|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-308 |
6.20e-137 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 390.73 E-value: 6.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 3 FVRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFG 81
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKvKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcAAATHEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDD-SGKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvHFQTKYNYTTEAFPDLLNHSVV 241
Cdd:cd19155 162 NFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAA-HFSPGTGSPSGSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGAAGRIF 308
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
4-308 |
1.11e-130 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 374.44 E-value: 1.11e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHFGN 82
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGvVKREDLFITTKLWTHEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcaAATHEDGSYILDfDTDPVLVWKEMENQVKSGRTRSIGLSN 162
Cdd:cd19154 84 APEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGE--SGTMENGMSIHD-AVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 163 FNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHfqTKYNYTTEAfPDLLNHSVVQ 242
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANF--TKSTGVSPA-PNLLQDPIVK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1153814477 243 NIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGAAGRIF 308
Cdd:cd19154 238 AIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFLF 303
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
9-308 |
1.18e-123 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 356.04 E-value: 1.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFGNRPSDV 87
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKlKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 88 EKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEatcaaatheDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQ 167
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKK---------DKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 168 ISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtKYNYTTEA-FPDLLNHSVVQNIAE 246
Cdd:cd19111 152 INKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPG-------RANQSLWPdQPDLLEDPTVLAIAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 247 RHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGAAGRIF 308
Cdd:cd19111 225 ELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYFDF 286
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
12-297 |
1.45e-119 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 344.47 E-value: 1.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKggsREELFITTKLPHFGNRPSDVEKFI 91
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVP---REELFITTKLWPTDHGYERVREAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 92 KLSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildfDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQISLI 171
Cdd:cd19071 78 EESLKDLGLDYLDLYLIHWPVPGKEGGS----------------KEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 172 WENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAkvhfqtkynytteafpDLLNHSVVQNIAERHKKS 251
Cdd:cd19071 142 LAAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR----------------PLLDDPVLKEIAKKYGKT 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1153814477 252 TAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19071 206 PAQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-303 |
6.54e-118 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 341.95 E-value: 6.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAK-SEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFG 81
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKdDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVvKREDLFITTKLWNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDeatCAAATHEDGSYIldfDTDPVLVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19116 83 HEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKEN---NDSESNGDGSLS---DIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHfqtkynyttEAFPDLLNHSVV 241
Cdd:cd19116 157 NFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQ---------TNPPPRLDDPTL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGA 303
Cdd:cd19116 228 VAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQ 289
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
8-308 |
4.01e-113 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 328.17 E-value: 4.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLPHFGNRPSDV 87
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA---ASGVPREELFVTTKVWNDNHGYDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 88 EKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildfdtdpvlvWKEMENQVKSGRTRSIGLSNFNEEQ 167
Cdd:COG0656 78 LAAFEESLERLGLDYLDLYLIHWPGPGPYVET-----------------------WRALEELYEEGLIRAIGVSNFDPEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 168 ISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynytteafpdLLNHSVVQNIAER 247
Cdd:COG0656 135 LEELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK------------------LLDDPVLAEIAEK 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 248 HKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGaaGRIF 308
Cdd:COG0656 197 HGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRG--ERLG 255
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
6-302 |
2.79e-110 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 322.80 E-value: 2.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 6 LLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGS-----REELFITTKLPHF 80
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALK---EKVGPgkavpREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 81 GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEAtcAAATHEDGSYILDfDTDPVLVWKEMENQVKSGRTRSIGL 160
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDN--PFPKNPDGTIRYD-STHYKETWKAMEKLVDKGLVKAIGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 161 SNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvhfqtkynYTTEAFPDLLNHSV 240
Cdd:cd19106 155 SNFNSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRP--------WAKPDEPVLLEEPK 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 241 VQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19106 227 VKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
2-297 |
1.64e-102 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 302.34 E-value: 1.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 2 HFVrLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHF 80
Cdd:cd19125 2 FFK-LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGvVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 81 GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAAThedgsyILDFDTDPVlvWKEMENQVKSGRTRSIGL 160
