|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
32-512 |
0e+00 |
|
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: 1012.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 32 NLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLAD 111
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 112 LVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLL 191
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 192 MFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLI 271
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 272 QEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 351
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 352 PFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 431
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 432 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 25777724 512 K 512
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
38-511 |
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: 874.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 198 APALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGR 277
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTT 357
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 358 EQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIER 437
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 438 ANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
35-509 |
0e+00 |
|
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: 737.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 35 IKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVE 114
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGP-WPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 115 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 274
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 275 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 354
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 355 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 434
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 435 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-517 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 721.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 30 TPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKL 109
Cdd:PLN02466 50 TPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGP-WPKMTAYERSRILLRF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 110 ADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFP 189
Cdd:PLN02466 129 ADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 190 LLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGK 269
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 270 LIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVV 349
Cdd:PLN02466 289 IVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 350 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 429
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 430 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
....*...
gi 25777724 510 TVkiPQKN 517
Cdd:PLN02466 529 VT--PLKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
38-513 |
0e+00 |
|
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: 710.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGLKVSGSKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:cd07143 86 DYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 198 APALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGR 277
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTT 357
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 358 EQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIER 437
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25777724 438 ANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 513
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
36-512 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 693.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 36 KYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVER 115
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 116 DRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 274
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 275 AGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 354
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 355 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 433
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 434 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
46-509 |
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: 686.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 46 WQNSESGRvFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMES 125
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 126 LNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGN 205
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 206 TVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTL 285
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 286 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 365
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 366 KQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGL 445
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 446 VAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-511 |
0e+00 |
|
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: 676.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 198 APALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGr 277
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRR-VVGSPFDPT 356
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 433
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777724 434 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
34-514 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 651.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 34 EIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLV 113
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGP-WPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 114 ERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQE 273
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 274 AAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 433
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 434 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 513
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
.
gi 25777724 514 P 514
Cdd:PLN02766 496 Y 496
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
41-509 |
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: 640.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07119 80 ARLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 201 LCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 280
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 281 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 360
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 361 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 436
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777724 437 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
78-511 |
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: 628.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 78 DKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKI 157
Cdd:cd07078 1 DAAVAAARAAFK---AWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 158 HGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVI 236
Cdd:cd07078 77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 237 NILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQ 316
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 317 GQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR-K 395
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 396 GFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYN 475
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 25777724 476 A-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
52-509 |
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: 627.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 52 GRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKP 131
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 132 FLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKS 291
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNK 370
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 371 ILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 448
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 449 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
57-511 |
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: 617.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPF---- 132
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIretr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 133 LQAFYVdlqgvIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07114 80 AQVRYL-----AEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKS 291
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 371
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 372 LELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVA 447
Cdd:cd07114 314 ERYVARAREEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 448 AVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
59-513 |
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: 608.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYV 138
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 139 DLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 218
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 219 ALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIFAD 298
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 299 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 378
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 379 VAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKAL 458
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 459 TVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 513
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
57-511 |
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: 589.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 217 LSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIF 296
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 297 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 376
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 377 SGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 452
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 453 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
38-512 |
0e+00 |
|
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: 582.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD----GDYFTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQE 273
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 274 AAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT--M 431
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 432 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 25777724 512 K 512
Cdd:cd07140 485 E 485
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
39-511 |
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: 563.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRs 278
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 279 NLKRVTLELGGKSPNIIFADA-----DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 429
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 430 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 25777724 510 TV 511
Cdd:cd07559 477 LV 478
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
40-510 |
0e+00 |
|
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: 543.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 40 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 120 LA---TMESlngGKPFLQAFYVDLQGVIKTFRYYAGWADKIHgMTIPVDGdyfTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:cd07138 78 LAqaiTLEM---GAPITLARAAQVGLGIGHLRAAADALKDFE-FEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 276
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 433
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777724 434 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 510
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
57-511 |
0e+00 |
|
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: 541.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07109 78 RADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 217 LSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIF 296
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 297 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG-SPFDPttEQGPQIDKKQYNKILELI 375
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpGLEDP--DLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 376 QSGVAEGAKLECGG---KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 452
Cdd:cd07109 315 ARARARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 453 DINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
57-511 |
0e+00 |
|
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: 540.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK---EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 217 LSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIF 296
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 297 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 376
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 377 SGVAEGAKLECGGKGLG-----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 451
Cdd:cd07090 315 SAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 452 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
41-511 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 539.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLV-ERDRAv 119
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK---IWAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 120 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSn 279
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 280 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 359
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 360 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 435
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25777724 436 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
57-511 |
0e+00 |
|
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: 536.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK---TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQT 215
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 216 PLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGK-LIQEAAgrSNLKRVTLELGGKSPNI 294
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 295 IFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 374
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 375 IQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI 454
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 25777724 455 NKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
41-507 |
0e+00 |
|
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: 530.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 201 LCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNL 280
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 281 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 360
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 361 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 436
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 437 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVK 507
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
39-511 |
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: 527.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRs 278
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 279 NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 358
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 359 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 434
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777724 435 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-511 |
0e+00 |
|
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: 523.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 60 PATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVD 139
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 140 LQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 218
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 219 ALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFAD 298
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 299 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 378
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 379 VAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKA 457
Cdd:cd07118 321 RAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 25777724 458 LTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
57-510 |
0e+00 |
|
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: 520.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP---RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YvDLQGVIKTFRYYAGWADKIH---GMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 213 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 292
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 293 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 372
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 373 ELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 450
Cdd:cd07110 316 SFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 451 TNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 510
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
38-513 |
3.57e-180 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 514.46 E-value: 3.57e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSEsGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDR 117
Cdd:PRK13473 3 TKLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGmtiPVDGDY---FT-FTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQE 273
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 274 AAGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:PRK13473 235 AAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEG-AKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMD 432
Cdd:PRK13473 314 DEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 433 EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
.
gi 25777724 513 I 513
Cdd:PRK13473 474 H 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
57-511 |
4.47e-177 |
|
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: 505.71 E-value: 4.47e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGmtiPVDGDYF----TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 213 EQTPLSALYMGALIKEaGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 292
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 293 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 372
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 373 ELIqSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 452
Cdd:cd07092 313 GFV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 453 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-505 |
1.48e-173 |
|
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: 498.07 E-value: 1.48e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIhgmtipvdgDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLL---------DT-ELAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 201 LCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGRSn 279
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 280 lKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 359
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 360 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERAN 439
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25777724 440 NSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSE 505
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
82-511 |
1.81e-173 |
|
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: 493.29 E-value: 1.81e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 82 QAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMT 161
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 162 IP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILP 240
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 241 GYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 320
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 321 TAGSRIFVEESIYEEFVRRSVerakrrvvgspfdptteqgpqidkkqynkileliqsgvaegaklecggkglgrkgffie 400
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 401 pTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-A 479
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 25777724 480 QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
57-509 |
2.35e-172 |
|
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: 494.07 E-value: 2.35e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHG-MTIPVDGDYFTFT----RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKS 291
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 371
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 372 LELIQSGVAEGAKLECGGK---GLGrKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 448
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGrpaGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 449 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
57-511 |
1.79e-170 |
|
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: 488.58 E-value: 1.79e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGwadkihgMTIPV-----DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07106 77 QFEVGGAVAWLRYTAS-------LDLPDeviedDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKS 291
Cdd:cd07106 150 SPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 371
Cdd:cd07106 227 AAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 372 LELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 451
Cdd:cd07106 307 KELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 452 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
41-509 |
5.21e-170 |
|
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: 488.68 E-value: 5.21e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRvfPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 120 LATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrS 278
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 279 NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 358
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 359 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 436
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 437 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTV 509
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
26-510 |
2.38e-169 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 488.09 E-value: 2.38e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 26 LPSPTPNleikyTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFS--LGSVWRRMDASERG 103
Cdd:PLN02467 1 MAIPVPR-----RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 104 RLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHG-----MTIPVDgDYFTFTRHEPIG 178
Cdd:PLN02467 76 KYLRAIAAKITERKSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLKEPLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 179 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDK 258
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 259 IAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVR 338
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 339 RSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKE 416
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 417 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 496
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
|
490
....*....|....
