|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
17-493 |
0e+00 |
|
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: 883.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGEL 96
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 97 AKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVA 176
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 177 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKR 256
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 257 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPV 335
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDeADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 336 ISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIV 415
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638878 416 NANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLW 493
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
18-493 |
0e+00 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 714.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 18 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 177
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 178 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 257
Cdd:TIGR01722 162 ACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 258 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVIS 337
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLIT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 338 AASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNA 417
Cdd:TIGR01722 322 PQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 418 NPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLW 493
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
15-509 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 638.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 15 PTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMG 94
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFP 174
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 175 VAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 254
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGP 334
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 335 VISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 414
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 415 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLWR 494
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|....*
gi 24638878 495 ktDVThTQAAVAMPT 509
Cdd:PLN02419 592 --DIH-SPFSLAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
14-493 |
1.18e-178 |
|
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: 510.44 E-value: 1.18e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 14 APTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENM 93
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 94 GELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 173
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTD 331
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 332 VGPVISAASRQRINDLIESGVKEGAKLILDGRkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDA 411
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGR---RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 412 IGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 491
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTI 477
|
..
gi 24638878 492 LW 493
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
25-489 |
7.01e-164 |
|
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: 472.02 E-value: 7.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 25 FVESKTNEwIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQ 104
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 105 GKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 184
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 185 LKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGA 263
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 264 KNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQ 342
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 343 RINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGN 422
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 423 GTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDhhFYGKQGIKFYTQTKTV 489
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-490 |
9.80e-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: 358.44 E-value: 9.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGET 136
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 137 VANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIH 216
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 217 G-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCM 295
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 296 ALStAVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitVPGYEDG 373
Cdd:cd07078 241 AAS-RLLVheSIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 374 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP 453
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 24638878 454 VPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07078 397 GAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
20-490 |
2.01e-116 |
|
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: 351.65 E-value: 2.01e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 178
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 179 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 257
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 258 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVI 336
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLiVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 337 SAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 416
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 417 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI---PVPLPmfsFTGTRGSFRGdHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP---FGGVKKSGNG-HREAGTTALDAFTEWKAVY 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
20-489 |
3.73e-113 |
|
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: 343.08 E-value: 3.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEwiDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 178
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 179 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 257
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 258 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVI 336
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGiHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 337 SAASRQRINDLIESGVKEGAKLILDGRKITVPgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 416
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRP--DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638878 417 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP-----IPVPlpmfsFTGTRGSFRGDHHfYGKQGIKFYTQTKTV 489
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYGPRE-QGEAALEFYTTIKTV 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
36-491 |
1.75e-104 |
|
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: 320.15 E-value: 1.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 LRGLQVV----EHCCSIpslqMGETVanVARDMDTYSLVL--PLGVTAGVAPFNFP-AMIPLWMFPvAITTGNTMLLKPS 188
Cdd:cd07103 81 DYAASFLewfaEEARRI----YGRTI--PSPAPGKRILVIkqPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 189 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAknHG 267
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 268 --IILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVgdaQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAAS 340
Cdd:cd07103 232 pfIVFDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYV---HESIYDefvekLVERVKKLKVGNGLDEGTDMGPLINERA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 341 RQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPY 420
Cdd:cd07103 308 VEKVEALVEDAVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24638878 421 GNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPvPLPMFSFTGTRGSfrGdhhfYG----KQGIKFYTQTKTVTQ 491
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVSL 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
20-489 |
2.92e-101 |
|
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: 312.28 E-value: 2.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 99
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 100 ITKEQGKTLADAEGDVLRGLQVVEHCCS---------IPSLQMGETVanvardmdtYSLVLPLGVTAGVAPFNFP-AMIP 169
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEwarriegeiIPSDRPNENI---------FIFKVPIGVVAGILPWNFPfFLIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 170 LWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYE 248
Cdd:cd07088 152 RKLAP-ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 249 RAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLKVNAGH 326
Cdd:cd07088 231 AAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKVGDPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 327 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 406
Cdd:cd07088 310 DAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 407 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSfTGTRGSFRG--DhhfyGKQGIKFYT 484
Cdd:cd07088 387 SLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGgaD----GKHGLEEYL 461
|
....*
gi 24638878 485 QTKTV 489
Cdd:cd07088 462 QTKVV 466
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
36-490 |
3.08e-98 |
|
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: 304.10 E-value: 3.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GD 114
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VLRGLQ----VVEHCcsipsLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSER 190
Cdd:cd07093 81 IPRAAAnfrfFADYI-----LQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 191 VPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII 269
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 270 LGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 347
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLA-GSRILVqrSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVNVPIPVPLPMfSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
20-449 |
2.80e-96 |
|
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: 300.00 E-value: 2.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 177
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 178 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKR 256
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 257 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGP 334
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 335 VISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 414
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 24638878 415 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
36-489 |
4.66e-95 |
|
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: 295.59 E-value: 4.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 LRGLQVVEHCCSIPSLQmgetvaNVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP 192
Cdd:cd07106 81 GGAVAWLRYTASLDLPD------EVIEDDDTRRVELrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 193 GATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 272
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 273 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 350
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESIydEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 351 GVKEGAKLILDGRKITVPgyedGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTN 430
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGP----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 24638878 431 GAAARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTV 489
Cdd:cd07106 389 LERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQS--GIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
19-449 |
5.86e-95 |
|
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: 295.95 E-value: 5.86e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGktladAEGDVLRGLQVvehccsipslQMGETVANVARD-MDTY--------SLVL--PLGVTAGVAPFNFPA- 166
Cdd:cd07138 81 AITLEMG-----APITLARAAQV----------GLGIGHLRAAADaLKDFefeerrgnSLVVrePIGVCGLITPWNWPLn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 167 MIPLWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKY 245
Cdd:cd07138 146 QIVLKVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 246 IYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALsTAVFVGDAQawIPDLVERA----QKLK 321
Cdd:cd07138 225 VAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAaaaaEAYV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 322 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLV 401
Cdd:cd07138 302 VGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLS 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24638878 402 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07138 381 IIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
36-489 |
2.99e-92 |
|
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: 288.68 E-value: 2.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPG 193
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 194 ATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 272
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 273 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdaQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 347
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLV---QRSIYDefverLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:cd07114 317 VARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTV 489
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDS--G----IGREngieAIREYTQTKSV 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
17-490 |
1.29e-91 |
|
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: 287.57 E-value: 1.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSI--LTRQQVMFKLQALIKENMG 94
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTL-ADAEGDVLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 173
Cdd:cd07091 84 ELAALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdaQAWIPD-----LVERAQKLKVNAGH 326
Cdd:cd07091 243 sNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFV---QESIYDefvekFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 327 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 406
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG----SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 407 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpIPVPLPMFSFTGTRGSFRGDHhfYGKQGIKFYTQT 486
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGRE--LGEEGLEEYTQV 471
|
....
gi 24638878 487 KTVT 490
Cdd:cd07091 472 KAVT 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-491 |
4.08e-91 |
|
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: 287.58 E-value: 4.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCCSiPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 177
Cdd:cd07124 113 AWMVLEVGKNWAEADADVAEAIDFLEYYAR-EMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 178 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK---- 252
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKvqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 --NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVPG 329
Cdd:cd07124 272 qkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGaKLILDGRkiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMF-SFTGTRGSFRGdhhfyGKQG----IKFYT 484
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMSGTG-----SKAGgpdyLLQFM 503
|
....*..
gi 24638878 485 QTKTVTQ 491
Cdd:cd07124 504 QPKTVTE 510
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
36-489 |
6.77e-90 |
|
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: 282.66 E-value: 6.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 LRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT 195
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHV-PLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 196 MLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANK 275
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 276 ENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVK 353
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSN-GTRVFVQRSikDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 354 EGAKLILDGRKITV-PGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 432
Cdd:cd07090 319 EGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638878 433 AARKFVNEIDAGQVGVN----VPIPVPlpmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07090 399 RAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
20-451 |
4.78e-89 |
|
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: 280.99 E-value: 4.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTnEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 99
Cdd:cd07086 2 VIGGEWVGSGG-ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 100 ITKEQGKTLADAEGDVLRGLQVVEHCCSIpSLQM-GETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 178
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGL-SRMLyGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 179 TGNTMLLKPSERVPGATMLLMELLNEA----GCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 254
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVG 333
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLiVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 334 PVISAASRQRINDLIESGVKEGAKLILDGRKITvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIG 413
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID--GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24638878 414 IVNANPYGNGTAVFTTNGAAARKFV--NEIDAGQVGVNVP 451
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIP 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
19-490 |
5.27e-87 |
|
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: 275.61 E-value: 5.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAF--RSWSNQSILTRQQVMFKLQALIKENMGEL 96
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 97 AKNITKEQGKTLA--------------DAEGDVLRGLQVVEHccsIPSLQMGETVanVARDmdtyslvlPLGVTAGVAPF 162
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVL--VRRE--------PVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 163 NFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQA 242
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 243 GKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALsTAVFVGDAQ--AWIPDLVERAQKL 320
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRydEVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 321 KVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVL 400
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 401 VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpipvplPMFSFTGTRGSFR--GDHHFYGKQ 478
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG------FRLDFGAPFGGFKqsGIGREGGPE 458
|
490
....*....|..
gi 24638878 479 GIKFYTQTKTVT 490
Cdd:cd07139 459 GLDAYLETKSIY 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
17-489 |
1.39e-86 |
|
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: 275.06 E-value: 1.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS-WSNQSILTRQQVMFKLQALIKENMGE 95
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 96 LAKNITKEQGKTL-ADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMFP 174
Cdd:cd07144 88 LAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 175 VAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGqHDAV--NFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERA-QKLKVNAGHVPG 329
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVkQNYKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP----IPVPlpmfsFTGTRGSFRGDHhfYGKQGIKFYTQ 485
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIGRE--LGEYGLETYTQ 476
|
....
