|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
28-477 |
0e+00 |
|
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: 654.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 28 KTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEV 107
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVD 267
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 268 VDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAV 347
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 348 SRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAE 427
Cdd:cd07150 322 AKGAKLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
5EK6_A 428 AVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07150 402 RLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
47-477 |
0e+00 |
|
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: 602.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 47 DAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQG 126
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 127 RVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT-GWLIAQMVAKAGLPKGVFN 205
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 206 LVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQ 285
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 286 ICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNFFE 365
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPR-DPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGLFYQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 366 PAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEES 445
Cdd:cd07104 320 PTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEP 399
|
410 420 430
....*....|....*....|....*....|..
5EK6_A 446 HVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
17-475 |
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: 564.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 17 FKEPSTGAFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEG 96
Cdd:pfam00171 1 WVDSESETIEV-INPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 97 GGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDsESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVV 176
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 177 YKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGG 256
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 257 SDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQV 336
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPL-DPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 337 ALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGA 413
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGldnGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
5EK6_A 414 VLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWV 475
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-479 |
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: 556.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 8 KVANYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKED 87
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 88 FMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAH 167
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 168 TLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTL 247
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 248 KTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDL 327
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL-DPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 328 GPLINERQVALMKEFVDDAVSRGGRLLIGGRSW----GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdgegGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTVTL 479
Cdd:COG1012 404 NDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
50-477 |
9.83e-173 |
|
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: 492.88 E-value: 9.83e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 50 EAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVL 129
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 130 QSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIG 209
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 210 PGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTS 289
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 290 AKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGR----SWGNFFE 365
Cdd:cd07078 242 ASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKrlegGKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 366 PAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEES 445
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP 400
|
410 420 430
....*....|....*....|....*....|..
5EK6_A 446 HVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07078 401 SAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
15-478 |
3.10e-166 |
|
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: 477.57 E-value: 3.10e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 15 GEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTV 94
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 95 EGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNT 174
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 175 VVYKPASDTPVT-GWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLE 253
Cdd:cd07151 161 VVLKPASDTPITgGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 254 LGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDEKVdLGPLINE 333
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV-VGPLINE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 334 RQVALMKEFVDDAVSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGA 413
Cdd:cd07151 320 SQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 414 VLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTVT 478
Cdd:cd07151 400 VFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
29-468 |
1.36e-163 |
|
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: 470.38 E-value: 1.36e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07103 82 YAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07103 162 ALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMKEFVDDAVS 348
Cdd:cd07103 242 DKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNG-LDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 349 RGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRI 425
Cdd:cd07103 321 KGAKVLTGGKRLglgGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
5EK6_A 426 AEAVESGMFHINDVTFLEEsHVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07103 401 AEALEAGMVGINTGLISDA-EAPFGGVKESGLGREGGKEGLEE 442
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-468 |
4.14e-153 |
|
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: 444.40 E-value: 4.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAV 171
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 172 GNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVT 251
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 252 LELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLI 331
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDP-FDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 332 NERQVALMKEFVDDAVSRGGRLLIGGR----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTD 407
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKrpegEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
5EK6_A 408 YGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleESHVPF-GGIKASGVGREGGEWSFHE 468
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINRENF--EAMQGFhAGWKKSGLGGADGKHGLEE 459
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-463 |
1.34e-148 |
|
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: 432.83 E-value: 1.34e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGAfqVKTSPVDGSKI-AEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07097 3 NYIDGEWVAGGDGE--ENRNPSDTSDVvGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGP 329
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL-DEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 330 LINERQVALMKEFVDDAVSRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGErlkrpDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 405 DTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVG-REGGE 463
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGpREQGE 459
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
30-461 |
2.42e-148 |
|
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: 431.77 E-value: 2.42e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVF 109
Cdd:cd07145 5 NPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 110 TERLIQNAAELARHYQGRVLQSD----SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPV 185
Cdd:cd07145 85 TIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 186 TGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDD 265
Cdd:cd07145 165 TAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 266 VDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDD 345
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPL-DESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 346 AVSRGGRLLIGG-RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFR 424
Cdd:cd07145 324 AVEKGGKILYGGkRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALK 403
|
410 420 430
....*....|....*....|....*....|....*..
5EK6_A 425 IAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREG 461
Cdd:cd07145 404 VARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
30-467 |
1.42e-146 |
|
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: 426.98 E-value: 1.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRkvwgevVF 109
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPIT------LA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 110 TERLIQNAAELARHYQGRVLQSDSES------TISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDT 183
Cdd:cd07093 77 RTRDIPRAAANFRFFADYILQLDGESypqdggALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 184 PVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIIL 263
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 264 DDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFV 343
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPL-DPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 344 DDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLT 416
Cdd:cd07093 316 ELARAEGATILTGGGRPelpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
5EK6_A 417 NNVNRAFRIAEAVESGMFHINDvTFLEESHVPFGGIKASGVGREGGEWSFH 467
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNC-WLVRDLRTPFGGVKASGIGREGGDYSLE 445
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-477 |
9.51e-146 |
|
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: 424.78 E-value: 9.51e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 34 GSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFTERL 113
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 114 IQNAAELARHYQGRVLQSdSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT-GWLIAQ 192
Cdd:cd07152 81 LHEAAGLPTQPQGEILPS-APGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSgGVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 193 MVAKAGLPKGVFNLVIGpGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAA 272
Cdd:cd07152 160 LFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 273 RLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGR 352
Cdd:cd07152 239 SNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPA-TGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 353 LLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESG 432
Cdd:cd07152 318 LEAGGTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
5EK6_A 433 MFHINDVTFLEESHVPFGGIKASGVG-REGGEWSFHETTYDRWVTV 477
Cdd:cd07152 398 MLHINDQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-479 |
1.73e-141 |
|
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: 415.21 E-value: 1.73e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGAFQVKTSPVDGSK-IAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGP 329
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGL-DEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 330 LINERQVALMKEFVDDAVSRGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEV 402
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGErltgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 403 ANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVG-REGGEWSFHETTydRWVTVTL 479
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFT--EWKAVYV 475
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
29-477 |
1.49e-139 |
|
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: 409.29 E-value: 1.49e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVv 108
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 ftERLIQN---AAELARHYQGRVLQSD----SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPAS 181
Cdd:cd07149 83 --DRAIETlrlSAEEAKRLAGETIPFDaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 182 DTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAgtLKTVTLELGGSDPLI 261
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 262 ILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKE 341
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPL-DEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 342 FVDDAVSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNR 421
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 422 AFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07149 398 ALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-468 |
2.10e-138 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 407.92 E-value: 2.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 3 DLNIMKVANYINGEFKEPSTGA-FQVKtSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVF 81
Cdd:PLN02278 19 NAGLLRTQGLIGGKWTDAYDGKtFPVY-NPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 82 RQMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSIS 161
Cdd:PLN02278 98 IANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 162 MKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAA 241
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 242 KAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRk 321
Cdd:PLN02278 258 GAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGF- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 322 DEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGG---RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQ 398
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGkrhSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 399 AVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEEShVPFGGIKASGVGREGGEWSFHE 468
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV-APFGGVKQSGLGREGSKYGIDE 485
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
53-477 |
1.03e-133 |
|
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: 391.21 E-value: 1.03e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 53 DSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSD 132
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 133 SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGP 212
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 213 VVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKR 292
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 293 IIVHKAVADKFIERYVHyvkmlriddprkdekvdlgplinerqvalmkefvddavsrggrlliggrswgnffepaIFVDV 372
Cdd:cd06534 241 LLVHESIYDEFVEKLVT----------------------------------------------------------VLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 373 DRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGI 452
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGV 342
|
410 420
....*....|....*....|....*
5EK6_A 453 KASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
31-470 |
9.16e-133 |
|
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: 391.91 E-value: 9.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALK--AWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07114 164 ELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMKEFVDDAVS 348
Cdd:cd07114 244 DAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDP-LDPETQMGPLATERQLEKVERYVARARE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 349 RGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNR 421
Cdd:cd07114 323 EGARVLTGGErpsgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLAR 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
5EK6_A 422 AFRIAEAVESGMFHINDVTFLEEShVPFGGIKASGVGREGGEWSFHETT 470
Cdd:cd07114 403 AHRVARAIEAGTVWVNTYRALSPS-SPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
11-461 |
3.13e-131 |
|
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: 388.47 E-value: 3.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEpSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANI-PAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07082 4 YLINGEWKE-SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSES----TISVVFKRSKGVVGVITPWNYPLSISMKKI 165
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPgtkgKIAQVRREPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 166 AHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIaAKAAG 245
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-KKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 246 TLKTVtLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKV 325
Cdd:cd07082 242 MKRLV-LELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW-DNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 326 DLGPLINERQVALMKEFVDDAVSRGGRLLIGG-RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGgREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELAN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 405 DTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREG 461
Cdd:cd07082 400 KSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQG 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-468 |
5.90e-131 |
|
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: 388.21 E-value: 5.90e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDsESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGP 329
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNG-LDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 330 LINERQVALMKEFVDDAVSRGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEV 402
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKrptgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 403 ANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIND--VTFLEeshVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyhPYFAE---APWGGYKQSGIGRELGPTGLEE 463
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
47-477 |
1.99e-130 |
|
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: 385.01 E-value: 1.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 47 DAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTyrKVWGE--VVFTERLIQNAAELARHY 124
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT--AAWAGfnVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 125 QGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVF 204
Cdd:cd07105 79 IGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 205 NLV-IGP--GPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLF 281
Cdd:cd07105 159 NVVtHSPedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 282 HQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDprkdekVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRS-- 359
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP------VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAde 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 360 --WGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN 437
Cdd:cd07105 313 spSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
5EK6_A 438 DVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07105 393 GMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
29-477 |
3.09e-129 |
|
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: 382.94 E-value: 3.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07094 4 HNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSD----SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTP 184
Cdd:cd07094 84 RAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 185 VTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGtlKTVTLELGGSDPLIILD 264
Cdd:cd07094 164 LSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 265 DVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVD 344
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPL-DEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 345 DAVSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFR 424
Cdd:cd07094 321 EAVEAGARLLCGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
5EK6_A 425 IAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07094 401 AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-468 |
4.53e-129 |
|
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: 382.75 E-value: 4.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWA-NIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEgggtyrkvWGEVV 108
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAE--------VGAPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQ--NAAELARHYQGRVLQSDSE-----------STISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTV 175
Cdd:cd07089 75 MTARAMQvdGPIGHLRYFADLADSFPWEfdlpvpalrggPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 176 VYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELG 255
Cdd:cd07089 155 VLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 256 GSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQ 335
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 336 VALMKEFVDDAVSRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGL 410
Cdd:cd07089 314 RDRVEGYIARGRDEGARLVTGGGrpaglDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 411 SGAVLTNNVNRAFRIAEAVESGMFHINDVTFLeESHVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGY-GPDAPFGGYKQSGLGRENGIEGLEE 450
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
50-468 |
1.12e-128 |
|
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: 380.65 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 50 EAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVvfterliQNAAELARHY----- 124
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV-------EKCAWICRYYaenae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 125 ---QGRVLQSDSEStiSVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPK 201
Cdd:cd07100 76 aflADEPIETDAGK--AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 202 GVF-NLVIGPGPVvgEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASL 280
Cdd:cd07100 154 GVFqNLLIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 281 FHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGR-- 358
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPM-DEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKrp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 359 -SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN 437
Cdd:cd07100 311 dGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|.