gi 25777724 497 EFGLREYSEVKTVT 510
Cdd:PLN02467 473 EWGLENYLSVKQVT 486
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
40-511 |
1.29e-168 |
|
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: 484.77 E-value: 1.29e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 40 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 120 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG------WADKIHGMTIpvdGDyfTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSGG---GH--VLVRREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQE 273
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 274 AAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:cd07139 234 VCGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK---GLGRkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 430
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpaGLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 431 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYnALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 510
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
.
gi 25777724 511 V 511
Cdd:cd07139 471 L 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-509 |
2.19e-166 |
|
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: 479.07 E-value: 2.19e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:cd07088 78 AKLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsN 279
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-N 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 280 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 359
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 360 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 438
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 439 NNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-511 |
1.01e-164 |
|
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: 475.30 E-value: 1.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQ-VCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 120 LATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRS 278
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 279 NlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 358
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 359 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 434
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 435 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNAlNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 511
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
41-515 |
2.41e-161 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 466.98 E-value: 2.41e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWA-DKIHGMTIPVDgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:TIGR02299 81 AVLECLDCGQPLRQT----RQQVIRAaenFRFFADKCeEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQeAAG 276
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG-------RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 429
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 430 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
490
....*....|.
gi 25777724 510 TV-----KIPQ 515
Cdd:TIGR02299 475 ALalgphHIPK 485
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
57-513 |
4.67e-160 |
|
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: 462.62 E-value: 4.67e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAF 136
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 217 LSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGGKSPNIIF 296
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 297 ADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI 375
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 376 QSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 451
Cdd:cd07107 315 DSAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777724 452 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 513
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
57-511 |
5.21e-160 |
|
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: 462.60 E-value: 5.21e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 217 LSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAGRsnLKRVTLELGGKSPNII 295
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIyRAAADR--LIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 296 FADADLDYAVEQAHQGV-FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 374
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 375 IQSGVAE-GAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07108 315 IDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 450 FTNDINKALTVSSAMQAGTVWIN-CYNALNAQSpFGGFKMSGNGREMG-EFGLREYSEVKTVTV 511
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNqGGGQQPGQS-YGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
55-511 |
1.21e-156 |
|
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: 453.59 E-value: 1.21e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-----DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 210 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGG 289
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 290 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 369
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 370 KILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777724 450 FTNDINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-509 |
1.79e-153 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 447.42 E-value: 1.79e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 32 NLEIKyTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLAD 111
Cdd:PRK09847 15 SLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERG-DWSLSSPAKRKAVLNKLAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 112 LVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLL 191
Cdd:PRK09847 93 LMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 192 MFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLI 271
Cdd:PRK09847 173 LTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 272 QEAAGRSNLKRVTLELGGKSPNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG 350
Cdd:PRK09847 253 LKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 351 SPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 430
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 431 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
55-511 |
6.15e-152 |
|
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: 441.77 E-value: 6.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 135 AFYvDLQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAE 213
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 214 QTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPN 293
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 294 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 373
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 374 LIQSGVAEGAKLECGGKGLGRkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 453
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 454 INKALTVSSAMQAGTVWINCYNAL-NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
38-509 |
7.40e-152 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 443.36 E-value: 7.40e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDR 117
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:PLN02278 102 EDLAQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 276
Cdd:PLN02278 181 VGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:PLN02278 261 AT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 436
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777724 437 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-512 |
8.26e-152 |
|
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: 442.27 E-value: 8.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTI------PVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEA 274
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 275 AGrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 354
Cdd:cd07113 240 AA-SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 355 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 434
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777724 435 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
76-511 |
6.13e-151 |
|
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: 438.50 E-value: 6.13e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWAD 155
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 156 KIHGMTIPVDGD-YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI-KEAGFPP 233
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIfEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 234 GVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF 313
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 314 FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglg 393
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 394 RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINC 473
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 25777724 474 YNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07104 393 QTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
55-511 |
1.12e-149 |
|
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: 436.01 E-value: 1.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD---VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-DY----FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyEYnerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 210 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGG 289
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 290 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 369
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 370 KILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777724 450 FTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
41-511 |
1.45e-149 |
|
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: 436.88 E-value: 1.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 201 LCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 280
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 281 KRVTLELGGKSPNIIFA------DADLDYAVEQAhqGVF-FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:cd07116 239 IPVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNvTDDMRIAKEEIFGPVQEILRFK 429
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 430 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
..
gi 25777724 510 TV 511
Cdd:cd07116 476 LV 477
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
41-513 |
8.28e-146 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 427.22 E-value: 8.28e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWqnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfsLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR03216 4 FINGAF--VESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA--LKGPWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHG----MTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTecfeMATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGP-TAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 275
Cdd:TIGR03216 160 VGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 276 GRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 355
Cdd:TIGR03216 240 ADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 356 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGG-----KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 430
Cdd:TIGR03216 319 ATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 431 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 510
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
...
gi 25777724 511 VKI 513
Cdd:TIGR03216 479 IKL 481
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
41-511 |
3.32e-143 |
|
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: 420.43 E-value: 3.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGrVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK---EWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGYGPtAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 275
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 276 GRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 355
Cdd:cd07086 236 ARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 356 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 433
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 434 VIERANNSDFGLVAAVFTNDINKALTVSSAM--QAGTVWIN--CYNAlNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
..
