEYGLSAGIIS--RDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367454336 484 NEAAKALRNAAGNYYVNDKsTGSIVAQQPFGGARASGTNDKPGGP 528
Cdd:cd07152 386 RAMALADRLRTGMLHINDQ-TVNDEPHNPFGGMGASGNGSRFGGP 429
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
90-520 |
3.00e-43 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 160.46 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GK---TVVQAEIDAAAELIDFFRF 165
Cdd:PRK13473 36 ASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAIVDVFRFFAG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHaveLESQQPLD-SDGSTnTMLYRGLEGFIAAVAPFNFtaiggnlagtPALM-----------GNVVLWKPSDTAMS 233
Cdd:PRK13473 114 AARC---LEGKAAGEyLEGHT-SMIRRDPVGVVASIAPWNY----------PLMMaawklapalaaGNTVVLKPSEITPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 234 ASYAVYNVLRDSgLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNF 313
Cdd:PRK13473 180 TALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK------RTHLELGGKAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 314 HFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFARI 393
Cdd:PRK13473 253 VIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP-DDEDTELGPLISAAHRDRV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 394 KKWLDHAKSSPKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTG 473
Cdd:PRK13473 332 AGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED--QAVRWA-NDSDYGLAS 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNDKstGSIVAQQPFGGARASG 520
Cdd:PRK13473 409 SVWTRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
90-540 |
3.12e-43 |
|
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: 160.08 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIG-QGKTVVQA--EIDAAAELIDFFrfn 166
Cdd:cd07099 15 TDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALA--DHADELAELLHAeTGKPRADAglEVLLALEAIDWA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 167 AKHAVELESQQPLDSD----GSTNTMLYRGLeGFIAAVAPFNF---TAIGGNLagtPALM-GNVVLWKPSD-TAMSASYA 237
Cdd:cd07099 90 ARNAPRVLAPRKVPTGllmpNKKATVEYRPY-GVVGVISPWNYpllTPMGDII---PALAaGNAVVLKPSEvTPLVGELL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 238 VyNVLRDSGLPPNIIQFVPADGPVfgdtitsSEHL--AGIN---FTGSVPTFKRLWKQVAQNLdvyknFPRVAgECGGKN 312
Cdd:cd07099 166 A-EAWAAAGPPQGVLQVVTGDGAT-------GAALidAGVDkvaFTGSVATGRKVMAAAAERL-----IPVVL-ELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 313 FHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIDDKSFAR 392
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGAD-DIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 393 IKKWLDHAKSSPKLnVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALT 472
Cdd:cd07099 311 VRRHVDDAVAKGAK-ALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADED--EAIALA-NDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 473 GAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVAQQPFGGARASGTNDKpGGPHYVLRWTSPQVV 540
Cdd:cd07099 387 ASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAI 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
88-520 |
6.19e-43 |
|
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: 159.43 E-value: 6.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 88 CYAD--KELLNKAILASVAARRE--WDLKPiQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EIDAAAELI 160
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLaLENGKILGEArfEISGAISEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 161 DFF----RFNAKHAVELESqqpldsdGSTNTMLYR--GLEGFIAavaPFNFTAIGGNLAGTPALM-GNVVLWKP-SDTAM 232
Cdd:cd07120 89 RYYaglaRTEAGRMIEPEP-------GSFSLVLREpmGVAGIIV---PWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 233 SASyAVYNVLRD-SGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGK 311
Cdd:cd07120 159 INA-AIIRILAEiPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK------RLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 312 NFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGdPVEDWSTFFSAVIDDKSFA 391
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVG-PGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 392 RIKKWLDHAKSSPKLNVIAGGHCNDK--KGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPY 469
Cdd:cd07120 311 RVDRMVERAIAAGAEVVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALA-NDTDY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1367454336 470 ALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKstGSIVAQQPFGGARASG 520
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIR--AGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
90-520 |
1.63e-42 |
|
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: 158.28 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQAEIDAAaELIDFFRFNAKH 169
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 170 AVELESQQ----PLDSDGSTNTMLYRGLeGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAVYNVLRD 244
Cdd:cd07110 94 AEQLDAKAeravPLPSEDFKARVRREPV-GVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQS 324
Cdd:cd07110 173 AGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIK------PVSLELGGKSPIIVFDDADLEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSp 404
Cdd:cd07110 247 AVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE-GVRLGPLVSQAQYEKVLSFIARGKEE- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KLNVIAGGHCND--KKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNV 482
Cdd:cd07110 325 GARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED--EAIALA-NDSEYGLAAAVISRDAER 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 1367454336 483 VNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07110 402 CDRVAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
83-521 |
7.11e-42 |
|
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: 156.74 E-value: 7.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 83 KLAKFCYADKELLNKAILASVAARR---EWDLKPIQDRAQVLFKAADIISGpKRAEILAKTMIGQGKTVVQAEIDAAAEL 159
Cdd:cd07141 34 KICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIER-DRAYLASLETLDNGKPFSKSYLVDLPGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 160 IDFFRFNAKHAVELESQQ-PLDSDGSTNTMLyrglE--GFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSD-TAMSA 234
Cdd:cd07141 113 IKVLRYYAGWADKIHGKTiPMDGDFFTYTRH----EpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLKPAEqTPLTA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 235 SYaVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTfKRLWKQVAQNldvyKNFPRVAGECGGKNFH 314
Cdd:cd07141 189 LY-LASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAGK----SNLKRVTLELGGKSPN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 315 FVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIK 394
Cdd:cd07141 263 IVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDP-KTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 395 KWLDHAKSS-PKLnvIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTsPYALTG 473
Cdd:cd07141 342 ELIESGKKEgAKL--ECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID--EVIERANNT-TYGLAA 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSivAQQPFGGARASGT 521
Cdd:cd07141 417 AVFTKDIDKAITFSNALR--AGTVWVNCYNVVS--PQAPFGGYKMSGN 460
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
75-520 |
1.03e-40 |
|
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: 153.65 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNhSHKLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQ--- 150
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLELLAVAeTLDNGKPIREtla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 151 AEIDAAaelIDFFRFNAKhAVELESQQPLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD 229
Cdd:cd07559 98 ADIPLA---IDHFRYFAG-VIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKPAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 230 TAmSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknFPrVAGECG 309
Cdd:cd07559 174 QT-PLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-VTLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 310 GK--NFHFvhksADVQS--------VVTGTIRSAFEYGgQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwST 379
Cdd:cd07559 247 GKspNIFF----DDAMDadddfddkAEEGQLGFAFNQG-EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP-ET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 380 FFSAVIDDKSFARIKKWLDHAKSSPKlNVIAGGHCN----DKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeND 455
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGA-EVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF--KD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1367454336 456 YLEVLHlIDNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07559 398 EEEAIA-IANDTEYGLGGGVWTRDINRALRVARGIQ--TGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
101-520 |
3.02e-40 |
|
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: 152.34 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 101 ASVAARRE------WDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQ-GKTVVQAEIDAAAELIDFFRFNAKHAVEL 173
Cdd:cd07139 40 AAVAAARRafdngpWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALARDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 174 ESQQPLDSDGSTNTMLYRGLEGFIAAVAPFN--FTAIGGNLAgtPALM-GNVVLWKPS-DTAMSAsYAVYNVLRDSGLPP 249
Cdd:cd07139 118 PFEERRPGSGGGHVLVRREPVGVVAAIVPWNapLFLAALKIA--PALAaGCTVVLKPSpETPLDA-YLLAEAAEEAGLPP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 250 NIIQFVPADGPVfgdtitsSEHLAG------INFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECGGKNFHFVHKSADVQ 323
