|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-487 |
0e+00 |
|
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: 802.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQ 332
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 333 TSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFIDT 487
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
13-487 |
0e+00 |
|
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: 793.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIILDDA-----NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKT 327
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 328 QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEE 407
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 408 AIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFIDT 487
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
13-487 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 632.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGSVNDID-KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAP 171
Cdd:COG1012 86 AALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 172 AIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRI 250
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMG 330
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 331 SQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGldsGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIK 410
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEG---GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402762489 411 IANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEG-APFGGYKNQVLDRETYKEALSNYQQVKNIFIDT 487
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
21-483 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 614.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 21 FVKGHSdETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNN 100
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 101 GKPIRETSGiDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIV 180
Cdd:pfam00171 80 GKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 181 IQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGG 259
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 260 KSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQME 339
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 340 KIQSYITYAEQSNAEILTGGKRitndGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGL 419
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 420 AGGVFSQDITRALNIAKAVKTGRIWINTYNQV-PEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-485 |
0e+00 |
|
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: 574.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 12 NYGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKT--ERANLLRQISNKMMENK 89
Cdd:cd07091 3 PTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDprERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 90 EKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKI 169
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK 248
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 RIV-PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKT 327
Cdd:cd07091 243 SNLkKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 328 QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDgldsGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDE 406
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK----GYFIQPTVFTdVKDDM-KIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 407 EAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
34-485 |
0e+00 |
|
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: 571.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiD 111
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA-Q 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSVNDIDK-DTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:cd07114 82 VRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 191 LLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDA 269
Cdd:cd07114 162 TLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAE 349
Cdd:cd07114 242 DLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 350 QSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT 429
Cdd:cd07114 322 EEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 430 RALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07114 402 RAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
16-495 |
0e+00 |
|
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: 551.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKIA 93
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 94 TIETLNNGKPIRETSgIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAI 173
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQ 332
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 333 TSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFIDTSNELK 492
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQPI 479
|
...
gi 402762489 493 GLY 495
Cdd:cd07119 480 GWF 482
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
53-485 |
0e+00 |
|
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: 544.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 53 DTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGS 132
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 133 V-NDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVV 210
Cdd:cd07078 80 ViPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 211 TGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVC 290
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 291 SAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitnDGLDSG 370
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKR---LEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 371 YFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQ 450
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 402762489 451 VPE-GAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07078 397 GAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
34-485 |
0e+00 |
|
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: 528.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIP 113
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLE 193
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 194 VAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLD 272
Cdd:cd07093 163 LAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 273 LAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSN 352
Cdd:cd07093 243 RAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 353 AEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRAL 432
Cdd:cd07093 323 ATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAH 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 402762489 433 NIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07093 403 RVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
34-485 |
0e+00 |
|
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: 528.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIP 113
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLE 193
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 194 VAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLD 272
Cdd:cd07115 163 IAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 273 LAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSN 352
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 353 AEILTGGKRITndglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRAL 432
Cdd:cd07115 323 ARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 402762489 433 NIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
28-485 |
0e+00 |
|
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: 525.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 28 ETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIR 105
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 106 ETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSS 185
Cdd:cd07112 82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 186 STPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQV----AEAGAKRIVpatLELGGK 260
Cdd:cd07112 162 QSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFleysGQSNLKRVW---LECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 261 SANIILDDA-NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQME 339
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 340 KIQSYITYAEQSNAEILTGGKRITNDGldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGL 419
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 420 AGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
13-485 |
0e+00 |
|
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: 518.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIIL------DDANLDLAVEGIQLgILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEK 326
Cdd:cd07116 241 VTLELGGKSPNIFFadvmdaDDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 327 TQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAvKDNADKLAQEEIFGPVLTIIKVKDDE 406
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFK-GGNKMRIFQEEIFGPVLAVTTFKDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 407 EAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-486 |
4.94e-175 |
|
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: 500.90 E-value: 4.94e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 12 NYGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFE-SWSLT-SKTERANLLRQISNKMMENK 89
Cdd:cd07143 6 PTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 90 EKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKI 169
Cdd:cd07143 86 DYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK 248
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 -RIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKT 327
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 328 QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGldsgYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEE 407
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEG----YFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 408 AIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFID 486
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-485 |
5.74e-174 |
|
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: 497.48 E-value: 5.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVI------ETHEGSVNDIdkdtmSIIRHEPIGVVGAVVAWNFPMLLAS 166
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALArdfpfeERRPGSGGGH-----VLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEA 245
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 246 GAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDE 325
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 326 KTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDD 405
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 406 EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPeGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
32-483 |
5.76e-170 |
|
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: 486.86 E-value: 5.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIREtSGID 111
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDE-AAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIE----THEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSST 187
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldaKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 188 PLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIIL 266
Cdd:cd07110 160 SLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYIT 346
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 347 YAEQSNAEILTGGKRitNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQ 426
Cdd:cd07110 320 RGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 427 DITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
32-488 |
1.29e-169 |
|
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: 486.04 E-value: 1.29e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIrETSGID 111
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 192 LEVAKIFQEI-LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDAN 270
Cdd:cd07090 160 LLLAEILTEAgLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQ 350
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 351 SNAEILTGGKRIT-NDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT 429
Cdd:cd07090 319 EGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 430 RALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFIDTS 488
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
32-485 |
2.10e-167 |
|
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: 480.59 E-value: 2.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWS-LTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGI 110
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 111 DIPYAARHFNYFASVIETHEGSVNDIDKD-----TMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSS 185
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPAlrggpGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 186 STPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANI 264
Cdd:cd07089 161 DTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 265 ILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSY 344
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 345 ITYAEQSNAEILTGGKRitNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVF 424
Cdd:cd07089 321 IARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402762489 425 SQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-484 |
6.19e-167 |
|
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: 479.69 E-value: 6.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIAT 94
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIRETSGIDIPYAARHFNYFASVI-----ETHEGSvndidkdtmSIIRHEPIGVVGAVVAWNFPMLLASWKI 169
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALkdfefEERRGN---------SLVVREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK 248
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 RIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQ 328
Cdd:cd07138 232 TVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 329 MGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITnDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEA 408
Cdd:cd07138 312 LGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRP-EGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 409 IKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPeGAPFGGYKNQVLDRETYKEALSNYQQVKNIF 484
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-485 |
1.71e-166 |
|
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: 479.15 E-value: 1.71e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFE---SWSLTSKTERANLLRQISNKMMENKEK 91
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 92 IATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAP 171
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 172 AIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGA--- 247
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGksn 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 248 -KRIvpaTLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEK 326
Cdd:cd07141 249 lKRV---TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 327 TQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDD 405
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG----DKGYFIQPTVFSdVTDDM-RIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 406 EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
13-485 |
3.25e-166 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 478.61 E-value: 3.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:PRK13252 87 AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGsESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIV 251
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 252 PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGS 331
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 332 QTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAvkDNAD--KLAQEEIFGPVLTIIKVKDDEEAI 409
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFT--DCTDdmTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 410 KIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
32-485 |
1.55e-165 |
|
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: 475.57 E-value: 1.55e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSL-TSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGi 110
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLrLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 111 DIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 191 LLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDA 269
Cdd:cd07109 160 ALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEkTQMGSQTSQEQMEKIQSYITYAE 349
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 350 QSNAEILTGGkRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT 429
Cdd:cd07109 319 ARGARIVAGG-RIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 430 RALNIAKAVKTGRIWINTYnqvpeGA------PFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07109 398 RALRVARRLRAGQVFVNNY-----GAgggielPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
16-481 |
2.84e-164 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 472.76 E-value: 2.84e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAA 175
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 176 GNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPAT 254
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 255 LELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTS 334
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 335 QEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIAND 414
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 415 SEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVK 481
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
6-486 |
7.34e-164 |
|
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: 472.28 E-value: 7.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 6 KNYLDENYGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES-WSLTSKTERANLLRQISNK 84
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 85 MMENKEKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLL 164
Cdd:cd07144 81 VEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 165 ASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVA 243
Cdd:cd07144 161 AAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 244 EAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAF-SNIKIGDP 322
Cdd:cd07144 241 KAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 323 LDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNdGLDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIK 401
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPE-GLGKGYFIPPTIFTdVPQDM-RIVKEEIFGPVVVISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 402 VKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVK 481
Cdd:cd07144 399 FKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
....*
gi 402762489 482 NIFID 486
Cdd:cd07144 479 AVHIN 483
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
15-488 |
1.92e-163 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 470.93 E-value: 1.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGhSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIAT 94
Cdd:PRK13473 5 LLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSV-NDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAI 173
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAaGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPA 253
Cdd:PRK13473 164 AAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 254 TLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQT 333
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 334 SQEQMEKIQSYITYA-EQSNAEILTGGKRItnDGldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:PRK13473 324 SAAHRDRVAGFVERAkALGHIRVVTGGEAP--DG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFIDTS 488
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-477 |
2.84e-163 |
|
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: 470.72 E-value: 2.84e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 10 DENYGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENK 89
Cdd:cd07111 19 DRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 90 EKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDidkdtmsiirHEPIGVVGAVVAWNFPMLLASWKI 169
Cdd:cd07111 99 RLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAG----------WKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSeSGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK 248
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 RIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQ 328
Cdd:cd07111 248 TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAID 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 329 MGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEA 408
Cdd:cd07111 328 MGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 409 IKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNY 477
Cdd:cd07111 404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
15-483 |
6.81e-163 |
|
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: 469.67 E-value: 6.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFE--SWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK-RI 250
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMG 330
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 331 SQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAI 409
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSdVKDDM-KIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402762489 410 KIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
32-483 |
3.61e-162 |
|
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: 466.91 E-value: 3.61e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiD 111
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFA--------SVIETHEGSVNdidkdtmSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQP 183
Cdd:cd07103 80 VDYAASFLEWFAeearriygRTIPSPAPGKR-------ILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 184 SSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSA 262
Cdd:cd07103 153 AEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQ 342
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 343 SYITYAEQSNAEILTGGKRITNDGldsgYFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAG 421
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLGG----YFYEPTVLTdVTDDML-IMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 422 GVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07103 388 YVFTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
32-485 |
4.02e-162 |
|
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: 466.84 E-value: 4.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGID 111
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 192 LEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANL 271
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 272 DLAVEGIQLGILFN-QGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYA-E 349
Cdd:cd07108 241 DDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGlS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 350 QSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT 429
Cdd:cd07108 321 TSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 430 RALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEA-LSNYQQVKNIFI 485
Cdd:cd07108 401 RALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
32-483 |
4.68e-161 |
|
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: 464.11 E-value: 4.68e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGID 111
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSV-NDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAaGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 191 LLEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDAN 270
Cdd:cd07092 161 TLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQ 350
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 351 sNAEILTGGKRitndGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITR 430
Cdd:cd07092 321 -HARVLTGGRR----AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 402762489 431 ALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
33-485 |
1.09e-153 |
|
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: 445.24 E-value: 1.09e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 33 KNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGi 110
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 111 DIPYAARHFNYFASVIETHEG-SVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPL 189
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 190 SLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDD 268
Cdd:cd07118 161 TTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 269 ANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYA 348
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 349 EQSNAEILTGGKRItnDGLDsGYFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQD 427
Cdd:cd07118 321 RAEGATLLLGGERL--ASAA-GLFYQPTIFTdVTPDMA-IAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 428 ITRALNIAKAVKTGRIWINTY-NQVPEgAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFlDGSPE-LPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
32-485 |
2.79e-150 |
|
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: 436.57 E-value: 2.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiD 111
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFAS------VIEthegsvndiDKDTMSII-RHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPS 184
Cdd:cd07106 80 VGGAVAWLRYTASldlpdeVIE---------DDDTRRVElRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 185 SSTPLSLLEVAKIFQEILPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANI 264
Cdd:cd07106 151 PFTPLCTLKLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 265 ILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSY 344
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 345 ITYAEQSNAEILTGGKRItnDGldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVF 424
Cdd:cd07106 310 VEDAKAKGAKVLAGGEPL--DG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402762489 425 SQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-483 |
6.51e-150 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 437.72 E-value: 6.51e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFE--SWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK-RI 250
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMG 330
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 331 SQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAI 409
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCG----DKGYYIEPTIFTdVTEDM-KIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402762489 410 KIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
16-485 |
1.29e-149 |
|
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: 435.91 E-value: 1.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDEtlEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIAT 94
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIRETSGiDIPYAARHFNYFAS-VIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAI 173
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGeALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQ 332
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 333 TSQEQMEKIQSYITYAEQSNAEILTGGKRITNDglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLKRP--DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN-TYNQVPEGAPFGGYKNQ-VLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSsYGPREQGEAALEFYTTIKTVYV 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
14-495 |
5.40e-148 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 432.62 E-value: 5.40e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 14 GLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAF-----ESWSLTSKTERANLLRQISNKMMEN 88
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 89 KEKIATIETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGSVN---DIDKDTM-SIIRHEPIGVVGAVVAWNFPMLL 164
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAKQKapvSLPMETFkGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 165 ASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVA 243
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 244 EAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPL 323
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 324 DEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVK 403
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 404 DDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
490
....*....|..