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHMPEPEE------VLPPDIPST--WKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 161 SNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynyTTEAFPDLLNHSV 240
Cdd:cd19125 153 SNFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPG-----------TTWVKKNVLKDPI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1153814477 241 VQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19125 222 VTKVAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
12-299 |
9.25e-95 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 281.83 E-value: 9.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAK-SEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPhfgnrPSDV-- 87
Cdd:cd19136 1 MPILGLGTFRLRgEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGlSREDIFITSKLA-----PKDQgy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 88 ---EKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAATHEDGSyildfdtdpvlvWKEMENQVKSGRTRSIGLSNFN 164
Cdd:cd19136 76 ekaRAACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRRES------------WRALEDLYKEGKLRAIGVSNYT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 165 EEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynytteafPDLLNHSVVQNI 244
Cdd:cd19136 144 VRHLEELLKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD----------------LRLLEDPTVLAI 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1153814477 245 AERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDL 299
Cdd:cd19136 208 AKKYGRTPAQVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-300 |
4.95e-91 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 272.14 E-value: 4.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAK-SEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKwfeKGGSREELFITTKLphfgn 82
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPdPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKK---SGIPREELFITTKL----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVE-----KFIKLSLDKLGLDYLDMYLVHMPFAfkldeatcaaathedgsyildfdtDPVLVWKEMENQVKSGRTRS 157
Cdd:cd19133 73 WIQDAGyekakKAFERSLKRLGLDYLDLYLIHQPFG------------------------DVYGAWRAMEELYKEGKIRA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 158 IGLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGspgakvhfqtkynyttEAFPDLLN 237
Cdd:cd19133 129 IGVSNFYPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA----------------EGRNNLFE 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 238 HSVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19133 193 NPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-302 |
5.35e-87 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 263.50 E-value: 5.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 1 MHFVRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPH 79
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKvKREDLWITSKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 FGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDeatcaAATHEDGSYILDFDTDPVL-VWKEMENQVKSGRTRSI 158
Cdd:cd19123 81 NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-----VGFPESGEDLLSLSPIPLEdTWRAMEELVDKGLCRHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 159 GLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHFQtkynytTEAFPDLLNH 238
Cdd:cd19123 156 GVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMK------AEGEPVLLED 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 239 SVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19123 230 PVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRH 293
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
4-300 |
1.47e-86 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 260.77 E-value: 1.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKwfeKGGSREELFITTKLPHFGNR 83
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA---SGVPREELFITTKLWNSDQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 84 PSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKldeatcaaathedGSYildfdtdpVLVWKEMENQVKSGRTRSIGLSNF 163
Cdd:cd19131 79 YDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQ-------------DKY--------VETWKALIELKKEGRVKSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 164 NEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynytteafpdLLNHSVVQN 243
Cdd:cd19131 138 TIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG------------------LLSDPVIGE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1153814477 244 IAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19131 200 IAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-301 |
1.02e-85 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 260.50 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHfgn 82
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGlVKREDLFITTKLWN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 rpSD---VEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDE-ATCAAATHEDGsyILDFDTDPVL--VWKEMENQVKSGRTR 156
Cdd:cd19112 80 --SDhghVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGvGTTGSALGEDG--VLDIDVTISLetTWHAMEKLVSAGLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 157 SIGLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHFqtkYNYTTEafpdlL 236
Cdd:cd19112 156 SIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEW---FGSVSP-----L 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1153814477 237 NHSVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDK 301
Cdd:cd19112 228 DDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDR 292
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
8-293 |
7.66e-85 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 257.20 E-value: 7.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGT--WQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG--GSREELFITTKLPHFGNR 83
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGlvKSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 84 PSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKlDEATCAAATHEDgsyILDFDTDPVlvWKEMENQVKSGRTRSIGLSNF 163
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLK-PGKFSFPIEEED---FLPFDIKGV--WEAMEECQRLGLTKAIGVSNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 164 NEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvhfqtkynYTTEAfpdLLNHSVVQN 243
Cdd:cd19124 155 SCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTK--------WGSNA---VMESDVLKE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1153814477 244 IAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDM 293
Cdd:cd19124 224 IAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-300 |
1.39e-82 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 250.43 E-value: 1.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKS-EEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLPHFGN 82
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIR---ESGVPREELFVTTKLWNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildfdtdpvlvWKEMENQVKSGRTRSIGLSN 162