gi 24638878 486 TKTV 489
Cdd:cd07144 477 TKAV 480
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
34-490 |
1.71e-86 |
|
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: 273.70 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVLRGLQVVEHCCSIPSLQMGETV----ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 189
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 190 RVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKngKRVQSNMGAKNHGI 268
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 269 ILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 346
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDiyDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 347 LIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 426
Cdd:cd07149 318 WVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 427 FTTNGAAARKFVNEIDAGQVGVNvPIPvplpmfsftgtrgSFRGDHHFYG--------KQGIKF----YTQTKTVT 490
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIN-DSS-------------TFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-490 |
4.70e-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: 269.48 E-value: 4.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 64 KKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARD 143
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 144 MDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAV 222
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 223 NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVF 302
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 303 VGDAQAwiPDLVERAQklkvnaghvpgtdvgpvisaasrqrindliesgvkegaklildgrkitvpgyedgyfvgpTILS 382
Cdd:cd06534 243 VHESIY--DEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 383 DVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFT 462
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 24638878 463 GTRGSFRGDHHfyGKQGIKFYTQTKTVT 490
Cdd:cd06534 341 GVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-451 |
3.37e-85 |
|
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: 270.35 E-value: 3.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 35 DVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 114
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 194
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 195 TMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 273
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 274 NKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGV 352
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPvYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 353 KEGAKLIldgrkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 432
Cdd:cd07150 322 AKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410
....*....|....*....
gi 24638878 433 AARKFVNEIDAGQVGVNVP 451
Cdd:cd07150 395 RAFKLAERLESGMVHINDP 413
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
36-490 |
5.58e-85 |
|
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: 269.87 E-value: 5.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQ-SILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 114
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 194
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 195 TMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 273
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 274 NKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQA-WIPDLVERAQKLKVNAGhVPGTDVGPVISAASRQRINDLIESGV 352
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDeVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 353 KEGAKLILDGRKITVPgYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 432
Cdd:cd07109 319 ARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638878 433 AARKFVNEIDAGQVGVNVPIP---VPLPmfsFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKS--GHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
37-490 |
7.24e-85 |
|
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: 269.59 E-value: 7.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 37 HDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 114
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VlrglqvvEHCCSI----PSLQM---GETVANVARDMdtYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLL 185
Cdd:cd07118 82 I-------EGAADLwryaASLARtlhGDSYNNLGDDM--LGLVLrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 186 KPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAK 264
Cdd:cd07118 153 KPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 265 NHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQ 342
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 343 RINDLIESGVKEGAKLILDGRKItvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGN 422
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 423 GTAVFTTNGAAARKFVNEIDAGQVGVNVPIP--VPLPmfsFTGTRGSFRGDHhfYGKQGIKFYTQTKTVT 490
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGRE--LGRYGVEEYTELKTVH 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
17-489 |
1.88e-82 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 264.63 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGEL 96
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 97 AKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFP-AMIPLWMFPv 175
Cdd:PLN02278 105 AQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 176 AITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 254
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVgdaQAWIPD-----LVERAQKLKVNAGHVPG 329
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILV---QEGIYDkfaeaFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIKYV 492
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
17-489 |
2.94e-82 |
|
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: 263.62 E-value: 2.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR-SWSNQ-SILTRQQVMFKLQALIKENMG 94
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKT-LADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMF 173
Cdd:cd07143 87 YLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPG 329
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVqeGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHG----NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTV 489
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-449 |
1.59e-81 |
|
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: 260.74 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL----PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 189
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFtvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 190 RVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 268
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 269 ILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 346
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 347 LIESGVKEGAKLILDGRKItvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 426
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420
....*....|....*....|...
gi 24638878 427 FTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVIN 416
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-493 |
2.16e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 262.18 E-value: 2.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCC-SIPSLQMGETVANVARDMDTYsLVLPLGVTAGVAPFNFPAMIPLWMFPVA 176
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEYYArQMLKLADGKPVESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 177 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK--N 253
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERAAKvqP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 254 G----KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVP 328
Cdd:PRK03137 276 GqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 329 gTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKitvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 408
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 409 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpmfsfTGTRGSFRGDHHFYG--------KQG- 479
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN------------RGCTGAIVGYHPFGGfnmsgtdsKAGg 497
|
490
....*....|....*..
gi 24638878 480 ---IKFYTQTKTVTQLW 493
Cdd:PRK03137 498 pdyLLLFLQAKTVSEMF 514
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
17-490 |
2.83e-81 |
|
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: 261.13 E-value: 2.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR---SWSNQSILTRQQVMFKLQALIKENM 93
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 94 GELAKNITKEQGKTLADA-EGDVLRGLQVVEHCCSIPSLQMGETVAnvardMD----TYSLVLPLGVTAGVAPFNFPAMI 168
Cdd:cd07141 87 AYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIP-----MDgdffTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 169 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIY 247
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 248 ERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNA 324
Cdd:cd07141 242 QAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 325 GHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvPGyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILK 404
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR---HG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 405 ADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSfrGDHHFYGKQGIKFYT 484
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMS--GNGRELGEYGLQEYT 473
|
....*.
gi 24638878 485 QTKTVT 490
Cdd:cd07141 474 EVKTVT 479
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-489 |
3.02e-81 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 260.97 E-value: 3.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 12 SAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKE 91
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 92 NMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCSI-PSLQmGETVAnvARDMD-TYSLVLPLGVTAGVAPFNFPAMI 168
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLaPALE-GEQIP--LRGGSfVYTRREPLGVCAGIGAWNYPIQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 169 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYE 248
Cdd:PRK13252 159 ACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 249 RAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGH 326
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSikAAFEARLLERVERIRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 327 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 406
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 407 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYT 484
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYT 472
|
....*
gi 24638878 485 QTKTV 489
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-449 |
2.34e-80 |
|
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: 257.07 E-value: 2.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 58 AALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETV 137
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 138 ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT-MLLMELLNEAGCPPGVVNVIH 216
Cdd:cd07104 84 PSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 217 GQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCM 295
Cdd:cd07104 164 GGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 296 ALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitvpgyEDG 373
Cdd:cd07104 244 AAGR-ILVHEsvYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------YEG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 374 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-489 |
3.13e-80 |
|
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: 257.37 E-value: 3.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 38 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG-DVL 116
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 117 RGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATM 196
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 197 LLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANK 275
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 276 ENTLNQLAGAAFGAAGQRCMALSTAVfvgdAQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 350
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLL----VHESIYDeflerFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 351 GVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTN 430
Cdd:cd07115 318 GREEGARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638878 431 GAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTynRFDPGSP---FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-490 |
3.15e-78 |
|
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: 253.13 E-value: 3.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS-WSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLAdaegdVLRGLQVVEHCC-------------------SIPSLQMGETVANVARDmdtyslvlPLGVTAG 158
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEVGQSANflryfagwatkingetlapSIPSMQGERYTAFTRRE--------PVGVVAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 159 VAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPgATML-LMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFV 237
Cdd:cd07113 149 IVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 238 GSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVgdAQAWIPDLVE-- 315
Cdd:cd07113 228 GSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYV--HRSKFDELVTkl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 316 --RAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkiTVPGyeDGYFVGPTILSDVTPSMKCYTE 393
Cdd:cd07113 305 kqALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE--ALAG--EGYFVQPTLVLARSADSRLMRE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 394 EIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHh 473
Cdd:cd07113 381 ETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE- 458
|
490
....*....|....*..
gi 24638878 474 fYGKQGIKFYTQTKTVT 490
Cdd:cd07113 459 -FGSAFIDDYTELKSVM 474
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
18-449 |
1.29e-77 |
|
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: 251.34 E-value: 1.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 18 KLFIDGKFVESKtNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSN-QSILTRQQVMFKLQALIKENMGEL 96
Cdd:cd07082 3 KYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 97 AKNITKEQGKTLADAEGDVLRGLQVVEHCcsipslqmgetvANVARDMDTYSLV----------------LPLGVTAGVA 160
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDT------------IEELKRLDGDSLPgdwfpgtkgkiaqvrrEPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 161 PFNFP------AMIPlwmfpvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKA 233
Cdd:cd07082 150 PFNYPlnltvsKLIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 234 VSFVGSDQAGKYIYERAGKngKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFV--GDAQAWIP 311
Cdd:cd07082 224 ISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVheSVADELVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 312 DLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrkitvpGYEDGYFVGPTILSDVTPSMKCY 391
Cdd:cd07082 301 LLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLA 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24638878 392 TEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07082 375 WEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
56-489 |
3.70e-77 |
|
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: 248.53 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 56 MQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVlrglqvvEHCCSI------- 128
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV-------EKCAWIcryyaen 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 129 -PSLQMGETVANVARDmdtySLV--LPLGVTAGVAPFNFPamipLW-MFPVA---ITTGNTMLLKPSERVPGATMLLMEL 201
Cdd:cd07100 74 aEAFLADEPIETDAGK----AYVryEPLGVVLGIMPWNFP----FWqVFRFAapnLMAGNTVLLKHASNVPGCALAIEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 202 LNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQ 281
Cdd:cd07100 146 FREAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 282 LAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLI 359
Cdd:cd07100 226 AVKGRLQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 360 LDGRKITVPGYedgyFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVN 439
Cdd:cd07100 305 LGGKRPDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24638878 440 EIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07100 381 RLEAGMVFINGMV-KSDPRLPFGGVKRSGYGREL--GRFGIREFVNIKTV 427
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
36-489 |
1.25e-76 |
|
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: 248.31 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWS-NQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-- 112
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 113 ------GDVLRGLQVV-----EHCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGN 181
Cdd:cd07089 81 qvdgpiGHLRYFADLAdsfpwEFDLPVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 182 TMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVN--FICDaPEIKAVSFVGSDQAGKYIYERAGKNGKRVQS 259
Cdd:cd07089 153 TVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGeaLTTD-PRVDMVSFTGSTAVGRRIMAQAAATLKRVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 260 NMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVGDAQawIPDLVERaqkLKVNAGHV-------PGTDV 332
Cdd:cd07089 232 ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSR--YDEVVEA---LAAAFEALpvgdpadPGTVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 333 GPVISAASRQRINDLIESGVKEGAKLILDGRkiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAI 412
Cdd:cd07089 306 GPLISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 413 GIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpMFSFTGTRGSFRGDHHF-----YGKQGIKFYTQTK 487
Cdd:cd07089 384 RIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN--------GGGGYGPDAPFGGYKQSglgreNGIEGLEEFLETK 455
|
..