gi 25777724 510 TV 511
Cdd:cd07086 474 TI 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
40-513 |
3.30e-140 |
|
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: 413.93 E-value: 3.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 40 IFINNEWQnsESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07124 35 LVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGR- 277
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 ----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 353
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 354 DPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 431
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 432 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG-NGREMGEFGLREYSEVKT 508
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
....*
gi 25777724 509 VTVKI 513
Cdd:cd07124 508 VTENF 512
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
58-511 |
3.38e-135 |
|
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: 399.03 E-value: 3.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRmDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfY 137
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 138 VDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPL 217
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 218 SALYMGALIKEA-GFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrSNLKRVTLELGGKSPNIIF 296
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 297 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 376
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 377 SGVAEGAK-LECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 453
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777724 454 INKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
77-511 |
5.31e-133 |
|
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: 392.59 E-value: 5.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 77 IDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY-VDLQGVIktFRYYAgwaD 155
Cdd:cd07100 1 IEAALDRAHAAFL---AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKCAWI--CRYYA---E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 156 KIHGM----TIPVDGDYfTFTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVIKPAEQTPLSALYMGALIKE 228
Cdd:cd07100 73 NAEAFladePIETDAGK-AYVRYEPLGVVLGIMPWNFPFwqvFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 229 AGFPPGVINILPGYGPTAGAAIASHIgIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQA 308
Cdd:cd07100 149 AGFPEGVFQNLLIDSDQVEAIIADPR-VRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 309 HQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECG 388
Cdd:cd07100 227 VKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 389 GKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 468
Cdd:cd07100 307 GKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 25777724 469 VWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
44-512 |
2.33e-130 |
|
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: 387.04 E-value: 2.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 44 NEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM 123
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 124 ESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP--VDGDYFTFTRhEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07151 78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 202 CCGNTVVIKPAEQTPLSA-LYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNL 280
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 281 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 360
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 361 PQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 440
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGE---AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 441 SDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALN--AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNdePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
57-511 |
3.83e-130 |
|
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: 386.02 E-value: 3.83e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAE---NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKS 291
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 371
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 372 LELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 451
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 452 NDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
58-511 |
5.39e-130 |
|
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: 385.81 E-value: 5.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFY 137
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR---AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 138 VDLQGVIKTFRYYAGWADKI-------HGMTIPVdgdyFTFT-RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlaprkvpTGLLMPN----KKATvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 210 KPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIAShiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGG 289
Cdd:cd07099 153 KPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA--GVDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 290 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 369
Cdd:cd07099 230 KDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 370 KILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07099 310 IVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 450 FTNDINKALTVSSAMQAGTVWINC--YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
55-507 |
1.07e-126 |
|
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: 377.36 E-value: 1.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGD-----YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07147 78 A-RGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 210 KPAEQTPLSALYMGALIKEAGFPPGVINILPGygPTAGAAI-ASHIGIDKIAFTGSTEVGKLIQEAAGRsnlKRVTLELG 288
Cdd:cd07147 157 KPASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 289 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 368
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 369 NKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 448
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 449 VFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVK 507
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINDVPTFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-511 |
5.51e-126 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 378.07 E-value: 5.51e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 49 SESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNG 128
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA---QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 129 GKPFLQAFYvDLQGVIKTFRYYAGWADKI-----HGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCC 203
Cdd:PRK09407 105 GKARRHAFE-EVLDVALTARYYARRAPKLlaprrRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 204 GNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHigIDKIAFTGSTEVGKLIQEAAGRsNLKRV 283
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGR-RLIGF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 284 TLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQI 363
Cdd:PRK09407 259 SLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 364 DKKQYNKILELIQSGVAEGAKLECGGKG---LGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 440
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVLAGGKArpdLG--PLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777724 441 SDFGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNALNA--QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
39-512 |
1.27e-125 |
|
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: 375.37 E-value: 1.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 39 KIFINNEWQNSeSGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWADKIHGMTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPL 190
Cdd:cd07082 80 EVANLLMWEIGKTLKDA----LKEVDRTidyIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 191 LMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKL 270
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 271 IQEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG 350
Cdd:cd07082 236 LKKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 351 SPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 430
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 431 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
...
gi 25777724 510 TVK 512
Cdd:cd07082 471 VIN 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-512 |
9.54e-124 |
|
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: 370.69 E-value: 9.54e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 118 AVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:cd07085 78 DELARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 276
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:cd07085 236 ANG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMD 432
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 433 EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMS--GNGREMGEFGLREYSEVKTV 509
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTV 474
|
...
gi 25777724 510 TVK 512
Cdd:cd07085 475 TSR 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
42-490 |
1.45e-121 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 366.18 E-value: 1.45e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 42 INNEWQNSEsgRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYA----GWADKIHgmTIPVDGDYFTFtRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:PRK03137 116 SAWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKP--VESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAG 276
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RSN-----LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 351
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 352 PFDPtTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 431
Cdd:PRK03137 352 PEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 432 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG 490
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
63-511 |
1.79e-121 |
|
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: 363.54 E-value: 1.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 63 GEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM---ESlnGGKPFLQAFYVD 139
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA---QRAWAATPPRERAAVLRRAADLLEEHADEIADWivrES--GSIRPKAGFEVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 140 LqgVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSA 219
Cdd:cd07152 76 A--AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 220 LYMGALI-KEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFAD 298
Cdd:cd07152 154 GVVIARLfEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 299 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 378
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 379 VAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKAL 458
Cdd:cd07152 312 VAAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 459 TVSSAMQAGTVWINCYNALN-AQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 511
Cdd:cd07152 389 ALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
76-511 |
1.44e-120 |
|
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: 360.74 E-value: 1.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL-ATMESLNGGKPFLQAFYVDLqgVIKTFRYYAGWA 154
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFiEAMMEETGATAAWAGFNVDL--AAGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 155 DKIHGMTIPVD--GDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFP 232
Cdd:cd07105 76 TQIIGGSIPSDkpGTL-AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 233 PGVINIL---PGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAH 309
Cdd:cd07105 155 KGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 310 QGVFFNQGQCCTAGSRIFVEESIYEEFVrrsvERAKRRVVGSPFDPTTEqGPQIDKKQYNKILELIQSGVAEGAKLECGG 389
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFV----EKLKAAAEKLFAGPVVL-GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 390 KG-LGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 468
Cdd:cd07105 309 LAdESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 25777724 469 VWINCYNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07105 389 VHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-511 |
3.84e-120 |
|
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: 360.47 E-value: 3.84e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 60 PATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvD 139
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA---QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 140 LQGVIKTFRYYAGWADKI-----HGMTIPVdgdyFTFTR--HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPV----LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 213 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 292
Cdd:cd07101 155 SQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNA--DYVMFTGSTATGRVVAERAGR-RLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 293 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 372
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 373 ELIQSGVAEGAKLECGGKG---LGRkgFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 450 FTNDINKALTVSSAMQAGTVWIN-CYNAL--NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
58-509 |
3.67e-113 |
|
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: 342.69 E-value: 3.67e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfy 137
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK---GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 138 vdlQGVIKTF----RYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07102 76 ---GGEIRGMleraRYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 213 EQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIgIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSP 292
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPR-IDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 293 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 372
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 373 ELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:cd07102 311 AQIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 450 FTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-511 |
9.47e-113 |
|
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: 341.65 E-value: 9.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAArlafslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07146 77 Y-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGrsnLKRVTLELGGKS 291
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 292 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 371
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 372 LELIQSGVAEGAKLECGGkglGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 451
Cdd:cd07146 313 ENRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777724 452 NDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 511
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-513 |
1.04e-112 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 342.66 E-value: 1.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP---AWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfyvdlQGVIKTFRYYAGW----ADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAW 195
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 196 KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 275
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 276 GRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 355
Cdd:PRK11241 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 356 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 435
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777724 436 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 513
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
58-511 |
2.44e-106 |
|
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: 325.41 E-value: 2.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY 137
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 138 vdlqGVIKTFryyagwADKI-----HG----MTIPVDGDYFTFTR-----HEPIGVCGQIIPWNFPLLMFAWKIAPALCC 203
Cdd:cd07098 78 ----GEILVT------CEKIrwtlkHGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 204 GNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGYGPTaGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSn 279
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 280 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 359
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 360 GPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 435
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777724 436 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCY--NALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 511
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
106-509 |
2.66e-104 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 318.22 E-value: 2.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 106 LDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD---GDYFTFTRhePIGVCGQ 182
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 183 IIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFT 262
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 263 GSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVE 342
Cdd:PRK10090 158 GSVSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 343 RAKRRVVGSPFD-PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGP 421
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 422 VQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLR 501
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 25777724 502 EYSEVKTV 509
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
59-509 |
7.62e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 305.89 E-value: 7.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYV 138
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 139 DLQGVIKTFRYYAgwaDKIHGMTIPVDGDYFT------FTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVI 209
Cdd:PRK09406 83 EALKCAKGFRYYA---EHAEALLADEPADAAAvgasraYVRYQPLGVVLAVMPWNFPLwqvVRFA---APALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 210 KPAEQTPLSALYMGALIKEAGFPPGVINILPgYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSnLKRVTLELGG 289
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDE-IKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 290 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 369
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 370 KILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 449
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 450 FTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-510 |
1.55e-91 |
|
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: 288.71 E-value: 1.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 40 IFINNEWqnSESGRVFPVYNP-ATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07083 21 LVIGGEW--VDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADKIHG---MTIPVDG-DYFTFTRhePIGVCGQIIPWNFPLLMFA 194
Cdd:cd07083 96 ELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpavEVVPYPGeDNESFYV--GLGAGVVISPWNFPVAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA 274
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 275 AGR-----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVV 349
Cdd:cd07083 253 AARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 350 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 429
Cdd:cd07083 333 GPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 430 TMD--EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFG-LREYS 504
Cdd:cd07083 412 DDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKTGGPHyLRRFL 491
|
....*.