5EK6_A 438 DVTfLEESHVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07100 391 GMV-KSDPRLPFGGVKRSGYGRELGRFGIRE 420
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-478 |
6.82e-128 |
|
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: 380.37 E-value: 6.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGAFQVKtSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07086 1 GVIGGEWVGSGGETFTSR-NPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLA 170
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 171 VGNTVVYKPASDTPVTGWLIAQMVAKA----GLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGT 246
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 LKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVD 326
Cdd:cd07086 239 FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL-DEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 327 LGPLINERQVALMKEFVDDAVSRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVE 401
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKridggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5EK6_A 402 VANDTDYGLSGAVLTNNVNRAFRIAEAVES--GMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHEttYDRWVTVT 478
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQ--YMRRSTCT 474
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-468 |
1.86e-127 |
|
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: 378.77 E-value: 1.86e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEP-STGAFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07138 1 FYIDGAWVAPaGTETIDV-INPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTyrkvwgeVVFTERL--------IQNAAELARHYqgrvlqsDSESTI--SVVFKRSKGVVGVITPWNYPLS 159
Cdd:cd07138 80 QAITLEMGAP-------ITLARAAqvglgighLRAAADALKDF-------EFEERRgnSLVVREPIGVCGLITPWNWPLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 160 ISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREI 239
Cdd:cd07138 146 QIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 240 AAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDP 319
Cdd:cd07138 226 AEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 320 RkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGG------RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVV 393
Cdd:cd07138 306 R-DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpegLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 394 ENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleESHVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAF--NPGAPFGGYKQSGNGREWGRYGLEE 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-470 |
2.43e-127 |
|
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: 378.86 E-value: 2.43e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTG-AFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDF 88
Cdd:cd07091 7 FINNEFVDSVSGkTFPT-INPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 89 MKILTVEGGGTYRKVW-GEVVFTERLIQNAAELARHYQGRVLQSDSEsTISVVFKRSKGVVGVITPWNYPLSISMKKIAH 167
Cdd:cd07091 86 AALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDGN-FLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 168 TLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGT- 246
Cdd:cd07091 165 ALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSn 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 LKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVD 326
Cdd:cd07091 245 LKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF-DPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 327 LGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGN---FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSkgyFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdvTF-LEESHVPFGGIKASGVGREGGEWSFHETT 470
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN--TYnVFDAAVPFGGFKQSGFGRELGEEGLEEYT 469
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-462 |
2.92e-126 |
|
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: 375.76 E-value: 2.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEAL--KAWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYR-KVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHT 168
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 169 LAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGpGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLK 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 249 TVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLG 328
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDP-LDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 329 PLINERQVALMKEFVDDAVSRGGRLLIGG-------RSWgnFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVE 401
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTGGgrpagldRGW--FVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5EK6_A 402 VANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdvTFLEESHVPFGGIKASGVGREGG 462
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN--GFRLDFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
31-471 |
1.35e-123 |
|
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: 368.01 E-value: 1.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVvft 110
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 111 erliQNAAELARHYQG----RVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT 186
Cdd:cd07106 81 ----GGAVAWLRYTASldlpDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 187 GWLIAQMVAKAgLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDV 266
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 267 DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMKEFVDDA 346
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDG-LDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 347 VSRGGRLLIGGR---SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAF 423
Cdd:cd07106 314 KAKGAKVLAGGEpldGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
5EK6_A 424 RIAEAVESGMFHINDVTFLeESHVPFGGIKASGVGREGGEWSFHETTY 471
Cdd:cd07106 394 AVARRLEAGTVWINTHGAL-DPDAPFGGHKQSGIGVEFGIEGLKEYTQ 440
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
29-477 |
1.67e-120 |
|
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: 360.38 E-value: 1.67e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELArhyqGRVLQSDSESTISVV-FKRSK------GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPAS 181
Cdd:cd07099 81 LALEAIDWAARNA----PRVLAPRKVPTGLLMpNKKATveyrpyGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 182 DTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHkRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLI 261
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 262 ILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDeKVDLGPLINERQVALMKE 341
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIG-DADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 342 FVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNN 418
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSnggGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 419 VNRAFRIAEAVESGMFHINDV-TFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
31-464 |
3.36e-120 |
|
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: 359.74 E-value: 3.36e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI-LTVEGGGTYRKVW--GEV 107
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELeARDNGKPLDEAAWdvDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07110 84 AGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVD 267
Cdd:cd07110 164 LELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 268 VDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAV 347
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPL-EEGVRLGPLVSQAQYEKVLSFIARGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 348 SRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRA 422
Cdd:cd07110 323 EEGARLLCGGRrpahlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERC 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
5EK6_A 423 FRIAEAVESGMFHIN--DVTFleeSHVPFGGIKASGVGREGGEW 464
Cdd:cd07110 403 DRVAEALEAGIVWINcsQPCF---PQAPWGGYKRSGIGRELGEW 443
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-460 |
4.82e-119 |
|
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: 357.81 E-value: 4.82e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRkvwgevvftERL---IQNAAELARHYQGRVL-QSDS-----ESTISVVFKRSKGVVGVITPWNYPLSIS 161
Cdd:cd07559 83 AETLDNGKPIR---------ETLaadIPLAIDHFRYFAGVIRaQEGSlseidEDTLSYHFHEPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 162 MKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAA 241
Cdd:cd07559 154 AWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 242 KAAGTLKTVTLELGGSDPLIILDDV-----DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRI 316
Cdd:cd07559 233 YAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 317 DDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRP 389
Cdd:cd07559 313 GNPL-DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5EK6_A 390 IVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEEsHVPFGGIKASGVGRE 460
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPA-HAPFGGYKKSGIGRE 461
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
12-463 |
7.07e-119 |
|
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: 357.49 E-value: 7.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKA-WANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYR-KVWGEVVFTERLIQNAAELARHYQGRVLQSDSEStISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07144 91 IEALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNK-LAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDEKVDLGP 329
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 330 LINERQVALMKEFVDDAVSRGGRLLIGGRSW------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKApeglgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKA 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDvTFLEESHVPFGGIKASGVGREGGE 463
Cdd:cd07144 410 NDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINS-SNDSDVGVPFGGFKMSGIGRELGE 468
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-470 |
2.64e-118 |
|
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: 355.11 E-value: 2.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEV 107
Cdd:cd07118 3 SPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVD 267
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 268 VDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAV 347
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPL-DPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 348 SRGGRLLIGG----RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAF 423
Cdd:cd07118 322 AEGATLLLGGerlaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
5EK6_A 424 RIAEAVESGMFHINdvTFLEES-HVPFGGIKASGVGREGGEWSFHETT 470
Cdd:cd07118 402 TVARRIRAGTVWVN--TFLDGSpELPFGGFKQSGIGRELGRYGVEEYT 447
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
30-479 |
1.05e-117 |
|
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: 353.28 E-value: 1.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWG-EVV 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSDSeSTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVS 348
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL-DPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 349 RGGRLLIGGRS---WGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRI 425
Cdd:cd07115 321 EGARLLTGGKRpgaRGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
5EK6_A 426 AEAVESGMFHINDVTFLeESHVPFGGIKASGVGREGGEWSFHETTYDRWVTVTL 479
Cdd:cd07115 401 AAALKAGTVWINTYNRF-DPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
31-462 |
1.06e-117 |
|
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: 353.53 E-value: 1.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFT 110
Cdd:cd07090 4 PATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 111 ERLIQNAAELARHYQGRVLQSDSEStisVVFKRSK--GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07090 84 ADCLEYYAGLAPTLSGEHVPLPGGS---FAYTRREplGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAVS 348
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPL-DEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 349 RGGRLLIGGRSW--------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVN 420
Cdd:cd07090 319 EGAKVLCGGERVvpedglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
5EK6_A 421 RAFRIAEAVESGMFHINDVTfLEESHVPFGGIKASGVGREGG 462
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTYN-ISPVEVPFGGYKQSGFGRENG 439
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
12-462 |
8.98e-116 |
|
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: 349.11 E-value: 8.98e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRK-VWGEVVFTERLIQNAAELARHYQGRVLQSdSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLA 170
Cdd:TIGR01804 81 ETLDTGKTLQEtIVADMDSGADVFEFFAGLAPALNGEIIPL-GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 171 VGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTV 250
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 251 TLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPL 330
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPF-DEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 331 INERQVALMKEFVDDAVSRGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGrpenvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIND--VTFLEeshVPFGGIKASGVGREGG 462
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAE---APFGGYKQSGIGRENG 456
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
30-477 |
5.41e-114 |
|
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: 343.93 E-value: 5.41e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVW-GEVV 108
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07092 83 GAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQMVAKaGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07092 163 LLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDAvS 348
Cdd:cd07092 242 DAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPD-DEDTEMGPLNSAAQRERVAGFVERA-P 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 349 RGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRI 425
Cdd:cd07092 320 AHARVLTGGRRAegpGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
5EK6_A 426 AEAVESGMFHINDvTFLEESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07092 400 SARLDFGTVWVNT-HIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
31-471 |
9.18e-114 |
|
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: 343.19 E-value: 9.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAfeaLKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFT 110
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALA---ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 111 ERLIQNAAELARHYQGRVLQSDSEST----ISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT 186
Cdd:cd07146 83 ADVLRFAAAEALRDDGESFSCDLTANgkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 187 GWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGtlKTVTLELGGSDPLIILDDV 266
Cdd:cd07146 163 AIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY--KRQLLELGGNDPLIVMDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 267 DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDA 346
Cdd:cd07146 241 DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPM-DPATDMGTVIDEEAAIQIENRVEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 347 VSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIA 426
Cdd:cd07146 320 IAQGARVLLGNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
5EK6_A 427 EAVESGMFHINDVTFLEESHVPFGGIKASG-VGREGGEWSFHETTY 471
Cdd:cd07146 400 ERLDVGTVNVNEVPGFRSELSPFGGVKDSGlGGKEGVREAMKEMTN 445
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-463 |
1.01e-113 |
|
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: 343.14 E-value: 1.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 fterliqNAAELARHY---QGRVLQSDSES------TISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKP 179
Cdd:cd07101 81 -------DVAIVARYYarrAERLLKPRRRRgaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 180 ASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHkrVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDP 259
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 260 LIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIdDPRKDEKVDLGPLINERQVALM 339
Cdd:cd07101 232 MIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRL-GAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 340 KEFVDDAVSRGGRLLIGGRSWGN----FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVL 415
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDlgpyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
5EK6_A 416 TNNVNRAFRIAEAVESGMFHIND--VTFLEESHVPFGGIKASGVGREGGE 463
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGLGRRHGA 440
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
3-464 |
4.60e-113 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 342.66 E-value: 4.60e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 3 DLNIMKVANYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFR 82
Cdd:PRK11241 5 DSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 83 QMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISM 162
Cdd:PRK11241 85 EHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 163 KKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAK 242
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 243 AAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkD 322
Cdd:PRK11241 245 CAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL-E 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 323 EKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQA 399
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHelgGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADV 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 400 VEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdvTFLEESHV-PFGGIKASGVGREGGEW 464
Cdd:PRK11241 404 IAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN--TGIISNEVaPFGGIKASGLGREGSKY 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
31-462 |
5.68e-113 |
|
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: 341.14 E-value: 5.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALKAWA-NIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVF 109