Cdd:cd07139 195 GVVNVVPADREV-------GEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERL------ARVTLELGGKSAAIVLDDADLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSS 403
Cdd:cd07139 262 AAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP-ATQIGPLASARQRERVEGYIAKGRAE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 PKLNVIAGGHCND-KKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpenDYLEVLHLIDNTSPYALTGAVFALDknv 482
Cdd:cd07139 341 GARLVTGGGRPAGlDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY---DDEDDAVRIANDSDYGLSGSVWTAD--- 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1367454336 483 vneAAKALRNA----AGNYYVNdksTGSIVAQQPFGGARASG 520
Cdd:cd07139 415 ---VERGLAVArrirTGTVGVN---GFRLDFGAPFGGFKQSG 450
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
96-520 |
3.36e-40 |
|
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: 151.19 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 96 NKAILASVAARREWDLKPIQDRAQVLFKAADIIsgPKRAEILAKTMigqgktvvQAEIDAAAElidFFRFNAKHAVEL-- 173
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLL--ESRRDEFIEAM--------MEETGATAA---WAGFNVDLAAGMlr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 174 ----------ESQQPLDSDGsTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAVYNVL 242
Cdd:cd07105 70 eaaslitqiiGGSIPSDKPG-TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 243 RDSGLPPNIIQFV---PADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKS 319
Cdd:cd07105 149 HEAGLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK------PVLLELGGKAPAIVLED 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 320 ADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEdwstffSAVIDDKSFARIKKWLDH 399
Cdd:cd07105 223 ADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL------GSLVSAAAADRVKELVDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 400 AKSSPKlNVIAGGHCND-KKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYP-ENDYLEVLhlidNTSPYALTGAVFA 477
Cdd:cd07105 297 ALSKGA-KLVVGGLADEsPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKdEEEAVRIA----NDSEYGLSAAVFT 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367454336 478 LDKNVVNEAAKALRnaAGNYYVNdkstGSIV---AQQPFGGARASG 520
Cdd:cd07105 372 RDLARALAVAKRIE--SGAVHIN----GMTVhdePTLPHGGVKSSG 411
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-526 |
4.68e-40 |
|
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: 151.36 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 98 AILASVAARREwDLKPiQDRAQVLFKAADIISgpKRAEILAkTMIGQ--GKTVVQA--EIDAAaelIDFFRFNAKHAVEL 173
Cdd:cd07146 25 EALALAASYRS-TLTR-YQRSAILNKAAALLE--ARREEFA-RLITLesGLCLKDTryEVGRA---ADVLRFAAAEALRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 174 ESQQpLDSDGSTNTMLYRGLE-----GFIAAVAPFNFTAiggNLAGT---PALM-GNVVLWKPSD-TAMSASYAVyNVLR 243
Cdd:cd07146 97 DGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAHkiaPAIAaNNRIVLKPSEkTPLSAIYLA-DLLY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 244 DSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvYKnfpRVAGECGGKNFHFVHKSADVQ 323
Cdd:cd07146 172 EAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG-----YK---RQLLELGGNDPLIVMDDADLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAkss 403
Cdd:cd07146 244 RAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDEEAAIQIENRVEEA--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 pklnVIAGGHC---NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTSpYALTGAVFALDK 480
Cdd:cd07146 320 ----IAQGARVllgNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLD--EAIAISNSTA-YGLSSGVCTNDL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367454336 481 NVVNEAAKALRNAAGNyyVNDkSTGSIVAQQPFGGARASGTNDKPG 526
Cdd:cd07146 393 DTIKRLVERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
97-528 |
1.12e-39 |
|
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: 150.53 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 97 KAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAK-TMIGQGKTVVQA---EIDAAAELIdffRFNAKHAvE 172
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKI---RWTLKHG-E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 173 lESQQPLDSDGSTNtMLYRGLE------GFIAAVAPFNF---TAIGGNLAGTPAlmGNVVLWKPSD-TAMSASY---AVY 239
Cdd:cd07098 96 -KALRPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIAALFA--GNAIVVKVSEqVAWSSGFflsIIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 240 NVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfPRVAgECGGKNFHFVHKS 319
Cdd:cd07098 172 ECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 320 ADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGdPVEDWSTFFSAVIDDKSFARIKKWL-D 398
Cdd:cd07098 245 ADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQG-PPLDGDVDVGAMISPARFDRLEELVaD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 399 HAKSSPKLnvIAGG----HCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYP-ENDYLEVLhlidNTSPYALTG 473
Cdd:cd07098 324 AVEKGARL--LAGGkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASdDEEAVEIA----NSTEYGLGA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVAQQPFGGARASGTnDKPGGP 528
Cdd:cd07098 398 SVFGKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
96-529 |
1.73e-39 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 150.61 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 96 NKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EIDAAAELIDFFRFNAKHAVE 172
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMtLEQGKPLKEAigEVAYGASFLEYFAEEAKRVYG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 173 LESQQPldsDGSTNTMLYRGLEGFIAAVAPFNFT-AIGGNLAGtPALM-GNVVLWKPSD-TAMSAsYAVYNVLRDSGLPP 249
Cdd:PLN02278 143 DIIPSP---FPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVG-PALAaGCTVVVKPSElTPLTA-LAAAELALQAGIPP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 250 NIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQSVVTGT 329
Cdd:PLN02278 218 GVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK------RVSLELGGNAPFIVFDDADLDVAVKGA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 330 IRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDWSTfFSAVIDDKSFARIKKWLDHAKSSPKlNVI 409
Cdd:PLN02278 292 LASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVT-QGPLINEAAVQKVESHVQDAVSKGA-KVL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 410 AGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHlIDNTSPYALTGAVFALDKNVVNEAAKA 489
Cdd:PLN02278 370 LGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE--EAIA-IANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1367454336 490 LRNaaGNYYVNDKSTGSIVAqqPFGGARASGTNdKPGGPH 529
Cdd:PLN02278 447 LEY--GIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKY 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
90-526 |
2.04e-39 |
|
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: 149.95 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARRE--WDLKPIQDRAQVLFKAADIISgpKRAEILAK-TMIGQGKTVVQAEIDAAAELIDFFRFN 166
Cdd:cd07142 38 GDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE--KHADELAAlETWDNGKPYEQARYAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 167 AKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSASYAVyNVLRD 244
Cdd:cd07142 116 AGWADKIHGMT-LPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEqTPLSALLAA-KLAAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGKNFHFVHKSADVQS 324
Cdd:cd07142 194 AGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKS-----NLKPVTLELGGKSPFIVCEDADVDK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvedwstFFSAV-----IDDKSFARIKKWLDH 399
Cdd:cd07142 269 AVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDP------FRKGVeqgpqVDKEQFEKILSYIEH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 400 AKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTSpYALTGAVFALD 479
Cdd:cd07142 343 GKEE-GATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD--EVIKRANNSK-YGLAAGVFSKN 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367454336 480 KNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASGTNDKPG 526
Cdd:cd07142 419 IDTANTLSRALK--AGTVWVN--CYDVFDASIPFGGYKMSGIGREKG 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
121-520 |
2.16e-39 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 148.35 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 121 LFKAADIISgpKRAEILAKTMIG-QGKTVVQAEIDAAAElIDFFRFNAKHAVELESQQpLDSD-GSTNTMLYRGLEGFIA 198
Cdd:PRK10090 1 LRKIAAGIR--ERASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEI-IQSDrPGENILLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 199 AVAPFNFT--AIGGNLAgtPALM-GNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGI 275
Cdd:PRK10090 77 GILPWNFPffLIARKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 276 NFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWP 355
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAA------KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 356 QIKQGLLDIHKQLKVGDPVEDWSTFFSAVIDDKSFARIKKWLDHAKSSPKlNVIAGGHCNDKKGYFVEPTIIESTDPQEA 435
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 436 IMAEEIFGPVLSVYVYpenDYLEVLHLIDNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKstgSIVAQQPF-G 514
Cdd:PRK10090 308 IMHEETFGPVLPVVAF---DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRE---NFEAMQGFhA 379
|
....*.