gi 25777724 505 EVKTVT 510
Cdd:cd07083 492 EMKAVA 497
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
43-511 |
2.69e-88 |
|
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: 279.09 E-value: 2.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 43 NNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLAT 122
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK---EWRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 123 MESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 202 CCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAG 276
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVgQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 277 RsnLKRVTLELGGKSPNIIFADADLDYAVeqahQGVFF----NQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSP 352
Cdd:cd07130 237 R--FGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 353 FDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMD 432
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 433 EVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 469
|
..
gi 25777724 510 TV 511
Cdd:cd07130 470 TI 471
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-516 |
7.21e-86 |
|
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: 274.07 E-value: 7.21e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 29 PTPNLEIKYTKI--FINNEWQNS--------ESGRVFPVYNPATGEQV-CEVQEADKADIDKAVQAARLAFSlgsVWRRM 97
Cdd:cd07125 12 LEVPLEALADALkaFDEKEWEAIpiingeetETGEGAPVIDPADHERTiGEVSLADAEDVDAALAIAAAAFA---GWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 98 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADK-IHGMTIPVDGDYFTFTRHEP 176
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD-AEVREAIDFCRYYAAQARElFSDPELPGPTGELNGLELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 177 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGI 256
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 257 DKIAFTGSTEVGKLIQEAagRSNLKRVTL----ELGGKspNIIFAD--ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 330
Cdd:cd07125 248 DGVIFTGSTETAKLINRA--LAERDGPILpliaETGGK--NAMIVDstALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 331 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEgAKLECGGKGLGRKGFFIEPTVFSNVTDD 410
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 411 MRiaKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFG 484
Cdd:cd07125 403 DL--TTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFG 478
|
490 500 510
....*....|....*....|....*....|....*
gi 25777724 485 GFKMSGNGREMGefG---LREYSEVKTVTVKIPQK 516
Cdd:cd07125 479 GWGLSGTGPKAG--GpnyLLRFGNEKTVSLNTTAA 511
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
59-509 |
7.21e-83 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 264.80 E-value: 7.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGrllDKLADLVE--RDRA-VLATMESLNGGKPFLQA 135
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRA---QKLRDIGKalRARSeEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 136 fyvdLQGVIKTFRYYAGWADKIHGMTIP----VDGDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:PRK13968 87 ----RAEVAKSANLCDWYAEHGPAMLKAeptlVENQQ-AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVInilpGYGPTAGAAIASHIGIDKIA---FTGSTEVGKLIQEAAGRSnLKRVTLELG 288
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVY----GWLNADNDGVSQMINDSRIAavtVTGSVRAGAAIGAQAGAA-LKKCVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 289 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 368
Cdd:PRK13968 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 369 NKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 448
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 449 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
57-492 |
1.71e-80 |
|
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: 258.50 E-value: 1.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWrrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 212 AEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHigidKIA---FTGSTEVGKLIqeaagRSNLK---RVTL 285
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDP----RVAffsFIGSARVGWML-----RSKLApgtRCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 286 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 365
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 366 KQYNKILELIQSGVAEGAKLECGGKGLGRKGFfiEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGL 445
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 25777724 446 VAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG 492
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
173-509 |
1.24e-78 |
|
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: 252.92 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 173 RHEPIGVCGQIIPWNFPL-LMFAwKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygptaGAAIA 251
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFnLAFG-PLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-----DAEVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 252 SHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 328
Cdd:cd07134 170 QALlelPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 329 EESIYEEFVRRsVERAKRRVVGSpfDPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKLECGGKgLGRKGFFIEPTVF 404
Cdd:cd07134 249 HESVKDAFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 405 SNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSamqAGTVWIN--CYNALNA 479
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkanVNKVLARTS---SGGVVVNdvVLHFLNP 401
|
330 340 350
....*....|....*....|....*....|
gi 25777724 480 QSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
76-493 |
8.23e-77 |
|
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: 247.96 E-value: 8.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY--------VDLQgvIKTF 147
Cdd:cd07095 1 QVDAAVAAARAAFP---GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 148 RYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIK 227
Cdd:cd07095 76 HERTG--ERATPM-----AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 228 EAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI-QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVE 306
Cdd:cd07095 149 EAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 307 QAHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL 385
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 386 ECGGKGLGRKGFFIEPTVFsNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQ 465
Cdd:cd07095 307 LLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430
....*....|....*....|....*....|.