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 110 TERLIQNAAELARHYQGRVLQSDSESTISVVfKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWL 189
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLGPGYFVYTV-REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 190 IAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVD 269
Cdd:cd07109 163 LAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 270 YAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRI----DDPrkdekvDLGPLINERQVALMKEFVDD 345
Cdd:cd07109 243 AALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVgpglEDP------DLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 346 AVSRGGRLLIGGR------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNV 419
Cdd:cd07109 317 ARARGARIVAGGRiaegapAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
5EK6_A 420 NRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGG 462
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKG 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
29-463 |
2.87e-112 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 341.86 E-value: 2.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:PRK09407 37 TAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTerliqnaAELARHY---QGRVLQSDSES------TISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKP 179
Cdd:PRK09407 117 DV-------ALTARYYarrAPKLLAPRRRAgalpvlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 180 ASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHkrVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDP 259
Cdd:PRK09407 190 DSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 260 LIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIdDPRKDEKVDLGPLINERQVALM 339
Cdd:PRK09407 268 MIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRL-GAGYDYSADMGSLISEAQLETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 340 KEFVDDAVSRGGRLLIGGRSWGN----FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVL 415
Cdd:PRK09407 347 SAHVDDAVAKGATVLAGGKARPDlgplFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVW 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
5EK6_A 416 TNNVNRAFRIAEAVESGMFHIND---VTFleESH-VPFGGIKASGVGREGGE 463
Cdd:PRK09407 427 TGDTARGRAIAARIRAGTVNVNEgyaAAW--GSVdAPMGGMKDSGLGRRHGA 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
29-473 |
9.19e-112 |
|
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: 338.07 E-value: 9.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVv 108
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 ftERLI---QNAAELARHYQGRVLQSD----SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPAS 181
Cdd:cd07147 83 --ARAIdtfRIAAEEATRIYGEVLPLDisarGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 182 DTPVTGWLIAQMVAKAGLPKGVFNLVigPGPVVGEEI-VTHKRVAHVTFTGESSTGREIAAKAAGtlKTVTLELGGSDPL 260
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVL--PCSRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 261 IILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMK 340
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDP-KDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 341 EFVDDAVSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVN 420
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
5EK6_A 421 RAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDR 473
Cdd:cd07147 396 KALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-464 |
9.87e-112 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 339.79 E-value: 9.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEAL-----KAWANIPAIRRAEYLYKMLEVFRQMKE 86
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 87 DFMKILTVEGGGTYRK-VWGevvfterlIQNAAELARHYQGRV--LQSDSESTISV--------VFKRSKGVVGVITPWN 155
Cdd:PLN02467 91 ELAKLETLDCGKPLDEaAWD--------MDDVAGCFEYYADLAeaLDAKQKAPVSLpmetfkgyVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 156 YPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESST 235
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 236 GREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLR 315
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 316 IDDPRkDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPI 390
Cdd:PLN02467 323 ISDPL-EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpehlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 391 VVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN--DVTFLEeshVPFGGIKASGVGREGGEW 464
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcsQPCFCQ---APWGGIKRSGFGRELGEW 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
30-458 |
1.03e-111 |
|
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: 338.07 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEV-V 108
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIrG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTER---LIQNAAE-LARHyqgRVLQSDS-ESTISvvfKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDT 183
Cdd:cd07102 82 MLERaryMISIAEEaLADI---RVPEKDGfERYIR---REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 184 PVTGWLIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIIL 263
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 264 DDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMKEFV 343
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDP-LDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 344 DDAVSRGGRLLIGGRSW------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTN 417
Cdd:cd07102 314 ADAIAKGARALIDGALFpedkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
5EK6_A 418 NVNRAFRIAEAVESGMFHINDVTFLEEShVPFGGIKASGVG 458
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPA-LAWTGVKDSGRG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-460 |
1.22e-111 |
|
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: 337.80 E-value: 1.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYR-KVWGEV 107
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSDsESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIAQMVAKAgLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVD 267
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 268 VDYAARLAVFASLFH-QGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVDDA 346
Cdd:cd07108 240 LDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPL-DEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 347 VSR-GGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNN 418
Cdd:cd07108 319 LSTsGATVLRGGPlpgegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
5EK6_A 419 VNRAFRIAEAVESGMFHINDvTFLEESHVPFGGIKASGVGRE 460
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQ-GGGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-462 |
2.69e-111 |
|
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: 338.81 E-value: 2.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGefKEPSTGAFQVKTSPVDGSKI-AEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07124 36 VIGG--KEVRTEEKIESRNPADPSEVlGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQsDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLA 170
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE-MVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 171 VGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGT---- 246
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVqpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 --LKTVTLELGGSDPLIILDDVDVDYAArLAVFASLF-HQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDE 323
Cdd:cd07124 273 kwLKRVIAEMGGKNAIIVDEDADLDEAA-EGIVRSAFgFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE-DP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 324 KVDLGPLINERQVALMKEFVDDAVsRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQ 398
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEvlelaAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 399 AVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN-DVT-FLEESHvPFGGIKASGVGREGG 462
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrKITgALVGRQ-PFGGFKMSGTGSKAG 494
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
11-462 |
4.68e-111 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 337.62 E-value: 4.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGA-FQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:PRK13252 9 LYIDGAYVEATSGEtFEV-INPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGgtyrKVWGE-----VVFTERLIQNAAELARHYQGRVLQSDSEStisVVFKRSK--GVVGVITPWNYPLSISM 162
Cdd:PRK13252 88 ALETLDTG----KPIQEtsvvdIVTGADVLEYYAGLAPALEGEQIPLRGGS---FVYTRREplGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 163 KKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAK 242
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 243 AAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkD 322
Cdd:PRK13252 240 AAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPM-D 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 323 EKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVEN 395
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 396 DDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdvTF-LEESHVPFGGIKASGVGREGG 462
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWgESPAEMPVGGYKQSGIGRENG 464
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-470 |
1.04e-109 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 333.41 E-value: 1.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 7 MKVANYINGEFkEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKE 86
Cdd:PRK13473 1 MQTKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 87 DFMKILTVEGGGTYRKVWG-EVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKI 165
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 166 AHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAG 245
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 246 TLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKV 325
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPD-DEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 326 DLGPLINERQVALMKEFVDDAVSRG-GRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVE 401
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPdgkGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5EK6_A 402 VANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDvTFLEESHVPFGGIKASGVGREGGEWSFHETT 470
Cdd:PRK13473 398 WANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT-HFMLVSEMPHGGQKQSGYGKDMSLYGLEDYT 465
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
30-462 |
1.70e-109 |
|
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: 332.39 E-value: 1.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALK--AWANIPAiRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEV 107
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSdSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEP-EPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIAQMVAKA-GLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDV 266
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 267 DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIdDPRKDEKVDLGPLINERQVALMKEFVDDA 346
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKV-GPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 347 VSRGGRLLI------GGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVN 420
Cdd:cd07120 320 IAAGAEVVLrggpvtEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
5EK6_A 421 RAFRIAEAVESGMFHIND-VTFLEESHvpFGGIKASGVGREGG 462
Cdd:cd07120 400 RAMRVARAIRAGTVWINDwNKLFAEAE--EGGYRQSGLGRLHG 440
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-460 |
2.67e-109 |
|
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: 332.03 E-value: 2.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 FTERLIQNAAELARHYQGRVLQSDSEStISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGW 188
Cdd:cd07107 82 VAAALLDYFAGLVTELKGETIPVGGRN-LHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 189 LIAQmVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDV 268
Cdd:cd07107 161 RLAE-LAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 269 DYAARLAVFASLFH-QGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALMKEFVDDAV 347
Cdd:cd07107 240 EAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDP-TDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 348 SRGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVN 420
Cdd:cd07107 319 REGARLVTGGGrpegpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
5EK6_A 421 RAFRIAEAVESGMFHINDVTfleeSH---VPFGGIKASGVGRE 460
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSS----RHflgAPFGGVKNSGIGRE 437
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-477 |
7.11e-108 |
|
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: 328.92 E-value: 7.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTG-AFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALK---AWANIPAIRRAEYLYKMLEVfrqMKED 87
Cdd:cd07141 10 FINNEWHDSVSGkTFPT-INPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADL---IERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 88 FMKILTVE---GGGTYRKVW-GEVVFTERLIQNAAELARHYQGRVLQSDSEStisVVFKRSK--GVVGVITPWNYPLSIS 161
Cdd:cd07141 86 RAYLASLEtldNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIPMDGDF---FTYTRHEpvGVCGQIIPWNFPLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 162 MKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIA- 240
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 241 AKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPR 320
Cdd:cd07141 243 AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 321 kDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGN---FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD 397
Cdd:cd07141 323 -DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 398 QAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN--DVTFleeSHVPFGGIKASGVGREGGEWSFHETTYDRWV 475
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNcyNVVS---PQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
..
5EK6_A 476 TV 477
Cdd:cd07141 479 TI 480
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
74-468 |
1.08e-107 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 326.31 E-value: 1.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 74 LYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITP 153
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 154 WNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGES 233
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 234 STGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKM 313
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 314 LRIDDPRKDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPI 390
Cdd:PRK10090 241 VQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVegkGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5EK6_A 391 VVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleESHVPF-GGIKASGVGREGGEWSFHE 468
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENF--EAMQGFhAGWRKSGIGGADGKHGLHE 397
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
30-470 |
1.94e-107 |
|
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: 327.25 E-value: 1.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRK-VWGE 106
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDaLAVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 107 VVFTERLIQNAAELARHYQGRVLQSDSESTiSVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT 186
Cdd:cd07112 88 VPSAANTFRWYAEAIDKVYGEVAPTGPDAL-ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 187 GWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGT-LKTVTLELGGSDPLIILDD 265
Cdd:cd07112 167 ALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPNIVFAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 266 V-DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVD 344
Cdd:cd07112 247 ApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 345 DAVSRGGRLLIGGR-----SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNV 419
Cdd:cd07112 326 SGKAEGARLVAGGKrvlteTGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 420 NRAFRIAEAVESGMFHIN-----DVTfleeshVPFGGIKASGVGREGGEWSFHETT 470
Cdd:cd07112 406 SRAHRVARRLRAGTVWVNcfdegDIT------TPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-460 |
1.03e-106 |
|
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: 325.95 E-value: 1.03e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVWG-EVVFTERLIQNAAELARHYQGRVLQSDsESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLA 170
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMID-EDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 171 VGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTV 250
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 251 TLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPL 330
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPL-DPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 331 INERQVALMKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLtengldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEEsHVPFGGIKASGVGRE 460
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPA-GAPFGGYKKSGIGRE 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-479 |
6.84e-104 |
|
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: 318.70 E-value: 6.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEF-KEPSTGAFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALK-AWA-NIPAIRRAEYLYKMLEVFRQMKEDF 88
Cdd:cd07143 10 FINGEFvDSVHGGTVKV-YNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGlKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 89 MKILTVEGGGTYRKVWGEVVfterliQNAAELARHY-------QGRVLQSDSEsTISVVFKRSKGVVGVITPWNYPLSIS 161
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDV------QASADTFRYYggwadkiHGQVIETDIK-KLTYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 162 MKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAA 241
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 242 KAAGT-LKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPR 320
Cdd:cd07143 242 AAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 321 kDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGN---FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD 397
Cdd:cd07143 322 -AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNegyFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 398 QAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLeESHVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLL-HHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
..