gi 402762489 484 FIDTSNELKGLY 495
Cdd:PLN02467 486 TKYISDEPWGWY 497
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
57-485 |
8.62e-147 |
|
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: 424.72 E-value: 8.62e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 57 AAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGS-VND 135
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPeLPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 136 IDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKG 214
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 215 SESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGS 294
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 295 RLLVQEGIYDKLISRLKeafsnikigdpldektqmgsqtsqeqmekiqsyityaeqsnaeiltggkritndgldsgyfle 374
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 375 pTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYN-QVPE 453
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 402762489 454 GAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
16-488 |
1.51e-145 |
|
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: 425.61 E-value: 1.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEK-DVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIAT 94
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVGTFPLSTAsDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIRETSG-----IDIPYaarhfnYFASVIETHEGSVND---IDKDTMSIIRhePIGVVGAVVAWNFPMLLAS 166
Cdd:cd07131 82 LVTREMGKPLAEGRGdvqeaIDMAQ------YAAGEGRRLFGETVPselPNKDAMTRRQ--PIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEA 245
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 246 GAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDE 325
Cdd:cd07131 234 CARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 326 KTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDD 405
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 406 EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINtynqVPE-GA----PFGGYK---NQvlDRETYKEALSNY 477
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN----APTiGAevhlPFGGVKksgNG--HREAGTTALDAF 467
|
490
....*....|.
gi 402762489 478 QQVKNIFIDTS 488
Cdd:cd07131 468 TEWKAVYVDYS 478
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
16-485 |
1.30e-144 |
|
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: 422.83 E-value: 1.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGSV--NDIDKDTMSIIRhEPIGVVGAVVAWNFPMLLASWKIAPAI 173
Cdd:cd07088 81 IVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIipSDRPNENIFIFK-VPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVP 252
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQ 332
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 333 TSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGldsGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
15-481 |
1.20e-143 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 423.06 E-value: 1.20e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAK-RI 250
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMG 330
Cdd:PLN02466 300 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 331 SQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAI 409
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSnVQDDM-LIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 410 KIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVK 481
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
32-485 |
5.18e-142 |
|
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: 415.62 E-value: 5.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 32 VKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiD 111
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 192 LEVAKIFQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANL 271
Cdd:cd07107 160 LRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 272 DLAVEGIQLGILFN-QGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQ 350
Cdd:cd07107 240 EAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 351 SNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITR 430
Cdd:cd07107 320 EGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 431 ALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07107 400 AHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
34-483 |
1.04e-138 |
|
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: 407.11 E-value: 1.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFE--SWSlTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiD 111
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 112 IPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 192 LEVAKIFQEI--LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDA 269
Cdd:cd07120 161 AAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAE 349
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 350 QSNAEILTGGKRITnDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT 429
Cdd:cd07120 321 AAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 402762489 430 RALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
30-485 |
1.19e-137 |
|
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: 404.42 E-value: 1.19e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIREtSG 109
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 IDIPYAARHFNYFASVIETHEGSVNDID-----KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPS 184
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDayeynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 185 SSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSAN 263
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 264 IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQS 343
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 344 YITYAEQSNAEILTGGKRitndglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGV 423
Cdd:cd07145 320 LVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402762489 424 FSQDITRALNIAKAVKTGRIWINTYNQV-PEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-485 |
4.67e-137 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 404.66 E-value: 4.67e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQ-VAEAGAKRI 250
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQlLKDAGDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDA-NLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQM 329
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 330 GSQTSQEQMEKIQSYITYAEQSNAEILtggkritnDGLDSGY--FLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEE 407
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQLLL--------DGRNAGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402762489 408 AIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
16-461 |
2.69e-135 |
|
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: 399.25 E-value: 2.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGhSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSG-----IDI-PYAA---RHFN--YFASVIEthegsvndiDKDTMSIiRHePIGVVGAVVAWNFPMLL 164
Cdd:cd07086 81 VSLEMGKILPEGLGevqemIDIcDYAVglsRMLYglTIPSERP---------GHRLMEQ-WN-PLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 165 ASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEIL-----PKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVG 239
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 240 YQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKI 319
Cdd:cd07086 229 RRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 320 GDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRItnDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTI 399
Cdd:cd07086 309 GDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 400 IKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNI--AKAVKTGRIWINTYNQVPE-GAPFGGYK 461
Cdd:cd07086 387 IKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEiGGAFGGEK 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
14-485 |
1.02e-134 |
|
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: 397.97 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 14 GLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES-WSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRETSGIDIPYAARHFNYFAsvietheGSVNDIDKDTM-------------SIIRHEPIGVVGAVVAWN 159
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFA-------GWATKINGETLapsipsmqgerytAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 160 FPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGsESGNAIFNHEGVNKLSFTGSTNV 238
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 239 GYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIK 318
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 319 IGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDgldsGYFLEPTLIAVKDNADKLAQEEIFGPVLT 398
Cdd:cd07113 313 VGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE----GYFVQPTLVLARSADSRLMREETFGPVVS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 399 IIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQ 478
Cdd:cd07113 389 FVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYT 468
|
....*..
gi 402762489 479 QVKNIFI 485
Cdd:cd07113 469 ELKSVMI 475
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-468 |
1.27e-129 |
|
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: 383.03 E-value: 1.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 51 DVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIatIETLnngkpIRETSGIdIPYAARHFNyfASVIETHE 130
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEI--ADWL-----IRESGST-RPKAAFEVG--AAIAILRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 131 ---------GSV--NDIDkDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL-LEVAKIF 198
Cdd:cd07104 71 aaglprrpeGEIlpSDVP-GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 199 QEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEG 277
Cdd:cd07104 150 EEAgLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 278 IQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILT 357
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 358 GGKRitnDGLdsgyFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAK 436
Cdd:cd07104 310 GGTY---EGL----FYQPTVLSdVTPDM-PIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430
....*....|....*....|....*....|....
gi 402762489 437 AVKTGRIWIN--TYNQVPEgAPFGGYKNQVLDRE 468
Cdd:cd07104 382 RLETGMVHINdqTVNDEPH-VPFGGVKASGGGRF 414
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-485 |
5.70e-129 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 384.04 E-value: 5.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSGiDIPYAARHFNYFAS--------VIETHegsvndiDKDTMSIIRHEPIGVVGAVVAWNFPMLLASW 167
Cdd:PLN02278 108 MTLEQGKPLKEAIG-EVAYGASFLEYFAEeakrvygdIIPSP-------FPDRRLLVLKQPVGVVGAITPWNFPLAMITR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 168 KIAPAIAAGNTIVIQPSSSTPLSLLEVAKI-FQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAG 246
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 247 AKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEK 326
Cdd:PLN02278 260 AATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 327 TQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDE 406
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 407 EAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-486 |
7.65e-128 |
|
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: 380.69 E-value: 7.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFES--WSLTSKTERANLLRQISNKMMENKE 90
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 91 KIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDK----DTMSIIRHEPIGVVGAVVAWNFPMLLAS 166
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarpnRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKI-FQEILPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEA 245
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 246 GAK-RIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLD 324
Cdd:cd07140 246 CAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 325 EKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNdgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKD 404
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 405 D--EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKN 482
Cdd:cd07140 402 GdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....