Cdd:cd19126 78 RARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDT-----------------------WKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 163 FNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynytteafpdLLNHSVVQ 242
Cdd:cd19126 135 FQEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG------------------LLSNPVLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 243 NIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19126 197 AIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
12-293 |
2.28e-82 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 249.50 E-value: 2.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLPHFGNRPSDVEKFI 91
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIA---ESGVPREDLFITTKVWRDHLRPEDLKKSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 92 KLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQISLI 171
Cdd:cd19073 78 DRSLEKLGTDYVDLLLIHWP----------------------NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 172 WENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGspgakvhfQTKynytteafpdLLNHSVVQNIAERHKKS 251
Cdd:cd19073 136 LDISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLA--------RGE----------VLRDPVIQEIAEKYDKT 197
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1153814477 252 TAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDM 293
Cdd:cd19073 198 PAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDV 239
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
6-300 |
5.76e-82 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 249.11 E-value: 5.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 6 LLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLPHFGNRPS 85
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVR---RSGVPREELFVTTKLPGRHHGYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 86 DVEKFIKLSLDKLGLDYLDMYLVHMPFAFKldeatcaaathedGSYildfdtdpVLVWKEMENQVKSGRTRSIGLSNFNE 165
Cdd:cd19132 78 EALRTIEESLYRLGLDYVDLYLIHWPNPSR-------------DLY--------VEAWQALIEAREEGLVRSIGVSNFLP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 166 EQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGakvhfqtkynytteafpDLLNHSVVQNIA 245
Cdd:cd19132 137 EHLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS-----------------GLLDEPVIKAIA 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1153814477 246 ERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19132 200 EKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-301 |
8.74e-82 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 249.72 E-value: 8.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 5 RLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLphFGNRP 84
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSGVPREEIFITTKL--WCTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 85 SDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcAAATHEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLSNF- 163
Cdd:cd19117 82 RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGND-FLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 164 --NEEQIsLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvhfqtkynytteafpdLLNHSVV 241
Cdd:cd19117 161 ikNLEKL-LASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP----------------LLKEPVI 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIfdFTLTDDDMNLLNDLDK 301
Cdd:cd19117 224 IKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
5-299 |
6.74e-81 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 247.06 E-value: 6.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 5 RLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGGSREELFITTKLPHFGNRp 84
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGVKREDLFVTTKLWSTYHR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 85 sDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAATHEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLSNFN 164
Cdd:cd19121 84 -RVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSRDLDWDWNHVDTWKQMEKVLKTGKTKAIGVSNYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 165 EEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvhfqtkynytteafpdLLNHSVVQNI 244
Cdd:cd19121 163 IPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP----------------LISDEPVVEI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1153814477 245 AERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFtlTDDDMNLLNDL 299
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
1-299 |
3.55e-80 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 244.93 E-value: 3.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 1 MHFVRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKL--P 78
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKAIK---ESGVPREDLFLTTKLwpS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 79 HFGNRpsDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeaTCAAATHEDGSYILDfdtdpvlVWKEMENQVKSGRTRSI 158
Cdd:cd19135 79 DYGYE--STKQAFEASLKRLGVDYLDLYLLHWP--------DCPSSGKNVKETRAE-------TWRALEELYDEGLCRAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 159 GLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLgSPGakvhfqtkynytteafpDLLNH 238
Cdd:cd19135 142 GVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKG-----------------KALEE 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 239 SVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDL 299
Cdd:cd19135 204 PTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
6-299 |
8.40e-80 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 244.63 E-value: 8.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 6 LLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG--SREELFITTKLPHFGNR 83
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPgvKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 84 PSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKL--DEATCAAATHEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPtgDLNPLTAVPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfqtkynyTTEAFPDLLNHSVV 241
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-------------NLAGLPLLVQHPEV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDifDFTLTDDDMNLLNDL 299
Cdd:cd19118 228 KAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
4-300 |
4.83e-78 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 239.62 E-value: 4.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKL--PHFG 81
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIR---RSGVDRSDIFVTTKLwiSDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NrpSDVEKFIKLSLDKLGLDYLDMYLVHMPFAfkldeatcaaathedgsyiLDFDtDPVLVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19127 78 Y--DKALRGFDASLRRLGLDYVDLYLLHWPVP-------------------NDFD-RTIQAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakVHFQTKYNytTEAFPDLLNHSVV 241
Cdd:cd19127 136 NFTPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGG----VMRYGASG--PTGPGDVLQDPTI 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19127 210 TGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-302 |
