|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
26-502 |
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: 882.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGEL 105
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 106 AKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVA 185
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 186 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKR 265
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 266 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPV 344
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDeADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 345 ISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIV 424
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638876 425 NANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLW 502
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
27-502 |
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 24638876 27 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 186
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 187 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 266
Cdd:TIGR01722 162 ACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 267 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVIS 346
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLIT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 347 AASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNA 426
Cdd:TIGR01722 322 PQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 427 NPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLW 502
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-518 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 639.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 24 PTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMG 103
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFP 183
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 184 VAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 263
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGP 343
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 344 VISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 423
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 424 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHFYGKQGIKFYTQTKTVTQLWR 503
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|....*
gi 24638876 504 ktDVThTQAAVAMPT 518
Cdd:PLN02419 592 --DIH-SPFSLAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
23-502 |
2.92e-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: 509.67 E-value: 2.92e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 23 APTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENM 102
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 103 GELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 182
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTD 340
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 341 VGPVISAASRQRINDLIESGVKEGAKLILDGRkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDA 420
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGR---RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 421 IGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 500
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTI 477
|
..
gi 24638876 501 LW 502
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-498 |
1.85e-163 |
|
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: 471.25 E-value: 1.85e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 34 FVESKTNEwIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQ 113
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 114 GKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 193
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETL-PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 194 LKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGA 272
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 273 KNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQ 351
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 352 RINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGN 431
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 432 GTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSFRGDhhFYGKQGIKFYTQTKTV 498
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
66-499 |
2.23e-119 |
|
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: 358.06 E-value: 2.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGET 145
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 146 VANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIH 225
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 226 G-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCM 304
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 305 ALStAVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitVPGYEDG 382
Cdd:cd07078 241 AAS-RLLVheSIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 383 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP 462
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 24638876 463 VPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07078 397 GAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
29-499 |
2.86e-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: 2.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 187
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 188 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 266
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 267 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVI 345
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLiVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 346 SAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 425
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 426 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI---PVPLPmfsFTGTRGSFRGdHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP---FGGVKKSGNG-HREAGTTALDAFTEWKAVY 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
29-498 |
8.42e-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: 342.31 E-value: 8.42e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEwiDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 187
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 188 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 266
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 267 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVI 345
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGiHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 346 SAASRQRINDLIESGVKEGAKLILDGRKITVPgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 425
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLKRP--DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638876 426 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP-----IPVPlpmfsFTGTRGSFRGDHHfYGKQGIKFYTQTKTV 498
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYGPRE-QGEAALEFYTTIKTV 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
45-500 |
3.43e-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: 319.38 E-value: 3.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 LRGLQVV----EHCCSIpslqMGETVanVARDMDTYSLVL--PLGVTAGVAPFNFP-AMIPLWMFPvAITTGNTMLLKPS 197
Cdd:cd07103 81 DYAASFLewfaEEARRI----YGRTI--PSPAPGKRILVIkqPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 198 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAknHG 276
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 277 --IILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVgdaQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAAS 349
Cdd:cd07103 232 pfIVFDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYV---HESIYDefvekLVERVKKLKVGNGLDEGTDMGPLINERA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 350 RQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPY 429
Cdd:cd07103 308 VEKVEALVEDAVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24638876 430 GNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPvPLPMFSFTGTRGSfrGdhhfYG----KQGIKFYTQTKTVTQ 500
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVSL 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
29-498 |
4.97e-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: 311.89 E-value: 4.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 108
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 109 ITKEQGKTLADAEGDVLRGLQVVEHCCS---------IPSLQMGETVanvardmdtYSLVLPLGVTAGVAPFNFP-AMIP 178
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEwarriegeiIPSDRPNENI---------FIFKVPIGVVAGILPWNFPfFLIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 179 LWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYE 257
Cdd:cd07088 152 RKLAP-ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 258 RAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLKVNAGH 335
Cdd:cd07088 231 AAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKVGDPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 336 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 415
Cdd:cd07088 310 DAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 416 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSfTGTRGSFRG--DhhfyGKQGIKFYT 493
Cdd:cd07088 387 SLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGgaD----GKHGLEEYL 461
|
....*
gi 24638876 494 QTKTV 498
Cdd:cd07088 462 QTKVV 466
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
45-499 |
4.69e-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: 303.72 E-value: 4.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GD 123
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VLRGLQ----VVEHCcsipsLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSER 199
Cdd:cd07093 81 IPRAAAnfrfFADYI-----LQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 200 VPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII 278
Cdd:cd07093 156 TPLTAWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 279 LGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 356
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLA-GSRILVqrSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVNVPIPVPLPMfSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
29-458 |
4.80e-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: 299.61 E-value: 4.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 186
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 187 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKR 265
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 266 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGP 343
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 344 VISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 423
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 24638876 424 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
45-498 |
8.13e-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: 295.21 E-value: 8.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 LRGLQVVEHCCSIPSLQmgetvaNVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP 201
Cdd:cd07106 81 GGAVAWLRYTASLDLPD------EVIEDDDTRRVELrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 202 GATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 281
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 282 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 359
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESIydEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 360 GVKEGAKLILDGRKITVPgyedGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTN 439
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGP----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 24638876 440 GAAARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTV 498
Cdd:cd07106 389 LERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQS--GIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
28-458 |
1.00e-94 |
|
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: 295.57 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGktladAEGDVLRGLQVvehccsipslQMGETVANVARD-MDTY--------SLVL--PLGVTAGVAPFNFPA- 175
Cdd:cd07138 81 AITLEMG-----APITLARAAQV----------GLGIGHLRAAADaLKDFefeerrgnSLVVrePIGVCGLITPWNWPLn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 176 MIPLWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKY 254
Cdd:cd07138 146 QIVLKVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 255 IYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALsTAVFVGDAQawIPDLVERA----QKLK 330
Cdd:cd07138 225 VAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAaaaaEAYV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 331 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLV 410
Cdd:cd07138 302 VGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLS 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24638876 411 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07138 381 IIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
45-498 |
6.44e-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: 288.30 E-value: 6.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPG 202
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 203 ATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 281
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 282 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdaQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 356
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLV---QRSIYDefverLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:cd07114 317 VARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTV 498
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 ... |
26-499 |
1.62e-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: 1.62e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSI--LTRQQVMFKLQALIKENMG 103
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTL-ADAEGDVLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 182
Cdd:cd07091 84 ELAALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdaQAWIPD-----LVERAQKLKVNAGH 335
Cdd:cd07091 243 sNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFV---QESIYDefvekFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 336 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 415
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHG----SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 416 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpIPVPLPMFSFTGTRGSFRGDHhfYGKQGIKFYTQT 495
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGRE--LGEEGLEEYTQV 471
|
....
gi 24638876 496 KTVT 499
Cdd:cd07091 472 KAVT 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
28-500 |
6.30e-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: 287.20 E-value: 6.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCCSiPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAI 186
Cdd:cd07124 113 AWMVLEVGKNWAEADADVAEAIDFLEYYAR-EMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 187 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK---- 261
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKvqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 --NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVPG 338
Cdd:cd07124 272 qkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGaKLILDGRkiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMF-SFTGTRGSFRGdhhfyGKQG----IKFYT 493
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMSGTG-----SKAGgpdyLLQFM 503
|
....*..
gi 24638876 494 QTKTVTQ 500
Cdd:cd07124 504 QPKTVTE 510
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
45-498 |
9.17e-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: 9.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 LRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT 204
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHV-PLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 205 MLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANK 284
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 285 ENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVK 362
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSN-GTRVFVQRSikDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 363 EGAKLILDGRKITV-PGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 441
Cdd:cd07090 319 EGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638876 442 AARKFVNEIDAGQVGVN----VPIPVPlpmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:cd07090 399 RAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
29-460 |
7.36e-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: 7.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTnEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 108
Cdd:cd07086 2 VIGGEWVGSGG-ETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 109 ITKEQGKTLADAEGDVLRGLQVVEHCCSIpSLQM-GETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAIT 187
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGL-SRMLyGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 188 TGNTMLLKPSERVPGATMLLMELLNEA----GCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 263
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVG 342
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLiVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 343 PVISAASRQRINDLIESGVKEGAKLILDGRKITvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIG 422
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID--GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24638876 423 IVNANPYGNGTAVFTTNGAAARKFV--NEIDAGQVGVNVP 460
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIP 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
28-499 |
1.28e-86 |
|
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: 274.84 E-value: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAF--RSWSNQSILTRQQVMFKLQALIKENMGEL 105
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 106 AKNITKEQGKTLA--------------DAEGDVLRGLQVVEHccsIPSLQMGETVanVARDmdtyslvlPLGVTAGVAPF 171
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVL--VRRE--------PVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 172 NFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQA 251
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 252 GKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALsTAVFVGDAQ--AWIPDLVERAQKL 329
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRydEVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 330 KVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVL 409
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 410 VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpipvplPMFSFTGTRGSFR--GDHHFYGKQ 487
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG------FRLDFGAPFGGFKqsGIGREGGPE 458
|
490
....*....|..
gi 24638876 488 GIKFYTQTKTVT 499
Cdd:cd07139 459 GLDAYLETKSIY 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
26-498 |
1.51e-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: 1.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS-WSNQSILTRQQVMFKLQALIKENMGE 104
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 105 LAKNITKEQGKTL-ADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMFP 183
Cdd:cd07144 88 LAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 184 VAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGqHDAV--NFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERA-QKLKVNAGHVPG 338
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVkQNYKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP----IPVPlpmfsFTGTRGSFRGDHhfYGKQGIKFYTQ 494
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIGRE--LGEYGLETYTQ 476
|
....
gi 24638876 495 TKTV 498
Cdd:cd07144 477 TKAV 480
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
43-499 |
3.28e-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: 273.32 E-value: 3.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLRGLQVVEHCCSIPSLQMGETV----ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 198
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIpfdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 199 RVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKngKRVQSNMGAKNHGI 277
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 278 ILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 355
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDiyDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 356 LIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 435
Cdd:cd07149 318 WVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 436 FTTNGAAARKFVNEIDAGQVGVNvPIPvplpmfsftgtrgSFRGDHHFYG--------KQGIKF----YTQTKTVT 499
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMIN-DSS-------------TFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
73-499 |
9.82e-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: 269.10 E-value: 9.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 73 KKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARD 152
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 153 MDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAV 231
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 232 NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVF 311
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 312 VGDAQAwiPDLVERAQklkvnaghvpgtdvgpvisaasrqrindliesgvkegaklildgrkitvpgyedgyfvgpTILS 391
Cdd:cd06534 243 VHESIY--DEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 392 DVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFT 471
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 24638876 472 GTRGSFRGDHHfyGKQGIKFYTQTKTVT 499
Cdd:cd06534 341 GVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
44-460 |
5.11e-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: 269.97 E-value: 5.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 44 DVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 123
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 203
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 204 TMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 282
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 283 NKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGV 361
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPvYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 362 KEGAKLIldgrkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 441
Cdd:cd07150 322 AKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410
....*....|....*....