gi 402762489 483 IFID 486
Cdd:cd07140 482 VTIE 485
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-461 |
9.56e-124 |
|
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: 371.17 E-value: 9.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 5 IKNYLDENYGLFINGEFVkgHSDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISN 83
Cdd:cd07124 25 VREELGREYPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 84 KMMENKEKIATIETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVvGAVVA-WNFPM 162
Cdd:cd07124 103 LLRRRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGV-GAVISpWNFPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 163 LLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQ 241
Cdd:cd07124 181 AILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 242 VAEA------GAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFS 315
Cdd:cd07124 261 IYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 316 NIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQsNAEILTGGKRItnDGLDSGYFLEPTLIAVKDNADKLAQEEIFGP 395
Cdd:cd07124 341 ALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS-EGRLLLGGEVL--ELAAEGYFVQPTIFADVPPDHRLAQEEIFGP 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402762489 396 VLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDitRAlNIAKA---VKTGRIWIN--TYNQVPEGAPFGGYK 461
Cdd:cd07124 418 VLAVIKAKDFDEALEIANDTEYGLTGGVFSRS--PE-HLERArreFEVGNLYANrkITGALVGRQPFGGFK 485
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
30-485 |
2.16e-123 |
|
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: 368.08 E-value: 2.16e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSG 109
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 idipyaarhfnYFASVIETHE----------GSVNDID-----KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIA 174
Cdd:cd07149 81 -----------EVDRAIETLRlsaeeakrlaGETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 175 AGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE-AGAKRIvp 252
Cdd:cd07149 150 AGNAVVLKPASQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARkAGLKKV-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 253 aTLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQ 332
Cdd:cd07149 228 -TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 333 TSQEQMEKIQSYITYAEQSNAEILTGGKRITNdgldsgyFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07149 307 ISEAEAERIEEWVEEAVEGGARLLTGGKRDGA-------ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 413 NDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN---TYNQvpEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07149 380 NDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdssTFRV--DHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
19-485 |
1.77e-122 |
|
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: 366.24 E-value: 1.77e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 19 GEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIatIETL 98
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEI--VEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 99 nngkpIRETSG------IDIPYAARHFNYFASVIETHEGSV--NDIDKDTMSIIRhEPIGVVGAVVAWNFPMLLASWKIA 170
Cdd:cd07151 79 -----IRESGStrikanIEWGAAMAITREAATFPLRMEGRIlpSDVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 171 PAIAAGNTIVIQPSSSTPLS--LLeVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGA 247
Cdd:cd07151 153 PALALGNAVVLKPASDTPITggLL-LAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 248 KRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKT 327
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 328 QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEE 407
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 408 AIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN--TYNQVPEgAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEPH-VPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
30-468 |
2.50e-117 |
|
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: 352.40 E-value: 2.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIatIETLnngkpIRETSG 109
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDL--IDLL-----IDEGGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 IdIPYAARHFNYFASVIETHEGSVNDI--------DKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVI 181
Cdd:cd07150 74 T-YGKAWFETTFTPELLRAAAGECRRVrgetlpsdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 182 QPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGK 260
Cdd:cd07150 153 KPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 261 SANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEK 340
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 341 IQSYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGL 419
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGKY-------DGNFYQPTVLTdVTPDMR-IFREETFGPVTSVIPAKDAEEALELANDTEYGL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 402762489 420 AGGVFSQDITRALNIAKAVKTGRIWIN--TYNQVPEgAPFGGYKNQVLDRE 468
Cdd:cd07150 385 SAAILTNDLQRAFKLAERLESGMVHINdpTILDEAH-VPFGGVKASGFGRE 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
34-462 |
1.24e-114 |
|
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: 345.75 E-value: 1.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPiRETSGIDIP 113
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFAS----VIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPL 189
Cdd:cd07099 81 LALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 190 SLLEVAKIFQEI-LPKGVVNVVTGKGsESGNAIFNhEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDD 268
Cdd:cd07099 161 VGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALID-AGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 269 ANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYA 348
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 349 EQSNAEILTGGKRITndglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDI 428
Cdd:cd07099 319 VAKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 402762489 429 TRALNIAKAVKTGRIWIN---TYNQVPEgAPFGGYKN 462
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdvlLTAGIPA-LPFGGVKD 430
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
52-462 |
1.86e-113 |
|
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: 341.75 E-value: 1.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 52 VDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIPYAARHFNYFA-------- 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAenaeafla 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 124 -SVIETHEGSvndidkdtmSIIRHEPIGVVGAVVAWNFPMllasWKI----APAIAAGNTIVIQPSSSTPLSLLEVAKIF 198
Cdd:cd07100 80 dEPIETDAGK---------AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 199 QEI-LPKGVVNVVTGKGSESGNAIfNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEG 277
Cdd:cd07100 147 REAgFPEGVFQNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 278 IQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILT 357
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 358 GGKRItnDGldSGYFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAK 436
Cdd:cd07100 306 GGKRP--DG--PGAFYPPTVLTdVTPGMP-AYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420
....*....|....*....|....*.
gi 402762489 437 AVKTGRIWINTYNQVPEGAPFGGYKN 462
Cdd:cd07100 381 RLEAGMVFINGMVKSDPRLPFGGVKR 406
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
16-481 |
1.85e-112 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 341.12 E-value: 1.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSGiDIPYAARHFNYFAS--------VIETHEgsvndidKDTMSIIRHEPIGVVGAVVAWNFPMLLASW 167
Cdd:PRK11241 94 MTLEQGKPLAEAKG-EISYAASFIEWFAEegkriygdTIPGHQ-------ADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 168 KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAG 246
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 247 AKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEK 326
Cdd:PRK11241 246 AKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 327 TQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDgldsGYFLEPT-LIAVKDNAdKLAQEEIFGPVLTIIKVKDD 405
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTiLVDVPANA-KVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 406 EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVK 481
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
16-474 |
2.68e-110 |
|
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: 335.31 E-value: 2.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGhSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSK-TERANLLRQISNKMMENKEKIAT 94
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIREtSGIDIPYAARHFNYFASVIETHEGSVNDID-----KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKI 169
Cdd:cd07082 84 LLMWEIGKTLKD-ALKEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgtKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAk 248
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 rIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQ 328
Cdd:cd07082 242 -MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 329 MGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndgldsGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEA 408
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG------GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 409 IKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYNQV-PEGAPFGGYKNQVLDRETYKEAL 474
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQGIGDAL 461
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
30-485 |
5.86e-110 |
|
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: 333.63 E-value: 5.86e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSG 109
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 iDIPYAARHFNYFASVIETHEGSVNDID-----KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPS 184
Cdd:cd07094 81 -EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 185 SSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE-AGAKRIvpaTLELGGKSA 262
Cdd:cd07094 160 SKTPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRAnAGGKRI---ALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQ 342
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 343 SYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGG 422
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 423 VFSQDITRALNIAKAVKTGRIWIN---TYNQvpEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNdssAFRT--DWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
15-483 |
9.29e-109 |
|
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: 331.40 E-value: 9.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIAT 94
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 95 IETLNNGKPIRETSG------------IDIPYAARHfnyfasviETHEGSVNDIDkdtmSIIRHEPIGVVGAVVAWNFPM 162
Cdd:cd07085 83 LITLEHGKTLADARGdvlrglevvefaCSIPHLLKG--------EYLENVARGID----TYSYRQPLGVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 163 LLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQ 241
Cdd:cd07085 151 MIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 242 VAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIqLGILF-NQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIG 320
Cdd:cd07085 230 IYERAAANGKRVQALGGAKNHAVVMPDADLEQTANAL-VGAAFgAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 321 DPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIA-VKDNAdKLAQEEIFGPVLTI 399
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDnVTPDM-KIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 400 IKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINtynqVPEGAP-----FGGYKNQVL-DRETY-KE 472
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFgDLHFYgKD 463
|
490
....*....|.
gi 402762489 473 ALSNYQQVKNI 483
Cdd:cd07085 464 GVRFYTQTKTV 474
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
38-459 |
4.17e-107 |
|
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: 325.79 E-value: 4.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 38 GETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIEtlnngkpIRETSGIdIPYAar 117
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWI-------VRESGSI-RPKA-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 118 HFNYFASVIETHE---------GSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTP 188
Cdd:cd07152 71 GFEVGAAIGELHEaaglptqpqGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 189 LSL-LEVAKIFQEI-LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIIL 266
Cdd:cd07152 151 VSGgVVIARLFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYIT 346
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 347 YAEQSNAEILTGGkriTNDGLdsgyFLEPTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFS 425
Cdd:cd07152 310 DSVAAGARLEAGG---TYDGL----FYRPTVLSgVKPGM-PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIIS 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 402762489 426 QDITRALNIAKAVKTGRIWIN--TYNQVPEgAPFGG 459
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHINdqTVNDEPH-NPFGG 416
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
51-483 |
2.32e-106 |
|
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: 323.76 E-value: 2.32e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 51 DVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPiRETSGIDIPYAARHFNYFASVIETH- 129
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 130 EGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVN 208
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 209 VVTGKGSESG---NAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFN 285
Cdd:cd07105 160 VVTHSPEDAPevvEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 286 QGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDpldekTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGkriTND 365
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGG---LAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 366 GLDSGYFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIW 444
Cdd:cd07105 312 ESPSGTSMPPTILDnVTPDMD-IYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 402762489 445 INTYNQVPE-GAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07105 391 INGMTVHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-461 |
1.55e-105 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 324.20 E-value: 1.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 5 IKNYLDENYGLFINGEFVKGhsDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISN 83
Cdd:PRK03137 29 VEKELGQDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 84 KMMENKEKIATIETLNNGKPIRETSGiDIPYAARHFNYFA-SVIETHEGS-VNDID--KDTMsiiRHEPIGVvGAVVA-W 158
Cdd:PRK03137 107 IIRRRKHEFSAWLVKEAGKPWAEADA-DTAEAIDFLEYYArQMLKLADGKpVESRPgeHNRY---FYIPLGV-GVVISpW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 159 NFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTN 237
Cdd:PRK03137 182 NFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSRE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 238 VGYQVAEAGA---------KRIVpatLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLIS 308
Cdd:PRK03137 262 VGLRIYERAAkvqpgqiwlKRVI---AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 309 RLKEAFSNIKIGDPlDEKTQMGSQTSQEQMEKIQSYITYAEQSnAEILTGGKRitndGLDSGYFLEPTLIAVKDNADKLA 388
Cdd:PRK03137 339 KVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEE-GRLVLGGEG----DDSKGYFIQPTIFADVDPKARIM 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 389 QEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDitRAlNIAKAVKTGRIWiNTY-NQVPEGA-----PFGGYK 461
Cdd:PRK03137 413 QEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN--RE-HLEKARREFHVG-NLYfNRGCTGAivgyhPFGGFN 487
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
34-486 |
1.75e-101 |
|
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: 312.31 E-value: 1.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIP 113
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFASVIETH------EGSVNDIDKDTMsiIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSST 187
Cdd:cd07098 82 VTCEKIRWTLKHGEKAlrpesrPGGLLMFYKRAR--VEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 188 PLSLLEVAKIFQEIL-----PKGVVNVVTGKGsESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSA 262
Cdd:cd07098 160 AWSSGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQ 342
Cdd:cd07098 239 AIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 343 SYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGG 422
Cdd:cd07098 319 ELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGAS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 423 VFSQDITRALNIAKAVKTGRIWIN-----TYNQvpeGAPFGGYKNQVLDRETYKEALSNYQQVKNIFID 486
Cdd:cd07098 399 VFGKDIKRARRIASQLETGMVAINdfgvnYYVQ---QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTED 464
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
30-485 |
2.86e-101 |
|
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: 311.10 E-value: 2.86e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSG 109
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 iDIPYAARHFNYFASVIETHEGSVNDIDKDTMS-----IIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPS 184
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDISARGegrqgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 185 SSTPLSLLEVAKIFQEI-LPKGVVNVVTGKgSESGNAIFNHEGVNKLSFTGSTNVGYQV-AEAGAKRIVpatLELGGKSA 262
Cdd:cd07147 160 SRTPLSALILGEVLAETgLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLkARAGKKKVV---LELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQ 342
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 343 SYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGG 422
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 423 VFSQDITRALNIAKAVKTGRIWIntyNQVP----EGAPFGGYKNQVLDRETYKEALSNYQQVKNIFI 485
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVI---NDVPtfrvDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
35-483 |
1.99e-100 |
|
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: 309.24 E-value: 1.99e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 35 PATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIR----ETsgI 110
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhafeEV--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 111 DIPYAARHFNYFA-SVIET--HEGSVNDIdkdTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSST 187
Cdd:cd07101 81 DVAIVARYYARRAeRLLKPrrRRGAIPVL---TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 188 PLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHegVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIIL 266
Cdd:cd07101 158 ALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYIT 346
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 347 YAEQSNAEILTGGKRITNDGldsGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQ 426
Cdd:cd07101 316 DAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 427 DITRALNIAKAVKTGRIWIN-----TYNQVpeGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNegyaaAWASI--DAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
78-449 |
1.12e-99 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 305.89 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 78 LRQISNKMMENKEKIATIETLNNGKpIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDKDTMSI-IRHEPIGVVGAVV 156
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENIlLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 157 AWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGS 235
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 236 TNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFS 315
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 316 NIKIGDPLDEKT-QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYFLEPTLIAVKDNADKLAQEEIFG 394
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 395 PVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTYN 449
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREN 370
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-483 |
1.45e-97 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 304.11 E-value: 1.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 22 VKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNG 101
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 102 KPIR----ETSgiDIPYAARHFNYFASVI---ETHEGSVNDIdkdTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIA 174
Cdd:PRK09407 106 KARRhafeEVL--DVALTARYYARRAPKLlapRRRAGALPVL---TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 175 AGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHegVNKLSFTGSTNVGYQVAEAGAKRIVPA 253
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 254 TLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQT 333
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 334 SQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSG-YFLEPTLIA-VKDNADkLAQEEIFGPVLTIIKVKDDEEAIKI 411
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKARP----DLGpLFYEPTVLTgVTPDME-LAREETFGPVVSVYPVADVDEAVER 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402762489 412 ANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN-----TYNQVpeGAPFGGYKNQVLDRETYKEALSNYQQVKNI 483
Cdd:PRK09407 414 ANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSV--DAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
34-462 |
8.06e-95 |
|
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: 294.54 E-value: 8.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIP 113
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFASVIETHEGSVNDIDKDTM-SIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLL 192
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFeRYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 193 EVAKIFQEI-LPKGVVNVVTGKGSESGnAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANL 271
Cdd:cd07102 161 RFAAAFAEAgLPEGVFQVLHLSHETSA-ALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 272 DLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQS 351
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 352 NAEILTGGKRiTNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRA 431
Cdd:cd07102 320 GARALIDGAL-FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430
....*....|....*....|....*....|.