gi 24638878 488 TV 489
Cdd:cd07089 456 SI 457
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
34-490 |
2.12e-76 |
|
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: 247.35 E-value: 2.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL----PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 189
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 190 RVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSNMGAKNHGI 268
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 269 ILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 347
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSfrgdhhFYGKQGIKF----YTQTKTVT 490
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
18-449 |
2.12e-75 |
|
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: 245.72 E-value: 2.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 18 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEG-DV-LrglqVVEHCCSIPSLQMGETVANVARDMDTYSLVL--PLGVTAGVAPFNFPAMIPLWMF 173
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIpL----AIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFhePLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 NGKRVQSNMGAKNHGIILGDANKENT--------------LNQlagaafgaaGQRCMALSTAvFVGDA--QAWIPDLVER 316
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAMDADDdfddkaeegqlgfaFNQ---------GEVCTCPSRA-LVQESiyDEFIERAVER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 317 AQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIF 396
Cdd:cd07559 307 FEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIF 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24638878 397 GPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07559 387 GPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN 439
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
36-490 |
4.53e-75 |
|
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: 243.77 E-value: 4.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 LRGlqVVEH-------CCSIPSLQMGETVAnvarDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPS 188
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLP----GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 189 ERVPGATMLLMELLNEaGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHG 267
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 268 IILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIN 345
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 346 DLIEsGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTA 425
Cdd:cd07092 313 GFVE-RAPAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24638878 426 VFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMfSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTVT 490
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVM 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
34-490 |
5.73e-73 |
|
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: 238.41 E-value: 5.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESnkkafrSWSNQSILTRQQ---VMFKLQALIKENMGELAKNITKEQGKTLAD 110
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 111 AEGDVLRGLQVVEHCCSIPSLQMGET----VANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLK 186
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRDDGESfscdLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 187 PSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSNMGAKN 265
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 266 HGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQR 343
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 344 INDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNG 423
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24638878 424 TAVFTTNGAAARKFVNEIDAGQVGVNvpiPVP---LPMFSFTGTRGSFRGdhhfyGKQG----IKFYTQTKTVT 490
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGvreaMKEMTNVKTYS 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
36-491 |
1.21e-72 |
|
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: 237.63 E-value: 1.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE--- 112
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 113 GDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP 192
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 193 GATMLLMELLNEAGCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILG 271
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 272 DANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIE 349
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 350 SGVKEGAKLILDGRkitVP-GYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFT 428
Cdd:cd07110 320 RGKEEGARLLCGGR---RPaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638878 429 TNGAAARKFVNEIDAGQVGVNVPIPVpLPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTVTQ 491
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGRE--LGEWGLDNYLEVKQITR 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
18-489 |
2.19e-72 |
|
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: 237.74 E-value: 2.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 18 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEG-DVLRGlqvVEHCCSIPSLQMGETVANVARDMDTYSLVL--PLGVTAGVAPFNFPAMIPLWMFP 174
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLA---ADHFRYFAGVIRAEEGSANMIDEDTLSIVLrePIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 175 VAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKN 253
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 254 GKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTD 331
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVqeGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 332 VGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDA 411
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 412 IGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRG-DHHfygKQGIKFYTQTKT 488
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGrETH---KSMLDAYTQMKN 470
|
.
gi 24638878 489 V 489
Cdd:cd07117 471 I 471
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
36-490 |
2.83e-72 |
|
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: 236.87 E-value: 2.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTL-ADAEGD 114
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 194
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 195 TMLLMELLNEAgCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 273
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 274 NKENTLNQ-LAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 350
Cdd:cd07108 239 DLDDAVDGaIAGMRFTRQGQSCTAGSR-LFVHEDiyDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 351 GVKE-GAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTT 429
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638878 430 NGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHhfYGKQG-IKFYTQTKTVT 490
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
36-490 |
2.94e-72 |
|
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: 236.89 E-value: 2.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 LRGLQVVEHCCSIPSLQMGETVANVARDMDtYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT 195
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLH-YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 196 MLLMELLNEAgCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDAN 274
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 275 KENTLNQLAGAAFGA-AGQRCMALSTAvFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESG 351
Cdd:cd07107 239 PEAAADAAVAGMNFTwCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 352 VKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNG 431
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 432 AAARKFVNEIDAGQVGVN--------VPipvplpmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTVT 490
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIGREE--CLEELLSYTQEKNVN 453
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
19-493 |
4.20e-72 |
|
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: 237.84 E-value: 4.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:TIGR01237 35 LVINGERVE--TENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCC-SIPSLQMGETVANVARDMDTYsLVLPLGVTAGVAPFNFPAMIPLWMFPVA 176
Cdd:TIGR01237 113 ALLVKEVGKPWNEADAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQY-VYTPTGVTVVISPWNFPFAIMVGMTVAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 177 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK--- 252
Cdd:TIGR01237 192 IVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVgDYLVDHPKTSLITFTGSREVGTRIFERAAKvqp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 ---NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVP 328
Cdd:TIGR01237 272 gqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVyDEVVERFVEITESLKVGPPDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 329 GTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKitvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 408
Cdd:TIGR01237 352 DVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCG----DDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 409 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP------VPLPMFSFTGTrGSFRGdhhfyGKQGIKF 482
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITgaivgyQPFGGFKMSGT-DSKAG-----GPDYLAL 500
|
490
....*....|.
gi 24638878 483 YTQTKTVTQLW 493
Cdd:TIGR01237 501 FMQAKTVTEMF 511
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
31-489 |
4.21e-72 |
|
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: 236.34 E-value: 4.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 31 NEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTL 108
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 109 ADAEGDVLRGlqvVEHCC-----SIPSLqMGEtVANVARDMdtYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGN 181
Cdd:cd07112 81 SDALAVDVPS---AANTFrwyaeAIDKV-YGE-VAPTGPDA--LALITrePLGVVGAVVPWNFPLLMAAWKIAPALAAGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 182 TMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK-NGKRVQS 259
Cdd:cd07112 154 SVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 260 NMGAKNHGIILGDANK-----ENTL-----NQlagaafgaaGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVP 328
Cdd:cd07112 234 ECGGKSPNIVFADAPDldaaaEAAAagifwNQ---------GEVCSAGSRLlVHESIKDEFLEKVVAAAREWKPGDPLDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 329 GTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 408
Cdd:cd07112 305 ATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 409 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN----VPIPVPlpmfsFTGTRGSfrGDHHFYGKQGIKFYT 484
Cdd:cd07112 383 EEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQS--GNGRDKSLHALDKYT 455
|
....*
gi 24638878 485 QTKTV 489
Cdd:cd07112 456 ELKTT 460
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-490 |
7.05e-72 |
|
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: 236.05 E-value: 7.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 23 GKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITK 102
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 103 EQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNT 182
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 183 MLLKPSERVP--GATmLLMELLNEAGCPPGVVNVIHGqhdAVNFICDA----PEIKAVSFVGSDQAGKYIYERAGKNGKR 256
Cdd:cd07151 161 VVLKPASDTPitGGL-LLAKIFEEAGLPKGVLNVVVG---AGSEIGDAfvehPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 257 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQA--WIPDLVERAQKLKVNAGHVPGTDVGP 334
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDVYdeFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 335 VISAASRQRINDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 414
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 415 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvPIPV-PLPMFSFTGTRGSFRGdhHFYGKQGIKFYTQTKTVT 490
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNSGLG--RFNGEWALEEFTTDKWIS 462
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
34-481 |
8.93e-71 |
|
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: 232.52 E-value: 8.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVLRgLQVVEHCCSIPSLQMGETVAnvarDMDTYS-------LV--LPLGVTAGVAPFNFPamIPLWMFPV--AITTGNT 182
Cdd:cd07147 81 EVAR-AIDTFRIAAEEATRIYGEVL----PLDISArgegrqgLVrrFPIGPVSAITPFNFP--LNLVAHKVapAIAAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 183 MLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQH-DAVNFICDaPEIKAVSFVGSDQAGKYIYERAGKngKRVQSNM 261
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRdDADLLVTD-ERIKLLSFTGSPAVGWDLKARAGK--KKVVLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 262 GAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAA 339
Cdd:cd07147 231 GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKTGDPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 340 SRQRINDLIESGVKEGAKLIldgrkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP 419
Cdd:cd07147 310 EAERVEGWVNEAVDAGAKLL-------TGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638878 420 YGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPipvplpmfsftgtrgSFRGDHHFYGkqGIK 481
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG--GVK 428
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-490 |
1.20e-70 |
|
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: 231.70 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGET 136
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 137 VANVARDmdTYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNV 214
Cdd:cd07105 83 IPSDKPG--TLAMVVkePVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 215 IHGQ----HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAA 290
Cdd:cd07105 161 VTHSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 291 GQRCMalSTA-VFVGD--AQAWIPDLVERAQKLKvnAGHVPgtdVGPVISAASRQRINDLIESGVKEGAKLILDGRKITV 367
Cdd:cd07105 241 GQICM--STErIIVHEsiADEFVEKLKAAAEKLF--AGPVV---LGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 368 PgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVG 447
Cdd:cd07105 314 P---SGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24638878 448 VNVPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07105 391 INGMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
43-449 |
6.23e-70 |
|
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: 230.26 E-value: 6.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 43 QVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVV 122
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 123 EHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT-MLLMEL 201
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 202 LNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQ 281
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 282 LAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLIL 360
Cdd:cd07152 241 GAWGAFLHQGQICMAAGRHlVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 361 DGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNE 440
Cdd:cd07152 321 GGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
....*....