5EK6_A 478 TL 479
Cdd:cd07143 480 NL 481
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-477 |
2.51e-102 |
|
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: 314.76 E-value: 2.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 10 ANYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALK-AWANIPAIRRAEYLYKMLEVFRQMKEDF 88
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 89 MKILTVEGG---GTYRKVwgEVVFTERLIQNAAELARHYQGRVLQSD-----SESTISVVFKRSKGVVGVITPWNYPLSI 160
Cdd:cd07113 81 AQLETLCSGksiHLSRAF--EVGQSANFLRYFAGWATKINGETLAPSipsmqGERYTAFTRREPVGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 161 SMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIA 240
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 241 AKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPR 320
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 321 kDEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD 397
Cdd:cd07113 318 -DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALageGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 398 QAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEEShVPFGGIKASGVGREGGEWSFHETTYDRWVTV 477
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPA-VPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-465 |
1.33e-99 |
|
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: 307.50 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALK--AWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYRKV-WGEVVFTERLIQNAAELARHYQGRVLQSDSeSTISVVFKRSKGVVGVITPWNYPLSISMKKIAHT 168
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADG-PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 169 LAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGT-L 247
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 248 KTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKdEKVDL 327
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR-KGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 328 GPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGN---FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSkgyYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRAN 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5EK6_A 405 DTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdVTFLEESHVPFGGIKASGVGREGGEWS 465
Cdd:cd07142 405 NSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN-CYDVFDASIPFGGYKMSGIGREKGIYA 464
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-468 |
1.92e-99 |
|
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: 307.40 E-value: 1.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVwgevvfTERLIQNAAELARHYQGRVLQSDSEstisvvFKRSK--GVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07111 105 ESLDNGKPIRES------RDCDIPLVARHFYHHAGWAQLLDTE------LAGWKpvGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGP 329
Cdd:cd07111 252 LSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL-DKAIDMGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 330 LINERQVALMKEFVDDAVSRGGRLLIGG---RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDT 406
Cdd:cd07111 331 IVDPAQLKRIRELVEEGRAEGADVFQPGadlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
5EK6_A 407 DYGLSGAVLTNNVNRAFRIAEAVESGMFHINdVTFLEESHVPFGGIKASGVGREGGEWSFHE 468
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWIN-GHNLFDAAAGFGGYRESGFGREGGKEGLYE 471
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-477 |
1.10e-97 |
|
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: 302.88 E-value: 1.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTY----RKVWGEVVFTERLIqnaAELARHYQGRVL---QSDSESTISVVFKRSKGVVGVITPWNYPLSISM 162
Cdd:cd07140 89 TIESLDSGAVYtlalKTHVGMSIQTFRYF---AGWCDKIQGKTIpinQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 163 KKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAK 242
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 243 AA-GTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRk 321
Cdd:cd07140 246 CAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 322 DEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD- 397
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVdrpGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDv 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 398 -QAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN-----DVTfleeshVPFGGIKASGVGREGGEWSFHETTY 471
Cdd:cd07140 405 dGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynktDVA------APFGGFKQSGFGKDLGEEALNEYLK 478
|
....*.
5EK6_A 472 DRWVTV 477
Cdd:cd07140 479 TKTVTI 484
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
12-456 |
1.03e-92 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 291.07 E-value: 1.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEpsTGAFQVKTSPVDGSK-IAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:PRK03137 40 IIGGERIT--TEDKIVSINPANKSEvVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGgtyrKVWGEVV--------FTERLIQNAAELArhyQGR-VLQSDSESTISvvFKRSKGVVGVITPWNYPLSIS 161
Cdd:PRK03137 118 WLVKEAG----KPWAEADadtaeaidFLEYYARQMLKLA---DGKpVESRPGEHNRY--FYIPLGVGVVISPWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 162 MKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAA 241
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 242 KAAGT------LKTVTLELGGSDPLIILDDVDVDYAARlAVFASLF-HQGQICTSAKRIIVHKAVADKFIERYVHYVKML 314
Cdd:PRK03137 269 RAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAE-SIVASAFgFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 315 RIDDPrkDEKVDLGPLINERQVALMKEFVDDAvSRGGRLLIGGR---SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIV 391
Cdd:PRK03137 348 TVGNP--EDNAYMGPVINQASFDKIMSYIEIG-KEEGRLVLGGEgddSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFI 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5EK6_A 392 VVENDDQAVEVANDTDYGLSGAVLTNnvNRAfRIAEAVESgmFHINDVTF-------LEESHvPFGGIKASG 456
Cdd:PRK03137 425 KAKDFDHALEIANNTEYGLTGAVISN--NRE-HLEKARRE--FHVGNLYFnrgctgaIVGYH-PFGGFNMSG 490
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
12-462 |
1.62e-92 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 290.18 E-value: 1.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALK--AWANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYrkVWGEVVFterlIQNAAELARHY-------QGRVLQSdSESTISVVFKRSKGVVGVITPWNYPLSISM 162
Cdd:PLN02766 104 ALDTIDAGKLF--ALGKAVD----IPAAAGLLRYYagaadkiHGETLKM-SRQLQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 163 KKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREI-AA 241
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKImQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 242 KAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRk 321
Cdd:PLN02766 257 AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 322 DEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGN---FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQ 398
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDkgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
5EK6_A 399 AVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdVTFLEESHVPFGGIKASGVGREGG 462
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN-CYFAFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-461 |
9.70e-92 |
|
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: 287.43 E-value: 9.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07116 3 NFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRKVWG-EVVFTERLIQNAAELARHYQGRVLQSDsESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEID-ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKT 249
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTLELGGSDPLIILDDV---DVDYAAR----LAVFAslFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkD 322
Cdd:cd07116 241 VTLELGGKSPNIFFADVmdaDDAFFDKalegFVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL-D 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 323 EKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDvDRNFRIMREEVFGPVRPIVVVEN 395
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNelggllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 396 DDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdVTFLEESHVPFGGIKASGVGREG 461
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN-CYHLYPAHAAFGGYKQSGIGREN 461
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
31-463 |
7.50e-90 |
|
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: 282.27 E-value: 7.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 31 PVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGT-YRKVWGEVVF 109
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEILV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 110 TERLIQnaaELARHYQgRVLQSDSEST-ISVVFKRSK------GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASD 182
Cdd:cd07098 83 TCEKIR---WTLKHGE-KALRPESRPGgLLMFYKRARveyeplGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 183 TPVTGWLIAQMVAKA----GLPKGVFNLVIGPGPVvGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSD 258
Cdd:cd07098 159 VAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 259 PLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVAL 338
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPP-LDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 339 MKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLS 411
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYphpeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
5EK6_A 412 GAVLTNNVNRAFRIAEAVESGMFHIND--VTFLEEShVPFGGIKASGVGREGGE 463
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDfgVNYYVQQ-LPFGGVKGSGFGRFAGE 449
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-467 |
1.93e-88 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 280.54 E-value: 1.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 13 INGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALK--AWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:PLN02466 62 INGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRKVWG-EVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKrSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:PLN02466 142 LETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHE-PIGVAGQIIPWNFPLLMFAWKVGPAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGR---EIAAKAagT 246
Cdd:PLN02466 221 ACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKivlELAAKS--N 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 LKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKdEKVD 326
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFK-KGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 327 LGPLINERQVALMKEFVDDAVSRGGRLLIGGR---SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGDrfgSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN--DVTfleESHVPFGGIKASGVGREGGEWSFH 467
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVF---DAAIPFGGYKMSGIGREKGIYSLN 520
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
30-478 |
1.36e-85 |
|
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: 271.39 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 30 SPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVvf 109
Cdd:cd07130 18 SPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 110 tERLI---QNAAELARHYQGRVLQSDsestisvvfkRSK----------GVVGVITPWNYPLSISMKKIAHTLAVGNTVV 176
Cdd:cd07130 96 -QEMIdicDFAVGLSRQLYGLTIPSE----------RPGhrmmeqwnplGVVGVITAFNFPVAVWGWNAAIALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 177 YKPASDTPVTGW----LIAQMVAKAGLPKGVFNLVIGPGPvVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTL 252
Cdd:cd07130 165 WKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 253 ELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLIN 332
Cdd:cd07130 244 ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL-DDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 333 ERQVALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIfVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYG 409
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVLFGGKVIdgpGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5EK6_A 410 LSGAVLTNNVNRAFRIAEAVES--GMFHINDVTFLEESHVPFGGIKASGVGREGGE--WSfhetTYDRWVTVT 478
Cdd:cd07130 402 LSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSdaWK----QYMRRSTCT 470
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
9-458 |
7.63e-85 |
|
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: 269.39 E-value: 7.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 9 VANYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDF 88
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 89 MKILTVEGGGTYRKVWGEVvftERLIQN---AAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKI 165
Cdd:cd07085 81 ARLITLEHGKTLADARGDV---LRGLEVvefACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 166 AHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVgEEIVTHKRVAHVTFTGESSTGREIAAKAAG 245
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 246 TLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIdDPRKDEKV 325
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKV-GAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 326 DLGPLINERQVALMKEFVDDAVSRGGRLLIGGR-------SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQ 398
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRgvkvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5EK6_A 399 AVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINdvtfleeshVP---------FGGIKASGVG 458
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---------VPipvplaffsFGGWKGSFFG 455
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
29-460 |
1.72e-84 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 268.14 E-value: 1.72e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVV 108
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 109 fterliqNAAELARHY--QGRVLQSDSESTISVV-----FKRSK--GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKP 179
Cdd:PRK09406 86 -------KCAKGFRYYaeHAEALLADEPADAAAVgasraYVRYQplGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 180 ASDTPVTGWLIAQMVAKAGLPKGVF-NLVIGPGPVvgEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSD 258
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 259 PLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVAL 338
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDP-TDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 339 MKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVL 415
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGKRPdgpGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
5EK6_A 416 TNNVNRAFRIAEAVESGMFHINDVTfleESH--VPFGGIKASGVGRE 460
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMT---VSYpeLPFGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
20-468 |
2.89e-83 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 264.80 E-value: 2.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 20 PSTGAFQVktSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGT 99