gi 402762489 432 LNIAKAVKTGRIWINTYNQVPEGAPFGGYKN 462
Cdd:cd07102 399 EALGEQLETGTVFMNRCDYLDPALAWTGVKD 429
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
18-431 |
5.01e-94 |
|
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: 293.34 E-value: 5.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 18 NGEFvkGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIET 97
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 98 LNNGKPIRETSG-----IDI-PYA---ARHFN--YFAS------VIETHEgsvndidkdtmsiirhePIGVVGAVVAWNF 160
Cdd:cd07130 82 LEMGKILPEGLGevqemIDIcDFAvglSRQLYglTIPSerpghrMMEQWN-----------------PLGVVGVITAFNF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 161 PMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEIL-----PKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGS 235
Cdd:cd07130 145 PVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 236 TNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFS 315
Cdd:cd07130 224 TAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 316 NIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDgldsGYFLEPTLIAVKDNADkLAQEEIFGP 395
Cdd:cd07130 304 QVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVEGLSDAP-IVKEETFAP 378
|
410 420 430
....*....|....*....|....*....|....*.
gi 402762489 396 VLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRA 431
Cdd:cd07130 379 ILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
30-485 |
2.32e-93 |
|
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: 290.80 E-value: 2.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDtavAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSg 109
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALR---EALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 110 IDIPYAARHFNYFASVIETHEGSVNDID-----KDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPS 184
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 185 SSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE-AGAKRIVpatLELGGKSA 262
Cdd:cd07146 157 EKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAAtAGYKRQL---LELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQ 342
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 343 SYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGG 422
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402762489 423 VFSQDITRALNIAKAVKTGRIWIntyNQVP----EGAPFGGYKNQVLD-RETYKEALSNYQQVKNIFI 485
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNV---NEVPgfrsELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-483 |
2.01e-89 |
|
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: 282.52 E-value: 2.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 5 IKNYLDENYGLFINGEFVKghSDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISN 83
Cdd:TIGR01237 25 VKEQLGKTYPLVINGERVE--TENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 84 KMMENKEKIATIETLNNGKPIREtSGIDIPYAARHFNYFASVIETHEGS--VNDIDKDTMSIIrHEPIGVVGAVVAWNFP 161
Cdd:TIGR01237 103 IVRRRRHEFSALLVKEVGKPWNE-ADAEVAEAIDFMEYYARQMIELAKGkpVNSREGETNQYV-YTPTGVTVVISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 162 MLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVG- 239
Cdd:TIGR01237 181 FAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGt 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 240 --YQVA---EAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAF 314
Cdd:TIGR01237 261 riFERAakvQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEIT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 315 SNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSnAEILTGGKritnDGLDSGYFLEPTLIAVKDNADKLAQEEIFG 394
Cdd:TIGR01237 341 ESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAE-GRLVSGGC----GDDSKGYFIGPTIFADVDRKARLAQEEIFG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 395 PVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRaLNIAKA-VKTGRIWIntyNQVPEGA-----PFGGYKNQVLDRE 468
Cdd:TIGR01237 416 PVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDH-INRAKAeFEVGNLYF---NRNITGAivgyqPFGGFKMSGTDSK 491
|
490
....*....|....*.
gi 402762489 469 T-YKEALSNYQQVKNI 483
Cdd:TIGR01237 492 AgGPDYLALFMQAKTV 507
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
14-459 |
2.58e-79 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 255.65 E-value: 2.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 14 GLFINGEFVKGHSdETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIA 93
Cdd:PRK09457 2 TLWINGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 94 TIETLNNGKPIRET--------SGIDIPYAARHfnyfasvieTHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLA 165
Cdd:PRK09457 81 EVIARETGKPLWEAatevtamiNKIAISIQAYH---------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 166 SWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE 244
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 245 --AGAKRIVPAtLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIY-DKLISRLKEAFSNIKIGD 321
Cdd:PRK09457 231 qfAGQPEKILA-LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 322 PlDEKTQ--MGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitndgLDSGY-FLEPTLIAVKDNADkLAQEEIFGPVLT 398
Cdd:PRK09457 310 W-DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQ-----LQAGTgLLTPGIIDVTGVAE-LPDEEYFGPLLQ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 399 IIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRI-WINTYNQVPEGAPFGG 459
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGG 444
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
51-459 |
1.52e-78 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 251.81 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 51 DVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSG--------IDIPYAARHfnyf 122
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDISIKAYH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 123 asvieTHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI- 201
Cdd:cd07095 77 -----ERTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 202 LPKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE--AGAKRIVPAtLELGGKSANIILDDANLDLAVEGIQ 279
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRqfAGRPGKILA-LEMGGNNPLVVWDVADIDAAAYLIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 280 LGILFNQGEVCSAGSRLLVQEGIY-DKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTG 358
Cdd:cd07095 230 QSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 359 GKRITndglDSGYFLEPTLIAVKDNADkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDIT---RALNIA 435
Cdd:cd07095 310 MERLV----AGTAFLSPGIIDVTDAAD-VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEAlfeRFLARI 384
|
410 420
....*....|....*....|....*
gi 402762489 436 KAvktGRI-WINTYNQVPEGAPFGG 459
Cdd:cd07095 385 RA---GIVnWNRPTTGASSTAPFGG 406
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
4-461 |
3.54e-78 |
|
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: 252.88 E-value: 3.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 4 DIKNYLDENYGLFINGEFVKGhSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISN 83
Cdd:cd07083 10 RVKEEFGRAYPLVIGGEWVDT-KERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 84 KMMENKEKIATIETLNNGKPIRETS-----GID-IPYAARH---FNYFASVIETHEGSVNDIdkdtmsiiRHEPIGVVGA 154
Cdd:cd07083 89 LLRRRRRELIATLTYEVGKNWVEAIddvaeAIDfIRYYARAalrLRYPAVEVVPYPGEDNES--------FYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 155 VVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFT 233
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 234 GSTNVGYQVAEAGAKR------IVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLI 307
Cdd:cd07083 241 GSLETGKKIYEAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 308 SRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSnAEILTGGKRITNDgldsGYFLEPTLIAVKDNADKL 387
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGE----GYFVAPTVVEEVPPKARI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 388 AQEEIFGPVLTIIKVKDDE--EAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpeGA-----PFGGY 460
Cdd:cd07083 396 AQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR-KIT--GAlvgvqPFGGF 472
|
.
gi 402762489 461 K 461
Cdd:cd07083 473 K 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
34-468 |
8.88e-74 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 240.41 E-value: 8.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIP 113
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-EAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFAsviETHEGSVNDIDKDTMSI------IRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSST 187
Cdd:PRK09406 86 KCAKGFRYYA---EHAEALLADEPADAAAVgasrayVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 188 PLSLLEVAKIFQEI-LPKGVVNVVTgKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIIL 266
Cdd:PRK09406 163 PQTALYLADLFRRAgFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYIT 346
Cdd:PRK09406 242 PSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 347 YAEQSNAEILTGGKRItnDGldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQ 426
Cdd:PRK09406 322 DAVAAGATILCGGKRP--DG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 402762489 427 DITRALNIAKAVKTGRIWIN----TYnqvPEgAPFGGYKNQVLDRE 468
Cdd:PRK09406 398 DEAEQERFIDDLEAGQVFINgmtvSY---PE-LPFGGVKRSGYGRE 439
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
50-459 |
1.42e-71 |
|
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: 233.65 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 50 KDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIET- 128
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 129 ---HEGSVNDIDKDTMSI-IRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPK 204
Cdd:cd07135 85 akdEKVKDGPLAFMFGKPrIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 205 GVVNVVTGkGSESGNAIFNHeGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILF 284
Cdd:cd07135 165 DAFQVVQG-GVPETTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 285 NQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPlDEKTQMGSQTSQEQMEKIQSYItyaEQSNAEILTGGKRItn 364
Cdd:cd07135 243 NAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLL---DTTKGKVVIGGEMD-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 365 dglDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIW 444
Cdd:cd07135 317 ---EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVV 393
|
410
....*....|....*..