6.21e-78 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 239.22 E-value: 6.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 3 FVRLLSGYDMPTVGLGTWQAK-SEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLphfG 81
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEeGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIK---ESGIPREELFITSKV---W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIK---LSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildfdtdpvlvWKEMENQVKSGRTRSI 158
Cdd:cd19157 75 NADQGYDSTLKafeASLERLGLDYLDLYLIHWPVKGKYKET-----------------------WKALEKLYKDGRVRAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 159 GLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLgspgakvhFQTKynytteafpdLLNH 238
Cdd:cd19157 132 GVSNFQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL--------MQGQ----------LLDN 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 239 SVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19157 194 PVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNEN 257
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
9-298 |
3.52e-77 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 237.13 E-value: 3.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGT---W-----QAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWfekGGSREELFITTKLphf 80
Cdd:cd19120 1 GSKIPAIAFGTgtaWyksgdDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES---GVPREDLFITTKV--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 81 GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRSIGL 160
Cdd:cd19120 75 SPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAK------------------EGGPTLAEAWAELEALKDAGLVRSIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 161 SNFNEEQISLIWENAQIKPSNLQVELHAYM--QQKSIRELCKKYNIVITGYSPLgSPgakvhfqtkynyTTEAFPDLLNH 238
Cdd:cd19120 137 SNFRIEDLEELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPL-SP------------LTRDAGGPLDP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 239 sVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLND 298
Cdd:cd19120 204 -VLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-327 |
1.09e-75 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 234.47 E-value: 1.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 11 DMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFGNRPSDVEK 89
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVvRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 90 FIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAathEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQIS 169
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPL---DRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 170 LIWE--NAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHfqtkynytteafpdLLNHSVVQNIAER 247
Cdd:cd19110 160 RLLNkpGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVD--------------LIDDPVIQRIAKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 248 HKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGaagriFNFLFFKGVQDHPHYPFKSE 327
Cdd:cd19110 226 HGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRN-----LRLATFPITENHKDYPFHIE 300
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
9-327 |
1.95e-75 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 234.23 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALK-KWFEKGGSREELFITTKL-PHFGNRpSD 86
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQeKIKEQVVKREDLFIVSKLwCTFHEK-GL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 87 VEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcaAATHEDGSYILDfDTDPVLVWKEMENQVKSGRTRSIGLSNFNEE 166
Cdd:cd19107 80 VKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEL--FPLDESGNVIPS-DTTFLDTWEAMEELVDEGLVKAIGVSNFNHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 167 QISLIWENAQIK--PSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKvhfqtkynYTTEAFPDLLNHSVVQNI 244
Cdd:cd19107 157 QIERILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRP--------WAKPEDPSLLEDPKIKEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 245 AERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGAagRIFNFLFFkgvQDHPHYPF 324
Cdd:cd19107 229 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNW--RACALLSC---SSHKDYPF 303
|
...
gi 1153814477 325 KSE 327
Cdd:cd19107 304 HAE 306
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-324 |
7.18e-74 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 230.07 E-value: 7.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSE----EIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFGNR 83
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTtpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKvKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 84 PSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcaAATHEDGSYILDfDTDPVLVWKEMENQVKSGRTRSIGLSNF 163
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEI--YPRDENGKWLYH-KTNLCATWEALEACKDAGLVKSIGVSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 164 NEEQISLIWENAQIK--PSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVhfqtkynYTTEAFPDLLNHSVV 241
Cdd:cd19109 158 NRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPI-------WVNVSSPPLLEDPLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGAagRIFNFLFFKgvqDHPH 321
Cdd:cd19109 231 NSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNV--RYVELLMWR---DHPE 305
|
...
gi 1153814477 322 YPF 324
Cdd:cd19109 306 YPF 308
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-302 |
3.65e-73 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 227.26 E-value: 3.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 3 FVRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLphFGN 82
Cdd:PRK11565 6 VIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALK---EASVAREELFITTKL--WND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatCAAATHedgsYildfdtdpVLVWKEMENQVKSGRTRSIGLSN 162
Cdd:PRK11565 81 DHKRPREALEESLKKLQLDYVDLYLMHWP---------VPAIDH----Y--------VEAWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 163 FNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVhfqtkynytteafpdlLNHSVVQ 242
Cdd:PRK11565 140 FQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGV----------------FDQKVIR 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 243 NIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:PRK11565 204 DLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQG 263
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-302 |
5.25e-73 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 228.07 E-value: 5.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHFGN 82
Cdd:cd19115 5 VKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGiVKREDLFIVSKLWNTFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFK-LDEATCAAATHEDGSYILDFDTDPVL-VWKEMENQVKSGRTRSIGL 160
Cdd:cd19115 85 DGERVEPICRKQLADWGIDYFDLFLIHFPIALKyVDPAVRYPPGWFYDGKKVEFSNAPIQeTWTAMEKLVDKGLARSIGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 161 SNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGsPGAKVHFQTKynyTTEAFPDLLNHSV 240