gi 25777724 466 AGTVWINcyNALNAQS---PFGGFKMSGNGR 493
Cdd:cd07095 386 AGIVNWN--RPTTGASstaPFGGVGLSGNHR 414
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
39-512 |
1.58e-75 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 245.95 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL---TWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAFYVDLQGvIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALGDVARG-LEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 198 APALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGR 277
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 SNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:TIGR01722 237 HG-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAaVLVGAA--DEWVPEIRERAEKIRIGPGDDPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGF----FIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMD 432
Cdd:TIGR01722 314 AEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 433 EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSP---FGGFKMS--GNGREMGEFGLREYSEVK 507
Cdd:TIGR01722 394 EAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGK 471
|
....*
gi 25777724 508 TVTVK 512
Cdd:TIGR01722 472 TVTTR 476
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
39-492 |
2.69e-75 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 246.21 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRA 118
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 119 VLATMESLNGGKPFLQAF-----------YVDLQGViktfrYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPW 186
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVtevvrsgdlisYTAEEGV-----RILGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 187 NFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGStE 266
Cdd:PLN00412 169 NYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 267 VGKLIQEAAGRSNLKrvtLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKR 346
Cdd:PLN00412 248 TGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 347 RVVGSPFDpTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEIL 426
Cdd:PLN00412 325 LTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777724 427 RFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNG 492
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
41-493 |
5.19e-75 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 244.87 E-value: 5.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP---AWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAFY--------VDLQgvIKTFRYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLM 192
Cdd:PRK09457 80 AEVIARETGKPLWEAATevtaminkIAIS--IQAYHERTG--EKRSEM-----ADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 193 FAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLI- 271
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 272 QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVG 350
Cdd:PRK09457 230 RQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 351 SPF-DPTTEQGPQIDKKQYNKILELIQSGVAEGAK----LECGGKGLGrkgfFIEPTVFsNVTDDMRIAKEEIFGPVQEI 425
Cdd:PRK09457 309 RWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKslleMTQLQAGTG----LLTPGII-DVTGVAELPDEEYFGPLLQV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 426 LRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTV-WINCYNALNAQSPFGGFKMSGNGR 493
Cdd:PRK09457 384 VRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
94-509 |
5.23e-72 |
|
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: 235.11 E-value: 5.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 94 WRRmdasergRLLDKLADLV-ERDRAVLATMES-LngGKPFLQAFYVDLQGVIKTFRYY----AGWADKIHGMTIPVDGD 167
Cdd:cd07087 21 WRK-------AQLKALKRMLtENEEEIAAALYAdL--GKPPAEAYLTEIAVVLGEIDHAlkhlKKWMKPRRVSVPLLLQP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 168 YFTFTRHEPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGygp 244
Cdd:cd07087 92 AKAYVIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 245 taGAAIASHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCT 321
Cdd:cd07087 165 --GVEVATALlaePFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 322 AGSRIFVEESIYEEFvrrsVERAKRRVV---GSPFDPTTEQGPQIDKKQYNKILELIQSGvaegaKLECGGkGLGRKGFF 398
Cdd:cd07087 242 APDYVLVHESIKDEL----IEELKKAIKefyGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 399 IEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNA 476
Cdd:cd07087 312 IAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHA 391
|
410 420 430
....*....|....*....|....*....|...
gi 25777724 477 LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07087 392 AIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
52-496 |
1.09e-70 |
|
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: 234.03 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 52 GRVFPVYNPAT-GEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGK 130
Cdd:TIGR01238 50 GEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFP---TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 131 PFLQAFyVDLQGVIKTFRYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIK 210
Cdd:TIGR01238 127 TIHNAI-AEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 211 PAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTL--ELG 288
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 289 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 368
Cdd:TIGR01238 275 GQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 369 NKILELIQSGVAEG---AKLECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDF 443
Cdd:TIGR01238 355 QNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGY 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 444 GLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMG 496
Cdd:TIGR01238 433 GLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
41-513 |
1.26e-69 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 240.87 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQN----SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVER 115
Cdd:PRK11904 546 FLEKQWQAgpiiNGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFP---AWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 116 DRAVLATMESLNGGKPfLQ--------AfyVDlqgviktF-RYYAGWADKIHGMTIPVDGdyftFT------RHEPIGV- 179
Cdd:PRK11904 623 NRAELIALCVREAGKT-LQdaiaevreA--VD-------FcRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVf 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 180 -CgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDK 258
Cdd:PRK11904 689 vC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAG 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 259 IAFTGSTEVGKLIQEA-AGRSNlKRVTL--ELGGKspNIIFADAD------LDYAVEQAhqgvFFNQGQCCTAGSRIFVE 329
Cdd:PRK11904 767 VAFTGSTETARIINRTlAARDG-PIVPLiaETGGQ--NAMIVDSTalpeqvVDDVVTSA----FRSAGQRCSALRVLFVQ 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 330 ESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG---AKLECGgkGLGRKGFFIEPTVFSn 406
Cdd:PRK11904 840 EDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP--AGTENGHFVAPTAFE- 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 407 vTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----Q 480
Cdd:PRK11904 917 -IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ 994
|
490 500 510
....*....|....*....|....*....|....*.
gi 25777724 481 sPFGGFKMSGNGREMGefG---LREYSEVKTVTVKI 513
Cdd:PRK11904 995 -PFGGQGLSGTGPKAG--GphyLLRFATEKTVTVNT 1027
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
48-492 |
1.32e-69 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 241.77 E-value: 1.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 48 NSESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESL 126
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFP---AWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 127 NGGKPFL-------QAfyVDlqgviktF-RYYAGWADKIHGMTipvdgdyftfTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:COG4230 642 EAGKTLPdaiaevrEA--VD-------FcRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 199 PALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGR 277
Cdd:COG4230 703 AALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 278 SNlKRVTL--ELGGKspNIIFADADldyA-VEQAHQGV----FFNQGQCCTAgSRI-FVEESIYEEFVRRSVERAKRRVV 349
Cdd:COG4230 783 DG-PIVPLiaETGGQ--NAMIVDSS---AlPEQVVDDVlasaFDSAGQRCSA-LRVlCVQEDIADRVLEMLKGAMAELRV 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 350 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRF 428
Cdd:COG4230 856 GDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRY 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777724 429 K--TMDEVIERANNSDFGLVAAVFT-NDiNKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 492
Cdd:COG4230 934 KadELDKVIDAINATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
26-510 |
2.86e-66 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 225.01 E-value: 2.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 26 LPSPTPNLeikytkifINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRL 105
Cdd:PLN02419 110 MPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQRV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 106 LDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQII 184
Cdd:PLN02419 179 MLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGIC 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 185 PWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIGIDKIAFTGS 264
Cdd:PLN02419 258 PFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 265 TEVGKLIQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFVRRSVER 343
Cdd:PLN02419 337 NTAGMHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVER 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 344 AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIF 419
Cdd:PLN02419 414 AKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 420 GPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSPFGGF-----KMSGNGRE 494
Cdd:PLN02419 494 GPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgnkaSFAGDLNF 571
|
490
....*....|....*.
gi 25777724 495 MGEFGLREYSEVKTVT 510
Cdd:PLN02419 572 YGKAGVDFFTQIKLVT 587
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
98-509 |
4.30e-66 |
|
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: 220.05 E-value: 4.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 98 DASERGRLLDKLADLVERDRAVLAtmESLN---GGKPFLQAFYVDLQGVIKTFRYY----AGW--ADKIHGMtipvdgdy 168
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWmkPSRRHVG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 169 FTFT------RHEPIGVCGQIIPWNFPL-LMFAWKIApALCCGNTVVIKPAEQTP-LSALyMGALIKEAgFPPGVINILP 240
Cdd:cd07133 88 LLFLpakaevEYQPLGVVGIIVPWNYPLyLALGPLIA-ALAAGNRVMIKPSEFTPrTSAL-LAELLAEY-FDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 241 GyGPTAGAAIaSHIGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 320
Cdd:cd07133 165 G-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 321 TAGSRIFVEESIYEEFVRRSVERAKRRVvgspfdPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKL-ECGGKG---- 391
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGedfa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 392 LGRKgffIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKAL--TVSsamqa 466
Cdd:cd07133 316 ATRK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaeQDRVLrrTHS----- 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 25777724 467 GTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07133 388 GGVTINdtLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-509 |
8.52e-66 |
|
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: 219.40 E-value: 8.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 75 ADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG-- 152
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKnl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 153 --WA--DKIHGMTIPvdgdYF---TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGAL 225
Cdd:cd07135 82 kkWAkdEKVKDGPLA----FMfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 226 IKEAgFPPGVINILPGYGPTAGAAIASHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAV 305
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTALLEQKF--DKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 306 EQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSvERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKL 385
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 386 ECGGKgLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQ 465
Cdd:cd07135 310 VIGGE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTR 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 25777724 466 AGTVWIN-------CYNAlnaqsPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07135 389 SGGVVINdtlihvgVDNA-----PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
175-509 |
1.32e-64 |
|
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: 216.60 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 175 EPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGYGPTAGAAIA 251
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 252 SHIgiDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES 331
Cdd:cd07136 175 QKF--DYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 332 IYEEFVRRSVERAKRRVVGSPFDptTEQGPQI-DKKQYNKILELIQSGvaegaKLECGGKGlGRKGFFIEPTVFSNVTDD 410
Cdd:cd07136 252 VKEKFIKELKEEIKKFYGEDPLE--SPDYGRIiNEKHFDRLAGLLDNG-----KIVFGGNT-DRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 411 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcyNAL----NAQSPFGGF 486
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTImhlaNPYLPFGGV 401
|
330 340
....*....|....*....|...