Cdd:PRK13968 5 PATHAISV--NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 100 YRKVWGEVVFTERLIQNAAElarhYQGRVLQSDS---ESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVV 176
Cdd:PRK13968 83 INQARAEVAKSANLCDWYAE----HGPAMLKAEPtlvENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 177 YKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVgEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGG 256
Cdd:PRK13968 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 257 SDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQV 336
Cdd:PRK13968 238 SDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPR-DEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 337 ALMKEFVDDAVSRGGRLLIGGRSW---GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGA 413
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIagaGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 414 VLTNNVNRAFRIAEAVESGMFHINDVTfLEESHVPFGGIKASGVGREGGEWSFHE 468
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYC-ASDARVAFGGVKKSGFGRELSHFGLHE 450
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
12-461 |
1.55e-78 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 253.52 E-value: 1.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVWGEVVFTERLIQNAAELARHY--QGRVLQSDS-----ESTISVVFKRSKGVVGVITPWNYPLSISMKK 164
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRIlgEGKFLVSDSfpgneRNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 165 IAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGeSSTGREIAAKAA 244
Cdd:PLN00412 179 IAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTG-GDTGIAISKKAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 245 gtLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDek 324
Cdd:PLN00412 258 --MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 325 VDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:PLN00412 334 CDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 405 DTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREG 461
Cdd:PLN00412 414 ASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQG 470
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
29-473 |
7.34e-76 |
|
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: 245.41 E-value: 7.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 29 TSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWAN-IPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKvwgEV 107
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVD---AK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLI---QNAAELARHYQGRVLQSD----SESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPA 180
Cdd:cd07148 81 VEVTRAIdgvELAADELGQLGGREIPMGltpaSAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 181 SDTPVTGWLIAQMVAKAGLPKGVFNLVIgPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAK-AAGTlkTVTLELGGSDP 259
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKlAPGT--RCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 260 LIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPrKDEKVDLGPLINERQVALM 339
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDP-TDPDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 340 KEFVDDAVSRGGRLLIGGRSWGN-FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNN 418
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRLSDtTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 419 VNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHETTYDR 473
Cdd:cd07148 397 LDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEK 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
50-462 |
3.16e-74 |
|
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: 240.64 E-value: 3.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 50 EAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGgtyRKVW---GEVvftERLIQNAAELARHYQG 126
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETG---KPLWeaqTEV---AAMAGKIDISIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 127 RV--LQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVF 204
Cdd:cd07095 78 RTgeRATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 205 NLVIGpGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAG-TLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQ 283
Cdd:cd07095 158 NLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGrPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 284 GQICTSAKRIIVH-KAVADKFIERYVHYVKMLRIDDPRKDEKVdLGPLINERQVALMKEFVDDAVSRGGRLLIGGR---S 359
Cdd:cd07095 237 GQRCTCARRLIVPdGAVGDAFLERLVEAAKRLRIGAPDAEPPF-MGPLIIAAAAARYLLAQQDLLALGGEPLLAMErlvA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 360 WGNFFEPAIfVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNN---VNRAFRIAEAvesGMFHI 436
Cdd:cd07095 316 GTAFLSPGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDealFERFLARIRA---GIVNW 391
|
410 420
....*....|....*....|....*.
5EK6_A 437 NDVTFLEESHVPFGGIKASGVGREGG 462
Cdd:cd07095 392 NRPTTGASSTAPFGGVGLSGNHRPSA 417
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
12-460 |
7.60e-73 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 238.64 E-value: 7.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKA--WANIPAIRRAEYLYKMLEVFRQMKEDFM 89
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 90 KILTVEGGGTYR-KVWGEVVFTERLIQNAAELARHYQGRVLQSDSEStISVVFKRSKGVVGVITPWNYPLSISMKKIAHT 168
Cdd:PRK09847 103 LLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHE-LAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 169 LAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIaAKAAG--T 246
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL-LKDAGdsN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 LKTVTLELGGSDPLIILDDV-DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKV 325
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 326 DLGPLINERQVALMKEFVDDAVSRgGRLLIGGR--SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESK-GQLLLDGRnaGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
5EK6_A 404 NDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN-----DVTfleeshVPFGGIKASGVGRE 460
Cdd:PRK09847 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNnyndgDMT------VPFGGYKQSGNGRD 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
12-484 |
1.94e-71 |
|
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: 235.17 E-value: 1.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEfkEPSTGAFQVKTSPVD-GSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07083 22 VIGGE--WVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGR-VLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTL 169
Cdd:cd07083 100 TLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAA----- 244
Cdd:cd07083 180 AVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArlapg 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 245 -GTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDe 323
Cdd:cd07083 260 qTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 324 KVDLGPLINERQVALMKEFVDDAVSRgGRLLIGGR---SWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD--Q 398
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKrleGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 399 AVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIND-VTFLEESHVPFGGIKASGVGREGGewSFHETTydRWVTV 477
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRkITGALVGVQPFGGFKLSGTNAKTG--GPHYLR--RFLEM 493
|
....*..
5EK6_A 478 TLRTRRF 484
Cdd:cd07083 494 KAVAERF 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-462 |
3.95e-71 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 234.78 E-value: 3.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 13 INGEFKEpsTGAFQVKTSPVDGSK-IAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:cd07125 37 INGEETE--TGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVWGEVvfterliQNAAELARHY--QGRVLQSDSESTISV-----VFKRSKGVVGVITPWNYPLSISMKK 164
Cdd:cd07125 115 AAAEAGKTLADADAEV-------REAIDFCRYYaaQARELFSDPELPGPTgelngLELHGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 165 IAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIA-AKA 243
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINrALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 244 AGTLKTVTL--ELGGSDPLIILDDVDVDYAARlAVFASLF-HQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPR 320
Cdd:cd07125 268 ERDGPILPLiaETGGKNAMIVDSTALPEQAVK-DVVQSAFgSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 321 kDEKVDLGPLINERQVALMKEFVDdavsrggrlLIGGRSW-----------GNFFEPAIFVDVdrNFRIMREEVFGPVRP 389
Cdd:cd07125 347 -DLSTDVGPLIDKPAGKLLRAHTE---------LMRGEAWliapaplddgnGYFVAPGIIEIV--GIFDLTTEVFGPILH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 390 IVVVEND--DQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTfleeshV-------PFGGIKASGVGRE 460
Cdd:cd07125 415 VIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI------TgaivgrqPFGGWGLSGTGPK 488
|
..
5EK6_A 461 GG 462
Cdd:cd07125 489 AG 490
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
53-475 |
4.77e-68 |
|
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: 224.41 E-value: 4.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 53 DSAFEALKA----WANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEgggtYRKVWGEVVFTERL--IQNAAELARHYQG 126
Cdd:cd07134 1 RRVFAAQQAhalaLRASTAAERIAKLKRLKKAILARREEIIAALAAD----FRKPAAEVDLTEILpvLSEINHAIKHLKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 127 -----RVLQSDS-ESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLP 200
Cdd:cd07134 77 wmkpkRVRTPLLlFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 201 KGVFnLVIGpGPVVGEEIVThKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASL 280
Cdd:cd07134 157 DEVA-VFEG-DAEVAQALLE-LPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 281 FHQGQICTSAKRIIVHKAVADKFIERYVHYV-KMLRIDDPRKDEKvDLGPLINERQVALMKEFVDDAVSRGGRLLIGG-- 357
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIeKFYGKDAARKASP-DLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGqf 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 358 RSWGNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNnvNRAF--RIAEAVESGMFH 435
Cdd:cd07134 313 DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSK--DKANvnKVLARTSSGGVV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
5EK6_A 436 INDVT--FLeESHVPFGGIKASGVGREGGEWSFHETTYDRWV 475
Cdd:cd07134 391 VNDVVlhFL-NPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
138-466 |
4.02e-67 |
|
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: 221.63 E-value: 4.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 138 SVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVvGEE 217
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEV-ATA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 218 IVTHkRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHK 297
Cdd:cd07087 172 LLAE-PFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 298 AVADKFIERYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDDA-VSRGGRLLIGGRswgnFFEPAIFVDVDRNF 376
Cdd:cd07087 251 SIKDELIEELKKAIKEFYGEDPKESP--DYGRIINERHFDRLASLLDDGkVVIGGQVDKEER----YIAPTILDDVSPDS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 377 RIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleesHV-----PFGG 451
Cdd:cd07087 325 PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL----HAaipnlPFGG 400
|
330
....*....|....*
5EK6_A 452 IKASGVGREGGEWSF 466
Cdd:cd07087 401 VGNSGMGAYHGKAGF 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
142-475 |
6.16e-67 |
|
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: 221.71 E-value: 6.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 142 KRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGPGPVVGEeIVTH 221
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTA-LLEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 222 KrVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVAD 301
Cdd:cd07135 184 K-FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 302 KFIERYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDDAvsrGGRLLIGGRSWG--NFFEPAIFVDVDRNFRIM 379
Cdd:cd07135 263 EFVEELKKVLDEFYPGGANASP--DYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDEatRFIPPTIVSDVSWDDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 380 REEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleesHV-----PFGGIKA 454
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLI----HVgvdnaPFGGVGD 413
|
330 340
....*....|....*....|.
5EK6_A 455 SGVGREGGEWSFHETTYDRWV 475
Cdd:cd07135 414 SGYGAYHGKYGFDTFTHERTV 434
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
12-479 |
4.40e-63 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 213.54 E-value: 4.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKepSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAHTLAV 171
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 172 GNTVVYKPASDTPV----TGWLIAQMVAKAGLPKGVFNLVIGpGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTL 247
Cdd:PLN02315 182 GNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 248 KTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDEKVdL 327
Cdd:PLN02315 261 GKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL-L 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 328 GPLINERQVALMKEFVDDAVSRGGRLLIGGR---SWGNFFEPAIfVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSaieSEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 405 DTDYGLSGAVLTNNVNRAFRI--AEAVESGMFHINDVTFLEESHVPFGGIKASGVGREGGEWSFHEttYDRWVTVTL 479
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQ--YMRRSTCTI 493
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
47-466 |
6.79e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 201.80 E-value: 6.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 47 DAREAIDSAFEALKAWANIPAIR----RAEYLYKMLEVFRQMKEDFMKILTVEGGGT--------YRKVWGEVvftERLI 114
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGKTRplefRKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetkmteVLLTVAEI---EHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 115 QNAAELARhyqgrvlqsDSESTISVVFKRSK--------GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVT 186
Cdd:PTZ00381 81 KHLDEYLK---------PEKVDTVGVFGPGKsyiipeplGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 187 GWLIAQMVAKAgLPKGVFNLVIGPGPVVGEeiVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDV 266
Cdd:PTZ00381 152 SKLMAKLLTKY-LDPSYVRVIEGGVEVTTE--LLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 267 DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDDa 346
Cdd:PTZ00381 229 NLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSE--DYSRIVNEFHTKRLAELIKD- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 347 vsRGGRLLIGGRSWGN--FFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFR 424
Cdd:PTZ00381 306 --HGGKVVYGGEVDIEnkYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKEL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|...