Cdd:cd19115 165 SNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PQSFLELDLP---GAKDTPPLFEHDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 241 VQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19115 241 IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIG 302
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-293 |
5.51e-73 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 225.99 E-value: 5.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKwfeKGGSREELFITTKLPHFGNRPSDVE 88
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAA---SGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 89 KFIKLSLDKLGLDYLDMYLVH-----MPFAFKLDeATCAAathedgsyildfdtdpvlvwKEMenqvksGRTRSIGLSNF 163
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHwpnkdVPLAETLG-ALNEA--------------------QEA------GLARHIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 164 NEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpGAkvhfqtkynytteafpdLLNHSVVQN 243
Cdd:cd19140 135 TVALLREAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLAR-GE-----------------VLKDPVLQE 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 244 IAERHKKSTAQVLLRHLLQ-LGIVIIPKSASPERIKSNIDIFDFTLTDDDM 293
Cdd:cd19140 197 IGRKHGKTPAQVALRWLLQqEGVAAIPKATNPERLEENLDIFDFTLSDEEM 247
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
2-301 |
5.96e-73 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 227.50 E-value: 5.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 2 HFVRLLSGYDMPTVGLGTWQA----KSEEIETVVItALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTK 76
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPeevpKSKALEATKL-AIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTvKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 77 LPHFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATcaAATHEDGSYILDfDTDPVLVWKEMENQVKSGRTR 156
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEEL--FPKDENGKLIFD-TVDLCATWEAMEKCKDAGLAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 157 SIGLSNFNEEQISLIWENAQIK--PSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfQTKYNYTTEAFPD 234
Cdd:cd19108 157 SIGVSNFNRRQLEMILNKPGLKykPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGS-------QRDKEWVDQNSPV 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1153814477 235 LLNHSVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDK 301
Cdd:cd19108 230 LLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNR 296
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-302 |
6.56e-73 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 227.71 E-value: 6.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHFGN 82
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGlVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFK---LDEATCAAATHEDGSYIlDFDTDPVL-VWKEMENQVKSGRTRSI 158
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpIEEKYPPGFYCGDGDNF-VYEDVPILdTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 159 GLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGsPGAKVHFQTKYNYTTeafPDLLNH 238
Cdd:cd19113 162 GVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFG-PQSFVELNQGRALNT---PTLFEH 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 239 SVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19113 238 DTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
4-299 |
3.65e-72 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 225.45 E-value: 3.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTW--QAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKL-PH 79
Cdd:cd19119 4 FKLNTGASIPALGLGTAspHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSiKREELFITTKVwPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 FGNRpsdVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAA---THEDGSYILDFDTDPVLVWKEMENQVKSGRTR 156
Cdd:cd19119 84 FYDE---VERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKPftpVNDDGKTRYAASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 157 SIGLSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHFqtkynytteafpdll 236
Cdd:cd19119 161 AIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLK--------------- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 237 NHSVVQnIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIfdFTLTDDDMNLLNDL 299
Cdd:cd19119 226 NPLVKK-IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDI 285
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-303 |
9.73e-72 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 224.36 E-value: 9.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKG-GSREELFITTKLPHFGNRPSDV 87
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGlVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 88 EKFIKLSLDKLGLDYLDMYLVHMPFAFK-LDEATCAAATHEDG-SYILDFDTDPVL-VWKEMENQVKSGRTRSIGLSNFN 164
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyVDPAENYPFLWKDKeLKKFPLEQSPMQeCWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 165 EEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSPGAKVHFQTKYNYTTeafpdLLNHSVVQNI 244
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHFTN-----LLEHPVVKKL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1153814477 245 AERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGA 303
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANA 294
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-302 |
1.11e-71 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 223.16 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKS-EEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLphfGN 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR---ESGVPREEVFVTTKL---WN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 RPSDVEKFIKL---SLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildfdtdpvlvWKEMENQVKSGRTRSIG 159
Cdd:cd19156 75 SDQGYESTLAAfeeSLEKLGLDYVDLYLIHWPVKGKFKDT-----------------------WKAFEKLYKEKKVRAIG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 160 LSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfqtkynytteafPDLLNHS 239
Cdd:cd19156 132 VSNFHEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ------------------GKLLSNP 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 240 VVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19156 194 VLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTD 256
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-302 |
1.78e-71 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 222.42 E-value: 1.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 4 VRLLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKwfeKGGSREELFITTKL--PHFG 81
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAA---SGIPRGELFVTTKLatPDQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSdvEKFIKLSLDKLGLDYLDMYLVHMPFAfkldeatcaaathEDGSYIldfDTdpvlvWKEMENQVKSGRTRSIGLS 161