gi 24638876 442 AARKFVNEIDAGQVGVNVP 460
Cdd:cd07150 395 RAFKLAERLESGMVHINDP 413
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
45-499 |
1.23e-84 |
|
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: 269.10 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQ-SILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 123
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 203
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 204 TMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 282
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 283 NKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQA-WIPDLVERAQKLKVNAGhVPGTDVGPVISAASRQRINDLIESGV 361
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDeVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 362 KEGAKLILDGRKITVPgYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 441
Cdd:cd07109 319 ARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638876 442 AARKFVNEIDAGQVGVNVPIP---VPLPmfsFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKS--GHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
46-499 |
1.27e-84 |
|
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: 269.21 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 46 HDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 123
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VlrglqvvEHCCSI----PSLQM---GETVANVARDMdtYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLL 194
Cdd:cd07118 82 I-------EGAADLwryaASLARtlhGDSYNNLGDDM--LGLVLrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 195 KPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAK 273
Cdd:cd07118 153 KPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 274 NHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQ 351
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 352 RINDLIESGVKEGAKLILDGRKItvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGN 431
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 432 GTAVFTTNGAAARKFVNEIDAGQVGVNVPIP--VPLPmfsFTGTRGSFRGDHhfYGKQGIKFYTQTKTVT 499
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGRE--LGRYGVEEYTELKTVH 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
26-498 |
2.58e-82 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 264.63 E-value: 2.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGEL 105
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 106 AKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFP-AMIPLWMFPv 184
Cdd:PLN02278 105 AQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 185 AITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 263
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVgdaQAWIPD-----LVERAQKLKVNAGHVPG 338
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILV---QEGIYDkfaeaFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIKYV 492
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
26-498 |
2.96e-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: 264.01 E-value: 2.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR-SWSNQ-SILTRQQVMFKLQALIKENMG 103
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKT-LADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMF 182
Cdd:cd07143 87 YLASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPG 338
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVqeGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHG----NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTV 498
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
28-502 |
2.90e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 262.18 E-value: 2.90e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCC-SIPSLQMGETVANVARDMDTYsLVLPLGVTAGVAPFNFPAMIPLWMFPVA 185
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEYYArQMLKLADGKPVESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 186 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK--N 262
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERAAKvqP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 263 G----KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVP 337
Cdd:PRK03137 276 GqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 338 gTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKitvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 417
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 418 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpmfsfTGTRGSFRGDHHFYG--------KQG- 488
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN------------RGCTGAIVGYHPFGGfnmsgtdsKAGg 497
|
490
....*....|....*..
gi 24638876 489 ---IKFYTQTKTVTQLW 502
Cdd:PRK03137 498 pdyLLLFLQAKTVSEMF 514
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
43-458 |
2.94e-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: 260.36 E-value: 2.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL----PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 198
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFtvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 199 RVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 277
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 278 ILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 355
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 356 LIESGVKEGAKLILDGRKItvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 435
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420
....*....|....*....|...
gi 24638876 436 FTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
26-499 |
3.06e-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: 3.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR---SWSNQSILTRQQVMFKLQALIKENM 102
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 103 GELAKNITKEQGKTLADA-EGDVLRGLQVVEHCCSIPSLQMGETVAnvardMD----TYSLVLPLGVTAGVAPFNFPAMI 177
Cdd:cd07141 87 AYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIP-----MDgdffTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 178 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIY 256
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 257 ERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNA 333
Cdd:cd07141 242 QAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 334 GHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvPGyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILK 413
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR---HG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 414 ADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSfrGDHHFYGKQGIKFYT 493
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMS--GNGRELGEYGLQEYT 473
|
....*.
gi 24638876 494 QTKTVT 499
Cdd:cd07141 474 EVKTVT 479
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-498 |
4.04e-81 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 260.97 E-value: 4.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 21 SAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKE 100
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 101 NMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCSI-PSLQmGETVAnvARDMD-TYSLVLPLGVTAGVAPFNFPAMI 177
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLaPALE-GEQIP--LRGGSfVYTRREPLGVCAGIGAWNYPIQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 178 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYE 257
Cdd:PRK13252 159 ACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 258 RAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGH 335
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSikAAFEARLLERVERIRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 336 VPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKAD 415
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 416 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYT 493
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYT 472
|
....*
gi 24638876 494 QTKTV 498
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
67-458 |
3.99e-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: 256.69 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 67 AALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETV 146
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 147 ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT-MLLMELLNEAGCPPGVVNVIH 225
Cdd:cd07104 84 PSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 226 GQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCM 304
Cdd:cd07104 164 GGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 305 ALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitvpgyEDG 382
Cdd:cd07104 244 AAGR-ILVHEsvYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------YEG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 383 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
47-498 |
5.69e-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: 256.98 E-value: 5.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 47 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG-DVL 125
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 126 RGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATM 205
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 206 LLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANK 284
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 285 ENTLNQLAGAAFGAAGQRCMALSTAVfvgdAQAWIPD-----LVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 359
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLL----VHESIYDeflerFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 360 GVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTN 439
Cdd:cd07115 318 GREEGARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24638876 440 GAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTynRFDPGSP---FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
28-499 |
4.92e-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: 252.75 E-value: 4.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS-WSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLAdaegdVLRGLQVVEHCC-------------------SIPSLQMGETVANVARDmdtyslvlPLGVTAG 167
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEVGQSANflryfagwatkingetlapSIPSMQGERYTAFTRRE--------PVGVVAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 168 VAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPgATML-LMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFV 246
Cdd:cd07113 149 IVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 247 GSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVgdAQAWIPDLVE-- 324
Cdd:cd07113 228 GSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYV--HRSKFDELVTkl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 325 --RAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRkiTVPGyeDGYFVGPTILSDVTPSMKCYTE 402
Cdd:cd07113 305 kqALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE--ALAG--EGYFVQPTLVLARSADSRLMRE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 403 EIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHh 482
Cdd:cd07113 381 ETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE- 458
|
490
....*....|....*..
gi 24638876 483 fYGKQGIKFYTQTKTVT 499
Cdd:cd07113 459 -FGSAFIDDYTELKSVM 474
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
27-458 |
2.17e-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: 250.95 E-value: 2.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 27 KLFIDGKFVESKtNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSN-QSILTRQQVMFKLQALIKENMGEL 105
Cdd:cd07082 3 KYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 106 AKNITKEQGKTLADAEGDVLRGLQVVEHCcsipslqmgetvANVARDMDTYSLV----------------LPLGVTAGVA 169
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDT------------IEELKRLDGDSLPgdwfpgtkgkiaqvrrEPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 170 PFNFP------AMIPlwmfpvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKA 242
Cdd:cd07082 150 PFNYPlnltvsKLIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 243 VSFVGSDQAGKYIYERAGKngKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFV--GDAQAWIP 320
Cdd:cd07082 224 ISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVheSVADELVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 321 DLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrkitvpGYEDGYFVGPTILSDVTPSMKCY 400
Cdd:cd07082 301 LLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLA 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24638876 401 TEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07082 375 WEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
65-498 |
6.55e-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: 248.14 E-value: 6.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 65 MQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVlrglqvvEHCCSI------- 137
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV-------EKCAWIcryyaen 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 138 -PSLQMGETVANVARDmdtySLV--LPLGVTAGVAPFNFPamipLW-MFPVA---ITTGNTMLLKPSERVPGATMLLMEL 210
Cdd:cd07100 74 aEAFLADEPIETDAGK----AYVryEPLGVVLGIMPWNFP----FWqVFRFAapnLMAGNTVLLKHASNVPGCALAIEEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 211 LNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQ 290
Cdd:cd07100 146 FREAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 291 LAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLI 368
Cdd:cd07100 226 AVKGRLQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 369 LDGRKITVPGYedgyFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVN 448
Cdd:cd07100 305 LGGKRPDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24638876 449 EIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
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 ... |
45-498 |
2.74e-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: 247.54 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWS-NQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-- 121
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 122 ------GDVLRGLQVV-----EHCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGN 190
Cdd:cd07089 81 qvdgpiGHLRYFADLAdsfpwEFDLPVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 191 TMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVN--FICDaPEIKAVSFVGSDQAGKYIYERAGKNGKRVQS 268
Cdd:cd07089 153 TVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGeaLTTD-PRVDMVSFTGSTAVGRRIMAQAAATLKRVLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 269 NMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVGDAQawIPDLVERaqkLKVNAGHV-------PGTDV 341
Cdd:cd07089 232 ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSR--YDEVVEA---LAAAFEALpvgdpadPGTVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 342 GPVISAASRQRINDLIESGVKEGAKLILDGRkiTVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAI 421
Cdd:cd07089 306 GPLISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 422 GIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpMFSFTGTRGSFRGDHHF-----YGKQGIKFYTQTK 496
Cdd:cd07089 384 RIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN--------GGGGYGPDAPFGGYKQSglgreNGIEGLEEFLETK 455
|
..