gi 25777724 487 KMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07136 402 GNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
57-490 |
2.38e-64 |
|
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: 217.84 E-value: 2.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 57 VYNPATGEQVC---------EVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVE---RDRAVLATMe 124
Cdd:cd07123 42 VRTGNTGKQVMphdhahvlaTYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 125 sLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTiPVDGDYFTFTR--HEPI-GVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07123 118 -LGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 202 CcGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRS--- 278
Cdd:cd07123 196 M-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 279 --NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 356
Cdd:cd07123 275 yrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 357 TEQGPQIDKKQYNKILELIQSGVAE-GAKLECGGKGLGRKGFFIEPTVFsnVTDD--MRIAKEEIFGPVQEILRFKTMD- 432
Cdd:cd07123 355 NFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI--ETTDpkHKLMTEEIFGPVLTVYVYPDSDf 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 433 -EVIERANN-SDFGLVAAVFTND---INKALTVSSaMQAGTVWIN--CYNALNAQSPFGGFKMSG 490
Cdd:cd07123 433 eETLELVDTtSPYALTGAIFAQDrkaIREATDALR-NAAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
49-492 |
2.97e-63 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 223.59 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 49 SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLN 127
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 128 GGKPFLQAF-----YVDlqgviktF-RYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:PRK11905 640 AGKTLANAIaevreAVD-------FlRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAAL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 202 CCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGRSNl 280
Cdd:PRK11905 702 VAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlAKRSG- 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 281 KRVTL--ELGGKSPNIIFADAdldyAVEQAHQGV----FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 354
Cdd:PRK11905 781 PPVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 355 PTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--M 431
Cdd:PRK11905 857 LSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKAdeL 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 432 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 492
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
17-492 |
2.45e-56 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 203.67 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 17 AALMASLHLLPSPTPNLEikytkifinnewQNSESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAfslGSVWR 95
Cdd:PRK11809 635 SALLASAHQKWQAAPMLE------------DPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNA---APIWF 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 96 RMDASERGRLLDKLADLVErdravlATMESLNG------GKPFLQAF-----YVDLqgviktFRYYAGWADkihgmtipv 164
Cdd:PRK11809 700 ATPPAERAAILERAADLME------AQMQTLMGllvreaGKTFSNAIaevreAVDF------LRYYAGQVR--------- 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 165 dgDYFTFTRHEPIG--VCgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGY 242
Cdd:PRK11809 759 --DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGR 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 243 GPTAGAAIASHIGIDKIAFTGSTEVGKLIQEA-AGR-SNLKRVT---LELGGKSPNIIFADADLDYAVEQAHQGVFFNQG 317
Cdd:PRK11809 835 GETVGAALVADARVRGVMFTGSTEVARLLQRNlAGRlDPQGRPIpliAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 318 QCCTAGSRIFVEESIYEefvrRSVERAK----RRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAK---LECGGK 390
Cdd:PRK11809 915 QRCSALRVLCLQDDVAD----RTLKMLRgamaECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENS 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 391 GLGRKGFFIEPTVFS-NVTDDMriaKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTN-DINKALTVSSAmQA 466
Cdd:PRK11809 991 EDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRiDETIAQVTGSA-HV 1066
|
490 500 510
....*....|....*....|....*....|
gi 25777724 467 GTVWINcYNALNA----QsPFGGFKMSGNG 492
Cdd:PRK11809 1067 GNLYVN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
41-511 |
3.24e-56 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 195.82 E-value: 3.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAArlaFSLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRAC---EEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKpFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEA----GFPPGVINILPGyGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAA 275
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 276 gRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 355
Cdd:PLN02315 257 -NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 356 TTEQGP---QIDKKQYNKILELIQSgvaEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMD 432
Cdd:PLN02315 336 GTLLGPlhtPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 433 EVIERANNSDFGLVAAVFTND---INKALTVSSAmQAGTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKT 508
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNpetIFKWIGPLGS-DCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
|
...
gi 25777724 509 VTV 511
Cdd:PLN02315 491 CTI 493
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
170-512 |
4.01e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 192.55 E-value: 4.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 170 TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgFPPGVINILPGyGPTAGAA 249
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 250 IASHiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVE 329
Cdd:PTZ00381 181 LLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 330 ESIYEEFVrRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECGGKgLGRKGFFIEPTVFSNVTD 409
Cdd:PTZ00381 259 RSIKDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 410 DMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFK 487
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVG 413
|
330 340
....*....|....*....|....*
gi 25777724 488 MSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
79-512 |
2.94e-46 |
|
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: 167.40 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 79 KAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVE--RDRAVLATMESLNggKPFLQAFYVDLQGVIKTFRY----YAG 152
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNEIKYaisnLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 153 WADkihgmTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI- 226
Cdd:cd07132 77 WMK-----PEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 227 ----KEAgFPpgVInilpgygpTAGAAIASHI---GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADA 299
Cdd:cd07132 152 kyldKEC-YP--VV--------LGGVEETTELlkqRFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 300 DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFvrrsVERAKRRVV---GSpfDPTTEQ--GPQIDKKQYNKILEL 374
Cdd:cd07132 220 DIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKF----VEALKKTLKefyGE--DPKESPdyGRIINDRHFQRLKKL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 375 IQSG-VA---EGAKLECggkglgrkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 450
Cdd:cd07132 294 LSGGkVAiggQTDEKER----------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVF 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 451 TND---INKALTVSSamqAGTVwinCYNALNAQS-----PFGGFKMSGNGREMGEFGLREYSEVKTVTVK 512
Cdd:cd07132 364 SNNkkvINKILSNTS---SGGV---CVNDTIMHYtldslPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
81-509 |
1.53e-40 |
|
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: 151.41 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 81 VQAARLAFSLGsvwRRMDASERGRLLDKLADLV-ERDRAVLATMESlNGGKPFLQAFYVDLQGVIKT----FRYYAGWAD 155
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSScklaIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 156 ----KIHGMTIPVDGDYFTftrhEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAgF 231
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 232 PPGVINILPGyGPTAGAAIASHiGIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQG 311
Cdd:cd07137 156 DTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 312 VF-FNQGQCCTAGSRIFVEESIYEEFVRrsverAKRRVVGSPF--DP-TTEQGPQIDKKQYNKILELIQSGVAEGAKLEC 387
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAPTLID-----ALKNTLEKFFgeNPkESKDLSRIVNSHHFQRLSRLLDDPSVADKIVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 388 GGkGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNdiNKALT--VSSAMQ 465
Cdd:cd07137 308 GG-ERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK--NKELKrrIVAETS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 25777724 466 AGTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 509
Cdd:cd07137 385 SGGVTFNdtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
41-501 |
2.37e-37 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 144.46 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQnSESGRVFPVYNPATGEQVCEVqEADKADIDKAVQAARLafSLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK11903 8 YVAGRWQ-AGSGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI----------GVCGQIIPWNFPl 190
Cdd:PRK11903 84 YDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 191 lmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGygptAGAAIASHIG-IDKIAFTGS 264
Cdd:PRK11903 162 ---AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 265 TEVGKLIQE--AAGRSNLkRVTLELGGKSPNIIFADAD-----LDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 337
Cdd:PRK11903 235 AETAAVLRShpAVVQRSV-RVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 338 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQsGVAEGAKLECGGKGLG------RKGFFIEPTVF-SNVTDD 410
Cdd:PRK11903 314 EALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgASDPDA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 411 MRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI--------------NKALTVSSAMQA-----GTVW 470
Cdd:PRK11903 393 ATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVAAlhtghGNVM 472
|
490 500 510
....*....|....*....|....*....|.