5EK6_A 425 IAEAVESGMFHINDVTF-LEESHVPFGGIKASGVGREGGEWSF 466
Cdd:PTZ00381 384 VLENTSSGAVVINDCVFhLLNPNLPFGGVGNSGMGAYHGKYGF 426
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
145-468 |
1.44e-58 |
|
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: 199.25 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 145 KGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVfnLVIGPGPVVGEEIvTHKRV 224
Cdd:cd07133 102 LGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AVVTGGADVAAAF-SSLPF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 225 AHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFI 304
Cdd:cd07133 179 DHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 305 ERYVHYVKMLRIDDPRKDekvDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNF-----FEPAIFVDVDRNFRIM 379
Cdd:cd07133 259 AAAKAAVAKMYPTLADNP---DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFaatrkLPPTLVLNVTDDMRVM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 380 REEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFleesHV-----PFGGIKA 454
Cdd:cd07133 336 QEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL----HVaqddlPFGGVGA 411
|
330
....*....|....
5EK6_A 455 SGVGREGGEWSFHE 468
Cdd:cd07133 412 SGMGAYHGKEGFLT 425
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-456 |
2.58e-58 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 200.18 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGEFKEPSTGAFQvKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKI 91
Cdd:PRK09457 4 WINGDWIAGQGEAFE-SRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 92 LTVEGGgtyRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSK--GVVGVITPWNYPLSISMKKIAHTL 169
Cdd:PRK09457 83 IARETG---KPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRphGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 170 AVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGpGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAG-TLK 248
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGqPEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 249 TVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHK-AVADKFIERYVHYVKMLRIDDPRKDEKVDL 327
Cdd:PRK09457 239 ILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQgAQGDAFLARLVAVAKRLTVGRWDAEPQPFM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 328 GPLINERQVALMKEFVDDAVSRGGRLLI------GGRSwgnFFEPAIfVDVDRNFRIMREEVFGPVRPIVVVENDDQAVE 401
Cdd:PRK09457 319 GAVISEQAAQGLVAAQAQLLALGGKSLLemtqlqAGTG---LLTPGI-IDVTGVAELPDEEYFGPLLQVVRYDDFDEAIR 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 402 VANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASG 456
Cdd:PRK09457 395 LANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
146-467 |
7.79e-58 |
|
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: 197.73 E-value: 7.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVfnLVIGPGPVVGEEIvTHKRVA 225
Cdd:cd07136 102 GVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV--AVVEGGVEENQEL-LDQKFD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 226 HVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIE 305
Cdd:cd07136 179 YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 306 RYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDDavsrgGRLLIGGRS--WGNFFEPAIFVDVDRNFRIMREEV 383
Cdd:cd07136 259 ELKEEIKKFYGEDPLESP--DYGRIINEKHFDRLAGLLDN-----GKIVFGGNTdrETLYIEPTILDNVTWDDPVMQEEI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 384 FGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIND-VTFLEESHVPFGGIKASGVGREGG 462
Cdd:cd07136 332 FGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtIMHLANPYLPFGGVGNSGMGSYHG 411
|
....*
5EK6_A 463 EWSFH 467
Cdd:cd07136 412 KYSFD 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
146-466 |
1.50e-55 |
|
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: 191.67 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAgLPKGVFNLVIGpGPVVGEEIVTHkRVA 225
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDKECYPVVLG-GVEETTELLKQ-RFD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 226 HVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIE 305
Cdd:cd07132 179 YIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 306 RYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDdavsrGGRLLIGGRSWGN--FFEPAIFVDVDRNFRIMREEV 383
Cdd:cd07132 259 ALKKTLKEFYGEDPKESP--DYGRIINDRHFQRLKKLLS-----GGKVAIGGQTDEKerYIAPTVLTDVKPSDPVMQEEI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 384 FGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDV---TFLEEshVPFGGIKASGVGRE 460
Cdd:cd07132 332 FGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTimhYTLDS--LPFGGVGNSGMGAY 409
|
....*.
5EK6_A 461 GGEWSF 466
Cdd:cd07132 410 HGKYSF 415
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
22-458 |
7.68e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 195.03 E-value: 7.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 22 TGAFQVKTSPVDGSK-IAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGgty 100
Cdd:PRK11904 560 EGEARPVVSPADRRRvVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAG--- 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 101 rKVWGEVVfTErlIQNAAELARHY--QGRVLQSDS--------ESTIsvVFKRSKGVVGVITPWNYPLSISMKKIAHTLA 170
Cdd:PRK11904 637 -KTLQDAI-AE--VREAVDFCRYYaaQARRLFGAPeklpgptgESNE--LRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 171 VGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREI----AAKAAgt 246
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlAARDG-- 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 247 lKTVTL--ELGGSDPLIilddvdVDYAARL-----AVFASLFHQ-GQICtSAKRII-VHKAVADKFIERYVHYVKMLRID 317
Cdd:PRK11904 789 -PIVPLiaETGGQNAMI------VDSTALPeqvvdDVVTSAFRSaGQRC-SALRVLfVQEDIADRVIEMLKGAMAELKVG 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 318 DPRkDEKVDLGPLIN-------ERQVALMKefvddavsRGGRLLI-----GGRSWGNFFEPAIFvDVDrNFRIMREEVFG 385
Cdd:PRK11904 861 DPR-LLSTDVGPVIDaeakanlDAHIERMK--------REARLLAqlplpAGTENGHFVAPTAF-EID-SISQLEREVFG 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 386 PVRPIVVVEND--DQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN--------DVTfleeshvPFGGIKAS 455
Cdd:PRK11904 930 PILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrnqigavvGVQ-------PFGGQGLS 1002
|
...
5EK6_A 456 GVG 458
Cdd:PRK11904 1003 GTG 1005
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
12-456 |
4.52e-51 |
|
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: 181.63 E-value: 4.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 12 YINGefKEPSTGAFQVKTSPVD-GSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMK 90
Cdd:cd07123 36 VIGG--KEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 91 ILTVEGGGtyRKVW-GEvvfterlIQNAAELA---R---HYQGRVLQSDSESTISVVFKRSK-----GVVGVITPWNYpl 158
Cdd:cd07123 114 AATMLGQG--KNVWqAE-------IDAACELIdflRfnvKYAEELYAQQPLSSPAGVWNRLEyrpleGFVYAVSPFNF-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 159 sismKKIAHTLA-----VGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGES 233
Cdd:cd07123 183 ----TAIGGNLAgapalMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGST 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 234 STGREIAAKAAGTLKT------VTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERY 307
Cdd:cd07123 259 PTFKSLWKQIGENLDRyrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 308 VHYVKMLRIDDPRKDEKVdLGPLINERQVALMKEFVDDA-VSRGGRLLIGGR---SWGNFFEPAIFVDVDRNFRIMREEV 383
Cdd:cd07123 339 LEELKEIKMGDPDDFSNF-MGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKcddSVGYFVEPTVIETTDPKHKLMTEEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 384 FGPVRPIVVVENDD--QAVEVANDT-DYGLSGAVLTNnvNRAFrIAEAVE-----SGMFHINDVTflEESHV---PFGGI 452
Cdd:cd07123 418 FGPVLTVYVYPDSDfeETLELVDTTsPYALTGAIFAQ--DRKA-IREATDalrnaAGNFYINDKP--TGAVVgqqPFGGA 492
|
....
5EK6_A 453 KASG 456
Cdd:cd07123 493 RASG 496
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
8-458 |
7.54e-51 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 182.64 E-value: 7.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 8 KVANYINGEFKEPSTGAFQVKTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKED 87
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 88 FMKILTVEGGGTYRKVWGEVVFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSKGVVGVITPWNYPLSISMKKIAH 167
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 168 TLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVgEEIVTHKRVAHVTFTGESSTGREIAAKAAGTL 247
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 248 KTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIV---HKAVADKFIERyvhyVKMLRIDDPRKDEk 324
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVER----AKALKVTCGSEPD- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 325 VDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSW-------GNFFEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDD 397
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
5EK6_A 398 QAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTFLEESHVPFGGIKASGVG 458
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAG 567
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
19-437 |
4.46e-48 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 178.21 E-value: 4.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 19 EPSTGAFQVKTSPVDGSKIA-EVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKM---LEvfRQMKEdFMKILTV 94
Cdd:COG4230 565 EAASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAadlLE--AHRAE-LMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 95 EGGGTyrkvwgevvfterlIQNA-AEL------ARHYQGRVLQSDSESTISvvfkRSKGVVGVITPWNYPLSISMKKIAH 167
Cdd:COG4230 642 EAGKT--------------LPDAiAEVreavdfCRYYAAQARRLFAAPTVL----RGRGVFVCISPWNFPLAIFTGQVAA 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 168 TLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIA---AKAA 244
Cdd:COG4230 704 ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINrtlAARD 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 245 GTLktVTL--ELGGSDPLIilddvdVDYAArLA------VFASLFH-QGQICtSAKRII-VHKAVADKFIERYVHYVKML 314
Cdd:COG4230 784 GPI--VPLiaETGGQNAMI------VDSSA-LPeqvvddVLASAFDsAGQRC-SALRVLcVQEDIADRVLEMLKGAMAEL 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 315 RIDDPRkDEKVDLGPLIN-------ERQVALMKefvddavsRGGRLLI-----GGRSWGNFFEPAIF-VDvdrNFRIMRE 381
Cdd:COG4230 854 RVGDPA-DLSTDVGPVIDaearanlEAHIERMR--------AEGRLVHqlplpEECANGTFVAPTLIeID---SISDLER 921
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 382 EVFGPVRPIVVVEND--DQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN 437
Cdd:COG4230 922 EVFGPVLHVVRYKADelDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
146-466 |
2.80e-46 |
|
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: 166.43 E-value: 2.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVfnLVIGPGPVVGEEIVTHKRvA 225
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI--KVIEGGVPETTALLEQKW-D 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 226 HVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAV---FASlfHQGQICTSAKRIIVHKAVADK 302
Cdd:cd07137 180 KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAggkWGC--NNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 303 FIERYVHYVKMLRIDDPRkdEKVDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNFF-EPAIFVDVDRNFRIMRE 381
Cdd:cd07137 258 LIDALKNTLEKFFGENPK--ESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYiEPTILLDPPLDSSIMTE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 382 EVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHINDVTF-LEESHVPFGGIKASGVGRE 460
Cdd:cd07137 336 EIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqYAIDTLPFGGVGESGFGAY 415
|
....*.