gi 24638876 497 TV 498
Cdd:cd07089 456 SI 457
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
43-499 |
3.63e-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: 246.96 E-value: 3.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL----PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSE 198
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 199 RVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSNMGAKNHGI 277
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 278 ILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 356
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSfrgdhhFYGKQGIKF----YTQTKTVT 499
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
27-458 |
2.90e-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: 2.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 27 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEG-DV-LrglqVVEHCCSIPSLQMGETVANVARDMDTYSLVL--PLGVTAGVAPFNFPAMIPLWMF 182
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIpL----AIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFhePLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 NGKRVQSNMGAKNHGIILGDANKENT--------------LNQlagaafgaaGQRCMALSTAvFVGDA--QAWIPDLVER 325
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAMDADDdfddkaeegqlgfaFNQ---------GEVCTCPSRA-LVQESiyDEFIERAVER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 326 AQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIF 405
Cdd:cd07559 307 FEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIF 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24638876 406 GPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07559 387 GPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN 439
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
45-499 |
6.68e-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: 6.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 LRGlqVVEH-------CCSIPSLQMGETVAnvarDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPS 197
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLP----GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 198 ERVPGATMLLMELLNEaGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHG 276
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 277 IILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIN 354
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 355 DLIEsGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTA 434
Cdd:cd07092 313 GFVE-RAPAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24638876 435 VFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMfSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTVT 499
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVM 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
43-499 |
1.13e-72 |
|
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: 238.03 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESnkkafrSWSNQSILTRQQ---VMFKLQALIKENMGELAKNITKEQGKTLAD 119
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 120 AEGDVLRGLQVVEHCCSIPSLQMGET----VANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLK 195
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRDDGESfscdLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 196 PSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSNMGAKN 274
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 275 HGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQR 352
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 353 INDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNG 432
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24638876 433 TAVFTTNGAAARKFVNEIDAGQVGVNvpiPVP---LPMFSFTGTRGSFRGdhhfyGKQG----IKFYTQTKTVT 499
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 ... |
45-500 |
2.55e-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: 237.25 E-value: 2.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE--- 121
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 122 GDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP 201
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 202 GATMLLMELLNEAGCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILG 280
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 281 DANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIE 358
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 359 SGVKEGAKLILDGRkitVP-GYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFT 437
Cdd:cd07110 320 RGKEEGARLLCGGR---RPaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638876 438 TNGAAARKFVNEIDAGQVGVNVPIPVpLPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTVTQ 500
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGRE--LGEWGLDNYLEVKQITR 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
27-498 |
3.45e-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: 237.35 E-value: 3.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 27 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEG-DVLRGlqvVEHCCSIPSLQMGETVANVARDMDTYSLVL--PLGVTAGVAPFNFPAMIPLWMFP 183
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLA---ADHFRYFAGVIRAEEGSANMIDEDTLSIVLrePIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 184 VAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKN 262
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 263 GKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFV--GDAQAWIPDLVERAQKLKVNAGHVPGTD 340
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVqeGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 341 VGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDA 420
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 421 IGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRG-DHHfygKQGIKFYTQTKT 497
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGrETH---KSMLDAYTQMKN 470
|
.
gi 24638876 498 V 498
Cdd:cd07117 471 I 471
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
45-499 |
4.94e-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: 236.50 E-value: 4.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 LRGLQVVEHCCSIPSLQMGETVANVARDMDtYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT 204
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLH-YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 205 MLLMELLNEAgCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDAN 283
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 284 KENTLNQLAGAAFGA-AGQRCMALSTAvFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESG 360
Cdd:cd07107 239 PEAAADAAVAGMNFTwCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 361 VKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNG 440
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 441 AAARKFVNEIDAGQVGVN--------VPipvplpmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTVT 499
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIGREE--CLEELLSYTQEKNVN 453
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
28-502 |
5.43e-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: 5.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVEskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:TIGR01237 35 LVINGERVE--TENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCC-SIPSLQMGETVANVARDMDTYsLVLPLGVTAGVAPFNFPAMIPLWMFPVA 185
Cdd:TIGR01237 113 ALLVKEVGKPWNEADAEVAEAIDFMEYYArQMIELAKGKPVNSREGETNQY-VYTPTGVTVVISPWNFPFAIMVGMTVAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 186 ITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGK--- 261
Cdd:TIGR01237 192 IVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVgDYLVDHPKTSLITFTGSREVGTRIFERAAKvqp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 ---NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDA-QAWIPDLVERAQKLKVNAGHVP 337
Cdd:TIGR01237 272 gqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVyDEVVERFVEITESLKVGPPDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 338 GTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKitvpGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 417
Cdd:TIGR01237 352 DVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCG----DDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 418 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP------VPLPMFSFTGTrGSFRGdhhfyGKQGIKF 491
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITgaivgyQPFGGFKMSGT-DSKAG-----GPDYLAL 500
|
490
....*....|.
gi 24638876 492 YTQTKTVTQLW 502
Cdd:TIGR01237 501 FMQAKTVTEMF 511
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
45-499 |
5.57e-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: 236.10 E-value: 5.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTL-ADAEGD 123
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VLRGLQVVEHCCSIPSLQMGETVAnVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 203
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 204 TMLLMELLNEAgCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDA 282
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 283 NKENTLNQ-LAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIES 359
Cdd:cd07108 239 DLDDAVDGaIAGMRFTRQGQSCTAGSR-LFVHEDiyDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 360 GVKE-GAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTT 438
Cdd:cd07108 318 GLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638876 439 NGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHhfYGKQG-IKFYTQTKTVT 499
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
40-498 |
7.46e-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: 235.96 E-value: 7.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 40 NEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTL 117
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 118 ADAEGDVLRGlqvVEHCC-----SIPSLqMGEtVANVARDMdtYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGN 190
Cdd:cd07112 81 SDALAVDVPS---AANTFrwyaeAIDKV-YGE-VAPTGPDA--LALITrePLGVVGAVVPWNFPLLMAAWKIAPALAAGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 191 TMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK-NGKRVQS 268
Cdd:cd07112 154 SVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 269 NMGAKNHGIILGDANK-----ENTL-----NQlagaafgaaGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVP 337
Cdd:cd07112 234 ECGGKSPNIVFADAPDldaaaEAAAagifwNQ---------GEVCSAGSRLlVHESIKDEFLEKVVAAAREWKPGDPLDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 338 GTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 417
Cdd:cd07112 305 ATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 418 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN----VPIPVPlpmfsFTGTRGSfrGDHHFYGKQGIKFYT 493
Cdd:cd07112 383 EEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQS--GNGRDKSLHALDKYT 455
|
....*
gi 24638876 494 QTKTV 498
Cdd:cd07112 456 ELKTT 460
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
32-499 |
1.11e-71 |
|
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: 235.66 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 32 GKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITK 111
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 112 EQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNT 191
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 192 MLLKPSERVP--GATmLLMELLNEAGCPPGVVNVIHGqhdAVNFICDA----PEIKAVSFVGSDQAGKYIYERAGKNGKR 265
Cdd:cd07151 161 VVLKPASDTPitGGL-LLAKIFEEAGLPKGVLNVVVG---AGSEIGDAfvehPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 266 VQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQA--WIPDLVERAQKLKVNAGHVPGTDVGP 343
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDVYdeFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 344 VISAASRQRINDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 423
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 424 VNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvPIPV-PLPMFSFTGTRGSFRGdhHFYGKQGIKFYTQTKTVT 499
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNSGLG--RFNGEWALEEFTTDKWIS 462
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
43-490 |
1.93e-70 |
|
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: 232.14 E-value: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLRgLQVVEHCCSIPSLQMGETVAnvarDMDTYS-------LV--LPLGVTAGVAPFNFPamIPLWMFPV--AITTGNT 191
Cdd:cd07147 81 EVAR-AIDTFRIAAEEATRIYGEVL----PLDISArgegrqgLVrrFPIGPVSAITPFNFP--LNLVAHKVapAIAAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 192 MLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQH-DAVNFICDaPEIKAVSFVGSDQAGKYIYERAGKngKRVQSNM 270
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRdDADLLVTD-ERIKLLSFTGSPAVGWDLKARAGK--KKVVLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 271 GAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAA 348
Cdd:cd07147 231 GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKTGDPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 349 SRQRINDLIESGVKEGAKLIldgrkitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP 428
Cdd:cd07147 310 EAERVEGWVNEAVDAGAKLL-------TGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638876 429 YGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPipvplpmfsftgtrgSFRGDHHFYGkqGIK 490
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG--GVK 428
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
66-499 |
2.24e-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: 231.31 E-value: 2.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGET 145
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 146 VANVARDmdTYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNV 223
Cdd:cd07105 83 IPSDKPG--TLAMVVkePVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 224 IHGQ----HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAA 299
Cdd:cd07105 161 VTHSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 300 GQRCMalSTA-VFVGD--AQAWIPDLVERAQKLKvnAGHVPgtdVGPVISAASRQRINDLIESGVKEGAKLILDGRKITV 376
Cdd:cd07105 241 GQICM--STErIIVHEsiADEFVEKLKAAAEKLF--AGPVV---LGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 377 PgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVG 456
Cdd:cd07105 314 P---SGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24638876 457 VNVPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07105 391 INGMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
52-458 |
1.20e-69 |
|
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: 229.87 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 52 QVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVV 131
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 132 EHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGAT-MLLMEL 210
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 211 LNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQ 290
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 291 LAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLIL 369
Cdd:cd07152 241 GAWGAFLHQGQICMAAGRHlVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 370 DGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNE 449
Cdd:cd07152 321 GGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
....*....
gi 24638876 450 IDAGQVGVN 458
Cdd:cd07152 394 LRTGMLHIN 402
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
25-462 |
1.20e-65 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 220.17 E-value: 1.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 25 TTKLFIDGKFVESKTNEWiDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGE 104
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 105 LAKNITKEQGK----TLAD---AEGDVLRGLQVVEHCCSIPSlqMGETVAN----VARDmdtyslvlPLGVTAGVAPFNF 173
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRFFAGAARCLEGKA--AGEYLEGhtsmIRRD--------PVGVVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 174 PAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAG 252
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 253 KYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLK 330
Cdd:PRK13473 230 KHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 331 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKItVPGyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLV 410
Cdd:PRK13473 309 VGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEA-PDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVS 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24638876 411 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP 462
Cdd:PRK13473 386 VTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
26-498 |
2.05e-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: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILTRQQVMFKLQALIKENMG 103
Cdd:cd07142 4 TKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCSIPSLQMGETVANVARDMdTYSLVLPLGVTAGVAPFNFPAMIPLWMF 182
Cdd:cd07142 84 ELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHH-VYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPG 338
Cdd:cd07142 243 sNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHESiyDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
47-500 |
4.37e-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: 215.29 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 47 DPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILtRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDV 124
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 lRGlqvvehccSIPSLQMgetVANVARDM---------DTYSLVL--PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 193
Cdd:cd07120 82 -SG--------AISELRY---YAGLARTEagrmiepepGSFSLVLrePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 194 LKPSERVPGATMLLMELLNEA-GCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMG 271
Cdd:cd07120 150 VKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 272 AKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTA-VFVGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASR 350
Cdd:cd07120 230 GKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVlVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 351 QRINDLIESGVKEGAKLILDGRKITvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYG 430
Cdd:cd07120 310 DRVDRMVERAIAAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 431 NGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVpLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 500
Cdd:cd07120 389 LAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIYL 455
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
21-500 |
5.00e-64 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 216.52 E-value: 5.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 21 SAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAF-----RSWSNQSILTRQQVMFKLQ 95
Cdd:PLN02467 3 IPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 96 ALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTY-SLVL--PLGVTAGVAPFN 172
Cdd:PLN02467 83 AKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFkGYVLkePLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 173 FPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ-HDAVNFICDAPEIKAVSFVGSDQA 251
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 252 GKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKL 329
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 330 KVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVL 409
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 410 VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIP--VPLPmfsFTGTRGSFRGDHhfYGKQ 487
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPcfCQAP---WGGIKRSGFGRE--LGEW 474
|
490
....*....|...