Cdd:cd19134 80 FTAS--QAACRASLERLGLDYVDLYLIHWPAG-------------REGKYV---DS-----WGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGspgakvhfqtkynytteaFPDLLNHSVV 241
Cdd:cd19134 137 NFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLG------------------VGRLLDNPAV 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKG 302
Cdd:cd19134 199 TAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDG 259
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
12-298 |
6.28e-67 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 211.93 E-value: 6.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFGNRPSDVEKF 90
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKiRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 91 IKLSLDKLGLDYLDMYLVHMPFAFKL-DEATcaaATHEDGSYILDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQIS 169
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPFAFQPgDEQD---PRDANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 170 LIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGspgakvHFQTkynytteafPDLLNHSVVQNIAERHK 249
Cdd:cd19129 163 EIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG------HGME---------PKLLEDPVITAIARRVN 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1153814477 250 KSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIfdFTLTDDDMNLLND 298
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREINE 274
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
6-300 |
7.54e-66 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 207.84 E-value: 7.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 6 LLSGYDMPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKwfeKGGSREELFITTKLPHFGNRPS 85
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAA---SGIPRDELFVTTKLWNDRHDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 86 DVEKFIKLSLDKLGLDYLDMYLVHMPFAFKldeatcaaathedGSYildfdtdpVLVWKEMENQVKSGRTRSIGLSNFNE 165
Cdd:cd19130 81 EPAAAFAESLAKLGLDQVDLYLVHWPTPAA-------------GNY--------VHTWEAMIELRAAGRTRSIGVSNFLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 166 EQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGspgakvhfQTKynytteafpdLLNHSVVQNIA 245
Cdd:cd19130 140 PHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLG--------QGK----------LLGDPPVGAIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1153814477 246 ERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
13-299 |
6.77e-64 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 203.52 E-value: 6.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGG-SREELFITTKLPHFGNRPSDVEKFI 91
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGvKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 92 KLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAatheDGSYILDFDTDPVL-VWKEMENQVKSGRTRSIGLSNFNEEQISL 170
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPR----DDNQIQSLSKKPLEdTWRAMEQCVDEKLTKNIGVSNYSTKLLTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 171 IWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfqtKYNYTTEAFpdlLNHSVVQNIAERHKK 250
Cdd:cd19128 158 LLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGG---------SYGDGNLTF---LNDSELKALATKYNT 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 251 STAQVLLRHLLQL---GIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDL 299
Cdd:cd19128 226 TPPQVIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
15-300 |
2.02e-59 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 192.53 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 15 VGLGTWQ--------AKSEEIETVViTALECGYRHIDTAANYN---NEDAIGKALKKWfekGGSREELFITTKLP----- 78
Cdd:pfam00248 1 IGLGTWQlgggwgpiSKEEALEALR-AALEAGINFIDTAEVYGdgkSEELLGEALKDY---PVKRDKVVIATKVPdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 79 -HFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRS 157
Cdd:pfam00248 77 wPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP----------------------DPDTPIEETWDALEELKKEGKIRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 158 IGLSNFNEEQISLIWENAQIKPSNLQVELHAY--MQQKSIRELCKKYNIVITGYSPLGSPGAKVHFQTKYNYTTEAFPDL 235
Cdd:pfam00248 135 IGVSNFDAEQIEKALTKGKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1153814477 236 LNHSVVQN---------IAERHKKSTAQVLLRHLLQ--LGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLD 300
Cdd:pfam00248 215 LKKGTPLNlealealeeIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
6-301 |
3.53e-57 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 186.67 E-value: 3.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 6 LLSGYDMPTVGLGTWQAKSEEIET--VVITALECGYRHIDTAANYNNEDAIGKALKKWFEKGGS--REELFITTKLPHFG 81
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAKGETyaAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSvkREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKlDEATCAAATHEDGSYIL--DFDTDPVLVWKEMENQVKSGRTRSIG 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAE-KNDQRSPKLGPDGKYVIlkDLTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 160 LSNFNEEQISLIWENAQIKPSNLQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfQTKYNYTTEAFPDllnHS 239
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGS-------QNQVPSTGERVSE---NP 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 240 VVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDftLTDDDMNLLNDLDK 301
Cdd:cd19122 232 TLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
12-293 |
4.72e-55 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 179.86 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKLpHFGN-RPSDVEKF 90
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA---ESGVPRDELFITTKI-WIDNlSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 91 IKLSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedGSYIldfdtdpvlvwKEMENQVKSGRTRSIGLSNFN----EE 166
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPNDEVPV---------EEYI-----------GALAEAKEQGLTRHIGVSNFTiallDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 167 QISLIWENAQIkpSNlQVELHAYMQQKSIRELCKKYNIVITGYSPLGSpgAKVhfqtkynytteafpdlLNHSVVQNIAE 246
Cdd:cd19139 137 AIAVVGAGAIA--TN-QIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY--GKV----------------LDDPVLAAIAE 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1153814477 247 RHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDM 293
Cdd:cd19139 196 RHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDM 242
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-309 |
4.96e-51 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 170.20 E-value: 4.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNNEDAIGKALKkwfEKGGSREELFITTKL--PHFGNrpsdvEK 89
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA---ESGVPRDELFITTKIwiDNLAK-----DK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 90 FI---KLSLDKLGLDYLDMYLVHMPfafkldeatcaaaTHEDGSyildfdtdPVLVWKEMENQVKS-GRTRSIGLSNFNe 165
Cdd:PRK11172 75 LIpslKESLQKLRTDYVDLTLIHWP-------------SPNDEV--------SVEEFMQALLEAKKqGLTREIGISNFT- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 166 eqISLIWEN-AQIKPSNL---QVELHAYMQQKSIRELCKKYNIVITGYSPLgspgakvhfqtkynytteAFPDLLNHSVV 241