gi 1367454336 515 GARASG 520
Cdd:PRK10090 380 GWRKSG 385
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
83-520 |
9.62e-39 |
|
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: 147.99 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 83 KLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGPKRAEILAKTMiGQGKTVVQ---AEIDAAAel 159
Cdd:cd07117 28 TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETL-DNGKPIREtraVDIPLAA-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 160 iDFFRFNAKhAVELESQQPLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAmSASYAV 238
Cdd:cd07117 105 -DHFRYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSSTT-SLSLLE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 239 YNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknFPRVAgECGGKNFHFVHK 318
Cdd:cd07117 182 LAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGGKSANIIFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 319 SADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLD 398
Cdd:cd07117 256 DANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP-DTQMGAQVNKDQLDKILSYVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 399 HAKSSpKLNVIAGGH----CNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGA 474
Cdd:cd07117 335 IAKEE-GAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED--EVIDMA-NDSEYGLGGG 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367454336 475 VFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07117 411 VFTKDINRALRVARAVE--TGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
90-520 |
3.04e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 147.19 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAA-----RREWDLKPIQDRAQVLFKAADIISGPKRAeiLAKT-MIGQGKTVVQAE--IDAAAELID 161
Cdd:PLN02467 42 ATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSE--LAKLeTLDCGKPLDEAAwdMDDVAGCFE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 162 FFrfnAKHAVELESQQ--PLD-SDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYA 237
Cdd:PLN02467 120 YY---ADLAEALDAKQkaPVSlPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 238 VYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfPrVAGECGGKNFHFVH 317
Cdd:PLN02467 197 LADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 318 KSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWL 397
Cdd:PLN02467 271 DDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE-GCRLGPVVSEGQYEKVLKFI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 398 DHAKSSpKLNVIAGG----HCndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTG 473
Cdd:PLN02467 350 STAKSE-GATILCGGkrpeHL--KKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED--EAIELA-NDSHYGLAG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1367454336 474 AVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:PLN02467 424 AVISNDLERCERVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
96-479 |
9.42e-38 |
|
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: 145.04 E-value: 9.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 96 NKAILASVAARREWDLKPIQDRAQVLFKAADIISGPKRAEIL---------AKTMIGQ------GKTVVQA--EIDaaaE 158
Cdd:cd07130 21 NGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVrqigdalrkKKEALGKlvslemGKILPEGlgEVQ---E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 159 LIDFFRFnakhAVELESQQPldsdGST------NTMLYR-----GLEGFIAAvapFNF-TAIGGNLAGTPALMGNVVLWK 226
Cdd:cd07130 98 MIDICDF----AVGLSRQLY----GLTipserpGHRMMEqwnplGVVGVITA---FNFpVAVWGWNAAIALVCGNVVVWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 227 PSDTAMSASYAVY----NVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTfkrlWKQVAQNldVYKNFP 302
Cdd:cd07130 167 PSPTTPLTAIAVTkivaRVLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGSTAV----GRQVGQA--VAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 303 RVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFS 382
Cdd:cd07130 240 RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD-GTLVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 383 AVIDDKSFARIKKWLDHAKSSPKlNVIAGGHCNDKKGYFVEPTIIEStDPQEAIMAEEIFGPVLsvYVYPENDYLEVLHl 462
Cdd:cd07130 319 PLHTKAAVDNYLAAIEEAKSQGG-TVLFGGKVIDGPGNYVEPTIVEG-LSDAPIVKEETFAPIL--YVLKFDTLEEAIA- 393
|
410
....*....|....*..
gi 1367454336 463 IDNTSPYALTGAVFALD 479
Cdd:cd07130 394 WNNEVPQGLSSSIFTTD 410
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
83-529 |
1.89e-35 |
|
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: 138.68 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 83 KLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILA--KTMIGqGKTVVQ---AEIDAAA 157
Cdd:cd07111 49 VLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQ--KHQRLFAvlESLDN-GKPIREsrdCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 158 ELidfFRFNAKHAvelesqQPLDSDGstntmlyRGLE--GFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSDTAMSA 234
Cdd:cd07111 126 RH---FYHHAGWA------QLLDTEL-------AGWKpvGVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTPLT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 235 SYAVYNVLRDSGLPPNIIQFVPADGPvFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECGGKNFH 314
Cdd:cd07111 190 ALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTG------KKLSLELGGKSPF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 315 FVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIK 394
Cdd:cd07111 263 IVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL-DKAIDMGAIVDPAQLKRIR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 395 KWLDHAKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTsPYALTGA 474
Cdd:cd07111 342 ELVEEGRAE-GADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAK--EAVALANNT-PYGLAAS 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367454336 475 VFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASGTNdKPGGPH 529
Cdd:cd07111 418 VWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
84-519 |
2.06e-35 |
|
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: 138.80 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EIDAAAELI 160
Cdd:cd07085 29 IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLItLEHGKTLADArgDVLRGLEVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 161 DF-----------FRFNAKHAVELESQ-QPLdsdgstntmlyrgleGFIAAVAPFNFTAIggnlagTPALM-------GN 221
Cdd:cd07085 107 EFacsiphllkgeYLENVARGIDTYSYrQPL---------------GVVAGITPFNFPAM------IPLWMfpmaiacGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 222 VVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNF 301
Cdd:cd07085 166 TFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA-VNALLDHPDIKAVSFVGSTPVGEYIYERAA------ANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 302 PRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFF 381
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP-GADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 382 SAVIDDKSFARIKKWLDHA-KSSPKL-----NVIAGGHcndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLS-VYVypeN 454
Cdd:cd07085 318 GPVISPAAKERIEGLIESGvEEGAKLvldgrGVKVPGY---ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSiVRV---D 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 455 DYLEVLHLIdNTSPYALTGAVFALDknvvneaakalrNAAGNYYVNDKSTGSI---------VAQQPFGGARAS 519
Cdd:cd07085 392 TLDEAIAII-NANPYGNGAAIFTRS------------GAAARKFQREVDAGMVginvpipvpLAFFSFGGWKGS 452
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
75-533 |
6.86e-35 |
|
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: 136.78 E-value: 6.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 75 LSPFNHSHkLAKFCYADKELLNKAILASVAA---RREWdlKPIQDRAQVLFKAADIISgpKRAEILAKTMIGQG-KTVVQ 150
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLME--ERADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 151 A--EIDAAaelIDFFRFNAKHAVELESQQ-PLD-SDGSTNTMLYRGLE--GFIAAVAPFNF----------TAIGgnlAG 214
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGlTPASAGRIAFTTREpiGVVVAISAFNHplnlivhqvaPAIA---AG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 215 TPalmgnvVLWKP-SDTAMSASyAVYNVLRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQ 293
Cdd:cd07148 153 CP------VIVKPaLATPLSCL-AFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWMLRSKLAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 294 NldvyknfPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDP 373
Cdd:cd07148 225 G-------TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 374 VeDWSTFFSAVIDDKSFARIKKWLDHAKSSPKlNVIAGGHCNDKKGYfvEPTIIESTDPQEAIMAEEIFGPVLSVYVYPE 453
Cdd:cd07148 298 T-DPDTEVGPLIRPREVDRVEEWVNEAVAAGA-RLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 454 -NDYLEvlhlIDNTSPYALTGAVFALDKNVVNEAAKALrnAAGNYYVNDKsTGSIVAQQPFGGARASGTNdkPGGPHYVL 532
Cdd:cd07148 374 lDEAIA----QANSLPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG--TGGIPYTM 444
|
.