gi 24638876 488 GIKFYTQTKTVTQ 500
Cdd:PLN02467 475 GLENYLSVKQVTK 487
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
26-498 |
2.57e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 214.68 E-value: 2.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFR--SWSNQSILTRQQVMFKLQALIKENMG 103
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTLADAEG-DVLRGLQVVEHCCSIPSLQMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMF 182
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 183 PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGK 261
Cdd:PLN02766 180 APALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 262 -NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV--GDAQAWIPDLVERAQKLKVNAGHVPG 338
Cdd:PLN02766 260 sNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVqeGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPlPMFSFTGTRGSFRGDHhfYGKQGIKFYTQTKTV 498
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFD-PDCPFGGYKMSGFGRD--QGMDALDKYLQVKSV 491
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
46-499 |
4.01e-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: 212.85 E-value: 4.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 46 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL 125
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 126 RGLQVVEHCCSI-----------PSLQMGETVANVARdmdtyslvLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLL 194
Cdd:cd07099 81 LALEAIDWAARNaprvlaprkvpTGLLMPNKKATVEY--------RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 195 KPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDApEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKN 274
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 275 HGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQR 352
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 353 INDLIESGVKEGAKLILDGRKITVpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNG 432
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNG----GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24638876 433 TAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTRGSfrGDHHFYGKQGIKFYTQTKTVT 499
Cdd:cd07099 387 ASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
46-499 |
1.45e-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: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 46 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDV 124
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 125 L-----------RGLQVVEHCCSIPSLQMGETVANVardmdTYSlvlPLGVTAGVAPFNFP------AMIPlwmfpvAIT 187
Cdd:cd07098 81 LvtcekirwtlkHGEKALRPESRPGGLLMFYKRARV-----EYE---PLGVVGAIVSWNYPfhnllgPIIA------ALF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 188 TGNTMLLKPSERVPGATMLLMELLNEA----GCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 263
Cdd:cd07098 147 AGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDV 341
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKIydKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 342 GPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAI 421
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 422 GIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN----VPIPVPLPmfsFTGTRGSfrGDHHFYGKQGIKFYTQTKT 497
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQLP---FGGVKGS--GFGRFAGEEGLRGLCNPKS 460
|
..
gi 24638876 498 VT 499
Cdd:cd07098 461 VT 462
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-458 |
1.12e-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: 209.56 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 10 EARHLAKRSYSSAAPTTKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQ 89
Cdd:cd07111 6 ESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 90 VMFKLQALIKENMGELAKNITKEQGKTLADA-EGDVLRGLQVVEHCCSIPSLQmgetvanvARDMDTYSlvlPLGVTAGV 168
Cdd:cd07111 86 HLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL--------DTELAGWK---PVGVVGQI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 169 APFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGS 248
Cdd:cd07111 155 VPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 249 DQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALST-AVFVGDAQAWIPDLVERAQ 327
Cdd:cd07111 235 TEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRlLVQESVAEELIRKLKERMS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 328 KLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGP 407
Cdd:cd07111 315 HLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGP 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 24638876 408 VLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07111 391 VLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
48-479 |
3.37e-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: 207.87 E-value: 3.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 48 PATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRG 127
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 128 LQVVEHCCSIP--SL--QMGETVANVARdmdtYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 203
Cdd:cd07102 83 LERARYMISIAeeALadIRVPEKDGFER----YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 204 TMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDAN 283
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 284 KENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGV 361
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 362 KEGAKLILDGRKITVPGyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGA 441
Cdd:cd07102 318 AKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 24638876 442 AARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSFRG 479
Cdd:cd07102 397 RAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
67-481 |
3.61e-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: 204.43 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 67 AALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEhcCSIPSLQmgETV 146
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID--ISIKAYH--ERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 147 ANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNV 223
Cdd:cd07095 80 GERATPMAQGRAVLrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 224 IHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYER-AGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQR 302
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 303 CMALSTAVFVGDAQ--AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyE 380
Cdd:cd07095 240 CTCARRLIVPDGAVgdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----A 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 381 DGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVP 460
Cdd:cd07095 316 GTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410 420
....*....|....*....|....
gi 24638876 461 I---PVPLPmfsFTGTRGSfrGDH 481
Cdd:cd07095 395 TtgaSSTAP---FGGVGLS--GNH 413
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
26-499 |
4.57e-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: 205.81 E-value: 4.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 103
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGK--TLAdAEGDVLRGLQVVEH----CCSIpslqMGETVA-NVARDMD--TYSLVLPLGVTAGVAPFNFP 174
Cdd:cd07140 86 ELATIESLDSGAvyTLA-LKTHVGMSIQTFRYfagwCDKI----QGKTIPiNQARPNRnlTLTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 175 AMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGK 253
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 254 YIYERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLK 330
Cdd:cd07140 241 HIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 331 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPgyedGYFVGPTILSDVTPSMKCYTEEIFGPVLV 410
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDVEDHMFIAKEESFGPIMI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 411 ILKADT--LDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNV--PIPVPLPmfsFTGTRGSFRGDHhfYGK 486
Cdd:cd07140 396 ISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAP---FGGFKQSGFGKD--LGE 470
|
490
....*....|...
gi 24638876 487 QGIKFYTQTKTVT 499
Cdd:cd07140 471 EALNEYLKTKTVT 483
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
26-458 |
1.05e-59 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 204.74 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 103
Cdd:PRK09847 20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGK----TLADAEGDVLRGL----QVVEHCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPA 175
Cdd:PRK09847 100 ELALLETLDTGKpirhSLRDDIPGAARAIrwyaEAIDKVYGEVATTSSHELAMIVRE--------PVGVIAAIVPWNFPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 176 MIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKY 254
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 255 IYERAGK-NGKRVQSNMGAKNHGIILGDA-NKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD--AQAWIPDLVERAQKLK 330
Cdd:PRK09847 252 LLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 331 VNAGHVPGTDVGPVISAASRQRINDLIESGVKEGaKLILDGRKITVPGYedgyfVGPTILSDVTPSMKCYTEEIFGPVLV 410
Cdd:PRK09847 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 24638876 411 ILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
91-498 |
1.43e-59 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 202.27 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 91 MFKLQALIKENMGELAKNITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAP 170
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 171 FNFPA-MIPLWMFPvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGS 248
Cdd:PRK10090 81 WNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 249 DQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRC-MALSTAVFVGDAQAWIPDLVERAQ 327
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 328 KLKV-NAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFG 406
Cdd:PRK10090 240 AVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 407 PVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNvpipvplpmfsftgtRGSFRGDHHFY-- 484
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHag 380
|
410 420
....*....|....*....|....
gi 24638876 485 ----------GKQGIKFYTQTKTV 498
Cdd:PRK10090 381 wrksgiggadGKHGLHEYLQTQVV 404
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
28-458 |
3.37e-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: 200.88 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVESKTNEWIdVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:cd07083 21 LVIGGEWVDTKERMVS-VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVL-PLGVTAGVAPFNFPAMIPLWMFPVAI 186
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYvGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 187 TTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNG-- 263
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 ----KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPD-LVERAQKLKVNAGHVPG 338
Cdd:cd07083 260 qtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLErLLKRAERLSVGPPEENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGaKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVL--VILKADT 416
Cdd:cd07083 340 TDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE----GEGYFVAPTVVEEVPPKARIAQEEIFGPVLsvIRYKDDD 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24638876 417 LDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07083 415 FAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
29-496 |
3.13e-57 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 197.82 E-value: 3.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 108
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 109 ITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFP-AMIPLWMFPvAIT 187
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 188 TGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRV 266
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 267 QSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPV 344
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVC-ANRLYVQDGvyDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 345 ISAASRQRINDLIESGVKEGAKLILDGRkitvPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIV 424
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638876 425 NANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIpVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTK 496
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
47-498 |
4.28e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 194.19 E-value: 4.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 47 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL- 125
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 126 --RGLQ-VVEHCcsiPSLQMGETvANVARDMDTYSLVL--PLGVTAGVAPFNFPamipLWM---FPV-AITTGNTMLLKP 196
Cdd:PRK09406 87 caKGFRyYAEHA---EALLADEP-ADAAAVGASRAYVRyqPLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 197 SERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHG 276
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 277 IILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRIND 355
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADvYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 356 LIESGVKEGAKLILDGRKITVPGYedgyFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAV 435
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 436 FTTNGAAARKFVNEIDAGQVGVNvPIPVPLPMFSFTGTRGSfrGdhhfYGKQ----GIKFYTQTKTV 498
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 ... |
29-458 |
2.62e-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: 192.67 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKN 108
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 109 ITKEQGK----TLAdaeGDVLRGLQVVEHCCSIPSLQMGeTVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPV 184
Cdd:cd07116 84 ETWDNGKpvreTLA---ADIPLAIDHFRYFAGCIRAQEG-SISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 185 AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHG-QHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNG 263
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKEN--------------TLNQlagaafgaaGQRCMALSTAVFVGDA-QAWIPDLVERAQK 328
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDADdaffdkalegfvmfALNQ---------GEVCTCPSRALIQESIyDRFMERALERVKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 329 LKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYEDGYFVGPTILSDvTPSMKCYTEEIFGPV 408
Cdd:cd07116 310 IKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPV 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24638876 409 LVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07116 389 LAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
47-458 |
1.79e-54 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 190.07 E-value: 1.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 47 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLR 126
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 127 GLQV----VEHCcsiPSlqMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPamipLWMF-----PVaITTGNTMLLKPS 197
Cdd:PRK13968 93 SANLcdwyAEHG---PA--MLKAEPTLVENQQAVIEYRPLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 198 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 277
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 278 ILGDANKENTLNQLAGAAFGAAGQRCMALSTAVF-VGDAQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDL 356
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420
....*....|....*....|..