5EK6_A 461 GGEWSF 466
Cdd:cd07137 416 HGKFSF 421
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
19-458 |
2.28e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 161.57 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 19 EPSTGAFQVKTSPVD-GSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVF-RQMKEdFMKILTVEG 96
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMeAHMPE-LFALAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 97 GGTYRKVWGEVvfterliQNAAELARHY--QGRVLQSDSEStisvvfkRSKGVVGVITPWNYPLSISMKKIAHTLAVGNT 174
Cdd:PRK11905 641 GKTLANAIAEV-------REAVDFLRYYaaQARRLLNGPGH-------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 175 VVYKPASDTPvtgwLIA----QMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTL-KT 249
Cdd:PRK11905 707 VLAKPAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSgPP 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 250 VTL--ELGGSDPLIilddvdVDYAArLA------VFASLFHQ-GQICtSAKRII-VHKAVADKFIERYVHYVKMLRIDDP 319
Cdd:PRK11905 783 VPLiaETGGQNAMI------VDSSA-LPeqvvadVIASAFDSaGQRC-SALRVLcLQEDVADRVLTMLKGAMDELRIGDP 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 320 rKDEKVDLGPLINERQVALMKEFVDDAVSRGGRL----LIGGRSWGNFFEPAIFvDVDrNFRIMREEVFGPVRPIVVVEN 395
Cdd:PRK11905 855 -WRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhqlpLPAETEKGTFVAPTLI-EID-SISDLEREVFGPVLHVVRFKA 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 396 D--DQAVEVANDTDYGLSGAVLTnnvnrafRIAEAVEsgmfhindvTFLEESHV-----------------PFGGIKASG 456
Cdd:PRK11905 932 DelDRVIDDINATGYGLTFGLHS-------RIDETIA---------HVTSRIRAgniyvnrniigavvgvqPFGGEGLSG 995
|
..
5EK6_A 457 VG 458
Cdd:PRK11905 996 TG 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
10-462 |
3.53e-42 |
|
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: 156.99 E-value: 3.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 10 ANYINGEFKepSTGAFQVKTSPVD-GSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDF 88
Cdd:TIGR01238 39 APIIGHSYK--ADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 89 MKILTVEGGGTYRKVWGEVvfterliQNAAELARHYQGRVLQSDSESTIsvvfkRSKGVVGVITPWNYPLSISMKKIAHT 168
Cdd:TIGR01238 117 MALCVREAGKTIHNAIAEV-------REAVDFCRYYAKQVRDVLGEFSV-----ESRGVFVCISPWNFPLAIFTGQISAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 169 LAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLK 248
Cdd:TIGR01238 185 LAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 249 T---VTLELGGSDPLIIlDDVDVDYAARLAVFASLFHQ-GQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRKdEK 324
Cdd:TIGR01238 265 ApvpLIAETGGQNAMIV-DSTALPEQVVRDVLRSAFDSaGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL-LT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 325 VDLGPLINER-QVALMKEFvdDAVSRGGR-----LLIGGRSW--GNFFEPAIFvDVDrNFRIMREEVFGPVRPIVVVEND 396
Cdd:TIGR01238 343 TDVGPVIDAEaKQNLLAHI--EHMSQTQKkiaqlTLDDSRACqhGTFVAPTLF-ELD-DIAELSEEVFGPVLHVVRYKAR 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
5EK6_A 397 --DQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIN-DVTFLEESHVPFGGIKASGVGREGG 462
Cdd:TIGR01238 419 elDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
146-466 |
6.96e-39 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 147.57 E-value: 6.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVfnLVIGPGPVVGEEIVTHkRVA 225
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV--KVIEGGPAVGEQLLQH-KWD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 226 HVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPlIILDDVDVDYAARLAV-------FASLfhQGQICTSAKRIIVHKA 298
Cdd:PLN02203 187 KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCP-CIVDSLSSSRDTKVAVnrivggkWGSC--AGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 299 VADKFIERYVHYVKMLRIDDPRKDEkvDLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNFF-EPAIFVDVDRNFR 377
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESK--SMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFiEPTILLNPPLDSD 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 378 IMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVESGMFHIND--VTFLEEShVPFGGIKAS 455
Cdd:PLN02203 342 IMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDaiIQYACDS-LPFGGVGES 420
|
330
....*....|.
5EK6_A 456 GVGREGGEWSF 466
Cdd:PLN02203 421 GFGRYHGKYSF 431
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
37-462 |
1.81e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 140.88 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 37 IAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEVvfterliQN 116
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEV-------RE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 117 AAELARHYQGRVLQSDSESTisvvfKRSKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPvtgwLIA-QMVA 195
Cdd:PRK11809 746 AVDFLRYYAGQVRDDFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP----LIAaQAVR 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 196 ---KAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTL----KTVTL--ELGGSDPLIilddv 266
Cdd:PRK11809 817 illEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLiaETGGQNAMI----- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 267 dVDYAArLA------VFASLFHQ-GQICtSAKRII-VHKAVADkfieryvHYVKML-------RIDDPRKdEKVDLGPLI 331
Cdd:PRK11809 892 -VDSSA-LTeqvvadVLASAFDSaGQRC-SALRVLcLQDDVAD-------RTLKMLrgamaecRMGNPDR-LSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 332 N-------ERQVALMKEfVDDAVSRGGRLLIGGRSWGNFFEPAIfVDVDrNFRIMREEVFGPVRPIVVV--ENDDQAVEV 402
Cdd:PRK11809 961 DaeakaniERHIQAMRA-KGRPVFQAARENSEDWQSGTFVPPTL-IELD-SFDELKREVFGPVLHVVRYnrNQLDELIEQ 1037
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 403 ANDTDYGLSGAVLTnnvnrafRIAEAvesgmfhINDVTflEESHV-----------------PFGGIKASGVGREGG 462
Cdd:PRK11809 1038 INASGYGLTLGVHT-------RIDET-------IAQVT--GSAHVgnlyvnrnmvgavvgvqPFGGEGLSGTGPKAG 1098
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
108-475 |
4.35e-32 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 128.24 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARHYQGRVLQSDSESTISVVFKRSK-------GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPA 180
Cdd:PLN02174 69 VYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAeivseplGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 181 SDTPVTGWLIAQMVAKAGLPKGVfnlVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTLKTVTLELGGSDPL 260
Cdd:PLN02174 149 ELAPASSALLAKLLEQYLDSSAV---RVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 261 IILDDVDVDYAARLAVFASL-FHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkdEKVDLGPLINERQVALM 339
Cdd:PLN02174 226 VVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPM--ESKDMSRIVNSTHFDRL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 340 KEFVDDAVSRGGRLLIGGRSWGNF-FEPAIFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNN 418
Cdd:PLN02174 304 SKLLDEKEVSDKIVYGGEKDRENLkIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 419 VNRAFRIAEAVESGMFHINDVTFLEESH-VPFGGIKASGVGREGGEWSFHETTYDRWV 475
Cdd:PLN02174 384 KKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
51-431 |
8.22e-29 |
|
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: 118.11 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 51 AIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKV--WGEVVFTERLIQNAAELARHYQGRV 128
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenICGDQVQLRARAFVIYSYRIPHEPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 129 LQSDSESTISVVFKRS-KGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAG-LPKGVFNL 206
Cdd:cd07084 84 NHLGQGLKQQSHGYRWpYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 207 VIGPGPvVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGTlkTVTLELGGSDPLIILDDVD-VDYAARLAVFASLFHQGQ 285
Cdd:cd07084 164 INGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 286 ICTSAKRIIVHKAVA-DKFIEryvhyvKMLRIDDPRKDEKVDLGPLINER---QVALMKEFVDDAVSRGGRLLIGGRSWG 361
Cdd:cd07084 241 KCTAQSMLFVPENWSkTPLVE------KLKALLARRKLEDLLLGPVQTFTtlaMIAHMENLLGSVLLFSGKELKNHSIPS 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 362 NF---FEPAIFVDVDRNFR---IMREEVFGPVRPIVVVENDDQA--VEVANDTDYGLSGAVLTNNVNRAFRIAEAVES 431
Cdd:cd07084 315 IYgacVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWV 392
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
50-404 |
2.04e-26 |
|
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: 111.48 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 50 EAIDSAFEALKAWANIPAIRRAEYLYKMLEVFRQMKEDFMKILTVEGGGTYRKVWGEV---VFTERLIQNAAELARHYQG 126
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELgrtTGQLRLFADLVREGSWLDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 127 RVlqsDSESTISVVFKRSK--------GVVGVITPWNYPLSISMK--KIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAK 196
Cdd:cd07129 83 RI---DPADPDRQPLPRPDlrrmlvplGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPGTSELVARAIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 197 A----GLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAG--TLKTVTLELGGSDPLIILDDVDVDY 270
Cdd:cd07129 160 AlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 271 AARLA-VFAS--LFHQGQICTSAKRIIVHK-AVADKFIERYVhyvkmlriddpRKDEKVDLGPLINERqvalMKEFVDDA 346
Cdd:cd07129 240 GEAIAqGFVGslTLGAGQFCTNPGLVLVPAgPAGDAFIAALA-----------EALAAAPAQTMLTPG----IAEAYRQG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
5EK6_A 347 VSR-----GGRLLIGGRSWGNFFE--PAIFVDVDRNFR---IMREEVFGPVRPIVVVENDDQAVEVAN 404
Cdd:cd07129 305 VEAlaaapGVRVLAGGAAAEGGNQaaPTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
9-462 |
5.75e-23 |
|
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: 101.58 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 9 VANYINGEFKEPSTGAFQVKtSPVDGSKIAEVPRSGReDAREAIDSAFE----ALKAWAnipAIRRAEYLYKMLEVFRQM 84
Cdd:cd07128 1 LQSYVAGQWHAGTGDGRTLH-DAVTGEVVARVSSEGL-DFAAAVAYAREkggpALRALT---FHERAAMLKALAKYLMER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 85 KEDFMKIlTVEGGGTYRKVWGEV---VFTerLIQNAAELAR-------HYQGRVLQSDSESTIS----VVFKRskGVVGV 150
Cdd:cd07128 76 KEDLYAL-SAATGATRRDSWIDIdggIGT--LFAYASLGRRelpnahfLVEGDVEPLSKDGTFVgqhiLTPRR--GVAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 151 ITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTP-VTGWLIAQMVAKAGLPKGVFNLVIG-PGPVVgeEIVTHKRVahVT 228
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAyLTEAVVKDIVESGLLPEGALQLICGsVGDLL--DHLGEQDV--VA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 229 FTGESSTGREIAAKAAGTLKTV--TLELGGSDPLIILDDVDVDyAARLAVFASLFHQ------GQICTSAKRIIVHKAVA 300
Cdd:cd07128 227 FTGSAATAAKLRAHPNIVARSIrfNAEADSLNAAILGPDATPG-TPEFDLFVKEVARemtvkaGQKCTAIRRAFVPEARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 301 DKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVdDAVSRGGRLLIGGRSW----------GNFFEPAIFV 370
Cdd:cd07128 306 DAVIEALKARLAKVVVGDPR-LEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRfevvgadaekGAFFPPTLLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 371 --DVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGLSGAVLTNNVNRAFRIAEAVES--GMFHINDVTFLEES- 445
Cdd:cd07128 384 cdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLNRDSAKESt 463
|
490
....*....|....*....