gi 24638878 441 IDAGQVGVN 449
Cdd:cd07152 394 LRTGMLHIN 402
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
16-453 |
8.59e-66 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 220.17 E-value: 8.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 16 TTKLFIDGKFVESKTNEWiDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGE 95
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 96 LAKNITKEQGK----TLAD---AEGDVLRGLQVVEHCCSIPSlqMGETVAN----VARDmdtyslvlPLGVTAGVAPFNF 164
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRFFAGAARCLEGKA--AGEYLEGhtsmIRRD--------PVGVVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 165 PAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAG 243
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 244 KYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLK 321
Cdd:PRK13473 230 KHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 322 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKItVPGyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLV 401
Cdd:PRK13473 309 VGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEA-PDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVS 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24638878 402 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP 453
Cdd:PRK13473 386 VTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
17-489 |
1.72e-65 |
|
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: 219.67 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILTRQQVMFKLQALIKENMG 94
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMF 173
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHH-VYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPG 329
Cdd:cd07142 243 sNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHESiyDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-491 |
2.06e-64 |
|
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: 216.06 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 38 DPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILtRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 115
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 lRGlqvvehccSIPSLQMgetVANVARDM---------DTYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 184
Cdd:cd07120 82 -SG--------AISELRY---YAGLARTEagrmiepepGSFSLVLrePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 185 LKPSERVPGATMLLMELLNEA-GCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMG 262
Cdd:cd07120 150 VKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 263 AKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASR 341
Cdd:cd07120 230 GKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVlVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 342 QRINDLIESGVKEGAKLILDGRKITvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYG 421
Cdd:cd07120 310 DRVDRMVERAIAAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 422 NGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVpLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 491
Cdd:cd07120 389 LAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIYL 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-491 |
4.02e-64 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 216.52 E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 12 SAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAF-----RSWSNQSILTRQQVMFKLQ 86
Cdd:PLN02467 3 IPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 87 ALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTY-SLVL--PLGVTAGVAPFN 163
Cdd:PLN02467 83 AKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFkGYVLkePLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 164 FPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQA 242
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 243 GKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKL 320
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 321 KVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVL 400
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 401 VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP--VPLPmfsFTGTRGSFRGDHhfYGKQ 478
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPcfCQAP---WGGIKRSGFGRE--LGEW 474
|
490
....*....|...
gi 24638878 479 GIKFYTQTKTVTQ 491
Cdd:PLN02467 475 GLENYLSVKQVTK 487
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
37-490 |
2.08e-63 |
|
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: 213.24 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 37 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL 116
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 117 RGLQVVEHCCSI-----------PSLQMGETVANVARdmdtyslvLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLL 185
Cdd:cd07099 81 LALEAIDWAARNaprvlaprkvpTGLLMPNKKATVEY--------RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 186 KPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDApEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKN 265
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 266 HGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQR 343
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 344 INDLIESGVKEGAKLILDGRKITVpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNG 423
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNG----GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638878 424 TAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 490
Cdd:cd07099 387 ASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-489 |
2.98e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 214.30 E-value: 2.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILTRQQVMFKLQALIKENMG 94
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTLADAEG-DVLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 173
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 252
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 253 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPG 329
Cdd:PLN02766 260 sNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVqeGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTV 489
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFD-PDCPFGGYKMSGFGRD--QGMDALDKYLQVKSV 491
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-490 |
1.03e-62 |
|
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: 211.77 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 37 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDV 115
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 116 L-----------RGLQVVEHCCSIPSLQMGETVANVardmdTYSlvlPLGVTAGVAPFNFP------AMIPlwmfpvAIT 178
Cdd:cd07098 81 LvtcekirwtlkHGEKALRPESRPGGLLMFYKRARV-----EYE---PLGVVGAIVSWNYPfhnllgPIIA------ALF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 179 TGNTMLLKPSERVPGATMLLMELLNEA----GCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 254
Cdd:cd07098 147 AGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDV 332
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKIydKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 333 GPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAI 412
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 413 GIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN----VPIPVPLPmfsFTGTRGSfrGDHHFYGKQGIKFYTQTKT 488
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQLP---FGGVKGS--GFGRFAGEEGLRGLCNPKS 460
|
..
gi 24638878 489 VT 490
Cdd:cd07098 461 VT 462
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
39-470 |
2.82e-61 |
|
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: 207.48 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 39 PATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRG 118
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 119 LQVVEHCCSIP--SL--QMGETVANVARdmdtYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 194
Cdd:cd07102 83 LERARYMISIAeeALadIRVPEKDGFER----YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 195 TMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDAN 274
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 275 KENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGV 352
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 353 KEGAKLILDGRKITVPGyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 432
Cdd:cd07102 318 AKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 24638878 433 AARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSFRG 470
Cdd:cd07102 397 RAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-449 |
7.57e-61 |
|
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: 207.25 E-value: 7.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 2 ARHLAKRSYSSAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQV 81
Cdd:cd07111 7 SAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 82 MFKLQALIKENMGELAKNITKEQGKTLADA-EGDVLRGLQVVEHCCSIPSLQmgetvanvARDMDTYSlvlPLGVTAGVA 160
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL--------DTELAGWK---PVGVVGQIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 161 PFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSD 240
Cdd:cd07111 156 PWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 241 QAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALST-AVFVGDAQAWIPDLVERAQK 319
Cdd:cd07111 236 EVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRlLVQESVAEELIRKLKERMSH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 320 LKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPV 399
Cdd:cd07111 316 LRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24638878 400 LVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07111 392 LVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-472 |
2.33e-60 |
|
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: 204.81 E-value: 2.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 58 AALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEhcCSIPSLQmgETV 137
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID--ISIKAYH--ERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 138 ANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNV 214
Cdd:cd07095 80 GERATPMAQGRAVLrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 215 IHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYER-AGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQR 293
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 294 CMALSTAVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyE 371
Cdd:cd07095 240 CTCARRLIVPDGAVgdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----A 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 372 DGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP 451
Cdd:cd07095 316 GTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410 420
....*....|....*....|....
gi 24638878 452 I---PVPLPmfsFTGTRGSfrGDH 472
Cdd:cd07095 395 TtgaSSTAP---FGGVGLS--GNH 413
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
17-490 |
4.43e-60 |
|
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: 205.42 E-value: 4.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 94
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGK--TLAdAEGDVLRGLQVVEH----CCSIpslqMGETVA-NVARDMD--TYSLVLPLGVTAGVAPFNFP 165
Cdd:cd07140 86 ELATIESLDSGAvyTLA-LKTHVGMSIQTFRYfagwCDKI----QGKTIPiNQARPNRnlTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 166 AMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGK 244
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 245 YIYERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLK 321
Cdd:cd07140 241 HIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 322 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPgyedGYFVGPTILSDVTPSMKCYTEEIFGPVLV 401
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDVEDHMFIAKEESFGPIMI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 402 ILKADT--LDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHhfYGK 477
Cdd:cd07140 396 ISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAP---FGGFKQSGFGKD--LGE 470
|
490
....*....|...
gi 24638878 478 QGIKFYTQTKTVT 490
Cdd:cd07140 471 EALNEYLKTKTVT 483
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
17-449 |
7.92e-60 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 205.13 E-value: 7.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 94
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGK----TLADAEGDVLRGL----QVVEHCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPA 166
Cdd:PRK09847 100 ELALLETLDTGKpirhSLRDDIPGAARAIrwyaEAIDKVYGEVATTSSHELAMIVRE--------PVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 167 MIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKY 245
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 246 IYERAGK-NGKRVQSNMGAKNHGIILGDA-NKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLK 321
Cdd:PRK09847 252 LLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 322 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKITVPGYedgyfVGPTILSDVTPSMKCYTEEIFGPVLV 401
Cdd:PRK09847 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24638878 402 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
82-489 |
8.34e-60 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 202.66 E-value: 8.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 82 MFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAP 161
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 162 FNFPA-MIPLWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGS 239
Cdd:PRK10090 81 WNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 240 DQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRC-MALSTAVFVGDAQAWIPDLVERAQ 318
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 319 KLKV-NAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFG 397
Cdd:PRK10090 240 AVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 398 PVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpmfsftgtRGSFRGDHHFY-- 475
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHag 380
|
410 420
....*....|....*....|....
gi 24638878 476 ----------GKQGIKFYTQTKTV 489
Cdd:PRK10090 381 wrksgiggadGKHGLHEYLQTQVV 404
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-449 |
2.47e-58 |
|
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: 201.27 E-value: 2.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVESKTNEWIdVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:cd07083 21 LVIGGEWVDTKERMVS-VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL-PLGVTAGVAPFNFPAMIPLWMFPVAI 177
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYvGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 178 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNG-- 254
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 ----KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPD-LVERAQKLKVNAGHVPG 329
Cdd:cd07083 260 qtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLErLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGaKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVL--VILKADT 407
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGPVLsvIRYKDDD 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24638878 408 LDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07083 415 FAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
20-487 |
1.84e-57 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 198.21 E-value: 1.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 99
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 100 ITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFP-AMIPLWMFPvAIT 178
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 179 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 257
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 258 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPV 335
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC-ANRLYVQDGvyDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 336 ISAASRQRINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIV 415
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638878 416 NANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTK 487
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-489 |
3.13e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 194.57 E-value: 3.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 38 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL- 116
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 117 --RGLQ-VVEHCcsiPSLQMGETvANVARDMDTYSLVL--PLGVTAGVAPFNFPamipLWM---FPV-AITTGNTMLLKP 187
Cdd:PRK09406 87 caKGFRyYAEHA---EALLADEP-ADAAAVGASRAYVRyqPLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 188 SERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHG 267
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 268 IILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 346
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADvYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 347 LIESGVKEGAKLILDGRKITVPGYedgyFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 426
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 427 FTTNGAAARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTV 489
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
20-449 |
1.92e-55 |
|
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: 193.05 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 99
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 100 ITKEQGK----TLAdaeGDVLRGLQVVEHCCSIPSLQMGeTVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPV 175
Cdd:cd07116 84 ETWDNGKpvreTLA---ADIPLAIDHFRYFAGCIRAQEG-SISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 176 AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 254
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKEN--------------TLNQlagaafgaaGQRCMALSTAVFVGDA-QAWIPDLVERAQK 319
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDADdaffdkalegfvmfALNQ---------GEVCTCPSRALIQESIyDRFMERALERVKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 320 LKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDvTPSMKCYTEEIFGPV 399
Cdd:cd07116 310 IKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPV 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24638878 400 LVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07116 389 LAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-449 |
1.52e-54 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 190.07 E-value: 1.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 38 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLR 117
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 118 GLQV----VEHCcsiPSlqMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPamipLWMF-----PVaITTGNTMLLKPS 188
Cdd:PRK13968 93 SANLcdwyAEHG---PA--MLKAEPTLVENQQAVIEYRPLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 189 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 268
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 269 ILGDANKENTLNQLAGAAFGAAGQRCMALSTAVF-VGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 347
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420
....*....|....*....|..