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVN 458
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
46-500 |
8.58e-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: 187.90 E-value: 8.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 46 HDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVL 125
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 126 --------------RGLQVVEHCCSIPSLqmGETVANVArdmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNT 191
Cdd:cd07101 81 dvaivaryyarraeRLLKPRRRRGAIPVL--TRTTVNRR----------PKGVVGVISPWNYPLTLAVSDAIPALLAGNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 192 MLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVnficdAPEIKA----VSFVGSDQAGKYIYERAGKNGKRVQ 267
Cdd:cd07101 149 VVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEV-----GGAIVDnadyVMFTGSTATGRVVAERAGRRLIGCS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 268 SNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVI 345
Cdd:cd07101 224 LELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 346 SAASRQRINDLIESGVKEGAKLILDGRKITVPGyedGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVN 425
Cdd:cd07101 303 SQAQLDRVTAHVDDAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 426 ANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVpipvplpmfSFTGTRGSF---------RGDHHFYGKQGIKFYTQTK 496
Cdd:cd07101 380 DTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE---------GYAAAWASIdapmggmkdSGLGRRHGAEGLLKYTETQ 450
|
....
gi 24638876 497 TVTQ 500
Cdd:cd07101 451 TVAV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
26-498 |
2.16e-53 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 188.86 E-value: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRS--WSNQSILTRQQVMFKLQALIKENMG 103
Cdd:PLN02466 58 TQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTLADAEGdvlrglqvvehcCSIPSlqmgetvanVARDMDTYS---------------------LVLPL 162
Cdd:PLN02466 138 ELAALETWDNGKPYEQSAK------------AELPM---------FARLFRYYAgwadkihgltvpadgphhvqtLHEPI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 163 GVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHG-QHDAVNFICDAPEIK 241
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 242 AVSFVGSDQAGKYIYERAGK-NGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALS-TAV-------FV 312
Cdd:PLN02466 277 KLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrTFVhervydeFV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 313 GDAQAwipdlveRAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILSD 392
Cdd:PLN02466 357 EKAKA-------RALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 393 VTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN------VPIPvplp 466
Cdd:PLN02466 426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP---- 501
|
490 500 510
....*....|....*....|....*....|..
gi 24638876 467 mfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:PLN02466 502 ---FGGYKMSGIGREK--GIYSLNNYLQVKAV 528
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-461 |
7.32e-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: 184.32 E-value: 7.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKfvESKTNEWIDVHDPATNQVVT-RVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPADHERTIgEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGKTLADAEGDV------LR----GLQVVEHCCSIPSLQmGETvanvardmDTYSLVlPLGVTAGVAPFNFPAMI 177
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfCRyyaaQARELFSDPELPGPT-GEL--------NGLELH-GRGVFVCISPWNFPLAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 178 PLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVI------HGQHdavnfICDAPEIKAVSFVGSDQA 251
Cdd:cd07125 184 FTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 252 GKYIYE-RAGKNGKRVQSN--MGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQ 327
Cdd:cd07125 259 AKLINRaLAERDGPILPLIaeTGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 328 KLKVNAGHVPGTDVGPVISAASRQRINDLIESGVKEgAKLIldgrKITVPGYEDGYFVGPTILSDVTPSmkCYTEEIFGP 407
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLI----APAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGP 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 408 VLVIL--KADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI 461
Cdd:cd07125 412 ILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
26-458 |
4.27e-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: 4.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 26 TKLFIDGKFVESKTNEWIDVhDPATNQVVTRVPKATQAEMQAALESNKKAF--RSWSNQSILtRQQVMFKLQALIKENMG 103
Cdd:TIGR04284 1 SRLLIDGKLVAGSAGTFPTV-NPATEEVLGVAADATAADMDAAIAAARRAFdeTDWSRDTAL-RVRCLRQLRDALRAHVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 104 ELAKNITKEQGKTLADAEGDVLRG-LQVVEHCCSIPSLQMGETVANVARDM--DTYSLVL--PLGVTAGVAPFNFPAMIP 178
Cdd:TIGR04284 79 ELRELTIAEVGAPRMLTAGAQLEGpVDDLGFAADLAESYAWTTDLGVASPMgiPTRRTLRreAVGVVGAITPWNFPHQIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 179 LWMFPVAITTGNTMLLKPSERVPGATMLLMELLNE-AGCPPGVVNVI-HGQHDAVNFICDAPEIKAVSFVGSDQAGKYIY 256
Cdd:TIGR04284 159 LAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATGRAVM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 257 ERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCmALSTAVFVgdAQAWIPDLVERAQK----LKVN 332
Cdd:TIGR04284 239 ADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGC-AITTRLVV--PRARYDEAVAAAAAtmgsIKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 333 AGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrkiTVP-GYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVI 411
Cdd:TIGR04284 316 DPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGG---GRPaDRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24638876 412 LKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:TIGR04284 393 IAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
43-500 |
9.93e-48 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 173.14 E-value: 9.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVLrglqvvehccsipslqmgeTVANVARD---------------------MDTYSLVLPLGVTAGVAPFNFPA------ 175
Cdd:PRK09407 114 EVL-------------------DVALTARYyarrapkllaprrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 176 MIPlwmfpvAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVnficdAPEIKA----VSFVGSDQA 251
Cdd:PRK09407 175 AIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV-----GTALVDnadyLMFTGSTAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 252 GKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKL 329
Cdd:PRK09407 244 GRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-IYVHEsiYDEFVRAFVAAVRAM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 330 KVNAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvpgYED-G-YFVGPTILSDVTPSMKCYTEEIFGP 407
Cdd:PRK09407 323 RLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKA-----RPDlGpLFYEPTVLTGVTPDMELAREETFGP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 408 VLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI-----PVPLPMfsfTGTRGSFRGDHH 482
Cdd:PRK09407 398 VVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYaaawgSVDAPM---GGMKDSGLGRRH 474
|
490
....*....|....*...
gi 24638876 483 fyGKQGIKFYTQTKTVTQ 500
Cdd:PRK09407 475 --GAEGLLKYTESQTIAT 490
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
28-461 |
1.97e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 171.68 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKFVESKTNEwIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAK 107
Cdd:PRK09457 3 LWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 108 NITKEQGKTLADAEGDVlrGLQVVEHCCSIPSLQmgETVANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPV 184
Cdd:PRK09457 82 VIARETGKPLWEAATEV--TAMINKIAISIQAYH--ERTGEKRSEMADGAAVLrhrPHGVVAVFGPYNFPGHLPNGHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 185 AITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYER-AGKNG 263
Cdd:PRK09457 158 ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQfAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 264 KRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFVGD---AQAWIPDLVERAQKLKVNAGHV-PGT 339
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQgaqGDAFLARLVAVAKRLTVGRWDAePQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 340 DVGPVISAASRQRI----NDLIESgvkeGAKLILDGRKITvpgyEDGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKAD 415
Cdd:PRK09457 317 FMGAVISEQAAQGLvaaqAQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYD 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24638876 416 TLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI 461
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPL 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
27-497 |
1.66e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 169.17 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 27 KLFIDGKFVESKTNEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELA 106
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 107 KNITKEQGKTLADAEGDVLRGLQVVEHCCS--IPSLQMGETVANVA---RDMDTYSLV--LPLGVTAGVAPFNFPAMIPL 179
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEegVRILGEGKFLVSDSfpgNERNKYCLTskIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 180 WMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDqAGKYIYER 258
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 259 AGKngKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALS-TAVFVGDAQAWIPDLVERAQKLKVNAGHvP 337
Cdd:PLN00412 256 AGM--VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKvVLVMESVADALVEKVNAKVAKLTVGPPE-D 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 338 GTDVGPVISAASRQRINDLIESGVKEGAKLILDGRKitvpgyeDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTL 417
Cdd:PLN00412 333 DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 418 DDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPiPVPLP-MFSFTGTRGSfrgdhhFYGKQGIK----FY 492
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQGITnsinMM 478
|
....*
gi 24638876 493 TQTKT 497
Cdd:PLN00412 479 TKVKS 483
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
43-491 |
2.76e-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: 164.90 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQ-SILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE 121
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 122 GDVLRGLQVVEHCCSIPSLQ------MGETVANVARDmdTYSLVLPLGVTAGVAPFNFPA-MIPLWMFPvAITTGNTMLL 194
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLggreipMGLTPASAGRI--AFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 195 KPSERVPGATMLLMELLNEAGCPPGVVN-VIHGQHDAVNFICDaPEIKAVSFVGSDQAGKYIYERAGKnGKRVqsnmgAK 273
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC-----AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 274 NHG-----IILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVIS 346
Cdd:cd07148 231 EHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR-VFVPAeiADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 347 AASRQRINDLIESGVKEGAKLILDGRKITVPGYEdgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNA 426
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24638876 427 NPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPIPVPLPMFSFTGTRGSfrGdhhfYGKQGIKF 491
Cdd:cd07148 384 LPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
43-460 |
2.08e-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: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 43 IDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DV----------------LRGLqvvehccSIPSLQMGEtvanvaRDMDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAI 186
Cdd:cd07130 94 EVqemidicdfavglsrqLYGL-------TIPSERPGH------RMMEQWN---PLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 187 TTGNTMLLKPSERVP----GATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKN 262
Cdd:cd07130 158 VCGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 263 GKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQAwiPDLVERAQKL--KVNAGH--VPG 338
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHESIY--DEVLERLKKAykQVRIGDplDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDLIESGVKEGAKLILDGRKITVPGYedgyFVGPTILSdVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN----YVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 24638876 419 DAIGIVNANPYGNGTAVFTTNGAAARKFVNEI--DAGQVGVNVP 460
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
9-458 |
6.38e-37 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 145.73 E-value: 6.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 9 AEARHLAKRSYSSAAPttklFIDGkfveskTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTR 87
Cdd:PRK11904 540 AAAIAAFLEKQWQAGP----IING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEER 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 88 QQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVlRglqvvehccsipslqmgETV------ANVARDMDTYSLVLP 161
Cdd:PRK11904 610 AAILERAADLLEANRAELIALCVREAGKTLQDAIAEV-R-----------------EAVdfcryyAAQARRLFGAPEKLP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 162 -------------LGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQH 228
Cdd:PRK11904 672 gptgesnelrlhgRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDG 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 229 DAV-NFICDAPEIKAVSFVGSDQAGKYIyER--AGKNGKRVQ--SNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRC 303
Cdd:PRK11904 752 ATVgAALTADPRIAGVAFTGSTETARII-NRtlAARDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRC 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 304 MALStAVFVGD--AQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESgVKEGAKLILdgrKITVP-GYE 380
Cdd:PRK11904 831 SALR-VLFVQEdiADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLA---QLPLPaGTE 905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 381 DGYFVGPTILSdvTPSMKCYTEEIFGPVL--VILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:PRK11904 906 NGHFVAPTAFE--IDSISQLEREVFGPILhvIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
73-500 |
5.57e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 134.39 E-value: 5.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 73 KKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHCCS-IPSLQMGETV--AN 148
Cdd:PTZ00381 17 KESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKhLDEYLKPEKVdtVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 149 VARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQH 228
Cdd:PTZ00381 97 VFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 229 DAVNFICDAPeIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALST 308
Cdd:PTZ00381 176 EVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 309 aVFVGDA--QAWIPDLverAQKLKVNAGHVPGT--DVGPVISAASRQRINDLIESgvkegaklilDGRKITVPGYED--G 382
Cdd:PTZ00381 255 -VLVHRSikDKFIEAL---KEAIKEFFGEDPKKseDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEVDieN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 383 YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVNVPI- 461
Cdd:PTZ00381 321 KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVf 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 24638876 462 ---PVPLPmfsFTGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 500
Cdd:PTZ00381 401 hllNPNLP---FGGVGNSGMGAYH--GKYGFDTFSHPKPVLN 437
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
45-458 |
5.88e-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: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPATNQ-VVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 123
Cdd:TIGR01238 55 VTNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VLrglQVVEHCcsipslqmgETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGA 203
Cdd:TIGR01238 135 VR---EAVDFC---------RYYAKQVRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 204 TMLLMELLNEAGCPPGVVNVIHGQHDAVN-FICDAPEIKAVSFVGSDQAGKYIYERAGKNGK---RVQSNMGAKNHGIIL 279
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 280 GDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVERA-QKLKVNAGHVPGTDVGPVISAASRQRINDLIE 358
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 359 SgVKEGAKLILDGRKITVPGYEDGYFVGPTILSdvTPSMKCYTEEIFGPVL--VILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:TIGR01238 363 H-MSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVH 439
|
410 420
....*....|....*....|..