gi 1367454336 533 R 533
Cdd:cd07148 445 H 445
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
84-520 |
1.47e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 136.49 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNkaiLASVAARREWDLKPIQ-----DRAQVLFKAADIISgpKRAEILAK-------TMIGQGKTVvqa 151
Cdd:PLN02766 49 IARIAEGDKEDVD---LAVKAAREAFDHGPWPrmsgfERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 152 EIDAAAELidfFRFNAKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD- 229
Cdd:PLN02766 121 DIPAAAGL---LRYYAGAADKIHGET-LKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEq 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 230 TAMSASYAVYnVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECG 309
Cdd:PLN02766 197 TPLSALFYAH-LAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATS-----NLKQVSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 310 GKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKS 389
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF-DPRARQGPQVDKQQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 390 FARIKKWLDHAKSSPKlNVIAGGHCNDKKGYFVEPTIIesTDPQE--AIMAEEIFGPVLSVYVYPENDylEVLHLIDNTS 467
Cdd:PLN02766 350 FEKILSYIEHGKREGA-TLLTGGKPCGDKGYYIEPTIF--TDVTEdmKIAQDEIFGPVMSLMKFKTVE--EAIKKANNTK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1367454336 468 pYALTGAVFALDKNVVNEAAKALRnaAGNYYVN-----DKSTgsivaqqPFGGARASG 520
Cdd:PLN02766 425 -YGLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
91-548 |
2.09e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 136.86 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 91 DKELLNKAILASVAARRE--WDLKPIQDRAQVLFKAADIISgPKRAEILAKTMIGQGKTVVQAeidAAAEL---IDFFRF 165
Cdd:PLN02466 93 DAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAELpmfARLFRY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQpLDSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSASYAVyNVLR 243
Cdd:PLN02466 169 YAGWADKIHGLT-VPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEqTPLSALYAA-KLLH 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 244 DSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKrlwkqVAQNLDVYKNFPRVAGECGGKNFHFVHKSADVQ 323
Cdd:PLN02466 247 EAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK-----IVLELAAKSNLKPVTLELGGKSPFIVCEDADVD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 324 SVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvedwstFFSAV-----IDDKSFARIKKWLD 398
Cdd:PLN02466 322 KAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDP------FKKGVeqgpqIDSEQFEKILRYIK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 399 HAKSSpKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLiDNTSPYALTGAVFAL 478
Cdd:PLN02466 396 SGVES-GATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKF--KDLDEVIRR-ANNTRYGLAAGVFTQ 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367454336 479 DKNVVNEAAKALRnaAGNYYVN--DKSTGSIvaqqPFGGARASGTNDKPGgpHYVLRwtSPQVVKATHVPLR 548
Cdd:PLN02466 472 NLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG--IYSLN--NYLQVKAVVTPLK 533
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
90-520 |
6.02e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 134.62 E-value: 6.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGK----TVVqAEIDAAAELIDFFr 164
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALeTLDTGKpiqeTSV-VDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 165 fnAKHAVELE-SQQPLDSDGSTNTMlyRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSD-TAMSAsYAVYNV 241
Cdd:PRK13252 117 --AGLAPALEgEQIPLRGGSFVYTR--REPLGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEvTPLTA-LKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 242 LRDSGLPPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSAD 321
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 322 VQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPvEDWSTFFSAVIddkSFARIKKWLDH-- 399
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDP-MDPATNFGPLV---SFAHRDKVLGYie 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 400 -AKSSpKLNVIAGGHC----NDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIDNTsPYALTGA 474
Cdd:PRK13252 341 kGKAE-GARLLCGGERltegGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED--EVIARANDT-EYGLAAG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1367454336 475 VFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:PRK13252 417 VFTADLSRAHRVIHQLE--AGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
90-525 |
1.38e-32 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 130.85 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 90 ADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAkTMIGQ--GKTVVQA--EIDAAAELIDFfRF 165
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAatEVTAMINKIAI-SI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQPLDsdGSTNTMLYRGLeGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAVYNVLRD 244
Cdd:PRK09457 110 QAYHERTGEKRSEMA--DGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVKLWQQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 245 SGLPPNIIQFVPAdGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDVYknfprVAGECGGKNFHFVHKSADVQS 324
Cdd:PRK09457 187 AGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVADIDA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 325 VVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQ-IKQGLLDIHKQLKVGDPVEDWSTFFSAVIDDKSFARIKKWLDHAKSS 403
Cdd:PRK09457 261 AVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQAAQGLVAAQAQLLAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 PKLNVIAGGHCNDKKGyFVEPTIIESTDPQEaIMAEEIFGPVLSVYVYPenDYLEVLHLIDNTSpYALTGAVFALDKNVV 483
Cdd:PRK09457 341 GGKSLLEMTQLQAGTG-LLTPGIIDVTGVAE-LPDEEYFGPLLQVVRYD--DFDEAIRLANNTR-FGLSAGLLSDDREDY 415
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1367454336 484 NEAAKALRnaAGNYYVNDKSTGSIVAqQPFGGARASGtNDKP 525
Cdd:PRK09457 416 DQFLLEIR--AGIVNWNKPLTGASSA-APFGGVGASG-NHRP 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
97-520 |
2.85e-32 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 129.64 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 97 KAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQA--EIDAAAELIDFFRFNAK--HAV 171
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 172 ELESQQPldsdgSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAVYNVLRDSGLPPN 250
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 251 IIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHKSADVQSVVTGTI 330
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK------KVSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 331 RSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDWSTfFSAVIDDKSFARIKKWLDHAKSSPKlNVIA 410
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT-IGPLIDEKAVAKVEEHIADALEKGA-RVVC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 411 GGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLIDNTSpYALTGAVFALDKNVVNEAAKAL 490
Cdd:PRK11241 357 GGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEADVIAQANDTE-FGLAAYFYARDLSRVFRVGEAL 433
|
410 420 430
....*....|....*....|....*....|.