gi 25777724 471 incynalnAQSPFGGFKMSGNGREMGefGLR 501
Cdd:PRK11903 473 --------PQSLHGGPGRAGGGEELG--GLR 493
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
82-492 |
1.77e-36 |
|
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: 140.45 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 82 QAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyvDLQGVIKTFRYYA--GWADKIHG 159
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 160 MTIPVDGDYFTFTRHE---PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGV 235
Cdd:cd07084 81 EPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 236 INILPGYGPTaGAAIASHIGIDKIAFTGSTEVGkliqeAAGRSNLK--RVTLELGGKSPNIIFADAD-LDYAVEQAHQGV 312
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 313 FFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGspfdpTTEQGPQidkkQYNKILELIQSGVAE-GAKLECGGK 390
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPV----QTFTTLAMIAHMENLlGSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 391 GLGRK------GFFIEPTVFSNVTDDMRIAK---EEIFGPVQEILRFK-----TMDEVIERANNSdfgLVAAVFTNDInk 456
Cdd:cd07084 306 ELKNHsipsiyGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDP-- 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 25777724 457 alTVSSAMqAGTVWINCYNALNAQSPFGGFKMSGNG 492
Cdd:cd07084 381 --IFLQEL-IGNLWVAGRTYAILRGRTGVAPNQNHG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
41-501 |
2.60e-34 |
|
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: 135.48 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQnSESGRVFPVYNPATGEQVCEVQeADKADIDKAVQAARLAFslGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREKG--GPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 121 ATMESLNGGKpfLQAFYVDLQGVIKTFRYYAGWADK--------IHGMTIPVDGDYFTFTRH--EPI-GVCGQIIPWNFP 189
Cdd:cd07128 80 YALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHilTPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 190 llmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAG-FPPGVINILPGygptAGAAIASHIGI-DKIAFTG 263
Cdd:cd07128 158 ----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG----SVGDLLDHLGEqDVVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 264 STEVG-KL-----IQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFV 337
Cdd:cd07128 230 SAATAaKLrahpnIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 338 RRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN----KILELIQSG-VAEGAKLECGGKGLGR-KGFFIEPTVF-SNVTDD 410
Cdd:cd07128 310 EALKARLAKVVVGDPRLEGVRMGPLVSREQREdvraAVATLLAEAeVVFGGPDRFEVVGADAeKGAFFPPTLLlCDDPDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 411 MRIAKE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINcyNALNAQ------S 481
Cdd:cd07128 390 ATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL--NRDSAKestghgS 467
|
490 500
....*....|....*....|....*
gi 25777724 482 PF-----GGFKMSGNGREMGefGLR 501
Cdd:cd07128 468 PLpqlvhGGPGRAGGGEELG--GLR 490
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
175-510 |
9.89e-30 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 121.76 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 175 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKeAGFPPGVINILPGyGPTAGAAIASHi 254
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEG-GPAVGEQLLQH- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 255 GIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNI---IFADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEE 330
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 331 siyeEFVRRSVERAK---RRVVGSPFDPTTEQGPQIDKKQYNKILEL-----IQSGVAEGAKLEcggkglgRKGFFIEPT 402
Cdd:PLN02203 263 ----RFAPILIELLKstiKKFFGENPRESKSMARILNKKHFQRLSNLlkdprVAASIVHGGSID-------EKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 403 VFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNA 479
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiIQYACDS 411
|
330 340 350
....*....|....*....|....*....|.
gi 25777724 480 qSPFGGFKMSGNGREMGEFGLREYSEVKTVT 510
Cdd:PLN02203 412 -LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
175-509 |
4.12e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 117.07 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 175 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIkEAGFPPGVINILPGYGPTAGAAIASHi 254
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQK- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 255 gIDKIAFTGSTEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF-FNQGQCCTAGSRIFVEESiY 333
Cdd:PLN02174 189 -WDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE-Y 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 334 EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI-QSGVAEgaKLECGGKGlGRKGFFIEPTVFSNVTDDMR 412
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLdEKEVSD--KIVYGGEK-DRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 413 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNAQsPFGGFKMS 489
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHTL-PFGGVGES 421
|
330 340
....*....|....*....|
gi 25777724 490 GNGREMGEFGLREYSEVKTV 509
Cdd:PLN02174 422 GMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
77-439 |
2.42e-16 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 81.43 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 77 IDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPflQAfyvDLQGVI-KT---FRYYA- 151
Cdd:cd07129 1 VDAAAAAAAAAFE---SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP--EA---RLQGELgRTtgqLRLFAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 152 -----GWadkiHGMTI-PVDGDYFTFTR------HEPIGVCGQIIPWNFPllmFAWKI-----APALCCGNTVVIK---- 210
Cdd:cd07129 73 lvregSW----LDARIdPADPDRQPLPRpdlrrmLVPLGPVAVFGASNFP---LAFSVaggdtASALAAGCPVVVKahpa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 211 -PAeqtpLSALYMGAL---IKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGK-LIQEAAGRSNLKRVTL 285
Cdd:cd07129 146 hPG----TSELVARAIraaLRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRaLFDAAAARPEPIPFYA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 286 ELGGKSPNIIFADAdLDYAVEQAHQG----VFFNQGQCCTAGSRIFVEESiyEEFvRRSVERAKRRVVGSPFDPTTEQGp 361
Cdd:cd07129 222 ELGSVNPVFILPGA-LAERGEAIAQGfvgsLTLGAGQFCTNPGLVLVPAG--PAG-DAFIAALAEALAAAPAQTMLTPG- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 362 qidkkqynkILELIQSGVAE----GAKLECGGKGLGRKGFFIEPTVFSNVTDDMR---IAKEEIFGPVQEILRFKTMDEV 434
Cdd:cd07129 297 ---------IAEAYRQGVEAlaaaPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAEL 367
|
....*
gi 25777724 435 IERAN 439
Cdd:cd07129 368 LAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
41-455 |
2.90e-16 |
|
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: 81.39 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 41 FINNEWQNSESGRVFPvyNPATGEQVCEVQEADKADIDKAVQAARlAFSLGSVWRRMDASER----GRLLDKLADLVERD 116
Cdd:cd07126 2 LVAGKWKGASNYTTLL--DPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPLKNPERyllyGDVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 117 RA--VLATMESLNGGKPFLQAfyvdLQGVIKTFRYYAGWA-DKIHGMT--IPVDGDYFTFTRHE---PIGVCGQIIPWNF 188