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVN 458
Cdd:TIGR01238 440 SRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
28-449 |
7.17e-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: 7.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 28 LFIDGKfvESKTNEWIDVHDPAT-NQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALI--KENMGE 104
Cdd:cd07123 35 LVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgKYRYEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 105 LAKNITKeQGKTLADAEGDV-------LRglQVVEHCCSIPSLQMGETVANVARDMDtYSlvlPL-GVTAGVAPFNFPAM 176
Cdd:cd07123 113 NAATMLG-QGKNVWQAEIDAacelidfLR--FNVKYAEELYAQQPLSSPAGVWNRLE-YR---PLeGFVYAVSPFNFTAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 177 ------IPLWMfpvaittGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSD 249
Cdd:cd07123 186 ggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 250 QAGKYIYERAG------KNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALStavfvgdaQAWIPD-- 321
Cdd:cd07123 259 PTFKSLWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAS--------RAYVPEsl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 322 -------LVERAQKLKVnaGHVP--GTDVGPVISAASRQRINDLIESGVKE-GAKLILDGRkitvpgYED--GYFVGPTI 389
Cdd:cd07123 331 wpevkerLLEELKEIKM--GDPDdfSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK------CDDsvGYFVEPTV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638876 390 LSDVTPSMKCYTEEIFGPVLVIL--KADTLDDAIGIVN-ANPYGNGTAVFttngAAARKFVNE 449
Cdd:cd07123 403 IETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDtTSPYALTGAIF----AQDRKAIRE 461
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
63-498 |
5.96e-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: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 63 AEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGK-----TLAD---AEGDVLRGLQVVE-- 132
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRppfetLLTEvsgVKNDILHMLKNLKkw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 133 ---HCCSIPSLQMGETVANVARDmdtyslvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLME 209
Cdd:cd07135 85 akdEKVKDGPLAFMFGKPRIRKE--------PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 210 LLNEAgCPPGVVNVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGD 281
Cdd:cd07135 157 LVPKY-LDPDAFQVVQG---------GVPETTAlleqkfdkIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 282 ANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQAwiPDLVERAQKlkVNAGHVPG-----TDVGPVISAASRQRINDL 356
Cdd:cd07135 227 ADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSVY--DEFVEELKK--VLDEFYPGganasPDYTRIVNPRHFNRLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IEsgvKEGAKLILDGRKItvpgyEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVF 436
Cdd:cd07135 302 LD---TTKGKVVIGGEMD-----EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIF 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24638876 437 TTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTRGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:cd07135 374 TDDKSEIDHILTRTRSGGVVINdTLIHVGVDNAPFGGVGDSGYGAYH--GKYGFDTFTHERTV 434
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
8-445 |
5.08e-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: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 8 GAEARHLAKRSYSSAAPTTK---LFIDGKFVeSKTNEWIDVHDPATNQ-VVTRVPKATQAEMQAALESNKKAFRSWSNQS 83
Cdd:TIGR01236 11 GSPERDLLRKSLKELKSSSLeipLVIGGEEV-YDSNERIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDAKKDWSNLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 84 ILTRQQVMFKLQALIK-ENMGELAKNITKEQGKTLADAEGDVLRGLQ---------VVEHCCSIPSLQMGETVANVARDM 153
Cdd:TIGR01236 90 FYDRAAIFLKAADLLSgPYRYEILAATMLGQSKTVYQAEIDAVAELIdffrfnvkyARELYAQQPISAPGEWNRTEYRPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 154 DtyslvlplGVTAGVAPFNFPAM------IPLWMfpvaittGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQ 227
Cdd:TIGR01236 170 E--------GFVYAISPFNFTAIagnlagAPALM-------GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 228 HDAVNFICDA-PEIKAVSFVGSDQAGKYIYERAGKN-GK-----RVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAG 300
Cdd:TIGR01236 235 GVQVSDQVLAdPDLAGIHFTGSTNTFKHLWKKVAQNlDRyhnfpRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 301 QRCMALSTAvFVGDA--QAWIPDLVERAQKLKVnaghVPGTDV----GPVISAASRQRINDLIESGVKEGAKL-ILDGRK 373
Cdd:TIGR01236 315 QKCSAASRL-YVPHSkwPEFKSDLLAELQSVKV----GDPDDFrgfmGAVIDEQSFDKIVKYIEDAKKDPEALtILYGGK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24638876 374 itvpgYED--GYFVGPTILSDVTPSMKCYTEEIFGPVL-VILKADTLDDAIG--IVNANPYGNGTAVFTTNGAAARK 445
Cdd:TIGR01236 390 -----YDDsqGYFVEPTVVESKDPDHPLMSEEIFGPVLtVYVYPDDKYKEILdlVDSTSQYGLTGAVFAKDRKAILE 461
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
66-458 |
6.49e-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: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAE-GDVLRGLQVVEHC---------- 134
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHAlkhlkkwmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 135 --CSIPSLQMGETvANVARDmdtyslvlPLGVTAGVAPFNFP---AMIPLwmfpV-AITTGNTMLLKPSERVPGATMLLM 208
Cdd:cd07087 81 rrVSVPLLLQPAK-AYVIPE--------PLGVVLIIGPWNYPlqlALAPL----IgAIAAGNTVVLKPSELAPATSALLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 209 ELLNEAgCPPGVVNVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILG 280
Cdd:cd07087 148 KLIPKY-FDPEAVAVVEG---------GVEVATAllaepfdhIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 281 DANKENTLNQLAGAAFGAAGQRCMALSTaVFVgdAQAWIPDLVERAQKlKVNA--GHVPG--TDVGPVISAASRQRINDL 356
Cdd:cd07087 218 DANLEVAARRIAWGKFLNAGQTCIAPDY-VLV--HESIKDELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 357 IESGvkegaklildgrKITVPGYED--GYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP-----Y 429
Cdd:cd07087 294 LDDG------------KVVIGGQVDkeERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY 361
|
410 420
....*....|....*....|....*....
gi 24638876 430 gngtaVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07087 362 -----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
45-430 |
9.50e-31 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 127.29 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 45 VHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGD 123
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 124 VlRglqvvehccsipslqmgETV------ANVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPS 197
Cdd:PRK11905 651 V-R-----------------EAVdflryyAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPA 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 198 ERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAGKYIY----ERAGKNGKRVqSNMGA 272
Cdd:PRK11905 713 EQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQrtlaKRSGPPVPLI-AETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 273 KNHGIILGDANKENTLNQLAGAAFGAAGQRCMALStAVFVGD--AQAWIPDLVERAQKLKV-NAGHVPgTDVGPVISAAS 349
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALR-VLCLQEdvADRVLTMLKGAMDELRIgDPWRLS-TDVGPVIDAEA 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 350 RQRINDLIESGVKEGAKLildgRKITVP-GYEDGYFVGPTI-----LSDVtpsmkcyTEEIFGPVLVIL--KADTLDDAI 421
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLV----HQLPLPaETEKGTFVAPTLieidsISDL-------EREVFGPVLHVVrfKADELDRVI 938
|
....*....
gi 24638876 422 GIVNANPYG 430
Cdd:PRK11905 939 DDINATGYG 947
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
47-460 |
4.95e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 123.02 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 47 DPATNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEGDVLR 126
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 127 GLQVVEHCCSIpSLQMGETVANVARD----MDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVP- 201
Cdd:PLN02315 120 IIDMCDFAVGL-SRQLNGSIIPSERPnhmmMEVWN---PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPl 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 202 ---GATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII 278
Cdd:PLN02315 196 itiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 279 LGDANKENTLNQLAGAAFGAAGQRC-----MALSTAVFvgdaQAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRI 353
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCttcrrLLLHESIY----DDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 354 NDLIESGVKEGAKLILDGRKITvpgyEDGYFVGPTILsDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGT 433
Cdd:PLN02315 352 EKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410 420
....*....|....*....|....*....