gi 1367454336 491 RnaagnYYVNDKSTGSIVAQ-QPFGGARASG 520
Cdd:PRK11241 434 E-----YGIVGINTGIISNEvAPFGGIKASG 459
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
87-520 |
6.38e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 125.24 E-value: 6.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 87 FCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGpkRAEILAKTM-IGQGKTVVQAEIDAAaELIDFFRF 165
Cdd:PRK09406 17 FTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEA--EADQVAALMtLEMGKTLASAKAEAL-KCAKGFRY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 166 NAKHAVELESQQPLDSD---GSTNTMLYRGLeGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWK-PSDTAMSASYaVYN 240
Cdd:PRK09406 94 YAEHAEALLADEPADAAavgASRAYVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTALY-LAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 241 VLRDSGLPPNIIQ--FVPADGPvfgDTITSSEHLAGINFTGSVPTfkrlWKQVAQnldvyknfprVAG--------ECGG 310
Cdd:PRK09406 172 LFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikktvlELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 311 KNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSF 390
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDP-DTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 391 ARIKKWLDHAKSSPKlNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPenDYLEVLHLIDNTSpya 470
Cdd:PRK09406 314 DEVEKQVDDAVAAGA-TILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATT--- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1367454336 471 ltgavFALDKNV-VNEAAKALRNA----AGNYYVNDKSTGSivAQQPFGGARASG 520
Cdd:PRK09406 388 -----FGLGSNAwTRDEAEQERFIddleAGQVFINGMTVSY--PELPFGGVKRSG 435
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
84-520 |
8.92e-31 |
|
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: 125.30 E-value: 8.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 84 LAKFCYADKELLNKAILASVAA--RREWDLKPIQDRAQVLFKAADIISGPKRaEILAKTMIGQGKTVVQAEIDAAAELID 161
Cdd:cd07140 34 ICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQE-ELATIESLDSGAVYTLALKTHVGMSIQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 162 FFRFNAKHAVELESQQ-PLDSDGSTNTMLYRGLE--GFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSD-TAMSA-S 235
Cdd:cd07140 113 TFRYFAGWCDKIQGKTiPINQARPNRNLTLTKREpiGVCGIVIPWNYPLMMLAWKMAACLAaGNTVVLKPAQvTPLTAlK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 236 YAVYNVLrdSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGKNFHF 315
Cdd:cd07140 193 FAELTVK--AGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVS-----NLKKVSLELGGKSPLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 316 VHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIKK 395
Cdd:cd07140 266 IFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL-DRSTDHGPQNHKAHLDKLVE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 396 WLDHA-KSSPKLnVIAGGHCnDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDYLEVLHLIdNTSPYALTGA 474
Cdd:cd07140 345 YCERGvKEGATL-VYGGKQV-DRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRA-NDTEYGLASG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1367454336 475 VFALDKNvvneaaKALRNA----AGNYYVNDKSTGSIVAqqPFGGARASG 520
Cdd:cd07140 422 VFTKDIN------KALYVSdkleAGTVFVNTYNKTDVAA--PFGGFKQSG 463
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
103-520 |
6.16e-29 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 120.00 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 103 VAARREWDLKPIQDRAQVLFKAADIISGPKRAEILAKTMiGQGKTV---VQAEIDAAAELIDFFrfnaKHAVELESQQPL 179
Cdd:PRK09847 69 VFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAIRWY----AEAIDKVYGEVA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 180 DSDGSTNTMLYRGLEGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAVYNVLRDSGLPPNIIQFVPAD 258
Cdd:PRK09847 144 TTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 259 GPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNldvykNFPRVAGECGGKNFHFVHKSA-DVQSVVTGTIRSAFEYG 337
Cdd:PRK09847 224 GHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 338 GQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSFARIKKWLDHAKSSPKLnvIAGGHCNDK 417
Cdd:PRK09847 299 GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCAHADSVHSFIREGESKGQL--LLDGRNAGL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 418 KGYfVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNY 497
Cdd:PRK09847 376 AAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEE--QALQLA-NDSQYGLGAAVWTRDLSRAHRMSRRLK--AGSV 449
|
410 420
....*....|....*....|...
gi 1367454336 498 YVNDKSTGSIVAqqPFGGARASG 520
Cdd:PRK09847 450 FVNNYNDGDMTV--PFGGYKQSG 470
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
87-520 |
1.58e-27 |
|
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: 115.63 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 87 FCYA---DKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISgpKRAEILAKT-MIGQGKTVVQAeidAAAEL--- 159
Cdd:cd07116 29 FCEVprsTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRME--ANLEMLAVAeTWDNGKPVRET---LAADIpla 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 160 IDFFRFnakHAVELESQQPLDSDGSTNTMLYRGLE--GFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDtAMSASY 236
Cdd:cd07116 104 IDHFRY---FAGCIRAQEGSISEIDENTVAYHFHEplGVVGQIIPWNFPLLMATWKLAPALAaGNCVVLKPAE-QTPASI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 237 AVYNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLdvyknFPrVAGECGGK--NFH 314
Cdd:cd07116 180 LVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI-----IP-VTLELGGKspNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 315 F----VHKSADVQSVVTGTIRSAFEYgGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVeDWSTFFSAVIDDKSF 390
Cdd:cd07116 254 FadvmDADDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL-DTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 391 ARIKKWLDHAKSSPKlNVIAGGHCN----DKKGYFVEPTIIESTDpQEAIMAEEIFGPVLSVYVYpeNDYLEVLHlIDNT 466
Cdd:cd07116 332 EKILSYIDIGKEEGA-EVLTGGERNelggLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTF--KDEEEALE-IAND 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 467 SPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNdkSTGSIVAQQPFGGARASG 520
Cdd:cd07116 407 TLYGLGAGVWTRDGNTAYRMGRGIQ--AGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
201-520 |
2.23e-27 |
|
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: 114.55 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 201 APFNF---TAIG---GNLAGtpalmGNVVLWKPSDTAMSASYAVYNVLRDsGLPPNIIQFVPADGPVfgdtitSSEHLAG 274
Cdd:cd07087 108 GPWNYplqLALApliGAIAA-----GNTVVLKPSELAPATSALLAKLIPK-YFDPEAVAVVEGGVEV------ATALLAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 275 ----INFTGSVPTFKRLWKQVAQNLDvyknfPrVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVP 350
Cdd:cd07087 176 pfdhIFFTGSPAVGKIVMEAAAKHLT-----P-VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 351 DSlwpqIKQGLLD-IHKQLK--VGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKsspklnVIAGGHCNDKKGYfVEPTII 427
Cdd:cd07087 250 ES----IKDELIEeLKKAIKefYGEDPKE-SPDYGRIINERHFDRLASLLDDGK------VVIGGQVDKEERY-IAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 428 ESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSI 507
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLD--EAIEFI-NSRPKPLALYLFSEDKAVQERVLAETS--SGGVCVNDVLLHAA 392
|
330
....*....|...
gi 1367454336 508 VAQQPFGGARASG 520
Cdd:cd07087 393 IPNLPFGGVGNSG 405
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
36-526 |
5.85e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 114.55 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 36 GSPERAELQkALDDLKGKTEEIPCVVGDEHVWTKDIRYQLSPFNHsHKLAKFCYADKELLNKAILASVAARREWDLKPIQ 115
Cdd:PLN02315 1 MGFARKEYE-FLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 116 DRAQVLFKAADIISgpKRAEILAKTM-IGQGKTVVQAeIDAAAELIDFFRFnakhAVELESQ---QPLDSDGSTNTMLY- 190
Cdd:PLN02315 79 KRGEIVRQIGDALR--AKLDYLGRLVsLEMGKILAEG-IGEVQEIIDMCDF----AVGLSRQlngSIIPSERPNHMMMEv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 191 ---RGLEGFIAAvapFNF-TAIGGNLAGTPALMGNVVLWKPSDTAMSASYA----VYNVLRDSGLPPNIIQFVpADGPVF 262
Cdd:PLN02315 152 wnpLGIVGVITA---FNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSF-CGGAEI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 263 GDTITSSEHLAGINFTGSvptfKRLWKQVAQNldVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCS 342
Cdd:PLN02315 228 GEAIAKDTRIPLVSFTGS----SKVGLMVQQT--VNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 343 ACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKlNVIAGGHCNDKKGYFV 422
Cdd:PLN02315 302 TCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLGPLHTPESKKNFEKGIEIIKSQGG-KILTGGSAIESEGNFV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 423 EPTIIESTdPQEAIMAEEIFGPVLsvYVYPENDYLEVLHlIDNTSPYALTGAVFALDKNVVNEAAKALRNAAGNYYVNDK 502
Cdd:PLN02315 380 QPTIVEIS-PDADVVKEELFGPVL--YVMKFKTLEEAIE-INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIP 455
|
490 500
....*....|....*....|....