Cdd:PRK11172 133 --IALMKQAiAAVGAENIatnQIELSPYLQNRKVVAFAKEHGIHVTSYMTL------------------AYGKVLKDPVI 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 242 QNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLNDLDKGaaGRIFN 309
Cdd:PRK11172 193 ARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRN--GRLVS 258
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
12-297 |
6.56e-51 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 169.72 E-value: 6.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTW---------QAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKKWfekggSREELFITTKLPH 79
Cdd:cd19072 4 VPVLGLGTWgigggmskdYSDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKGF-----DREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 FGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedGSYILDFDTdpvlvWKEMENQVKSGRTRSIG 159
Cdd:cd19072 79 DHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP-----------------NPSIPIEET-----LRAMEELVEEGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 160 LSNFNEEQISLIWENAQ-IKPSNLQVELHAYMQ--QKSIRELCKKYNIVITGYSPLGspgakvhfQTKYNYTTEafpdll 236
Cdd:cd19072 137 VSNFSLEELEEAQSYLKkGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLE--------KGKLSNAKG------ 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 237 nHSVVQNIAERHKKSTAQVLLRHLLQL-GIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19072 203 -SPLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
2-297 |
6.04e-44 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 151.63 E-value: 6.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 2 HFVRLLSGYDMPTVGLGTW------QAKSEEIETVvITALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELF 72
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWymgedpAKRAQEIEAL-RAGIDLGMTLIDTAEMYGDggsEELVGEAIR------GRRDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 73 ITTK-LPHFGNRpSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEaTCAAathedgsyildfdtdpvlvwkeMENQVK 151
Cdd:cd19138 74 LVSKvLPSNASR-QGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAE-TVAA----------------------MEELKK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 152 SGRTRSIGLSNFNEEQISLIWENAQIKP--SNlQVELHayMQQKSIR-EL---CKKYNIVITGYSPLGSPGakvhfqtky 225
Cdd:cd19138 130 EGKIRAWGVSNFDTDDMEELWAVPGGGNcaAN-QVLYN--LGSRGIEyDLlpwCREHGVPVMAYSPLAQGG--------- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 226 nyttEAFPDLLNHSVVQNIAERHKKSTAQVLLRHLLQLGIVI-IPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19138 198 ----LLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
13-297 |
1.96e-41 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 145.83 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQAKS-----------EEIETVVITALECGYRHIDTAANY---NNEDAIGKALKKwfekGGSREELFITTKLP 78
Cdd:cd19093 3 SPLGLGTWQWGDrlwwgygeygdEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKE----LGDRDEVVIATKFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 79 HFGNR--PSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFklDEATCAaathedgsyildfdtdpvlVWKEMENQVKSGRTR 156
Cdd:cd19093 79 PLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPW--YSQIEA-------------------LMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 157 SIGLSNFNEEQISLIWE---NAQIKPSNLQVE---LHAYMQQKSIRELCKKYNIVITGYSPLG--------SPGAKVHFQ 222
Cdd:cd19093 138 AVGVSNYSADQLRRAHKalkERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPPPGG 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 223 TKYNYTTEAFPD---LLNhsVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19093 218 RRRLFGRKNLEKvqpLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-299 |
4.01e-41 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 145.71 E-value: 4.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 1 MHFVRL-LSGYDMPTVGLGTWQ-------AKSEEIETVVITALECGYRHIDTAANYN---NEDAIGKALKKWfekggSRE 69
Cdd:COG0667 1 MEYRRLgRSGLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR-----PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 70 ELFITTKL--------PHFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVL 141
Cdd:COG0667 76 DVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP----------------------DPDTPIEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 142 VWKEMENQVKSGRTRSIGLSNFNEEQISLIWENAQ--IKPSNLQVELHAYMQQ--KSIRELCKKYNIVITGYSPLGS--- 214
Cdd:COG0667 134 TLGALDELVREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGgll 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 215 -----PGAKV--------HFQTKYNytTEAFPDLLnhSVVQNIAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKS 279
Cdd:COG0667 214 tgkyrRGATFpegdraatNFVQGYL--TERNLALV--DALRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEE 289
|
330 340
....*....|....*....|
gi 1153814477 280 NIDIFDFTLTDDDMNLLNDL 299
Cdd:COG0667 290 NLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
9-297 |
2.84e-38 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 136.55 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQ---------AKSEEIETVVITALECGYRHIDTAANY---NNEDAIGKALKKWfekggSREELFITTK 76
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF-----PREDLFIVTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 77 LPHFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFA-FKLDEATCAaathedgsyildfdtdpvlvwkeMENQVKSGRT 155
Cdd:cd19137 76 VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPnIPLEETLSA-----------------------MAEGVRQGLI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 156 RSIGLSNFNEEQISLIWENAQIKPSNLQVELHAY---MQQKSIRELCKKYNIVITGYSPLGSpGAkvhfqtkynytteaf 232
Cdd:cd19137 133 RYIGVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRR-GL--------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1153814477 233 pdLLNHSVVQNIAERHKKSTAQVLLRHLLQL-GIVIIPKSASPERIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19137 197 --EKTNRTLEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-298 |
1.16e-35 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 130.78 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQ---------AKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELFITTKLPHF 80
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALK------GRRDDVVIATKVSPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 81 GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAfkldeatcaaathedgsyilDFDTDPVLvwKEMENQVKSGRTRSIGL 160
Cdd:cd19085 76 NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--------------------DVPLEETM--EALEKLKEEGKIRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 161 SNFNEEQISLIWENAQIK----PSNL---QVElhaymqqKSIRELCKKYNIVITGYSPLG--------SPGAKV------ 219
Cdd:cd19085 134 SNFGPAQLEEALDAGRIDsnqlPYNLlwrAIE-------YEILPFCREHGIGVLAYSPLAqglltgkfSSAEDFppgdar 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 220 -----HFQTKYNYTTEAFPDLLNHsvvqnIAERHKKSTAQVLLRHLL-QLGIV-IIPKSASPERIKSNIDIFDFTLTDDD 292
Cdd:cd19085 207 trlfrHFEPGAEEETFEALEKLKE-----IADELGVTMAQLALAWVLqQPGVTsVIVGARNPEQLEENAAAVDLELSPSV 281
|
....*.