gi 24638876 434 AVFTTNGAAARKFVNEI--DAGQVGVNVP 460
Cdd:PLN02315 427 SIFTRNPETIFKWIGPLgsDCGIVNVNIP 455
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
161-458 |
8.06e-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: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 161 PLGVTAGVAPFNFP---AMIPLwmfPVAITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDA 237
Cdd:cd07134 100 PKGVCLIISPWNYPfnlAFGPL---VSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 238 PeIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTaVFVGDAQA 317
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 318 wiPDLVERAQKL--KV---NAGHVPGTDVGPVISAASRQRINDLIESGVKEGAKLILDGrKITvpgyEDGYFVGPTILSD 392
Cdd:cd07134 254 --DAFVEHLKAEieKFygkDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFD----AAQRYIAPTVLTN 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24638876 393 VTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07134 327 VTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
22-458 |
2.76e-29 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 122.74 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 22 AAPTtklfIDGkfvESKTNEWIDVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKE 100
Cdd:COG4230 558 AAPL----IAG---EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 101 NMGELAKNITKEQGKTLADAEGDVlRglqvvehccsipslqmgETV-------ANVARDMDTYSLVLPLGVTAGVAPFNF 173
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIAEV-R-----------------EAVdfcryyaAQARRLFAAPTVLRGRGVFVCISPWNF 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 174 PAMIplwmF----PVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV--NFICDaPEIKAVSFVG 247
Cdd:COG4230 693 PLAI----FtgqvAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgaALVAD-PRIAGVAFTG 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 248 SDQAGKYIyER--AGKNGKRV--------QSNM-----------------------Gaknhgiilgdankentlnqlaga 294
Cdd:COG4230 768 STETARLI-NRtlAARDGPIVpliaetggQNAMivdssalpeqvvddvlasafdsaG----------------------- 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 295 afgaagQRCMALStAVFVGDAQAwiPDLVER----AQKLKV-NAGHvPGTDVGPVISAASRQRINDLIESGVKEGAKLIl 369
Cdd:COG4230 824 ------QRCSALR-VLCVQEDIA--DRVLEMlkgaMAELRVgDPAD-LSTDVGPVIDAEARANLEAHIERMRAEGRLVH- 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 370 dgrKITVP-GYEDGYFVGPTI-----LSDVtpsmkcyTEEIFGPVLVIL--KADTLDDAIGIVNANPYGNGTAVFTTNGA 441
Cdd:COG4230 893 ---QLPLPeECANGTFVAPTLieidsISDL-------EREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDE 962
|
490
....*....|....*..
gi 24638876 442 AARKFVNEIDAGQVGVN 458
Cdd:COG4230 963 TIDRVAARARVGNVYVN 979
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
66-458 |
9.20e-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: 9.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGK------TLADaegdVLRGLQVVEHCCS--- 136
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHrsrhetLLAE----ILPSIAGIKHARKhlk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 137 --------IPSLQMGETVANVardmdTYSlvlPLGVTAGVAPFNFP---AMIPLwmfPVAITTGNTMLLKPSERVPGATM 205
Cdd:cd07133 77 kwmkpsrrHVGLLFLPAKAEV-----EYQ---PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 206 LLMELLNEAGcPPGVVNVIHGqhdavnficDAPEIKAVS--------FVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGI 277
Cdd:cd07133 146 LLAELLAEYF-DEDEVAVVTG---------GADVAAAFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 278 ILGDANKENTLNQLAGAAFGAAGQRCMA----L----STAVFVGDAQAWI----PDLVEraqklkvnaghvpGTDVGPVI 345
Cdd:cd07133 216 IAPDADLAKAAERIAFGKLLNAGQTCVApdyvLvpedKLEEFVAAAKAAVakmyPTLAD-------------NPDYTSII 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 346 SAASRQRINDLIESGVKEGAKLI---------LDGRKITvpgyedgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADT 416
Cdd:cd07133 283 NERHYARLQGLLEDARAKGARVIelnpagedfAATRKLP-----------PTLVLNVTDDMRVMQEEIFGPILPILTYDS 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24638876 417 LDDAIGIVNANP-----YgngtaVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07133 352 LDEAIDYINARPrplalY-----YFGEDKAEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
161-498 |
1.24e-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: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 161 PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGQHDAVNFICDAP 238
Cdd:cd07137 101 PLGVVLVISAWNFP--FLLSLEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 239 EIKaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAA-FGAAGQRCMALStavFVGDAQA 317
Cdd:cd07137 178 WDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQACIAPD---YVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 318 WIPDLVERAQK-LKVNAGHVPGT--DVGPVISAASRQRINDLIESgvKEGAKLILDGRKITvpgyEDGYFVGPTILSDVT 394
Cdd:cd07137 254 FAPTLIDALKNtLEKFFGENPKEskDLSRIVNSHHFQRLSRLLDD--PSVADKIVHGGERD----EKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 395 PSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGT 473
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGGV 407
|
330 340
....*....|....*....|....*
gi 24638876 474 RGSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:cd07137 408 GESGFGAYH--GKFSFDAFSHKKAV 430
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
161-458 |
3.22e-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: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 161 PLGVTAGVAPFNFP---AMIPLwmfpV-AITTGNTMLLKPSERVPGATMLLMELLNEAgCPPGVVNVIHGqhdavnficD 236
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlALAPL----IgAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG---------G 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 237 APEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENT---------LNqlagaafgaA 299
Cdd:cd07136 166 VEENQElldqkfdyIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAakrivwgkfLN---------A 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 300 GQRCMAlstavfvgdaqawiPD--LVERAQKLKV--------------NAGHVPgtDVGPVISAASRQRINDLIESG-VK 362
Cdd:cd07136 237 GQTCVA--------------PDyvLVHESVKEKFikelkeeikkfygeDPLESP--DYGRIINEKHFDRLAGLLDNGkIV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 363 EGAKLILDGRKITvpgyedgyfvgPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANP-----YgngtaVFT 437
Cdd:cd07136 301 FGGNTDRETLYIE-----------PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFS 364
|
330 340
....*....|....*....|.
gi 24638876 438 TNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07136 365 EDKKVEKKVLENLSFGGGCIN 385
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
66-413 |
2.16e-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: 96.54 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKT---LADAEGDV--LRGLQVVEHCCSIPSl 140
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 141 QMGETVaNVARDMDTYSLVLPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAG-CPPG 219
Cdd:cd07084 81 EPGNHL-GQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 220 VVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAgKNGkRVQSNMGAKNHGIILGDAN-KENTLNQLAGAAFGA 298
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA-KQA-RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 299 AGQRCMALStAVFVGDAQAWIPdLVERAQKLkVNAGHVPGTDVGPVISAASRQRINDLIESGvkeGAKLILDGRKitVPG 378
Cdd:cd07084 238 SGQKCTAQS-MLFVPENWSKTP-LVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKE--LKN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24638876 379 YEDGYFVGPTILSDV-------TPSMKCYTEEIFGPVLVILK 413
Cdd:cd07084 310 HSIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVE 351
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
44-430 |
5.96e-21 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 96.97 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 44 DVHDPA-TNQVVTRVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLADAEG 122
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 123 DVlRglqvvehccsipslqmgETV------ANVAR---DMDTYSlvlPLGVTAGVAPFNFPAMIPLWMFPVAITTGNTML 193
Cdd:PRK11809 742 EV-R-----------------EAVdflryyAGQVRddfDNDTHR---PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 194 LKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAV-NFICDAPEIKAVSFVGSDQAG----KYIYERAGKNGKRVQ- 267
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVArllqRNLAGRLDPQGRPIPl 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 268 -SNMGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMALSTAVFVGD-AQAWIPDLVERAQKLKV-NAGHVpGTDVGPV 344
Cdd:PRK11809 881 iAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMgNPDRL-STDIGPV 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 345 ISAASRQRINDLIESgvkegakLILDGRKITVPGYED------GYFVGPTI--LSDVTPsmkcYTEEIFGPVLVIL--KA 414
Cdd:PRK11809 960 IDAEAKANIERHIQA-------MRAKGRPVFQAARENsedwqsGTFVPPTLieLDSFDE----LKREVFGPVLHVVryNR 1028
|
410
....*....|....*.
gi 24638876 415 DTLDDAIGIVNANPYG 430
Cdd:PRK11809 1029 NQLDELIEQINASGYG 1044
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
66-458 |
2.15e-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: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 66 QAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGE----LAKNITKEQGKTLAdAEGDVLRGlqvvEHCCSIPSLQ 141
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEiveaLAKDLRKPKFEAVL-SEILLVKN----EIKYAISNLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 142 mgETVAN--VARDMDTY--SLVL---PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELL- 211
Cdd:cd07132 76 --EWMKPepVKKNLATLldDVYIykePLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 212 ----NEagCPPgvvnVIHGqhdavnficDAPEIKA--------VSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIIL 279
Cdd:cd07132 152 kyldKE--CYP----VVLG---------GVEETTEllkqrfdyIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 280 GDANKENTLNQLAGAAFGAAGQRCMAlstavfvgdaqawiPD-----------LVERAQK-LKVNAGHVPGT--DVGPVI 345
Cdd:cd07132 217 KSCDIDVAARRIAWGKFINAGQTCIA--------------PDyvlctpevqekFVEALKKtLKEFYGEDPKEspDYGRII 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 346 SAASRQRINDLIESGvkegaklildgrKITVPGYEDG--YFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLDDAIGI 423
Cdd:cd07132 283 NDRHFQRLKKLLSGG------------KVAIGGQTDEkeRYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEF 350
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24638876 424 VNA--NP---YgngtaVFTTNGAAARKFVNEIDAGQVGVN 458
Cdd:cd07132 351 INSreKPlalY-----VFSNNKKVINKILSNTSSGGVCVN 385
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
161-498 |
7.52e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 86.25 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 161 PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLnEAGCPPGVVNVIHGQHDAVNFICDAPEI 240
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 241 KaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGIILGDANKENTLNQLAGAA-FGAAGQRCMALStavFVGDAQAWI 319
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKwGCNNGQACISPD---YILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 320 PDLVERAQK-LKVNAGHVP--GTDVGPVISAASRQRINDLIESgvKEGA-KLILDGRKitvpgYEDGYFVGPTILSDVTP 395
Cdd:PLN02174 267 PKVIDAMKKeLETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSdKIVYGGEK-----DRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 396 SMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSFTGTR 474
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVG 419
|
330 340
....*....|....*....|....