gi 402762489 445 IN-TYNQVP-EGAPFGG 459
Cdd:cd07135 394 INdTLIHVGvDNAPFGG 410
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
34-486 |
1.71e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 234.37 E-value: 1.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 34 NPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGiDIP 113
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 114 YAARHFNYFA----SVIETHEGSVndidKDTMSIIRHEPIGVVGAVVAWNFPMllasWKI----APAIAAGNTIVIQPSS 185
Cdd:PRK13968 92 KSANLCDWYAehgpAMLKAEPTLV----ENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 186 STPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIfNHEGVNKLSFTGSTNVGYQV-AEAGA--KRIVpatLELGGKS 261
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIgAQAGAalKKCV---LELGGSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 262 ANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKI 341
Cdd:PRK13968 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 342 QSYITYAEQSNAEILTGGKRITNdgldSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAG 421
Cdd:PRK13968 320 HHQVEATLAEGARLLLGGEKIAG----AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 402762489 422 GVFSQDITRALNIAKAVKTGRIWINTYNQVPEGAPFGGYKNQVLDRETYKEALSNYQQVKNIFID 486
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKD 460
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-461 |
3.01e-71 |
|
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: 235.17 E-value: 3.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFvkGHSDETLEVKNPATGE-TLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEK--- 91
Cdd:cd07125 36 IINGEE--TETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGElia 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 92 IATIE---TLNNGKP-IREtsGIDI----PYAARHFNYFASVIETHeGSVNDIDKdtmsiirhEPIGVVGAVVAWNFPML 163
Cdd:cd07125 114 LAAAEagkTLADADAeVRE--AIDFcryyAAQARELFSDPELPGPT-GELNGLEL--------HGRGVFVCISPWNFPLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 164 LASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQV 242
Cdd:cd07125 183 IFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 243 AEAGAKR---IVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKI 319
Cdd:cd07125 263 NRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 320 GDPLDEKTQMGSQTSQEQMEKIQSYITyAEQSNAEILTGGKritnDGLDSGYFLEPTLIAVkDNADKLaQEEIFGPVLTI 399
Cdd:cd07125 343 GDPWDLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIAPAP----LDDGNGYFVAPGIIEI-VGIFDL-TTEVFGPILHV 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 400 I--KVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpeGA-----PFGGYK 461
Cdd:cd07125 416 IrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NIT--GAivgrqPFGGWG 481
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
13-462 |
3.95e-70 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 231.95 E-value: 3.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 13 YGLFINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPIRET------SGIDIPYAARH-FNYFASVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLA 165
Cdd:PLN00412 96 AECLVKEIAKPAKDAvtevvrSGDLISYTAEEgVRILGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 166 SWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGStNVGYQVAE 244
Cdd:PLN00412 176 VSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 245 AGakRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLD 324
Cdd:PLN00412 255 KA--GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 325 EkTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRitndgldSGYFLEPTLIavkDNAD---KLAQEEIFGPVLTIIK 401
Cdd:PLN00412 333 D-CDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLL---DNVRpdmRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 402 VKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTY-NQVPEGAPFGGYKN 462
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKD 463
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
53-459 |
1.68e-63 |
|
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: 212.39 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 53 DTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIatIETLNN--GKP-----IRETSGI--DIPYAARHFNyfa 123
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEI--AAALYAdlGKPpaeayLTEIAVVlgEIDHALKHLK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 124 SVIETHEGSVNDIDKDTMSIIRHEPIGVVGAVVAWNFPMLLAswkIAP---AIAAGNTIVIQPSSSTPLSLLEVAKIFQE 200
Cdd:cd07087 76 KWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 201 ILPKGVVNVVTGKGSESgNAI----FNHegvnkLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVE 276
Cdd:cd07087 153 YFDPEAVAVVEGGVEVA-TALlaepFDH-----IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 277 GIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNiKIGDPLDEKTQMGSQTSQEQMEKIQSYITyaeqsNAEIL 356
Cdd:cd07087 227 RIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRLASLLD-----DGKVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 357 TGGKRITNDgldsgYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAK 436
Cdd:cd07087 301 IGGQVDKEE-----RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLA 375
|
410 420
....*....|....*....|....*...
gi 402762489 437 AVKTGRIwinTYNQV-----PEGAPFGG 459
Cdd:cd07087 376 ETSSGGV---CVNDVllhaaIPNLPFGG 400
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-459 |
3.36e-61 |
|
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: 208.98 E-value: 3.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKghSDETLEVKNPAT-GETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERAN-LLRQ---ISNKMmenK 89
Cdd:cd07123 35 LVIGGKEVR--TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiFLKAadlLSGKY---R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 90 EKIATIETLNNGKPIRETsgiDIPYAAR-----HFN-YFASVIE------THEGSVNDIDkdtmsiirHEPI-GVVGAVV 156
Cdd:cd07123 110 YELNAATMLGQGKNVWQA---EIDAACElidflRFNvKYAEELYaqqplsSPAGVWNRLE--------YRPLeGFVYAVS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 157 AWNFPMLLASWKIAPAIAaGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGS 235
Cdd:cd07123 179 PFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 236 TNV----GYQVAEAGAK-----RIVPatlELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKL 306
Cdd:cd07123 258 TPTfkslWKQIGENLDRyrtypRIVG---ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 307 ISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYA-EQSNAEILTGGKritndGLDS-GYFLEPTLIAVKDNA 384
Cdd:cd07123 335 KERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGK-----CDDSvGYFVEPTVIETTDPK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 385 DKLAQEEIFGPVLTIIKVKDD--EEAIKIAND-SEYGLAGGVFSQDiTRALNIAKAV---KTGRIWINTYnqvPEGA--- 455
Cdd:cd07123 410 HKLMTEEIFGPVLTVYVYPDSdfEETLELVDTtSPYALTGAIFAQD-RKAIREATDAlrnAAGNFYINDK---PTGAvvg 485
|
....*.
gi 402762489 456 --PFGG 459
Cdd:cd07123 486 qqPFGG 491
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
144-459 |
9.54e-60 |
|
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: 202.72 E-value: 9.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 144 IRHEPIGVVGAVVAWNFPMLLAswkIAP---AIAAGNTIVIQPSSSTP-LSLLeVAKIFQEILPKGVVNVVTGkGSESGN 219
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEYFDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 220 AI----FNHegvnkLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSR 295
Cdd:cd07133 172 AFsslpFDH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 296 LLVQEGIYDKLISRLKEAFSNIkIGDPLDEKtQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKriTNDGLDSGYFLEP 375
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIELNP--AGEDFAATRKLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 376 TLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN--TYNQVPE 453
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtLLHVAQD 402
|
....*.
gi 402762489 454 GAPFGG 459
Cdd:cd07133 403 DLPFGG 408
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-491 |
9.74e-58 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 199.29 E-value: 9.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 11 ENYGLFINGEFvkGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKE 90
Cdd:PLN02315 19 RNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 91 KIATIETLNNGKPIRETSG-----IDI-PYA---ARHFNyfASVIETHEgsvndidKDTMSIIRHEPIGVVGAVVAWNFP 161
Cdd:PLN02315 97 YLGRLVSLEMGKILAEGIGevqeiIDMcDFAvglSRQLN--GSIIPSER-------PNHMMMEVWNPLGIVGVITAFNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 162 MLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEIL-----PKGVVNVVTGkGSESGNAIFNHEGVNKLSFTGST 236
Cdd:PLN02315 168 CAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 237 NVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSN 316
Cdd:PLN02315 247 KVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 317 IKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDgldsGYFLEPTLIAVKDNADkLAQEEIFGPV 396
Cdd:PLN02315 327 VKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESE----GNFVQPTIVEISPDAD-VVKEELFGPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 397 LTIIKVKDDEEAIKIANDSEYGLAGGVFSQditRALNIAKAV-----KTGRIWINTYNQVPE-GAPFGGYKNQVLDRETY 470
Cdd:PLN02315 402 LYVMKFKTLEEAIEINNSVPQGLSSSIFTR---NPETIFKWIgplgsDCGIVNVNIPTNGAEiGGAFGGEKATGGGREAG 478
|
490 500
....*....|....*....|.