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVN 449
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
37-491 |
4.59e-54 |
|
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: 188.67 E-value: 4.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 37 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL 116
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 117 --------------RGLQVVEHCCSIPSLqmGETVANVArdmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNT 182
Cdd:cd07101 81 dvaivaryyarraeRLLKPRRRRGAIPVL--TRTTVNRR----------PKGVVGVISPWNYPLTLAVSDAIPALLAGNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 183 MLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVnficdAPEIKA----VSFVGSDQAGKYIYERAGKNGKRVQ 258
Cdd:cd07101 149 VVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEV-----GGAIVDnadyVMFTGSTATGRVVAERAGRRLIGCS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 259 SNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVI 336
Cdd:cd07101 224 LELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 337 SAASRQRINDLIESGVKEGAKLILDGRKITVPGyedGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 416
Cdd:cd07101 303 SQAQLDRVTAHVDDAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 417 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpipvplpmfSFTGTRGSF---------RGDHHFYGKQGIKFYTQTK 487
Cdd:cd07101 380 DTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE---------GYAAAWASIdapmggmkdSGLGRRHGAEGLLKYTETQ 450
|
....
gi 24638878 488 TVTQ 491
Cdd:cd07101 451 TVAV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
17-489 |
1.80e-53 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 188.86 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 94
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTLADAEGdvlrglqvvehcCSIPSlqmgetvanVARDMDTYS---------------------LVLPL 153
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAK------------AELPM---------FARLFRYYAgwadkihgltvpadgphhvqtLHEPI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 154 GVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIK 232
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 233 AVSFVGSDQAGKYIYERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALS-TAV-------FV 303
Cdd:PLN02466 277 KLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrTFVhervydeFV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 304 GDAQAwipdlveRAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSD 383
Cdd:PLN02466 357 EKAKA-------RALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 384 VTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN------VPIPvplp 457
Cdd:PLN02466 426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP---- 501
|
490 500 510
....*....|....*....|....*....|..
gi 24638878 458 mfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:PLN02466 502 ---FGGYKMSGIGREK--GIYSLNNYLQVKAV 528
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
20-452 |
4.37e-52 |
|
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: 184.71 E-value: 4.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKfvESKTNEWIDVHDPATNQVVT-RVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPADHERTIgEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGKTLADAEGDV------LR----GLQVVEHCCSIPSLQmGETvanvardmDTYSLVlPLGVTAGVAPFNFPAMI 168
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfCRyyaaQARELFSDPELPGPT-GEL--------NGLELH-GRGVFVCISPWNFPLAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 169 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVI------HGQHdavnfICDAPEIKAVSFVGSDQA 242
Cdd:cd07125 184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 243 GKYIYE-RAGKNGKRVQSN--MGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQ 318
Cdd:cd07125 259 AKLINRaLAERDGPILPLIaeTGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 319 KLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEgAKLIldgrKITVPGYEDGYFVGPTILSDVTPSmkCYTEEIFGP 398
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLI----APAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGP 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 399 VLVIL--KADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI 452
Cdd:cd07125 412 ILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
17-449 |
3.08e-51 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 181.50 E-value: 3.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 17 TKLFIDGKFVESKTNEWIDVhDPATNQVVTRVPKATQAEMQAALESNKKAF--RSWSNQSILtRQQVMFKLQALIKENMG 94
Cdd:TIGR04284 1 SRLLIDGKLVAGSAGTFPTV-NPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 95 ELAKNITKEQGKTLADAEGDVLRG-LQVVEHCCSIPSLQMGETVANVARDM--DTYSLVL--PLGVTAGVAPFNFPAMIP 169
Cdd:TIGR04284 79 ELRELTIAEVGAPRMLTAGAQLEGpVDDLGFAADLAESYAWTTDLGVASPMgiPTRRTLRreAVGVVGAITPWNFPHQIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 170 LWMFPVAITTGNTMLLKPSERVPGATMLLMELLNE-AGCPPGVVNVI-HGQHDAVNFICDAPEIKAVSFVGSDQAGKYIY 247
Cdd:TIGR04284 159 LAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATGRAVM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 248 ERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVgdAQAWIPDLVERAQK----LKVN 323
Cdd:TIGR04284 239 ADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGC-AITTRLVV--PRARYDEAVAAAAAtmgsIKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 324 AGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrkiTVP-GYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVI 402
Cdd:TIGR04284 316 DPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGG---GRPaDRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24638878 403 LKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:TIGR04284 393 IAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
34-491 |
6.81e-48 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 173.53 E-value: 6.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVL--------------RGLQVVEHCCSIPSLqmgeTVANVARDmdtyslvlPLGVTAGVAPFNFPA------MIPlwmf 173
Cdd:PRK09407 114 EVLdvaltaryyarrapKLLAPRRRAGALPVL----TKTTELRQ--------PKGVVGVISPWNYPLtlavsdAIP---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 174 pvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVnficdAPEIKA----VSFVGSDQAGKYIYER 249
Cdd:PRK09407 178 --ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV-----GTALVDnadyLMFTGSTATGRVLAEQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 250 AGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHV 327
Cdd:PRK09407 251 AGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-IYVHEsiYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 328 PGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvpgYED-G-YFVGPTILSDVTPSMKCYTEEIFGPVLVILKA 405
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKA-----RPDlGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 406 DTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI-----PVPLPMfsfTGTRGSFRGDHHfyGKQGI 480
Cdd:PRK09407 405 ADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYaaawgSVDAPM---GGMKDSGLGRRH--GAEGL 479
|
490
....*....|.
gi 24638878 481 KFYTQTKTVTQ 491
Cdd:PRK09407 480 LKYTESQTIAT 490
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
19-452 |
1.58e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 171.68 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVESKTNEwIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 98
Cdd:PRK09457 3 LWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 99 NITKEQGKTLADAEGDVlrGLQVVEHCCSIPSLQmgETVANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPV 175
Cdd:PRK09457 82 VIARETGKPLWEAATEV--TAMINKIAISIQAYH--ERTGEKRSEMADGAAVLrhrPHGVVAVFGPYNFPGHLPNGHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 176 AITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYER-AGKNG 254
Cdd:PRK09457 158 ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 255 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD---AQAWIPDLVERAQKLKVNAGHV-PGT 330
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQgaqGDAFLARLVAVAKRLTVGRWDAePQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 331 DVGPVISAASRQRI----NDLIESgvkeGAKLILDGRKITvpgyEDGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKAD 406
Cdd:PRK09457 317 FMGAVISEQAAQGLvaaqAQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYD 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24638878 407 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI 452
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPL 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
18-488 |
1.40e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 169.17 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 18 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 97
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 98 KNITKEQGKTLADAEGDVLRGLQVVEHCCS--IPSLQMGETVANVA---RDMDTYSLV--LPLGVTAGVAPFNFPAMIPL 170
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEegVRILGEGKFLVSDSfpgNERNKYCLTskIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 171 WMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDqAGKYIYER 249
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 250 AGKngKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALS-TAVFVGDAQAWIPDLVERAQKLKVNAGHvP 328
Cdd:PLN00412 256 AGM--VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKvVLVMESVADALVEKVNAKVAKLTVGPPE-D 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 329 GTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 408
Cdd:PLN00412 333 DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 409 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPiPVPLP-MFSFTGTRGSfrgdhhFYGKQGIK----FY 483
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQGITnsinMM 478
|
....*
gi 24638878 484 TQTKT 488
Cdd:PLN00412 479 TKVKS 483
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
34-482 |
2.00e-45 |
|
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: 165.28 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQ-SILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE 112
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 113 GDVLRGLQVVEHCCSIPSLQ------MGETVANVARDmdTYSLVLPLGVTAGVAPFNFPA-MIPLWMFPvAITTGNTMLL 185
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLggreipMGLTPASAGRI--AFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 186 KPSERVPGATMLLMELLNEAGCPPGVVN-VIHGQHDAVNFICDaPEIKAVSFVGSDQAGKYIYERAGKnGKRVqsnmgAK 264
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC-----AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 265 NHG-----IILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVIS 337
Cdd:cd07148 231 EHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR-VFVPAeiADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 338 AASRQRINDLIESGVKEGAKLILDGRKITVPGYEdgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNA 417
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24638878 418 NPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSfrGdhhfYGKQGIKF 482
Cdd:cd07148 384 LPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
34-451 |
1.46e-44 |
|
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: 163.15 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 34 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DV----------------LRGLqvvehccSIPSLQMGEtvanvaRDMDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAI 177
Cdd:cd07130 94 EVqemidicdfavglsrqLYGL-------TIPSERPGH------RMMEQWN---PLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 178 TTGNTMLLKPSERVP----GATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKN 253
Cdd:cd07130 158 VCGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 254 GKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQAwiPDLVERAQKL--KVNAGH--VPG 329
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHESIY--DEVLERLKKAykQVRIGDplDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYedgyFVGPTILSdVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN----YVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 24638878 410 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEI--DAGQVGVNVP 451
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-449 |
5.93e-37 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 145.73 E-value: 5.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 6 AKRSYSSAAPttklFIDGkfveskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFK 84
Cdd:PRK11904 546 FLEKQWQAGP----IING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILER 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 85 LQALIKENMGELAKNITKEQGKTLADAEGDVlRglqvvehccsipslqmgETV------ANVARDMDTYSLVLP------ 152
Cdd:PRK11904 616 AADLLEANRAELIALCVREAGKTLQDAIAEV-R-----------------EAVdfcryyAAQARRLFGAPEKLPgptges 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 153 -------LGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NF 224
Cdd:PRK11904 678 nelrlhgRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 225 ICDAPEIKAVSFVGSDQAGKYIyER--AGKNGKRV--------QSNMgaknhgIILGDANKENTLNQLAGAAFGAAGQRC 294
Cdd:PRK11904 758 LTADPRIAGVAFTGSTETARII-NRtlAARDGPIVpliaetggQNAM------IVDSTALPEQVVDDVVTSAFRSAGQRC 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 295 MALStAVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESgVKEGAKLILdgrKITVP-GYE 371
Cdd:PRK11904 831 SALR-VLFVQEdiADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLA---QLPLPaGTE 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 372 DGYFVGPTILSdvTPSMKCYTEEIFGPVL--VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:PRK11904 906 NGHFVAPTAFE--IDSISQLEREVFGPILhvIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
36-449 |
4.93e-34 |
|
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: 134.27 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPATNQ-VVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 114
Cdd:TIGR01238 55 VTNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VLrglQVVEHCcsipslqmgETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 194
Cdd:TIGR01238 135 VR---EAVDFC---------RYYAKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 195 TMLLMELLNEAGCPPGVVNVIHGQHDAVN-FICDAPEIKAVSFVGSDQAGKYIYERAGKNGK---RVQSNMGAKNHGIIL 270
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 271 GDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERA-QKLKVNAGHVPGTDVGPVISAASRQRINDLIE 349
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 350 SgVKEGAKLILDGRKITVPGYEDGYFVGPTILSdvTPSMKCYTEEIFGPVL--VILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:TIGR01238 363 H-MSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVH 439
|
410 420
....*....|....*....|..