gi 24638876 475 GSFRGDHHfyGKQGIKFYTQTKTV 498
Cdd:PLN02174 420 ESGMGAYH--GKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
161-500 |
1.46e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 79.00 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 161 PLGVTAGVAPFNFPamIPLWMFPV--AITTGNTMLLKPSERVPGATMLLMELLnEAGCPPGVVNVIHGQHDAVNFICDAP 238
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 239 EIKaVSFVGSDQAGKYIYERAGKNGKRVQSNMGAKNHGII--LGDA-NKENTLNQLAGAA-FGAAGQRCMALStavFVGD 314
Cdd:PLN02203 185 WDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKwGSCAGQACIAID---YVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 315 AQAWIPDLVERAQK-LKVNAGHVPG--TDVGPVISAASRQRINDLIESgvKEGAKLILDGRKITvpgyEDGYFVGPTILS 391
Cdd:PLN02203 261 EERFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD--PRVAASIVHGGSID----EKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 392 DVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNANPYGNGTAVFTTNGAAARKFVNEIDAGQVGVN-VPIPVPLPMFSF 470
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdAIIQYACDSLPF 414
|
330 340 350
....*....|....*....|....*....|
gi 24638876 471 TGTRGSFRGDHHfyGKQGIKFYTQTKTVTQ 500
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 ... |
29-450 |
8.06e-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: 67.29 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESkTNEWIDVHDPATNQVVTRVPKATqAEMQAAL----ESNKKAFRSWSNQsilTRQQVMFKLQALIKENMGE 104
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVSSEG-LDFAAAVayarEKGGPALRALTFH---ERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 105 LAKnITKEQGKTLADAEGDVLRGLQVVEHCCSIPSLQMGEtvANVARDMDTYSL-----------VLPL-GVTAGVAPFN 172
Cdd:cd07128 79 LYA-LSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPN--AHFLVEGDVEPLskdgtfvgqhiLTPRrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 173 FPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAG-CPPGvvnvihgqhdAVNFICDAP--------EIKAV 243
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEG----------ALQLICGSVgdlldhlgEQDVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 244 SFVGSDQAGKYIYERAGKNGKRVQSNMGAKN-HGIILGDANKENT------LNQLAGAAFGAAGQRCMALSTAvFVGDAQ 316
Cdd:cd07128 226 AFTGSAATAAKLRAHPNIVARSIRFNAEADSlNAAILGPDATPGTpefdlfVKEVAREMTVKAGQKCTAIRRA-FVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 317 --AWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIESgVKEGAKLIL---DGRKITVPGYEDGYFVGPTIL- 390
Cdd:cd07128 305 vdAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGAFFPPTLLl 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24638876 391 -SDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNAnpyGNG---TAVFTTNGAAARKFVNEI 450
Cdd:cd07128 384 cDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELVLGA 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
29-488 |
9.89e-12 |
|
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: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 29 FIDGKFVESKtnEWIDVHDPATNQVVTRVPKATQAEMQAALESNKKAFRSW------SNQSILTRQQVMFKLQALIKENM 102
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhnplkNPERYLLYGDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 103 GE--LAKNITKEQGKTLADAEGDVLRGLQVVEHCC--SIPSLQMGETVANVARDMDTYSLVLPLGVTAGVAPFNFPAMIP 178
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 179 LWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGS---------D 249
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSskvaerlalE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 250 QAGKYIYERAGKNGKrvqsnmgaknhgiILG-DANKENTLN-QLAGAAFGAAGQRCMALSTaVFVGD--AQAWIPDlver 325
Cdd:cd07126 240 LHGKVKLEDAGFDWK-------------ILGpDVSDVDYVAwQCDQDAYACSGQKCSAQSI-LFAHEnwVQAGILD---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 326 aqKLKVNAGHVPGTD--VGPVISAASrQRINDLIESGVK-EGAKLILDGRKITVPGYEDGY--------FVgPTILSDVT 394
Cdd:cd07126 302 --KLKALAEQRKLEDltIGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKPLTNHSIPSIYgayeptavFV-PLEEIAIE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 395 PSMKCYTEEIFGP--VLVILKADTLDDAIGIVNANPYgNGTAVFTTNGAaarKFVNEIDAGQV-GVnvpipvplpmfSFT 471
Cdd:cd07126 378 ENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHA-HLTAAVVSNDI---RFLQEVLANTVnGT-----------TYA 442
|
490
....*....|....*....
gi 24638876 472 GTRGSFRG--DHHFYGKQG 488
Cdd:cd07126 443 GIRARTTGapQNHWFGPAG 461
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
62-461 |
3.16e-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: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 62 QAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNI--TKEQGKTLADAEG-----DvlRGLQVV--- 131
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVmhTTGQAFMMAFQAGgphaqD--RGLEAVaya 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 132 --------EHCCSIPSLQMGETVAnvardMDTYSLVLPLGVTAGVAPFNFPAmiplW-----MFpVAITTGNTMLLKPSe 198
Cdd:cd07127 161 wremsripPTAEWEKPQGKHDPLA-----MEKTFTVVPRGVALVIGCSTFPT----WngypgLF-ASLATGNPVIVKPH- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 199 rvPGATMLLM-------ELLNEAGCPPGVVNVI--HGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAGknGKRVQSN 269
Cdd:cd07127 230 --PAAILPLAitvqvarEVLAEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANAR--QAQVYTE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 270 MGAKNHGIILGDANKENTLNQLAGAAFGAAGQRCMAlSTAVFV-----GDAQAWI------PDLVERAQKLKVNaGHVPG 338
Cdd:cd07127 306 KAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT-PQNIYVprdgiQTDDGRKsfdevaADLAAAIDGLLAD-PARAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 339 TDVGPVISAASRQRINDliesgVKEGAKLILDGRKITVPGYEDGYFVGPTILSDVTPSMKCYTEEIFGPVLVILKADTLD 418
Cdd:cd07127 384 ALLGAIQSPDTLARIAE-----ARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTD 458
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24638876 419 DAIGIVNANPYGNGT---AVFTTNGAAARKFVNEidAGQVGVNVPI 461
Cdd:cd07127 459 HSIELARESVREHGAmtvGVYSTDPEVVERVQEA--ALDAGVALSI 502
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
165-450 |
5.09e-08 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 55.48 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 165 TAGVA----PFNFPAMiPLW-MFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGC-PPGVVNVIHGQH----DAVNfi 234
Cdd:PRK11903 148 TRGVAlfinAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSagllDHLQ-- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 235 cdapEIKAVSFVGSDQAGKYIYERAGKNGKRVQSNMGAK--NHGIILGDANKENT-----LNQLAGAAFGAAGQRCMALS 307
Cdd:PRK11903 225 ----PFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADslNSALLGPDAAPGSEafdlfVKEVVREMTVKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 308 TaVFVGDA--QAWIPDLVERAQKLKVNAGHVPGTDVGPVISAASRQRINDLIEsGVKEGAKLILDGRKITVPGYED--GY 383
Cdd:PRK11903 301 R-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavAA 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638876 384 FVGPTIL--SDVTPSMKCYTEEIFGPVLVILKADTLDDAIGIVNAnpyGNG---TAVFTTNGAAARKFVNEI 450
Cdd:PRK11903 379 CVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARR---GQGslvASVYSDDAAFLAAAALEL 447
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
56-334 |
3.87e-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: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 56 RVPKATQAEMQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKT---LADAEgDVLRGL-QVV 131
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSeskLYKNI-DTERGItASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 132 EHCCSIPSLQMGETvanvardmdtYSLVLPLGVTAGVAPFNFPAMIPLWMFpVAITTGNTMLLKPSERVP----GATMLL 207
Cdd:cd07077 81 GHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPftnrALALLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 208 MELLNEAGCPPGVVNVIHGQHDAVNFICDAPEIKAVSFVGSDQAGKYIYERAgkNGKRVQSnMGAKNHGIILGDANKENT 287
Cdd:cd07077 150 QAADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIG-FGAGNSPVVVDETADEER 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24638876 288 LNQLAGAAFGAAGQRCMALSTAVFVGDAQAWIPDLVE---RAQKLKVNAG 334
Cdd:cd07077 227 ASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKlklVVEGLKVPQE 276
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
153-434 |
6.01e-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: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 153 MDTYSLVLPLGVTAGVAPFNFP-AmiplwmFPV-------AITTGNTMLLKPSERVPGATMLLMEL----LNEAGCPPGV 220
Cdd:cd07129 97 PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 221 VNVIHGQHDAVNF-ICDAPEIKAVSFVGSDQAGKYIYERAGK--NGKRVQSNMGAKNHGIILGDANKEN--TLNQ-LAGA 294
Cdd:cd07129 171 FSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 295 AFGAAGQRCmalsTA---VFV---GDAQAWIPDLVERAQKlkvnagHVPGTDVGPVISAASRQRINDLIESGvkeGAKLI 368
Cdd:cd07129 251 LTLGAGQFC----TNpglVLVpagPAGDAFIAALAEALAA------APAQTMLTPGIAEAYRQGVEALAAAP---GVRVL 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24638876 369 LDGrkitvPGYEDGYFVGPTILS-DVT-----PSMkcyTEEIFGPVLVILKADTLDDAIGIVNANPyGNGTA 434
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 ... |
65-460 |
8.26e-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: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 65 MQAALESNKKAFRSWSNQSILTRQQVMFKLQALIKENMGELAKNITKEQGKTLAdaEGDVLRGLQVVEHccsIPSLQMGE 144
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRV--EDKVIKNHFAAEY---IYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 145 TVANVARDMDTYSLVL---PLGVTAGVAPFNFPAMIPLWMFPVAITTGNTMLLKPSERVPGATMLLMELLNEAGCPPG-- 219
Cdd:cd07081 76 KTCGVLTGDENGGTLIiaePIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGap 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 220 ---VVNVIHGQHDAVNFICDAPEIKAVSFVGsdqaGKYIYERAGKNGKRVQSnMGAKNHGIILGD-ANKENTLNQLAGAA 295
Cdd:cd07081 156 enlIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVIDEtADIKRAVQSIVKSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 296 FGAAGQRCMALSTAVFVGDAQAWIPDLVERAQKLKVNAGHVpgTDVGPVIsaasrQRINDLIESGVKEGAKLILDGRKIT 375
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEEL--QQVQPVI-----LKNGDVNRDIVGQDAYKIAAAAGLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24638876 376 VPGYEDGYFVGPTILSDVTPsmkcYTEEIFGPVLVILKADTLDD----AIGIVNANPYGNGTAVFTTNGAAARK---FVN 448
Cdd:cd07081 304 VPQETRILIGEVTSLAEHEP----FAHEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYSDNIKAIENmnqFAN 379
|
410
....*....|..
gi 24638876 449 EIDAGQVGVNVP 460
Cdd:cd07081 380 AMKTSRFVKNGP 391
|
|
| |