gi 1367454336 503 STGSIVAqQPFGGARASGTNDKPG 526
Cdd:PLN02315 456 TNGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-542 |
1.58e-26 |
|
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: 112.33 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 95 LNKAILASVAARREWDLKPIQDRAQVLfkaADIIS--GPKRAEILAKTMIGQGKTVVQAEiDAAAELIDFFRFNAKHAVE 172
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFL---ARIIQrlAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 173 LESQQPLDSDGSTNTMLYRGLE---GFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKPSDTAMSASYAVYNVLRDSG-L 247
Cdd:cd07084 77 RIPHEPGNHLGQGLKQQSHGYRwpyGPVLVIGAFNFPLWIPLLQLAGALaMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 248 PPNIIQFVPADGPVfGDTITSSEHLAGINFTGSVptfkrlwkQVAQNLDVYKNFPRVAGECGGKNFHFVHKSAD-VQSVV 326
Cdd:cd07084 157 PPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 327 TGTIRSAFEYGGQKCSACSRMYVP--DSLWPQIKQGLLDIHKQlKVGDpvedwsTFFSAVIDDKSFARIKkwldHAKSSP 404
Cdd:cd07084 228 WQCVQDMTACSGQKCTAQSMLFVPenWSKTPLVEKLKALLARR-KLED------LLLGPVQTFTTLAMIA----HMENLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 405 KLNVIAGG-----HCNDKKGYFVEPT----IIESTDPQEAIMAEEIFGPVLSVYVYPENDYLEVLHLIDNTSPyALTGAV 475
Cdd:cd07084 297 GSVLLFSGkelknHSIPSIYGACVASalfvPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHG-SLTAAI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1367454336 476 FALDKNVVNEAAKALRNAAGNYYVNDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVVKA 542
Cdd:cd07084 376 YSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
83-520 |
3.25e-25 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 108.80 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 83 KLAKFCYADKELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGpkRAEILAKTMIGQ-GKTVVQA--EIDAAAEL 159
Cdd:PRK13968 19 QLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRA--RSEEMAQMITREmGKPINQAraEVAKSANL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 160 IDFFrfnAKHAVELESQQPLDSDGSTNTMLYRGLeGFIAAVAPFNFTAIGGNLAGTPALM-GNVVLWKPSDTAMSASYAV 238
Cdd:PRK13968 97 CDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNFPLWQVMRGAVPILLaGNGYLLKHAPNVMGCAQLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 239 YNVLRDSGLPPNIIQFVPADGPVFGDTITSSEhLAGINFTGSVPTFKRLWKQVAQNLDvyknfpRVAGECGGKNFHFVHK 318
Cdd:PRK13968 173 AQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 319 SADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVE---DWSTFFSAVIDDKSFARIKK 395
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDeenALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 396 WLDHAKSspklnVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDYleVLHLIdNTSPYALTGAV 475
Cdd:PRK13968 326 TLAEGAR-----LLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEH--ALELA-NDSEFGLSATI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1367454336 476 FALDKNVVNEAAKALRnaAGNYYVNDKSTGSivAQQPFGGARASG 520
Cdd:PRK13968 398 FTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
202-520 |
1.51e-24 |
|
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: 106.16 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 202 PFNFTAigGNLAGTPAlMGNVVLWKPSDTAMSASYAVYNVLRDSglppniiqFVPADGPVF-GDTITSSEHLA----GIN 276
Cdd:cd07134 113 PFNLAF--GPLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--------FDEDEVAVFeGDAEVAQALLElpfdHIF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 277 FTGSvptfKRLWKQVAQnlDVYKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSAcsrmyvPDSLW-- 354
Cdd:cd07134 182 FTGS----PAVGKIVMA--AAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA------PDYVFvh 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 355 PQIKQGLLD-----IHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKLnVIAGGHcNDKKGYFVEPTIIES 429
Cdd:cd07134 250 ESVKDAFVEhlkaeIEKFYGKDAARKA-SPDLARIVNDRHFDRLKGLLDDAVAKGAK-VEFGGQ-FDAAQRYIAPTVLTN 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 430 TDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNeaaKALRN-AAGNYYVNDkstgsiV 508
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLD--EVIEYI-NAKPKPLALYVFSKDKANVN---KVLARtSSGGVVVND------V 394
|
330
....*....|....*...
gi 1367454336 509 AQQ------PFGGARASG 520
Cdd:cd07134 395 VLHflnpnlPFGGVNNSG 412
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
202-520 |
2.77e-24 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 106.27 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 202 PFNFTAIggNLAGTPAlMGNVVLWKPSDTAMSASYAVYNVLrDSGLPPNIIQFVPADGPVfgDTITSSEHLAGINFTGSV 281
Cdd:PTZ00381 122 PLNLTLI--PLAGAIA-AGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEV--TTELLKEPFDHIFFTGSP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 282 PTFKRLWKQVAQNLdvyknFPrVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDSlwpqIKQGL 361
Cdd:PTZ00381 196 RVGKLVMQAAAENL-----TP-CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS----IKDKF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 362 LDIHKQLKV----GDPVEdwSTFFSAVIDDKSFARIKKWLDHAKSspklNVIAGGHCNDKKGYfVEPTIIESTDPQEAIM 437
Cdd:PTZ00381 266 IEALKEAIKeffgEDPKK--SEDYSRIVNEFHTKRLAELIKDHGG----KVVYGGEVDIENKY-VAPTIIVNPDLDSPLM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 438 AEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKalRNAAGNYYVNDKSTGSIVAQQPFGGAR 517
Cdd:PTZ00381 339 QEEIFGPILPILTYENID--EVLEFI-NSRPKPLALYYFGEDKRHKELVLE--NTSSGAVVINDCVFHLLNPNLPFGGVG 413
|
...
gi 1367454336 518 ASG 520
Cdd:PTZ00381 414 NSG 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
200-521 |
3.51e-23 |
|
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: 102.30 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 200 VAPFNF---TAIG---GNLAGtpalmGNVVLWKPSDTAMSASYAVYNVLRdSGLPPNIIQFVPADGPVFGDTITSS-EHl 272
Cdd:cd07135 115 IGPWNYpvlLALSplvGAIAA-----GCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKfDK- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 273 agINFTGSVPTFKRLWKQVAQNLDvyknfPrVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSACSRMYVPDS 352
Cdd:cd07135 188 --IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 353 LWPQIKQGLLDIHKQLKVGDPVEDwsTFFSAVIDDKSFARIKKWLDHAKSspklNVIAGGHCNDKKgYFVEPTIIESTDP 432
Cdd:cd07135 260 VYDEFVEELKKVLDEFYPGGANAS--PDYTRIVNPRHFNRLKSLLDTTKG----KVVIGGEMDEAT-RFIPPTIVSDVSW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 433 QEAIMAEEIFGPVLSVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRnaAGNYYVNDKSTGSIVAQQP 512
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLD--EAIKVI-NSRDTPLALYIFTDDKSEIDHILTRTR--SGGVVINDTLIHVGVDNAP 407
|
....*....