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVN 449
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGNCYVN 461
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
64-491 |
4.95e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 134.39 E-value: 4.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 64 KKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCS-IPSLQMGETV--AN 139
Cdd:PTZ00381 17 KESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKhLDEYLKPEKVdtVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 140 VARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQH 219
Cdd:PTZ00381 97 VFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 220 DAVNFICDAPeIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALST 299
Cdd:PTZ00381 176 EVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 300 aVFVGDA--QAWIPDLverAQKLKVNAGHVPGT--DVGPVISAASRQRINDLIESgvkegaklilDGRKITVPGYED--G 373
Cdd:PTZ00381 255 -VLVHRSikDKFIEAL---KEAIKEFFGEDPKKseDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEVDieN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 374 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI- 452
Cdd:PTZ00381 321 KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVf 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24638878 453 ---PVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 491
Cdd:PTZ00381 401 hllNPNLP---FGGVGNSGMGAYH--GKYGFDTFSHPKPVLN 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
19-440 |
7.09e-34 |
|
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: 134.25 E-value: 7.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKfvESKTNEWIDVHDPAT-NQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALI--KENMGE 95
Cdd:cd07123 35 LVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 96 LAKNITKeQGKTLADAEGDV-------LRglQVVEHCCSIPSLQMGETVANVARDMDtYSlvlPL-GVTAGVAPFNFPAM 167
Cdd:cd07123 113 NAATMLG-QGKNVWQAEIDAacelidfLR--FNVKYAEELYAQQPLSSPAGVWNRLE-YR---PLeGFVYAVSPFNFTAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 168 ------IPLWMfpvaittGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSD 240
Cdd:cd07123 186 ggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 241 QAGKYIYERAG------KNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALStavfvgdaQAWIPD-- 312
Cdd:cd07123 259 PTFKSLWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAS--------RAYVPEsl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 313 -------LVERAQKLKVnaGHVP--GTDVGPVISAASRQRINDLIESGVKE-GAKLILDGRkitvpgYED--GYFVGPTI 380
Cdd:cd07123 331 wpevkerLLEELKEIKM--GDPDdfSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK------CDDsvGYFVEPTV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638878 381 LSDVTPSMKCYTEEIFGPVLVIL--KADTLDDAIGIVN-ANPYGNGTAVFttngAAARKFVNE 440
Cdd:cd07123 403 IETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDtTSPYALTGAIF----AQDRKAIRE 461
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
54-489 |
5.40e-33 |
|
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: 130.42 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 54 AEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGK-----TLAD---AEGDVLRGLQVVE-- 123
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRppfetLLTEvsgVKNDILHMLKNLKkw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 124 ---HCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLME 200
Cdd:cd07135 85 akdEKVKDGPLAFMFGKPRIRKE--------PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 201 LLNEAgCPPGVVNVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 272
Cdd:cd07135 157 LVPKY-LDPDAFQVVQG---------GVPETTAlleqkfdkIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 273 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQAwiPDLVERAQKlkVNAGHVPG-----TDVGPVISAASRQRINDL 347
Cdd:cd07135 227 ADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSVY--DEFVEELKK--VLDEFYPGganasPDYTRIVNPRHFNRLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IEsgvKEGAKLILDGRKItvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 427
Cdd:cd07135 302 LD---TTKGKVVIGGEMD-----EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIF 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638878 428 TTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07135 374 TDDKSEIDHILTRTRSGGVVINdTLIHVGVDNAPFGGVGDSGYGAYH--GKYGFDTFTHERTV 434
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
19-436 |
5.31e-32 |
|
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: 129.13 E-value: 5.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 19 LFIDGKFVeSKTNEWIDVHDPATNQ-VVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIK-ENMGEL 96
Cdd:TIGR01236 34 LVIGGEEV-YDSNERIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSgPYRYEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 97 AKNITKEQGKTLADAEGDVLRGLQ---------VVEHCCSIPSLQMGETVANVARDMDtyslvlplGVTAGVAPFNFPAM 167
Cdd:TIGR01236 113 LAATMLGQSKTVYQAEIDAVAELIdffrfnvkyARELYAQQPISAPGEWNRTEYRPLE--------GFVYAISPFNFTAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 168 ------IPLWMfpvaittGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDA-PEIKAVSFVGSD 240
Cdd:TIGR01236 185 agnlagAPALM-------GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLAdPDLAGIHFTGST 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 241 QAGKYIYERAGKN-GK-----RVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAvFVGDA--QAWIPD 312
Cdd:TIGR01236 258 NTFKHLWKKVAQNlDRyhnfpRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRL-YVPHSkwPEFKSD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 313 LVERAQKLKVnaghVPGTDV----GPVISAASRQRINDLIESGVKEGAKL-ILDGRKitvpgYED--GYFVGPTILSDVT 385
Cdd:TIGR01236 337 LLAELQSVKV----GDPDDFrgfmGAVIDEQSFDKIVKYIEDAKKDPEALtILYGGK-----YDDsqGYFVEPTVVESKD 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 24638878 386 PSMKCYTEEIFGPVL-VILKADTLDDAIG--IVNANPYGNGTAVFTTNGAAARK 436
Cdd:TIGR01236 408 PDHPLMSEEIFGPVLtVYVYPDDKYKEILdlVDSTSQYGLTGAVFAKDRKAILE 461
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
57-449 |
5.88e-31 |
|
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: 124.56 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHC---------- 125
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHAlkhlkkwmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 126 --CSIPSLQMGETvANVARDmdtyslvlPLGVTAGVAPFNFP---AMIPLwmfpV-AITTGNTMLLKPSERVPGATMLLM 199
Cdd:cd07087 81 rrVSVPLLLQPAK-AYVIPE--------PLGVVLIIGPWNYPlqlALAPL----IgAIAAGNTVVLKPSELAPATSALLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 200 ELLNEAgCPPGVVNVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILG 271
Cdd:cd07087 148 KLIPKY-FDPEAVAVVEG---------GVEVATAllaepfdhIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 272 DANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdAQAWIPDLVERAQKlKVNA--GHVPG--TDVGPVISAASRQRINDL 347
Cdd:cd07087 218 DANLEVAARRIAWGKFLNAGQTCIAPDY-VLV--HESIKDELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 348 IESGvkegaklildgrKITVPGYED--GYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP-----Y 420
Cdd:cd07087 294 LDDG------------KVVIGGQVDkeERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY 361
|
410 420
....*....|....*....|....*....
gi 24638878 421 gngtaVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07087 362 -----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
36-421 |
6.52e-31 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 127.67 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 36 VHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 114
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 115 VlRglqvvehccsipslqmgETV------ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPS 188
Cdd:PRK11905 651 V-R-----------------EAVdflryyAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPA 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 189 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIY----ERAGKNGKRVqSNMGA 263
Cdd:PRK11905 713 EQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQrtlaKRSGPPVPLI-AETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 264 KNHGIILGDANKENTLNQLAGAAFGAAGQRCMALStAVFVGD--AQAWIPDLVERAQKLKV-NAGHVPgTDVGPVISAAS 340
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALR-VLCLQEdvADRVLTMLKGAMDELRIgDPWRLS-TDVGPVIDAEA 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 341 RQRINDLIESGVKEGAKLildgRKITVP-GYEDGYFVGPTI-----LSDVtpsmkcyTEEIFGPVLVIL--KADTLDDAI 412
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLV----HQLPLPaETEKGTFVAPTLieidsISDL-------EREVFGPVLHVVrfKADELDRVI 938
|
....*....