5EK6_A 446 -H-VPFGGIKASGVGREGG 462
Cdd:cd07128 464 gHgSPLPQLVHGGPGRAGG 482
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
11-420 |
3.03e-20 |
|
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: 93.33 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 11 NYINGEFKEpSTGAFQVkTSPVDGSKIAEVPRSGREDAREAIDSAFEALKAWANIPAIRRAEYL------YKMLEVFRQM 84
Cdd:cd07126 1 NLVAGKWKG-ASNYTTL-LDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLlygdvsHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 85 K-EDFMKILTVE-GGGTYRKVWGEVVFTERLIQNAAE-----LARHYqgrVLQSDSESTISVVFKRSKGVVGVITPWNYP 157
Cdd:cd07126 79 EvEDFFARLIQRvAPKSDAQALGEVVVTRKFLENFAGdqvrfLARSF---NVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 158 LSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVgEEIVTHKRVAHVTFTGESSTGR 237
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTM-NKILLEANPRMTLFTGSSKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 238 EIAAKAAGTLKtvtLELGGSDPLIILDDV-DVDYAARLAVFASLFHQGQICTSAKRIIVHKAVADKFIERyvhyvKMLRI 316
Cdd:cd07126 235 RLALELHGKVK---LEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAGILD-----KLKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 317 DDPRKDEKVDLGPLI---NERqvalMKEFVDDAVS-RGGRLLIGGRSWGNF--------FEP-AIFV-----DVDRNFRI 378
Cdd:cd07126 307 AEQRKLEDLTIGPVLtwtTER----ILDHVDKLLAiPGAKVLFGGKPLTNHsipsiygaYEPtAVFVpleeiAIEENFEL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
5EK6_A 379 MREEVFGPVRpiVVVENDDQ----AVEVANDTDYGLSGAVLTNNVN 420
Cdd:cd07126 383 VTTEVFGPFQ--VVTEYKDEqlplVLEALERMHAHLTAAVVSNDIR 426
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
7-403 |
1.09e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.61 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 7 MKVANYINGEFKEpSTGAFQVKTSPVDGSKIAEVPRSGREDARE---AIDSAFEALKAwanIPAIRRAEYLYKMLEVFRQ 83
Cdd:PRK11903 3 ELLANYVAGRWQA-GSGAGTPLFDPVTGEELVRVSATGLDLAAAfafAREQGGAALRA---LTYAQRAALLAAIVKVLQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 84 MKEDFMKILT-------------VEGG----GTYRKvWGEVVFTERLIQN--AAELARH--YQGRVLQSDSestisvvfk 142
Cdd:PRK11903 79 NRDAYYDIATansgttrndsavdIDGGiftlGYYAK-LGAALGDARLLRDgeAVQLGKDpaFQGQHVLVPT--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 143 rsKGVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASdtpVTGWLIAQMVA---KAG-LPKGVFNLVIGPGP----VV 214
Cdd:PRK11903 149 --RGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPAT---ATAWLTQRMVKdvvAAGiLPAGALSVVCGSSAglldHL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 215 GEEIVthkrvahVTFTGESSTGREIAAKAAGTLKTVTLELGgSDPL---IILDDVDVDYAArlavFASLFHQ-------- 283
Cdd:PRK11903 224 QPFDV-------VSFTGSAETAAVLRSHPAVVQRSVRVNVE-ADSLnsaLLGPDAAPGSEA----FDLFVKEvvremtvk 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 284 -GQICTSAKRIIVHKAVADKFIERYVHYVKMLRIDDPRkDEKVDLGPLINERQVALMKEFVdDAVSRGGRLLIGGRSW-- 360
Cdd:PRK11903 292 sGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPR-NDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFal 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
5EK6_A 361 -------GNFFEPAIFV--DVDRNFRIMREEVFGPVRPIVVVENDDQAVEVA 403
Cdd:PRK11903 370 vdadpavAACVGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
146-434 |
1.51e-12 |
|
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: 69.19 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPL------SISMkkiahtLAVGNTVVYKP-ASDTPVTGWLIAQM---VAKAGLPKGVFNLVIGPGPVVG 215
Cdd:cd07121 99 GVIGAITPSTNPTetiinnSISM------LAAGNAVVFNPhPGAKKVSAYAVELInkaIAEAGGPDNLVVTVEEPTIETT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 216 EEIVTHKRVAHVTFTG--------ESSTGREIAAKAagtlktvtlelgGSDPLIILDDVDVDYAARLAVFASLFHQGQIC 287
Cdd:cd07121 173 NELMAHPDINLLVVTGgpavvkaaLSSGKKAIGAGA------------GNPPVVVDETADIEKAARDIVQGASFDNNLPC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 288 TSAKRIIVHKAVADKFIEryvhyvKMLR-----IDDPRKDEKVDLgPLINERQVALMKEFVddavsrggrlligGRSWGN 362
Cdd:cd07121 241 IAEKEVIAVDSVADYLIA------AMQRngayvLNDEQAEQLLEV-VLLTNKGATPNKKWV-------------GKDASK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 363 FFEPA----------IFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGL--SGAVLTNNVNRAFRIAEAVE 430
Cdd:cd07121 301 ILKAAgievpadirlIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMARAMQ 380
|
....
5EK6_A 431 SGMF 434
Cdd:cd07121 381 TTIF 384
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
146-461 |
1.00e-11 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 66.85 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPL------SISMkkiahtLAVGNTVVYKP-ASDTPVTGWLIAQM---VAKAGLPKGVFNLVIGPGPVVG 215
Cdd:PRK15398 131 GVIGAVTPSTNPTetiinnAISM------LAAGNSVVFSPhPGAKKVSLRAIELLneaIVAAGGPENLVVTVAEPTIETA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 216 EEIVTHKRVAHVTFTGesstGREIAAKAAGTLKTVTLELGGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIV 295
Cdd:PRK15398 205 QRLMKHPGIALLVVTG----GPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 296 HKAVADKFIERyvhyvkMLRID----DPRKDEKvdLGPLINERQVALMKEFVddavsrggrlligGRSWGNFFEPA---- 367
Cdd:PRK15398 281 VDSVADELMRL------MEKNGavllTAEQAEK--LQKVVLKNGGTVNKKWV-------------GKDAAKILEAAginv 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 368 ------IFVDVDRNFRIMREEVFGPVRPIVVVENDDQAVEVANDTDYGL--SGAVLTNNVNRAFRIAEAVESGMFHINDV 439
Cdd:PRK15398 340 pkdtrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQTSIFVKNGP 419
|
330 340
....*....|....*....|..
5EK6_A 440 TfleeshvpFGGIkasGVGREG 461
Cdd:PRK15398 420 S--------YAGL---GLGGEG 430
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
146-437 |
7.00e-11 |
|
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: 64.21 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKP---ASD-TPVTGWLIAQMVAKAGLPKGVFNLVIGPGPVVGEEIVTH 221
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKvTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 222 KRVAHVTFTG--------ESSTGREIAAKAagtlktvtlelgGSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRI 293
Cdd:cd07081 177 PGIGLLLATGgpavvkaaYSSGKPAIGVGA------------GNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 294 IVHKAVADKFIERYV-HYVKMLRIDDPRKDEKV-----DLGPLINERQVALMKEFVDDAVSRGGRLLIGGRSWGNFFEPA 367
Cdd:cd07081 245 IVVDSVYDEVMRLFEgQGAYKLTAEELQQVQPVilkngDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAEHEPF 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5EK6_A 368 IfvdvdrnfrimrEEVFGPVRPIVVVENDDQAVEVA----NDTDYGLSGAVLTNNVN---RAFRIAEAVESGMFHIN 437
Cdd:cd07081 325 A------------HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKN 389
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
108-437 |
4.64e-10 |
|
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: 61.47 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 108 VFTERLIQNAAELARhyqgRVLQSDSESTISVVFkrSKGVVGVITPWNYPLSIsMKKIAHTLAVGNTVVYKPASDTPVTG 187
Cdd:cd07077 70 IDTERGITASVGHIQ----DVLLPDNGETYVRAF--PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 188 WLIA---QMVAKAGLPKGVFNLVIGPGPVVGEEIVTHKRVAHVTFTGESSTGReiAAKAAGTLKTVTLELGGSDPLIILD 264
Cdd:cd07077 143 RALAllfQAADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 265 DVDVDYAARLAVfASLFHQGQICTSAKRIIVHKAVADKFIERYVHYVKMLRIddprkdeKVDLGPLINERQValMKEFVD 344
Cdd:cd07077 221 TADEERASGSVH-DSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGL-------KVPQETKPLSKET--TPSFDD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 345 DAVsrggrlliggrswgnffepaifvdvdrnfrimreEVFGPVRPIVVVENDDQAVEVANDT--DYG--LSGAVLTNNVN 420
Cdd:cd07077 291 EAL----------------------------------ESMTPLECQFRVLDVISAVENAWMIieSGGgpHTRCVYTHKIN 336
|
330
....*....|....*..
5EK6_A 421 RAFRIAEAVESGMFHIN 437
Cdd:cd07077 337 KVDDFVQYIDTASFYPN 353
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
125-403 |
1.35e-09 |
|
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: 60.18 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 125 QGRVLQSDSESTISVVFKRSKGVVGVIT--PWN-YPlsismkKIAHTLAVGNTVVYKP--ASDTPVTGWL-IAQMV-AKA 197
Cdd:cd07127 177 QGKHDPLAMEKTFTVVPRGVALVIGCSTfpTWNgYP------GLFASLATGNPVIVKPhpAAILPLAITVqVAREVlAEA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 198 GLPKGVFNLVI-GPGPVVGEEIVTHKRVAHVTFTGESSTGREIAAKAAGtlKTVTLELGGSDPLIIlDDVDvDYAARLA- 275
Cdd:cd07127 251 GFDPNLVTLAAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVV-DSTD-DLKAMLRn 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 276 -VFASLFHQGQICTSAKRIIVHK---------AVADKFIERYVHYVKMLRIDDPRKDEKvdLGPLINERQVALMKEfvdd 345
Cdd:cd07127 327 lAFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAAIDGLLADPARAAAL--LGAIQSPDTLARIAE---- 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
5EK6_A 346 aVSRGGRLLIGGRSWGN-FFEPA-----IFVDVDRNFRIM-REEVFGPVRPIVVVENDDQAVEVA 403
Cdd:cd07127 401 -ARQLGEVLLASEAVAHpEFPDArvrtpLLLKLDASDEAAyAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
146-305 |
5.66e-04 |
|
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: 42.09 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 146 GVVGVITPWNYPLSISMKKIAHTLAVGNTVVYKPASDTPVTGWLIAQMV----AKAGLPKGVFNLVIGPGPVVGEEIVTH 221
Cdd:cd07122 97 GVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELTQELMKH 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5EK6_A 222 KRVAHVTftgesSTGREIAAKAAGTLKTVTLELG-GSDPLIILDDVDVDYAARLAVFASLFHQGQICTSAKRIIVHKAVA 300
Cdd:cd07122 177 PDVDLIL-----ATGGPGMVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIY 251
|
....*
5EK6_A 301 DKFIE 305
Cdd:cd07122 252 DEVRA 256
|
|
| |