gi 1367454336 513 FGGARASGT 521
Cdd:cd07135 408 FGGVGDSGY 416
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
92-481 |
2.99e-22 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 100.22 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 92 KELLNKAILASVAARREWDLKPIQDRAQVLFKAADIISGPKR--AEILAKTMIGQGKTVVqAEIDAAAELIDFfrfNAKH 169
Cdd:PLN00412 52 QEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPAKDAV-TEVVRSGDLISY---TAEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 170 AVELESQ-QPLDSD---GSTNT---MLYRGLEGFIAAVAPFNFTAiggNLAGT---PALM-GNVVLWKPSDTAMSASYAV 238
Cdd:PLN00412 128 GVRILGEgKFLVSDsfpGNERNkycLTSKIPLGVVLAIPPFNYPV---NLAVSkiaPALIaGNAVVLKPPTQGAVAALHM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 239 YNVLRDSGLPPNIIQFVPADGPVFGDTITSSEHLAGINFTGSvptfkrlwkqvaqnlDVYKNFPRVAG------ECGGKN 312
Cdd:PLN00412 205 VHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG---------------DTGIAISKKAGmvplqmELGGKD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 313 FHFVHKSADVQSVVTGTIRSAFEYGGQKCSA----CSRMYVPDSLWPQIKQGLldihKQLKVGDPVEDWStfFSAVIDDK 388
Cdd:PLN00412 270 ACIVLEDADLDLAAANIIKGGFSYSGQRCTAvkvvLVMESVADALVEKVNAKV----AKLTVGPPEDDCD--ITPVVSES 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 389 SFARIKKWLDHAKSSpklnviAGGHCND--KKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYpeNDYLEVLHLIdNT 466
Cdd:PLN00412 344 SANFIEGLVMDAKEK------GATFCQEwkREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI--NSVEEGIHHC-NA 414
|
410
....*....|....*
gi 1367454336 467 SPYALTGAVFALDKN 481
Cdd:PLN00412 415 SNFGLQGCVFTRDIN 429
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
220-520 |
8.69e-21 |
|
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: 95.26 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 220 GNVVLWKPSDTAMSASYAVYNVLRDSgLPPNIIQFVPadgpvfGDTITSSEHLAG----INFTGSVPTFKRLWKQVAQNL 295
Cdd:cd07136 128 GNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENQELLDQkfdyIFFTGSVRVGKIVMEAAAKHL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 296 DvyknfPrVAGECGGKNFHFVHKSADVQ----SVVTGTIRSAfeygGQKCSACSRMYVPDSlwpqIKQGLLD-----IHK 366
Cdd:cd07136 201 T-----P-VTLELGGKSPCIVDEDANLKlaakRIVWGKFLNA----GQTCVAPDYVLVHES----VKEKFIKelkeeIKK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 367 QLKvGDPVEdwSTFFSAVIDDKSFARIKKWLDHAKsspklnVIAGGHCNDKKGYfVEPTIIESTDPQEAIMAEEIFGPVL 446
Cdd:cd07136 267 FYG-EDPLE--SPDYGRIINEKHFDRLAGLLDNGK------IVFGGNTDRETLY-IEPTILDNVTWDDPVMQEEIFGPIL 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 447 SVYVYPENDylEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALRNAAGnyYVNDKSTGSIVAQQPFGGARASG 520
Cdd:cd07136 337 PVLTYDTLD--EAIEII-KSRPKPLALYLFSEDKKVEKKVLENLSFGGG--CINDTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
275-520 |
8.30e-19 |
|
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: 89.20 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 275 INFTGSVPTFKRLWKQVAQNLdvyknfPRVAGECGGKNFHFVHKSADVQSVVTGTIRSAFEYGGQKCSA-----CSRmYV 349
Cdd:cd07132 180 IFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdyvlCTP-EV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 350 PDSLWPQIKQGLldihKQLKVGDPVEdwSTFFSAVIDDKSFARIKKWLDhaksspKLNVIAGGHCNDKKGYfVEPTIIES 429
Cdd:cd07132 253 QEKFVEALKKTL----KEFYGEDPKE--SPDYGRIINDRHFQRLKKLLS------GGKVAIGGQTDEKERY-IAPTVLTD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 430 TDPQEAIMAEEIFGPVLSvyVYPENDYLEVLHLIDNTS-PYALTgaVFALDKNVVNeaaKALRN-AAGNYYVNDKSTGSI 507
Cdd:cd07132 320 VKPSDPVMQEEIFGPILP--IVTVNNLDEAIEFINSREkPLALY--VFSNNKKVIN---KILSNtSSGGVCVNDTIMHYT 392
|
250
....*....|...
gi 1367454336 508 VAQQPFGGARASG 520
Cdd:cd07132 393 LDSLPFGGVGNSG 405
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
96-476 |
8.35e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 86.72 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 96 NKAILASVAARRE----WDLKPIQDRAQVLFKAADIISgpKRAEILAKTMIG-QGKTV--VQAEIDAAAELIDffrfnak 168
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLkdSHGDIFRGLEVVE------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 169 HAVELESQQ-----PLDSDGsTNTMLYRGLEGFIAAVAPFNFTAIggnlagTPALM-------GNVVLWKPSDTAMSASY 236
Cdd:PLN02419 221 HACGMATLQmgeylPNVSNG-VDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 237 AVYNVLRDSGLPPNIIQFVPADGPVFgDTITSSEHLAGINFTGSVPTFKRLWKQVAqnldvyKNFPRVAGECGGKNFHFV 316
Cdd:PLN02419 294 ILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAA------AKGKRIQSNMGAKNHGLV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 317 HKSADVQSVVTGTIRSAFEYGGQKCSACSRM-YVPDSL-WpqiKQGLLDIHKQLKV---GDPVEDwstfFSAVIDDKSFA 391
Cdd:PLN02419 367 LPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDAKsW---EDKLVERAKALKVtcgSEPDAD----LGPVISKQAKE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 392 RIKKWLDHA-KSSPKL-----NVIAGGHcndKKGYFVEPTIIESTDPQEAIMAEEIFGPVLsvYVYPENDYLEVLHLIdN 465
Cdd:PLN02419 440 RICRLIQSGvDDGAKLlldgrDIVVPGY---EKGNFIGPTILSGVTPDMECYKEEIFGPVL--VCMQANSFDEAISII-N 513
|
410
....*....|.
gi 1367454336 466 TSPYALTGAVF 476
Cdd:PLN02419 514 KNKYGNGAAIF 524
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
183-520 |
2.47e-15 |
|
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: 78.30 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 183 GSTNTMLYRGLeGFIAAVAPFNF---TAIGGnLAGtpAL-MGNVVLWKPSDT--AMSAsyavynVLRD---SGLPPNIIQ 253
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIA--ALaAGNRVMIKPSEFtpRTSA------LLAEllaEYFDEDEVA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 254 FVPADGPV---FgdtitSS---EHLAginFTGSVPTFKRLWKQVAQNLdvyknFPrVAGECGGKNFHFVHKSADVQSVVT 327
Cdd:cd07133 162 VVTGGADVaaaF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL-----TP-VTLELGGKSPAIIAPDADLAKAAE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 328 GTIRSAFEYGGQKCSACSRMYVPDSLWPQIKQGLLDIHKQL---KVGDPveDwstfFSAVIDDKSFARIKKWLDHAKSS- 403
Cdd:cd07133 228 RIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP--D----YTSIINERHYARLQGLLEDARAKg 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 404 PKLNVIAGGHCNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVYPENDylEVLHLI-DNTSPYALTgaVFALDKnv 482
Cdd:cd07133 302 ARVIELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLD--EAIDYInARPRPLALY--YFGEDK-- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1367454336 483 vNEAAKALRN-AAGNYYVNDksTGSIVAQ--QPFGGARASG 520
Cdd:cd07133 376 -AEQDRVLRRtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
220-521 |
4.53e-15 |
|