Cdd:cd07126 79 EVedFFARLIQRVAPKSDAQA----LGEVVVTRKFLENFAgDQVRFLArsFNVPGDHQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 189 PLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGaAIASHIGIDKIAFTGSTEVG 268
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 269 -KLIQEAAGrsnlkRVTLELGGKSPNIIFAD-ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES-IYEEFVRRSVERAK 345
Cdd:cd07126 234 eRLALELHG-----KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 346 RR-----VVGSPFDPTTEqgpqidkkqynKILELIQSGVA-EGAKLECGGKGLGRKGF-----FIEPT-VF-----SNVT 408
Cdd:cd07126 309 QRkledlTIGPVLTWTTE-----------RILDHVDKLLAiPGAKVLFGGKPLTNHSIpsiygAYEPTaVFvpleeIAIE 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 25777724 409 DDMRIAKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDIN 455
Cdd:cd07126 378 ENFELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
78-472 |
1.82e-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: 69.17 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 78 DKAVQAARLA-FSLGSVWRRMDASERGRLLDKLAdlverdrAVLATMESLNGGKpflqafyvdLQGVIKTFRYYAGWADK 156
Cdd:cd07077 19 DLIINAIANAlYDTRQRLASEAVSERGAYIRSLI-------ANWIAMMGCSESK---------LYKNIDTERGITASVGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 157 IHGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAwKIAPALCCGNTVVIKPAEQTPLSALYMgALIKEAGFPPGVI 236
Cdd:cd07077 83 IQDVLLPDNGE--TYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 237 NILPGYGPTAGAAIA----SHIGIDKIAFTGSTEVGKLIQEAagrSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGV 312
Cdd:cd07077 159 KILVLYVPHPSDELAeellSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 313 FFNQGQCctagsriFVEESIYeefvrrsverakrrVVGSPFDPTTEQgpqidkkqynkileLIQSGVAEGAKLECGGKGL 392
Cdd:cd07077 236 FFDQNAC-------ASEQNLY--------------VVDDVLDPLYEE--------------FKLKLVVEGLKVPQETKPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 393 grkgffieptvFSNVTDDMRIAKEEIFGPVQeiLRFKTMDEVIERANNSDF------GLVAAVFTNDINKALTVSSAMQA 466
Cdd:cd07077 281 -----------SKETTPSFDDEALESMTPLE--CQFRVLDVISAVENAWMIiesgggPHTRCVYTHKINKVDDFVQYIDT 347
|
....*.
gi 25777724 467 GTVWIN 472
Cdd:cd07077 348 ASFYPN 353
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
165-472 |
2.97e-08 |
|
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: 56.12 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 165 DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP----AEQTPLSALYMGALIKEAGFPPGVINILP 240
Cdd:cd07081 84 DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWID 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 241 GYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 320
Cdd:cd07081 164 NPSIELAQRLMKFPGIGLLLATGGPAVVK-----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 321 TAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE-------QGPQIDKKQYNKILELIQSGVAEGAKLecggkglg 393
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPvilkngdVNRDIVGQDAYKIAAAAGLKVPQETRI-------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 394 rkgFFIEPTVFsnvtDDMRIAKEEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTV---SSAMQA 466
Cdd:cd07081 311 ---LIGEVTSL----AEHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENMnqfANAMKT 383
|
....*.
gi 25777724 467 GTVWIN 472
Cdd:cd07081 384 SRFVKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
175-473 |
1.20e-06 |
|
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: 50.95 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 175 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSAL-YMGALIKEAGFPPGVINILPGygPT--AGA 248
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAkIMREAAVAAGAPEGLIQWIEE--PSieLTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 249 AIASHIGIDKIAFTGSTEVGKliqeAAGRSNlkrvTLELG---GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR 325
Cdd:cd07122 172 ELMKHPDVDLILATGGPGMVK----AAYSSG----KPAIGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 326 IFVEESIYEEFVRRSVER--------AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL---ECGGKGLGr 394
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRgayflneeEKEKLEKALFDDGGTLNPDIVGKSAQKIAELAGIEVPEDTKVlvaEETGVGPE- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 395 kgffiEPtvFSNvtddmriakeEIFGPVQEILRFKTMDEVIERA----NNSDFGLVAAVFTNDINKALTVSSAMQAGTVW 470
Cdd:cd07122 323 -----EP--LSR----------EKLSPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSRIL 385
|
...
gi 25777724 471 INC 473
Cdd:cd07122 386 VNT 388
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
75-438 |
8.40e-06 |
|
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: 48.00 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 75 ADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGViktfryyagwA 154
Cdd:cd07121 4 ATVDDAVAAAKAAQK---QYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLA----------A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 155 DKIHGM----TIPVDGDY-FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP---AEQTPLSALYM-GAL 225
Cdd:cd07121 71 EKTPGTedltTTAWSGDNgLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVELiNKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 226 IKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKliqeaAGRSNLKRVTLELGGKSPNIIFADADLDYAV 305
Cdd:cd07121 151 IAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVK-----AALSSGKKAIGAGAGNPPVVVDETADIEKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 306 EQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRR------------SVERAKRRVVgspfdpTTEQGPQIDK----KQYN 369
Cdd:cd07121 226 RDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAmqrngayvlndeQAEQLLEVVL------LTNKGATPNKkwvgKDAS 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25777724 370 KILELIqsGVAEGAKLECggkglgrkgffieptVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERA 438
Cdd:cd07121 300 KILKAA--GIEVPADIRL---------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
73-328 |
9.72e-05 |
|
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: 45.16 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 73 DKADIDKAVQAARLAFSlgsVWRrmDASERGR------LLDKLADLV-ERDRAVLATmeslnGGKPFLQAF--------- 136
Cdd:cd07127 82 PQCDPDALLAAARAAMP---GWR--DAGARARagvcleILQRLNARSfEMAHAVMHT-----TGQAFMMAFqaggphaqd 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 137 ---------YVDLQGVIKTFRYyagwaDKIHGMTIPVDGDYfTFTRhEPIGV-----CGQIIPWNFPLLMFAwkiapALC 202
Cdd:cd07127 152 rgleavayaWREMSRIPPTAEW-----EKPQGKHDPLAMEK-TFTV-VPRGValvigCSTFPTWNGYPGLFA-----SLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777724 203 CGNTVVIKPAeqtPLSALYMG-------ALIKEAGFPPGVInILPGYGPTAGAA--IASHIGIDKIAFTGSTEVGKLIQE 273
Cdd:cd07127 220 TGNPVIVKPH---PAAILPLAitvqvarEVLAEAGFDPNLV-TLAADTPEEPIAqtLATRPEVRIIDFTGSNAFGDWLEA 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 25777724 274 AAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFV 328
Cdd:cd07127 296 NARQ---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV 347
|
|
| |