gi 24638878 413 GIVNANPYG 421
Cdd:PRK11905 939 DDINATGYG 947
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
38-451 |
3.93e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 123.41 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 38 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLR 117
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 118 GLQVVEHCCSIpSLQMGETVANVARD----MDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP- 192
Cdd:PLN02315 120 IIDMCDFAVGL-SRQLNGSIIPSERPnhmmMEVWN---PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPl 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 193 ---GATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII 269
Cdd:PLN02315 196 itiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 270 LGDANKENTLNQLAGAAFGAAGQRC-----MALSTAVFvgdaQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRI 344
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCttcrrLLLHESIY----DDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 345 NDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGT 424
Cdd:PLN02315 352 EKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410 420
....*....|....*....|....*....
gi 24638878 425 AVFTTNGAAARKFVNEI--DAGQVGVNVP 451
Cdd:PLN02315 427 SIFTRNPETIFKWIGPLgsDCGIVNVNIP 455
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
152-449 |
6.36e-30 |
|
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: 121.56 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 152 PLGVTAGVAPFNFP---AMIPLwmfPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDA 228
Cdd:cd07134 100 PKGVCLIISPWNYPfnlAFGPL---VSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 229 PeIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQA 308
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 309 wiPDLVERAQKL--KV---NAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrKITvpgyEDGYFVGPTILSD 383
Cdd:cd07134 254 --DAFVEHLKAEieKFygkDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFD----AAQRYIAPTVLTN 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638878 384 VTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-449 |
1.44e-29 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 123.51 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 13 AAPTtklfIDGkfvESKTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKE 91
Cdd:COG4230 558 AAPL----IAG---EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 92 NMGELAKNITKEQGKTLADAEGDVlRglqvvehccsipslqmgETV-------ANVARDMDTYSLVLPLGVTAGVAPFNF 164
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIAEV-R-----------------EAVdfcryyaAQARRLFAAPTVLRGRGVFVCISPWNF 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 165 PAMIplwmF----PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV--NFICDaPEIKAVSFVG 238
Cdd:COG4230 693 PLAI----FtgqvAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgaALVAD-PRIAGVAFTG 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 239 SDQAGKYIyER--AGKNGKRV--------QSNMgaknhgI-------------IL-------Gdankentlnqlagaafg 288
Cdd:COG4230 768 STETARLI-NRtlAARDGPIVpliaetggQNAM------IvdssalpeqvvddVLasafdsaG----------------- 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 289 aagQRCMALStAVFVGDAQAwiPDLVER----AQKLKV-NAGHvPGTDVGPVISAASRQRINDLIESGVKEGAKLIldgr 363
Cdd:COG4230 824 ---QRCSALR-VLCVQEDIA--DRVLEMlkgaMAELRVgDPAD-LSTDVGPVIDAEARANLEAHIERMRAEGRLVH---- 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 364 KITVP-GYEDGYFVGPTI-----LSDVtpsmkcyTEEIFGPVLVIL--KADTLDDAIGIVNANPYGNGTAVFTTNGAAAR 435
Cdd:COG4230 893 QLPLPeECANGTFVAPTLieidsISDL-------EREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETID 965
|
490
....*....|....
gi 24638878 436 KFVNEIDAGQVGVN 449
Cdd:COG4230 966 RVAARARVGNVYVN 979
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
57-449 |
8.27e-29 |
|
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: 118.36 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGK------TLADaegdVLRGLQVVEHCCS--- 127
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHrsrhetLLAE----ILPSIAGIKHARKhlk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 128 --------IPSLQMGETVANVardmdTYSlvlPLGVTAGVAPFNFP---AMIPLwmfPVAITTGNTMLLKPSERVPGATM 196
Cdd:cd07133 77 kwmkpsrrHVGLLFLPAKAEV-----EYQ---PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 197 LLMELLNEAGcPPGVVNVIHGqhdavnficDAPEIKAVS--------FVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 268
Cdd:cd07133 146 LLAELLAEYF-DEDEVAVVTG---------GADVAAAFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 269 ILGDANKENTLNQLAGAAFGAAGQRCMA----L----STAVFVGDAQAWI----PDLVEraqklkvnaghvpGTDVGPVI 336
Cdd:cd07133 216 IAPDADLAKAAERIAFGKLLNAGQTCVApdyvLvpedKLEEFVAAAKAAVakmyPTLAD-------------NPDYTSII 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 337 SAASRQRINDLIESGVKEGAKLI---------LDGRKITvpgyedgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADT 407
Cdd:cd07133 283 NERHYARLQGLLEDARAKGARVIelnpagedfAATRKLP-----------PTLVLNVTDDMRVMQEEIFGPILPILTYDS 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24638878 408 LDDAIGIVNANP-----YgngtaVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07133 352 LDEAIDYINARPrplalY-----YFGEDKAEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
152-489 |
1.09e-24 |
|
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: 106.34 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 152 PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDAP 229
Cdd:cd07137 101 PLGVVLVISAWNFP--FLLSLEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 230 EIKaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAA-FGAAGQRCMALStavFVGDAQA 308
Cdd:cd07137 178 WDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQACIAPD---YVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 309 WIPDLVERAQK-LKVNAGHVPGT--DVGPVISAASRQRINDLIESgvKEGAKLILDGRKITvpgyEDGYFVGPTILSDVT 385
Cdd:cd07137 254 FAPTLIDALKNtLEKFFGENPKEskDLSRIVNSHHFQRLSRLLDD--PSVADKIVHGGERD----EKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 386 PSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGT 464
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGGV 407
|
330 340
....*....|....*....|....*
gi 24638878 465 RGSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:cd07137 408 GESGFGAYH--GKFSFDAFSHKKAV 430
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-449 |
3.01e-24 |
|
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: 105.28 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 152 PLGVTAGVAPFNFP---AMIPLwmfpV-AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGqhdavnficD 227
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlALAPL----IgAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG---------G 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 228 APEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENT---------LNqlagaafgaA 290
Cdd:cd07136 166 VEENQElldqkfdyIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAakrivwgkfLN---------A 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 291 GQRCMAlstavfvgdaqawiPD--LVERAQKLKV--------------NAGHVPgtDVGPVISAASRQRINDLIESG-VK 353
Cdd:cd07136 237 GQTCVA--------------PDyvLVHESVKEKFikelkeeikkfygeDPLESP--DYGRIINEKHFDRLAGLLDNGkIV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 354 EGAKLILDGRKITvpgyedgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP-----YgngtaVFT 428
Cdd:cd07136 301 FGGNTDRETLYIE-----------PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFS 364
|
330 340
....*....|....*....|.
gi 24638878 429 TNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07136 365 EDKKVEKKVLENLSFGGGCIN 385
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
57-404 |
1.72e-21 |
|
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: 96.92 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKT---LADAEGDV--LRGLQVVEHCCSIPSl 131
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 132 QMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAG-CPPG 210
Cdd:cd07084 81 EPGNHL-GQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 211 VVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAgKNGkRVQSNMGAKNHGIILGDAN-KENTLNQLAGAAFGA 289
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA-KQA-RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 290 AGQRCMALStAVFVGDAQAWIPdLVERAQKLkVNAGHVPGTDVGPVISAASRQRINDLIESGvkeGAKLILDGRKitVPG 369
Cdd:cd07084 238 SGQKCTAQS-MLFVPENWSKTP-LVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKE--LKN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24638878 370 YEDGYFVGPTILSDV-------TPSMKCYTEEIFGPVLVILK 404
Cdd:cd07084 310 HSIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVE 351
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
35-421 |
4.55e-21 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 97.35 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 35 DVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 113
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 114 DVlRglqvvehccsipslqmgETV------ANVAR---DMDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 184
Cdd:PRK11809 742 EV-R-----------------EAVdflryyAGQVRddfDNDTHR---PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 185 LKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAG----KYIYERAGKNGKRVQ- 258
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVArllqRNLAGRLDPQGRPIPl 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 259 -SNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKV-NAGHVpGTDVGPV 335
Cdd:PRK11809 881 iAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMgNPDRL-STDIGPV 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 336 ISAASRQRINDLIESgvkegakLILDGRKITVPGYED------GYFVGPTI--LSDVTPsmkcYTEEIFGPVLVIL--KA 405
Cdd:PRK11809 960 IDAEAKANIERHIQA-------MRAKGRPVFQAARENsedwqsGTFVPPTLieLDSFDE----LKREVFGPVLHVVryNR 1028
|
410
....*....|....*.
gi 24638878 406 DTLDDAIGIVNANPYG 421
Cdd:PRK11809 1029 NQLDELIEQINASGYG 1044
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
57-449 |
1.96e-18 |
|
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: 87.66 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 57 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGE----LAKNITKEQGKTLAdAEGDVLRGlqvvEHCCSIPSLQ 132
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEiveaLAKDLRKPKFEAVL-SEILLVKN----EIKYAISNLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 133 mgETVAN--VARDMDTY--SLVL---PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELL- 202
Cdd:cd07132 76 --EWMKPepVKKNLATLldDVYIykePLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 203 ----NEagCPPgvvnVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIIL 270
Cdd:cd07132 152 kyldKE--CYP----VVLG---------GVEETTEllkqrfdyIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 271 GDANKENTLNQLAGAAFGAAGQRCMAlstavfvgdaqawiPD-----------LVERAQK-LKVNAGHVPGT--DVGPVI 336
Cdd:cd07132 217 KSCDIDVAARRIAWGKFINAGQTCIA--------------PDyvlctpevqekFVEALKKtLKEFYGEDPKEspDYGRII 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 337 SAASRQRINDLIESGvkegaklildgrKITVPGYEDG--YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 414
Cdd:cd07132 283 NDRHFQRLKKLLSGG------------KVAIGGQTDEkeRYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEF 350
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24638878 415 VNA--NP---YgngtaVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:cd07132 351 INSreKPlalY-----VFSNNKKVINKILSNTSSGGVCVN 385
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
152-489 |
6.57e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 86.25 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 152 PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLnEAGCPPGVVNVIHGQHDAVNFICDAPEI 231
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 232 KaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAA-FGAAGQRCMALStavFVGDAQAWI 310
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKwGCNNGQACISPD---YILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 311 PDLVERAQK-LKVNAGHVP--GTDVGPVISAASRQRINDLIESgvKEGA-KLILDGRKitvpgYEDGYFVGPTILSDVTP 386
Cdd:PLN02174 267 PKVIDAMKKeLETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSdKIVYGGEK-----DRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 387 SMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTR 465
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVG 419
|
330 340
....*....|....*....|....