gi 402762489 471 KEALSNYQQVKNIFIDTSNEL 491
Cdd:PLN02315 479 SDSWKQYMRRSTCTINYGNEL 499
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
15-459 |
1.06e-57 |
|
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: 199.63 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 15 LFINGEFVKGhSDETLEVKNPAT-GETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNkMMENK--EK 91
Cdd:TIGR01236 34 LVIGGEEVYD-SNERIPQVNPHNhQAVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAAD-LLSGPyrYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 92 IATIETLNNGKPIRETSgIDIPYAA----RHFNYFASVIETHE-----GSVNDIDkdtmsiirHEPI-GVVGAVVAWNFP 161
Cdd:TIGR01236 112 ILAATMLGQSKTVYQAE-IDAVAELidffRFNVKYARELYAQQpisapGEWNRTE--------YRPLeGFVYAISPFNFT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 162 MLLASWKIAPAIAaGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGY 240
Cdd:TIGR01236 183 AIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAgLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 241 QVAEAGAKRIV-----PATL-ELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAF 314
Cdd:TIGR01236 262 HLWKKVAQNLDryhnfPRIVgETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAEL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 315 SNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQ--SNAEILTGGKRitnDglDS-GYFLEPTLIAVKDNADKLAQEE 391
Cdd:TIGR01236 342 QSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKdpEALTILYGGKY---D--DSqGYFVEPTVVESKDPDHPLMSEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 392 IFGPVLTIIkVKDDEEAIKIA----NDSEYGLAGGVFSQDITRALNIAKAVK--TGRIWIntyNQVPEGA-----PFGG 459
Cdd:TIGR01236 417 IFGPVLTVY-VYPDDKYKEILdlvdSTSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYI---NDKCTGAvvgqqPFGG 491
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
142-427 |
2.18e-54 |
|
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: 188.87 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 142 SIIRHEPIGVVGAVVAWNFPMLLAswkIAP---AIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGkGSESG 218
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEG-GVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 219 NAIFnHEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV 298
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 299 QEGIYDKLISRLKEAFSNIKIGDPLDEKTqMGSQTSQEQMEKIQSYItyaeqSNAEILTGGKriTNDGldsGYFLEPTLI 378
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLL-----DNGKIVFGGN--TDRE---TLYIEPTIL 317
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 402762489 379 AVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQD 427
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-459 |
1.14e-53 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 195.08 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 26 SDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEK---IATIE---TL 98
Cdd:PRK11905 565 DGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPElfaLAVREagkTL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 99 NNG-KPIREtsGIDIP--YAARhfnyfasVIETHEGSvndidkdtmsiiRHEPIGVVGAVVAWNFPMLLASWKIAPAIAA 175
Cdd:PRK11905 645 ANAiAEVRE--AVDFLryYAAQ-------ARRLLNGP------------GHKPLGPVVCISPWNFPLAIFTGQIAAALVA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 176 GNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKR---IV 251
Cdd:PRK11905 704 GNTVLAKPAEQTPLIAARAVRLLHEAgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRsgpPV 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 252 PATLELGGKSAnIILDDANL------DLAVEGIQlgilfNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDE 325
Cdd:PRK11905 784 PLIAETGGQNA-MIVDSSALpeqvvaDVIASAFD-----SAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 326 KTQMGSQTSQEQMEKIQSYITYAEQSnaeiltgGKRI----TNDGLDSGYFLEPTLIAVKDNADklAQEEIFGPVLTIIK 401
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAA-------GRLVhqlpLPAETEKGTFVAPTLIEIDSISD--LEREVFGPVLHVVR 928
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402762489 402 VKDDE-----EAIkiaNDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpeGA-----PFGG 459
Cdd:PRK11905 929 FKADEldrviDDI---NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NII--GAvvgvqPFGG 990
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
30-461 |
3.73e-53 |
|
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: 185.70 E-value: 3.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 30 LEVKNPATGETLSHITKANEKDVDTAVAAAQEAF---ESWslTSKTERANLLRQISNKMMENKEKIATIETLNNGKPI-- 104
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 105 ------RETSGIDIpyAARHFNYFASV---IETHEGSVNDIDKDTmsiirHEPIGVVGAVVAWNFPMLLASWKIAPAIAA 175
Cdd:cd07148 79 akvevtRAIDGVEL--AADELGQLGGReipMGLTPASAGRIAFTT-----REPIGVVVAISAFNHPLNLIVHQVAPAIAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 176 GNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKgSESGNAIFNHEGVNKLSFTGSTNVGYQVAEagakRIVPAT 254
Cdd:cd07148 152 GCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLRS----KLAPGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 255 ---LELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGS 331
Cdd:cd07148 227 rcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 332 QTSQEQMEKIQSYITYAEQSNAEILTGGKRITndglDSGYflEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKI 411
Cdd:cd07148 307 LIRPREVDRVEEWVNEAVAAGARLLCGGKRLS----DTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQ 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 402762489 412 ANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN--TYNQVpEGAPFGGYK 461
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdhTAFRV-DWMPFAGRR 431
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
17-459 |
1.50e-52 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 191.69 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 17 INGEfvkGHSDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEK---I 92
Cdd:COG4230 562 IAGE---AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAElmaL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIE---TLNNG-KPIRETsgIDipyaarhF-NYFASVIETHEGSVndidkdtmsiIRHEPIGVVGAVVAWNFPmlLASW 167
Cdd:COG4230 639 LVREagkTLPDAiAEVREA--VD-------FcRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFP--LAIF 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 168 --KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAE 244
Cdd:COG4230 698 tgQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAgVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 245 AGAKR---IVPATLELGGKSANI-------------ILDDAnldlavegiqlgilFNqgevcSAGSR------LLVQEGI 302
Cdd:COG4230 778 TLAARdgpIVPLIAETGGQNAMIvdssalpeqvvddVLASA--------------FD-----SAGQRcsalrvLCVQEDI 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 303 YDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITYAEQSnaeiltgGKRIT----NDGLDSGYFLEPTLI 378
Cdd:COG4230 839 ADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-------GRLVHqlplPEECANGTFVAPTLI 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 379 AVkDNADKLaQEEIFGPVLTIIKVKDDE-----EAIkiaNDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpe 453
Cdd:COG4230 912 EI-DSISDL-EREVFGPVLHVVRYKADEldkviDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR-NII-- 983
|
490
....*....|.
gi 402762489 454 GA-----PFGG 459
Cdd:COG4230 984 GAvvgvqPFGG 994
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
46-459 |
1.50e-52 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 184.85 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 46 KANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPiretsgidiPYAARHFNYFASV 125
Cdd:PTZ00381 3 PDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRH---------PFETKMTEVLLTV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 126 IETHEgSVNDIDK-------DTM-------SIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:PTZ00381 74 AEIEH-LLKHLDEylkpekvDTVgvfgpgkSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 192 LEVAKIFQEILPKGVVNVVTGkGSESGNAI----FNHegvnkLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILD 267
Cdd:PTZ00381 153 KLMAKLLTKYLDPSYVRVIEG-GVEVTTELlkepFDH-----IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 268 DANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIkIGDPLDEKTQMGSQTSQEQMEKIQSYIty 347
Cdd:PTZ00381 227 SCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELI-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 348 aEQSNAEILTGGKRITNDgldsgYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQD 427
Cdd:PTZ00381 304 -KDHGGKVVYGGEVDIEN-----KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED 377
|
410 420 430
....*....|....*....|....*....|....
gi 402762489 428 ITRALNIAKAVKTGRIWIN--TYNQVPEGAPFGG 459
Cdd:PTZ00381 378 KRHKELVLENTSSGAVVINdcVFHLLNPNLPFGG 411
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
17-459 |
6.78e-52 |
|
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: 183.57 E-value: 6.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 17 INGEFVKGHSDETleVKNPAT-GETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:TIGR01238 42 IGHSYKADGEAQP--VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETsgIDIPYAARHF-NYFASVIEthegsvNDIDKDTmsiirHEPIGVVGAVVAWNFPMLLASWKIAPAIA 174
Cdd:TIGR01238 120 CVREAGKTIHNA--IAEVREAVDFcRYYAKQVR------DVLGEFS-----VESRGVFVCISPWNFPLAIFTGQISAALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 175 AGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRI--- 250
Cdd:TIGR01238 187 AGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdap 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMG 330
Cdd:TIGR01238 267 VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 331 SQTSQEQMEKIQSYITYAEQSNAEIltgGKRITNDGLDS--GYFLEPTLIAVkDNADKLaQEEIFGPVLTIIKVKDDE-- 406
Cdd:TIGR01238 347 PVIDAEAKQNLLAHIEHMSQTQKKI---AQLTLDDSRACqhGTFVAPTLFEL-DDIAEL-SEEVFGPVLHVVRYKAREld 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 402762489 407 EAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpeGA-----PFGG 459
Cdd:TIGR01238 422 QIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQV--GAvvgvqPFGG 476
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
16-457 |
5.37e-51 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 183.02 E-value: 5.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGHSDETLEVKNPATGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI 95
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 96 ETLNNGKPIRETSGiDIPYAARHFNYFASVIETHEGS-VNDIDK--DTMSIirHEPIGVVGAVVAWNFPMLLASWKIAPA 172
Cdd:PLN02419 197 ITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEyLPNVSNgvDTYSI--REPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKgSESGNAIFNHEGVNKLSFTGSTNVG---YQVAEAGAK 248
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGT-NDTVNAICDDEDIRAVSFVGSNTAGmhiYARAAAKGK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 249 RIVPatlELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV---QEGIYDKLISRLKEafsnIKIGDPLDE 325
Cdd:PLN02419 353 RIQS---NMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAKA----LKVTCGSEP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 326 KTQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDD 405
Cdd:PLN02419 426 DADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSF 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 402762489 406 EEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTynQVPEGAPF 457
Cdd:PLN02419 506 DEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPF 555
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
140-427 |
4.99e-49 |
|
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: 173.95 E-value: 4.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 140 TMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGkGSESGN 219
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG-DAEVAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 220 AI----FNHegvnkLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSR 295
Cdd:cd07134 171 ALlelpFDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 296 LLVQEGIYDKLISRLKEAFSNIKIGDPLDEKT-QMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRItndglDSGYFLE 374
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIA 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 402762489 375 PTLIA-VKDNAdKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQD 427
Cdd:cd07134 321 PTVLTnVTPDM-KIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
14-459 |
6.32e-49 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 180.78 E-value: 6.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 14 GLFINGefvkghSDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI 92
Cdd:PRK11904 554 GPIING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 93 ATIETLNNGKPI-------REtsGIDipyaarhF-NYFASVIETHEGSVNDIDKDT--MSIIRHEPIGVVGAVVAWNFPm 162
Cdd:PRK11904 628 IALCVREAGKTLqdaiaevRE--AVD-------FcRYYAAQARRLFGAPEKLPGPTgeSNELRLHGRGVFVCISPWNFP- 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 163 lLASW--KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVG 239
Cdd:PRK11904 698 -LAIFlgQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAgIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETA 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 240 YQVAEAGAKR---IVPATLELGGKSANI---------ILDDAnldlavegiqLGILFNQ-GEVCSAGSRLLVQEGIYDKL 306
Cdd:PRK11904 777 RIINRTLAARdgpIVPLIAETGGQNAMIvdstalpeqVVDDV----------VTSAFRSaGQRCSALRVLFVQEDIADRV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 307 ISRLKEAFSNIKIGDPLDEKTQMG---SQTSQEQMEKiqsyitYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVkDN 383
Cdd:PRK11904 847 IEMLKGAMAELKVGDPRLLSTDVGpviDAEAKANLDA------HIERMKREARLLAQLPLPAGTENGHFVAPTAFEI-DS 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 384 ADKLaQEEIFGPVLTIIKVKDDE-----EAIkiaNDSEYGLAGGVFSQDITRALNIAKAVKTGRIWINTyNQVpeGA--- 455
Cdd:PRK11904 920 ISQL-EREVFGPILHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQI--GAvvg 992
|
....*.