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: 77.45 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 220 GNVVLWKPSDTAMSASyavynvlrdSGLPPNIIQFVPADG-PVFGDTITSSEHLA-----GINFTGSvPTFKRLWKQVAQ 293
Cdd:cd07137 129 GNAVVLKPSELAPATS---------ALLAKLIPEYLDTKAiKVIEGGVPETTALLeqkwdKIFFTGS-PRVGRIIMAAAA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 294 nldvyKNFPRVAGECGGKNFHFVHKSADVQSVVTGTIrsAFEYG---GQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKV 370
Cdd:cd07137 199 -----KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIA--GGKWGcnnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 371 GDPVEdwSTFFSAVIDDKSFARIKKWLDHAKSSPKlnVIAGGHCNDKKGYfVEPTIIESTDPQEAIMAEEIFGPVLSVY- 449
Cdd:cd07137 272 ENPKE--SKDLSRIVNSHHFQRLSRLLDDPSVADK--IVHGGERDEKNLY-IEPTILLDPPLDSSIMTEEIFGPLLPIIt 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1367454336 450 VYPENDYLEVLhlidNTSPYALTGAVFALDKNVVNEAAKALrnAAGNYYVNDKSTGSIVAQQPFGGARASGT 521
Cdd:cd07137 347 VKKIEESIEII----NSRPKPLAAYVFTKNKELKRRIVAET--SSGGVTFNDTVVQYAIDTLPFGGVGESGF 412
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
220-520 |
2.67e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 65.84 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 220 GNVVLWKPSDTAmSASYAVYNVLRDSGLPPNIIQFVpaDGPVFGDTITSSEHLAGINFTGSVPTFKRLWKQVAQNLDvyk 299
Cdd:PLN02174 140 GNAVVLKPSELA-PASSALLAKLLEQYLDSSAVRVV--EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLT--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 300 nfpRVAGECGGKNFHFVHKSADVQSVVTGTIrsAFEYG---GQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEd 376
Cdd:PLN02174 214 ---PVVLELGGKSPVVVDSDTDLKVTVRRII--AGKWGcnnGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 377 wSTFFSAVIDDKSFARIKKWLDHAKSSPKlnVIAGGHcNDKKGYFVEPTIIESTDPQEAIMAEEIFGPVLSVYVyPENDY 456
Cdd:PLN02174 288 -SKDMSRIVNSTHFDRLSKLLDEKEVSDK--IVYGGE-KDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILT-LNNLE 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1367454336 457 lEVLHLIdNTSPYALTGAVFALDKNVVNEAAKALrnAAGNYYVNDKSTGSIVAQQPFGGARASG 520
Cdd:PLN02174 363 -ESFDVI-RSRPKPLAAYLFTHNKKLKERFAATV--SAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
220-520 |
1.14e-10 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 63.98 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 220 GNVVLWKPSDTAMSASYAVYNVLrDSGLPPNIIQFVPAdGPVFGDTITssEH-LAGINFTGSvPTFKRLWKQVAQnldvy 298
Cdd:PLN02203 136 GNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEG-GPAVGEQLL--QHkWDKIFFTGS-PRVGRIIMTAAA----- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 299 KNFPRVAGECGGKN---FHFVHKSADVQSVVTGTIRSAFEY-GGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPV 374
Cdd:PLN02203 206 KHLTPVALELGGKCpciVDSLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 375 EdwSTFFSAVIDDKSFARIKKWLDhaKSSPKLNVIAGGHCNDKKgYFVEPTIIESTDPQEAIMAEEIFGPVLSVY-VYPE 453
Cdd:PLN02203 286 E--SKSMARILNKKHFQRLSNLLK--DPRVAASIVHGGSIDEKK-LFIEPTILLNPPLDSDIMTEEIFGPLLPIItVKKI 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 454 NDYLEVLhlidNTSPYALtgAVFALDKnvvNEAAKAL---RNAAGNYYVNDKSTGSIVAQQPFGGARASG 520
Cdd:PLN02203 361 EDSIAFI----NSKPKPL--AIYAFTN---NEKLKRRilsETSSGSVTFNDAIIQYACDSLPFGGVGESG 421
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
191-451 |
5.36e-09 |
|
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: 58.82 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 191 RGLEGFIAAvapFNFTAIG--GNLAgtPALMGNV-VLWKP-SDTAMSAsYAVYNVLRDSG-LPPNIIQFVPAD-GPVFgD 264
Cdd:cd07128 145 RGVAVHINA---FNFPVWGmlEKFA--PALLAGVpVIVKPaTATAYLT-EAVVKDIVESGlLPEGALQLICGSvGDLL-D 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 265 TITSSEHLAginFTGSVPTFKRLwkqvaqnldvyKNFPRVAGEcggkNFHFVHKSADVQSVVTG---------------- 328
Cdd:cd07128 218 HLGEQDVVA---FTGSAATAAKL-----------RAHPNIVAR----SIRFNAEADSLNAAILGpdatpgtpefdlfvke 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 329 -----TIRSafeygGQKCSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSF----ARIKKWLDH 399
Cdd:cd07128 280 varemTVKA-----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLE-GVRMGPLVSREQRedvrAAVATLLAE 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1367454336 400 AK---SSPKLNVIAGGHCNdkKGYFVEPTIIESTDPQEA--IMAEEIFGPVLSVYVY 451
Cdd:cd07128 354 AEvvfGGPDRFEVVGADAE--KGAFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPY 408
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-451 |
8.82e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 58.18 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 191 RGLEGFIAAvapFNFTAIGGNLAGTPALMGNV-VLWKP-SDTAMSASYAVYNVLRDSGLPPNIIQFVPADGpvfGDTIts 268
Cdd:PRK11903 149 RGVALFINA---FNFPAWGLWEKAAPALLAGVpVIVKPaTATAWLTQRMVKDVVAAGILPAGALSVVCGSS---AGLL-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 269 sEHLAG---INFTGSVPTFKRLWKQVAqnldVYKNFPRVAGECGGKNFHF-----VHKSADVQSVVTGTIRSAFEYGGQK 340
Cdd:PRK11903 221 -DHLQPfdvVSFTGSAETAAVLRSHPA----VVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 341 CSACSRMYVPDSLWPQIKQGLLDIHKQLKVGDPVEDwSTFFSAVIDDKSFARIKKWLDHAKSSPKLnVIAGGHC-----N 415
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRND-GVRMGPLVSRAQLAAVRAGLAALRAQAEV-LFDGGGFalvdaD 373
|
250 260 270
....*....|....*....|....*....|....*...
gi 1367454336 416 DKKGYFVEPTIIESTDPQEAIMAE--EIFGPVLSVYVY 451
Cdd:PRK11903 374 PAVAACVGPTLLGASDPDAATAVHdvEVFGPVATLLPY 411
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
190-485 |
1.00e-08 |
|
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: 57.89 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 190 YRGLEGFIAAVAPFNFTAIGGNLAGTPAL-MGNVVLWKpSDTAMSASYAVY-NVLRDSGLPPNIIQFVPADGPVFGDTIT 267
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALfMGNKPLLK-VDSKVSVVMEQFlRLLHLCGMPATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 268 SSEHLAgINFTGSvptfkrlwKQVAQNLDVYKNfPRVAGECGGknFHFVHKSADVQS---VVTGTIRSAFEYGGQKCSAC 344
Cdd:cd07126 218 EANPRM-TLFTGS--------SKVAERLALELH-GKVKLEDAG--FDWKILGPDVSDvdyVAWQCDQDAYACSGQKCSAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 345 SRMYVPDSlWpqIKQGLLDIHKQL----KVGD----PVEDWSTffsaviddksfARIKKWLDHAKSSPKLNVIAGG---- 412
Cdd:cd07126 286 SILFAHEN-W--VQAGILDKLKALaeqrKLEDltigPVLTWTT-----------ERILDHVDKLLAIPGAKVLFGGkplt 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1367454336 413 --HCNDKKGYfVEPTII-----ESTDPQE-AIMAEEIFGPVLSVYVYPENDYLEVLHLIDNTsPYALTGAVFALDKNVVN 484
Cdd:cd07126 352 nhSIPSIYGA-YEPTAVfvpleEIAIEENfELVTTEVFGPFQVVTEYKDEQLPLVLEALERM-HAHLTAAVVSNDIRFLQ 429
|
.
gi 1367454336 485 E 485
Cdd:cd07126 430 E 430
|
|
| |