gi 24638878 466 GSFRGDHHfyGKQGIKFYTQTKTV 489
Cdd:PLN02174 420 ESGMGAYH--GKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
152-491 |
1.20e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 79.39 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 152 PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELLnEAGCPPGVVNVIHGQHDAVNFICDAP 229
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 230 EIKaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII--LGDA-NKENTLNQLAGAA-FGAAGQRCMALStavFVGD 305
Cdd:PLN02203 185 WDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKwGSCAGQACIAID---YVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 306 AQAWIPDLVERAQK-LKVNAGHVPG--TDVGPVISAASRQRINDLIESgvKEGAKLILDGRKITvpgyEDGYFVGPTILS 382
Cdd:PLN02203 261 EERFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD--PRVAASIVHGGSID----EKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 383 DVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSF 461
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdAIIQYACDSLPF 414
|
330 340 350
....*....|....*....|....*....|
gi 24638878 462 TGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 491
Cdd:PLN02203 415 GGVGESGFGRYH--GKYSFDTFSHEKAVLR 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
20-441 |
6.30e-12 |
|
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: 67.68 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESkTNEWIDVHDPATNQVVTRVPKATqAEMQAAL----ESNKKAFRSWSNQsilTRQQVMFKLQALIKENMGE 95
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVSSEG-LDFAAAVayarEKGGPALRALTFH---ERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 96 LAKnITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGEtvANVARDMDTYSL-----------VLPL-GVTAGVAPFN 163
Cdd:cd07128 79 LYA-LSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPN--AHFLVEGDVEPLskdgtfvgqhiLTPRrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 164 FPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAG-CPPGvvnvihgqhdAVNFICDAP--------EIKAV 234
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEG----------ALQLICGSVgdlldhlgEQDVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 235 SFVGSDQAGKYIYERAGKNGKRVQSNMGAKN-HGIILGDANKENT------LNQLAGAAFGAAGQRCMALSTAvFVGDAQ 307
Cdd:cd07128 226 AFTGSAATAAKLRAHPNIVARSIRFNAEADSlNAAILGPDATPGTpefdlfVKEVAREMTVKAGQKCTAIRRA-FVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 308 --AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESgVKEGAKLIL---DGRKITVPGYEDGYFVGPTIL- 381
Cdd:cd07128 305 vdAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGAFFPPTLLl 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24638878 382 -SDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNAnpyGNG---TAVFTTNGAAARKFVNEI 441
Cdd:cd07128 384 cDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELVLGA 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
20-479 |
1.01e-11 |
|
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: 67.14 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 20 FIDGKFVESKtnEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSW------SNQSILTRQQVMFKLQALIKENM 93
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhnplkNPERYLLYGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 94 GE--LAKNITKEQGKTLADAEGDVLRGLQVVEHCC--SIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIP 169
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 170 LWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGS---------D 240
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSskvaerlalE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 241 QAGKYIYERAGKNGKrvqsnmgaknhgiILG-DANKENTLN-QLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDlver 316
Cdd:cd07126 240 LHGKVKLEDAGFDWK-------------ILGpDVSDVDYVAwQCDQDAYACSGQKCSAQSI-LFAHEnwVQAGILD---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 317 aqKLKVNAGHVPGTD--VGPVISAASrQRINDLIESGVK-EGAKLILDGRKITVPGYEDGY--------FVgPTILSDVT 385
Cdd:cd07126 302 --KLKALAEQRKLEDltIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKPLTNHSIPSIYgayeptavFV-PLEEIAIE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 386 PSMKCYTEEIFGP--VLVILKADTLDDAIGIVNANPYgNGTAVFTTNGAaarKFVNEIDAGQV-GVnvpipvplpmfSFT 462
Cdd:cd07126 378 ENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHA-HLTAAVVSNDI---RFLQEVLANTVnGT-----------TYA 442
|
490
....*....|....*....
gi 24638878 463 GTRGSFRG--DHHFYGKQG 479
Cdd:cd07126 443 GIRARTTGapQNHWFGPAG 461
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
53-452 |
3.29e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 55.95 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 53 QAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNI--TKEQGKTLADAEG-----DvlRGLQVV--- 122
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVmhTTGQAFMMAFQAGgphaqD--RGLEAVaya 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 123 --------EHCCSIPSLQMGETVAnvardMDTYSLVLPLGVTAGVAPFNFPAmiplW-----MFpVAITTGNTMLLKPSe 189
Cdd:cd07127 161 wremsripPTAEWEKPQGKHDPLA-----MEKTFTVVPRGVALVIGCSTFPT----WngypgLF-ASLATGNPVIVKPH- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 190 rvPGATMLLM-------ELLNEAGCPPGVVNVI--HGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSN 260
Cdd:cd07127 230 --PAAILPLAitvqvarEVLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANAR--QAQVYTE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 261 MGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV-----GDAQAWI------PDLVERAQKLKVNaGHVPG 329
Cdd:cd07127 306 KAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT-PQNIYVprdgiQTDDGRKsfdevaADLAAAIDGLLAD-PARAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 330 TDVGPVISAASRQRINDliesgVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 409
Cdd:cd07127 384 ALLGAIQSPDTLARIAE-----ARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTD 458
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24638878 410 DAIGIVNANPYGNGT---AVFTTNGAAARKFVNEidAGQVGVNVPI 452
Cdd:cd07127 459 HSIELARESVREHGAmtvGVYSTDPEVVERVQEA--ALDAGVALSI 502
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
156-441 |
4.04e-08 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 55.87 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 156 TAGVA----PFNFPAMiPLW-MFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGC-PPGVVNVIHGQH----DAVNfi 225
Cdd:PRK11903 148 TRGVAlfinAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSagllDHLQ-- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 226 cdapEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAK--NHGIILGDANKENT-----LNQLAGAAFGAAGQRCMALS 298
Cdd:PRK11903 225 ----PFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADslNSALLGPDAAPGSEafdlfVKEVVREMTVKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 299 TaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIEsGVKEGAKLILDGRKITVPGYED--GY 374
Cdd:PRK11903 301 R-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavAA 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638878 375 FVGPTIL--SDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNAnpyGNG---TAVFTTNGAAARKFVNEI 441
Cdd:PRK11903 379 CVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARR---GQGslvASVYSDDAAFLAAAALEL 447
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
47-325 |
3.57e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 52.23 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 47 RVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKT---LADAEgDVLRGL-QVV 122
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSeskLYKNI-DTERGItASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 123 EHCCSIPSLQMGETvanvardmdtYSLVLPLGVTAGVAPFNFPAMIPLWMFpVAITTGNTMLLKPSERVP----GATMLL 198
Cdd:cd07077 81 GHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPftnrALALLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 199 MELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAgkNGKRVQSnMGAKNHGIILGDANKENT 278
Cdd:cd07077 150 QAADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIG-FGAGNSPVVVDETADEER 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24638878 279 LNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVE---RAQKLKVNAG 325
Cdd:cd07077 227 ASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKlklVVEGLKVPQE 276
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
144-425 |
5.31e-06 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 48.69 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 144 MDTYSLVLPLGVTAGVAPFNFP-AmiplwmFPV-------AITTGNTMLLKPSERVPGATMLLMEL----LNEAGCPPGV 211
Cdd:cd07129 97 PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 212 VNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGK--NGKRVQSNMGAKNHGIILGDANKEN--TLNQ-LAGA 285
Cdd:cd07129 171 FSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 286 AFGAAGQRCmalsTA---VFV---GDAQAWIPDLVERAQKlkvnagHVPGTDVGPVISAASRQRINDLIESGvkeGAKLI 359
Cdd:cd07129 251 LTLGAGQFC----TNpglVLVpagPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGVEALAAAP---GVRVL 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638878 360 LDGrkitvPGYEDGYFVGPTILS-DVT-----PSMkcyTEEIFGPVLVILKADTLDDAIGIVNANPyGNGTA 425
Cdd:cd07129 318 AGG-----AAAEGGNQAAPTLFKvDAAafladPAL---QEEVFGPASLVVRYDDAAELLAVAEALE-GQLTA 380
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
56-451 |
7.52e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 38.79 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 56 MQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLAdaEGDVLRGLQVVEHccsIPSLQMGE 135
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRV--EDKVIKNHFAAEY---IYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 136 TVANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPG-- 210
Cdd:cd07081 76 KTCGVLTGDENGGTLIiaePIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGap 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 211 ---VVNVIHGQHDAVNFICDAPEIKAVSFVGsdqaGKYIYERAGKNGKRVQSnMGAKNHGIILGD-ANKENTLNQLAGAA 286
Cdd:cd07081 156 enlIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVIDEtADIKRAVQSIVKSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 287 FGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVpgTDVGPVIsaasrQRINDLIESGVKEGAKLILDGRKIT 366
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEEL--QQVQPVI-----LKNGDVNRDIVGQDAYKIAAAAGLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638878 367 VPGYEDGYFVGPTILSDVTPsmkcYTEEIFGPVLVILKADTLDD----AIGIVNANPYGNGTAVFTTNGAAARK---FVN 439
Cdd:cd07081 304 VPQETRILIGEVTSLAEHEP----FAHEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYSDNIKAIENmnqFAN 379
|
410
....*....|..
gi 24638878 440 EIDAGQVGVNVP 451
Cdd:cd07081 380 AMKTSRFVKNGP 391
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
380-449 |
9.59e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.51 E-value: 9.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638878 380 ILSDVTPSmkcyTEEIFG-----PVLVILKADTLDDAIGIVNAnpYGNG-T-AVFTTNGAAARKFVNEIDAGQVGVN 449
Cdd:PRK00197 297 LLPDVVPA----TEEDWDteyldLILAVKVVDSLDEAIAHINR--YGSGhTeAIVTEDYAAAERFLNEVDSAAVYVN 367
|
|
| |