gi 402762489 456 --PFGG 459
Cdd:PRK11904 993 vqPFGG 998
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
55-433 |
1.54e-47 |
|
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: 170.48 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 55 AVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI--ATIETLNngKPIRETSGIDIPYAARHFNYfaSVIETHEGS 132
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIveALAKDLR--KPKFEAVLSEILLVKNEIKY--AISNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 133 VND-IDKDTMSI-----IRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPlsllEVAKIFQEILPKGV 206
Cdd:cd07132 79 KPEpVKKNLATLlddvyIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----ATAKLLAELIPKYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 207 VN----VVTGkGSESGNAIFNHEgVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGI 282
Cdd:cd07132 155 DKecypVVLG-GVEETTELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 283 LFNQGEVCSAGSRLLVQEGIYDKLISRLKEAfsnIK--IGDPLDEKTQMGSQTSQEQMEKIQSYItyaeqSNAEILTGGk 360
Cdd:cd07132 233 FINAGQTCIAPDYVLCTPEVQEKFVEALKKT---LKefYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG- 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 361 ritnDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFS---QDITRALN 433
Cdd:cd07132 304 ----QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSnnkKVINKILS 375
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
25-459 |
3.29e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 164.38 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 25 HSDETLEVKNPA-TGETLSHITKANEKDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI------ET 97
Cdd:PRK11809 656 AAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLlvreagKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 98 LNNG-KPIREtsgidipyAARHFNYFASVIEthegsvNDIDKDTmsiirHEPIGVVGAVVAWNFPMLLASWKIAPAIAAG 176
Cdd:PRK11809 736 FSNAiAEVRE--------AVDFLRYYAGQVR------DDFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 177 NTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRI----- 250
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAgVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgr 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 251 -VPATLELGGKSAnIILDDANLDLAVEGIQLGILFNQ-GEVCSAGSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQ 328
Cdd:PRK11809 877 pIPLIAETGGQNA-MIVDSSALTEQVVADVLASAFDSaGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTD 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 329 MGSQTSQEQMEKIQSYITyAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVkDNADKLaQEEIFGPVLTIIKVKDDE-- 406
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQ-AMRAKGRPVFQAARENSEDWQSGTFVPPTLIEL-DSFDEL-KREVFGPVLHVVRYNRNQld 1032
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402762489 407 ---EAIkiaNDSEYGLAGGVFSQ-DITRALNIAKAvKTGRIWINTyNQVpeGA-----PFGG 459
Cdd:PRK11809 1033 eliEQI---NASGYGLTLGVHTRiDETIAQVTGSA-HVGNLYVNR-NMV--GAvvgvqPFGG 1087
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
16-473 |
4.76e-43 |
|
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: 159.74 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 16 FINGEFVKGhSDETLEVKNPATGETLSHITkANEKDVDTAVAAAQE----AFESWSLTsktERANLLRQISNKMMENKEK 91
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREkggpALRALTFH---ERAAMLKALAKYLMERKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 92 IATIETLNNGKpiRETSGIDIP--------YA--ARHFNYFASVIetHEGSVNDIDKDTMSIIRH--EPI-GVVGAVVAW 158
Cdd:cd07128 79 LYALSAATGAT--RRDSWIDIDggigtlfaYAslGRRELPNAHFL--VEGDVEPLSKDGTFVGQHilTPRrGVAVHINAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 159 NFPmllaSW----KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQE--ILPKGVVNVVTGkgseSGNAIFNH-EGVNKLS 231
Cdd:cd07128 155 NFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG----SVGDLLDHlGEQDVVA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 232 FTGSTNVGYQ--VAEAGAKRIVPATLELGGKSANIILDDAN-----LDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYD 304
Cdd:cd07128 227 FTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDATpgtpeFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 305 KLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITyAEQSNAEILTGGK-RITNDGLDS--GYFLEPTLIAVK 381
Cdd:cd07128 307 AVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVA-TLLAEAEVVFGGPdRFEVVGADAekGAFFPPTLLLCD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 382 D--NADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDitralniakavktgRIWINTYnqVPEGAPFGG 459
Cdd:cd07128 386 DpdAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND--------------PAFAREL--VLGAAPYHG 449
|
490
....*....|....
gi 402762489 460 yKNQVLDRETYKEA 473
Cdd:cd07128 450 -RLLVLNRDSAKES 462
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
147-459 |
8.23e-41 |
|
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: 151.79 E-value: 8.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 147 EPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGkGSESGNAIFNHEG 226
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 227 vNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGIL-FNQGEVCSAGSRLLVQEGIYDK 305
Cdd:cd07137 179 -DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 306 LISRLKEAFSNIKIGDPLDEKtQMGSQTSQEQMEKIQSYITYAEQSnAEILTGGkRITNDGLdsgyFLEPTLIAVKDNAD 385
Cdd:cd07137 258 LIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGG-ERDEKNL----YIEPTILLDPPLDS 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402762489 386 KLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN-TYNQVP-EGAPFGG 459
Cdd:cd07137 331 SIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAiDTLPFGG 406
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-427 |
8.23e-35 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 136.76 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 1 MTVDIKNYLdenyglfiNGEFVKGHSDETLeVKNPATGETLSHiTKANEKDVDTAVAAAQE----AFESWSLTsktERAN 76
Cdd:PRK11903 1 MTELLANYV--------AGRWQAGSGAGTP-LFDPVTGEELVR-VSATGLDLAAAFAFAREqggaALRALTYA---QRAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 77 LLRQISNKMMENKEKIATIETLNNGKpIRETSGIDIPYAARHFNYFA----SVIETH---EGSVNDIDKDTMSIIRH--E 147
Cdd:PRK11903 68 LLAAIVKVLQANRDAYYDIATANSGT-TRNDSAVDIDGGIFTLGYYAklgaALGDARllrDGEAVQLGKDPAFQGQHvlV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 148 PI-GVVGAVVAWNFPmllaSW----KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQE--ILPKGVVNVVTGkgseSGNA 220
Cdd:PRK11903 147 PTrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCG----SSAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 221 IFNH-EGVNKLSFTGSTNVGYQVAEAGA--KRIVPATLELGGKSANIILDDAN-----LDLAVEGIQLGILFNQGEVCSA 292
Cdd:PRK11903 219 LLDHlQPFDVVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 293 GSRLLVQEGIYDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQMEKIQSYITyAEQSNAEILTGGKRITNDGLDS--G 370
Cdd:PRK11903 299 IRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 371 YFLEPTLIAVKD--NADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQD 427
Cdd:PRK11903 378 ACVGPTLLGASDpdAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
52-408 |
1.41e-30 |
|
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: 123.50 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 52 VDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIPYAarHFNYFASVIET--- 128
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQV--QLRARAFVIYSyri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 129 HEGSVNDIDKDTMSIIRHE--PIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQE--ILPK 204
Cdd:cd07084 79 PHEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 205 GVVNVVTGKGsESGNAIFNHEGVNKLSFTGSTNVGYQVAeAGAKRIvPATLELGGKSANIILDDAN-LDLAVEGIQLGIL 283
Cdd:cd07084 159 EDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLA-LDAKQA-RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 284 FNQGEVCSAGSRLLVQEGIY-DKLISRLKEAFSNIKIGDPLdektqmgsqTSQEQMEKIQSYITYAEQSNAEILT-GGKR 361
Cdd:cd07084 236 ACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLEDLL---------LGPVQTFTTLAMIAHMENLLGSVLLfSGKE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 402762489 362 ITNDGLDSGY-FLEPTLIAVKDNAD----KLAQEEIFGPVLTIIKVKDDEEA 408
Cdd:cd07084 307 LKNHSIPSIYgACVASALFVPIDEIlktyELVTEEIFGPFAIVVEYKKDQLA 358
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
144-459 |
6.20e-29 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 119.38 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 144 IRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGKGSESGNAIfn 223
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALL-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 224 HEGVNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGIL-FNQGEVCSAGSRLLVQEGI 302
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 303 YDKLISRLKEAFSNIKIGDPLDEKtQMGSQTSQEQMEKIQSYITYAEQSNAEILTGGKRITNDGLDSGYFLEPTLIAVkd 382
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSL-- 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 383 nadkLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIWIN--TYNQVPEGAPFGG 459
Cdd:PLN02174 343 ----IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPFGG 417
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
147-459 |
2.24e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 117.52 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 147 EPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEILPKGVVNVVTGkGSESGNAIFNHEG 226
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 227 vNKLSFTGSTNVGYQVAEAGAKRIVPATLELGGKSANII--LDDA-NLDLAVEGIqLGILFN--QGEVCSAGSRLLVQEG 301
Cdd:PLN02203 186 -DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRI-VGGKWGscAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 302 IYDKLISRLKeafSNIK--IGDPLDEKTQMGSQTSQEQMEKIQSYITyAEQSNAEILTGGKrITNDGLdsgyFLEPTLIA 379
Cdd:PLN02203 264 FAPILIELLK---STIKkfFGENPRESKSMARILNKKHFQRLSNLLK-DPRVAASIVHGGS-IDEKKL----FIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 380 VKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIANDSEYGLAGGVFSQDITRALNIAKAVKTGRIwinTYNQ-----VPEG 454
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDaiiqyACDS 411
|
....*
gi 402762489 455 APFGG 459
Cdd:PLN02203 412 LPFGG 416
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
52-454 |
1.16e-27 |
|
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: 114.95 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 52 VDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKI---ATIETlnnGKPIRETSGiDIPYAARHFNYFASVIEt 128
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLPEARLQG-ELGRTTGQLRLFADLVR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 129 hEGSVNDIDKDTMSIIRHE-----------PIGVVGAVVAWNFPML--LASWKIAPAIAAGNTIVIQPSSSTP-LSLLeV 194
Cdd:cd07129 76 -EGSWLDARIDPADPDRQPlprpdlrrmlvPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPgTSEL-V 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 195 AKIFQEI-----LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRI--VPATLELGgkSAN--II 265
Cdd:cd07129 154 ARAIRAAlratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELG--SVNpvFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 266 LDDAnldLAVEGIQLG------ILFNQGEVCSAGSRLLVQEGI-YDKLISRLKEAFSNIKIGDPLDEKTQMGSQTSQEQM 338
Cdd:cd07129 232 LPGA---LAERGEAIAqgfvgsLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 339 ekiqsyityAEQSNAEILTGGkritnDGLDSGYFLEPTLIAVKDN---ADKLAQEEIFGPVLTIIKVKDDEEAIKIAN-- 413
Cdd:cd07129 309 ---------AAAPGVRVLAGG-----AAAEGGNQAAPTLFKVDAAaflADPALQEEVFGPASLVVRYDDAAELLAVAEal 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 402762489 414 -----------DSEYGLAggvfsQDITRALniakAVKTGRIwinTYNQVPEG 454
Cdd:cd07129 375 egqltatihgeEDDLALA-----RELLPVL----ERKAGRL---LFNGWPTG 414
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
50-440 |
1.86e-21 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 96.54 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 50 KDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIEtlnngkpIRETsGIDipyaarhfNYFASVIETH 129
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMA-------VEET-GMG--------RVEDKIAKNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 130 -----EGSVNDIDKDT------MSIIRHEPIGVVGAV---------VAWNFPMLLAswkiapaiaAGNTIVIQP-SSSTP 188
Cdd:cd07121 68 laaekTPGTEDLTTTAwsgdngLTLVEYAPFGVIGAItpstnptetIINNSISMLA---------AGNAVVFNPhPGAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 189 LSLLEVAKIFQEIL----PKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIvpatlelGGKSAN- 263
Cdd:cd07121 139 VSAYAVELINKAIAeaggPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAI-------GAGAGNp 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 264 -IILDD-ANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEafsnikigdpldektQMGSQTSQEQMEKI 341
Cdd:cd07121 212 pVVVDEtADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR---------------NGAYVLNDEQAEQL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 342 QSYItyaeqsnaeILTGGKRITND---GLDSGYFLE----------PTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEA 408
Cdd:cd07121 277 LEVV---------LLTNKGATPNKkwvGKDASKILKaagievpadiRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEA 347
|
410 420 430
....*....|....*....|....*....|....
gi 402762489 409 IKIANDSEYGL--AGGVFSQDITRALNIAKAVKT 440
Cdd:cd07121 348 IELAVELEHGNrhTAIIHSKNVENLTKMARAMQT 381
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
50-440 |
4.94e-21 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 95.74 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 50 KDVDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATI---ET---------LNNGKPIRETSGIDIpyaar 117
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELaveETgmgrvedkiAKNVAAAEKTPGVED----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 118 hfnyfasvIEThEGSVNDidkDTMSIIRHEPIGVVGAVVAWNFPmllASWKIAPAI---AAGNTIVIQP-SSSTPLSLLE 193
Cdd:PRK15398 111 --------LTT-EALTGD---NGLTLIEYAPFGVIGAVTPSTNP---TETIINNAIsmlAAGNSVVFSPhPGAKKVSLRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 194 VAKIFQEIL----PKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGYQVAEAGAKRIvpatlelGGKSAN--IILD 267
Cdd:PRK15398 176 IELLNEAIVaaggPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAI-------GAGAGNppVVVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 268 D-ANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKE--AFsnikigdpldektqmgsQTSQEQMEKIQSY 344
Cdd:PRK15398 249 EtADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKngAV-----------------LLTAEQAEKLQKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 345 ItyaeqsnaeiLTGGKRITND--GLDSGYFLE----------PTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:PRK15398 312 V----------LKNGGTVNKKwvGKDAAKILEaaginvpkdtRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
410 420 430
....*....|....*....|....*....|
gi 402762489 413 NDSEYGL--AGGVFSQDITRALNIAKAVKT 440
Cdd:PRK15398 382 VKLEHGNrhTAIMHSRNVDNLNKMARAIQT 411
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
120-459 |
1.61e-16 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 81.77 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 120 NYFASviethEGSVNDI-DKDTMSIIRH----------EPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTP 188
Cdd:cd07122 61 NHFAS-----EYVYNDIkDMKTVGVIEEdeekgiveiaEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 189 LSLLEVAKIFQEI-----LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVgyqVAEA---GAkrivPAtleLGGK 260
Cdd:cd07122 136 KCSIEAAKIMREAavaagAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGM---VKAAyssGK----PA---IGVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 261 SAN---IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEafsnikigdpldektQMGSQTSQEQ 337
Cdd:cd07122 206 PGNvpaYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKR---------------RGAYFLNEEE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 338 MEKIQSYityaeqsnaeILTGGKRITND--GLDSGYFLEPTLIAVKDNADKLAQE------------EIFGPVLTIIKVK 403
Cdd:cd07122 271 KEKLEKA----------LFDDGGTLNPDivGKSAQKIAELAGIEVPEDTKVLVAEetgvgpeeplsrEKLSPVLAFYRAE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 404 DDEEAIKIAND-SEYGLAG---GVFSQDITRALNIAKAVKTGRIWINTynqvpeGAPFGG 459
Cdd:cd07122 341 DFEEALEKARElLEYGGAGhtaVIHSNDEEVIEEFALRMPVSRILVNT------PSSLGG 394
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
52-447 |
6.85e-16 |
|
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: 79.62 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 52 VDTAVAAAQEAFESWSLTSKTERANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIPYAARhFNYFASVIETHEG 131
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAE-YIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 132 SVNDiDKDTMSIIRHEPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEIL-----PKGV 206
Cdd:cd07081 80 VLTG-DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagaPENL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 207 VNVVTGKGSESGNAIFNHEGVNKLSFTGstnvGYQVAEAGAKRIVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQ 286
Cdd:cd07081 159 IGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 287 GEVCSAGSRLLVQEGIYDKLISRLKEafsnikigdpldektQMGSQTSQEQMEKIQSYITYAEQSNAEILtggkritndG 366
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEG---------------QGAYKLTAEELQQVQPVILKNGDVNRDIV---------G 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 367 LDSGYFLEPTLIAVKDNADKLAQE------------EIFGPVLTIIKVKD----DEEAIKIANDSEYGLAGGVFSQDITR 430
Cdd:cd07081 291 QDAYKIAAAAGLKVPQETRILIGEvtslaehepfahEKLSPVLAMYRAANfadaDAKALALKLEGGCGHTSAMYSDNIKA 370
|
410 420
....*....|....*....|
gi 402762489 431 ALNI---AKAVKTGRIWINT 447
Cdd:cd07081 371 IENMnqfANAMKTSRFVKNG 390
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
74-459 |
1.98e-12 |
|
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: 68.79 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 74 RANLLRQISNKMMENKEKIATIETLNNGKPIRETSGIDIPYAARHFNYFASVIETHEGSVNDIDK--------DTMSIIR 145
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITASVGHiqdvllpdNGETYVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 146 HEPIGVVGAVVAWNFPmLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEIL----PKGVVNVVTGKGSESGNAI 221
Cdd:cd07077 98 AFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADaahgPKILVLYVPHPSDELAEEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 222 FNHEGVNKLSFTGstnvGYQVAEAGAK--RIVPAtLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQ 299
Cdd:cd07077 177 LSHPKIDLIVATG----GRDAVDAAVKhsPHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 300 EGIYDKLISRLKEAFSNIKIGDPldektqmgsqtsqeQMEKIQSYITYAEQsnaeiltggkritndgldsgyfleptlia 379
Cdd:cd07077 252 DDVLDPLYEEFKLKLVVEGLKVP--------------QETKPLSKETTPSF----------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 380 vkdnaDKLAQEEiFGPVLTIIKVKDDEEAIKIAND--SEYG--LAGGVFSQDITRALNIAKAVKTGRIWINTYNQVPEGA 455
Cdd:cd07077 289 -----DDEALES-MTPLECQFRVLDVISAVENAWMiiESGGgpHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGA 362
|
....
gi 402762489 456 PFGG 459
Cdd:cd07077 363 FAGK 366
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
120-447 |
1.33e-10 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 64.05 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 120 NYFASviethEGSVNDI-DKDTMSIIRH----------EPIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTP 188
Cdd:PRK13805 74 NHFAS-----EYIYNSYkDEKTVGVIEEddefgiieiaEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 189 LSLLEVAKIFQEI-----LPKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVgyqVAEA---GAkrivPAtleLG-- 258
Cdd:PRK13805 149 KSSIAAAKIVLDAavaagAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGM---VKAAyssGK----PA---LGvg 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 259 -GKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVQEGIYDKLISRLKEafsnikigdpldektqMGSQT-SQE 336
Cdd:PRK13805 219 aGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAVIVDDEIYDEVKEEFAS----------------HGAYFlNKK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 337 QMEKIQSYITYAEQS--NAEILtgGKRITNDGLDSGYFLEPT---LIAV---KDNADKLAQEEIFgPVLTIIKVKDDEEA 408
Cdd:PRK13805 283 ELKKLEKFIFGKENGalNADIV--GQSAYKIAEMAGFKVPEDtkiLIAEvkgVGESEPLSHEKLS-PVLAMYKAKDFEDA 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 402762489 409 IKIAND-SEYGLAG---GVFSQDITRALNIAKAVKTGRIWINT 447
Cdd:PRK13805 360 VEKAEKlVEFGGLGhtaVIYTNDDELIKEFGLRMKACRILVNT 402
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
51-446 |
1.25e-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: 57.49 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 51 DVDTAVAAAQEAFESWSLTSKTERANL----LRQISNKMMENKEKI------ATIETLNNGKPIRETSGID-IPYAARHF 119
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVcleiLQRLNARSFEMAHAVmhttgqAFMMAFQAGGPHAQDRGLEaVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 120 NYFASVIETHE-GSVND---IDKdTMSIIrhePIGVvGAVVA------WN-FPMLLASwkiapaIAAGNTIVIQPSSSTP 188
Cdd:cd07127 165 SRIPPTAEWEKpQGKHDplaMEK-TFTVV---PRGV-ALVIGcstfptWNgYPGLFAS------LATGNPVIVKPHPAAI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 189 LSLLEVAKIFQEIL------PKGVVNVVTGKGSESGNAIFNHEGVNKLSFTGSTNVGyQVAEAGAKRIVPATlELGGKSA 262
Cdd:cd07127 234 LPLAITVQVAREVLaeagfdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFG-DWLEANARQAQVYT-EKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV-QEGI--------YDKLISRLKEAFSNIkIGDPLDEKTQMGSQT 333
Cdd:cd07127 312 VVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQ 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 334 SQEQMEKIqsyityAEQSN-AEILTGGKRITNDGLDSGYFLEPTLIAVKDNADKLAQEEIFGPVLTIIKVKDDEEAIKIA 412
Cdd:cd07127 391 SPDTLARI------AEARQlGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 402762489 413 NDS--EYG-LAGGVFSQD---ITRALNIAKAVK-------TGRIWIN 446
Cdd:cd07127 465 RESvrEHGaMTVGVYSTDpevVERVQEAALDAGvalsinlTGGVFVN 511
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
148-428 |
2.49e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 56.35 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 148 PIGVVGAVVAWNFPMLLASWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEI-LPKGVVNVVTGKGsESGNAIFNHEG 226
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDG-PTMNKILLEAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 227 VNKLSFTGSTNVGYQVAeagakrivpatLELGGKsanIILDDANLDLAVEGIQLGIL------FNQ------GEVCSAGS 294
Cdd:cd07126 221 PRMTLFTGSSKVAERLA-----------LELHGK---VKLEDAGFDWKILGPDVSDVdyvawqCDQdayacsGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402762489 295 RLL-----VQEGIYDKLISRL-KEAFSNIKIGDPLDEKTqmgsQTSQEQMEKIqsyityAEQSNAEILTGGKRITNDGLD 368
Cdd:cd07126 287 ILFahenwVQAGILDKLKALAeQRKLEDLTIGPVLTWTT----ERILDHVDKL------LAIPGAKVLFGGKPLTNHSIP 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402762489 369 SGY-FLEPTLIAV--KDNADK----LAQEEIFGPVLTIIKVKDDEE--AIKIANDSEYGLAGGVFSQDI 428
Cdd:cd07126 357 SIYgAYEPTAVFVplEEIAIEenfeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDI 425
|
|
| |