gi 1153814477 293 MNLLND 298
Cdd:cd19085 282 LERLDE 287
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
1.36e-32 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 122.63 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQ---------AKSEEIETVViTALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELFITTKL-PH 79
Cdd:cd19084 5 SRIGLGTWAiggtwwgevDDQESIEAIK-AAIDLGINFFDTAPVYGFghsEEILGKALK------GRRDDVVIATKCgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 FGN--------RPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATCAAAThedgsyildfdtdpvlvWKEMENQVK 151
Cdd:cd19084 78 WDGgkgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP-----DPNTPIEET-----------------AEALEKLKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 152 SGRTRSIGLSNFNEEQISLIWENAQIkpSNLQVELHAYMQQ--KSIRELCKKYNIVITGYSPL------GSPGAKVHF-- 221
Cdd:cd19084 136 EGKIRYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLaqglltGKYKKEPTFpp 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 222 ----QTKYNYTTEAFPDLLNH-SVVQNIAERHKKSTAQVLLRHLL-QLGI-VIIPKSASPERIKSNIDIFDFTLTDDDMN 294
Cdd:cd19084 214 ddrrSRFPFFRGENFEKNLEIvDKLKEIAEKYGKSLAQLAIAWTLaQPGVtSAIVGAKNPEQLEENAGALDWELTEEELK 293
|
...
gi 1153814477 295 LLN 297
Cdd:cd19084 294 EID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
13-282 |
2.21e-31 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 117.62 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQAKS----EEIETVVITALECGYRHIDTAANYNN---EDAIGKalkkWFEKGGSREELFITTKLPH------ 79
Cdd:cd06660 1 SRLGLGTMTFGGdgdeEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGR----WLKGRGNRDDVVIATKGGHppggdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 --FGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRS 157
Cdd:cd06660 77 srSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD----------------------DPSTPVEETLEALNELVREGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 158 IGLSNFNEEQISLIWENAQ----IKPSNLQVE---LHAYMQQKSIRELCKKYNIVITGYSPLGSpGAkvhfqtkynytte 230
Cdd:cd06660 135 IGVSNWSAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR-GP------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 231 afpdllnhsvvqniaerhkkstAQVLLRHLLQ--LGIVIIPKSASPERIKSNID 282
Cdd:cd06660 201 ----------------------AQLALAWLLSqpFVTVPIVGARSPEQLEENLA 232
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-299 |
9.34e-29 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 113.76 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTW--QAKSEE-IETVVITALECGYRHIDTAANY-NNEDAIGKALKKWfekggsREELFITTKLPHFGNRP 84
Cdd:COG1453 10 GLEVSVLGFGGMrlPRKDEEeAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP------RDKVILATKLPPWVRDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 85 SDVEKFIKLSLDKLGLDYLDMYLVHMPfafkLDEATCAAATHEDGsyILDFdtdpvlvwkeMENQVKSGRTRSIGLSNFN 164
Cdd:COG1453 84 EDMRKDLEESLKRLQTDYIDLYLIHGL----NTEEDLEKVLKPGG--ALEA----------LEKAKAEGKIRHIGFSTHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 165 EEQI------SLIWENAQIkPSNlqvelhaYMQQKSIR-----ELCKKYNIVITGYSPLGspGAKvhfqtkynytteafp 233
Cdd:COG1453 148 SLEVikeaidTGDFDFVQL-QYN-------YLDQDNQAgeealEAAAEKGIGVIIMKPLK--GGR--------------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 234 dLLNHS-VVQNIAErHKKSTAQVLLRHLLQL-GI-VIIPKSASPERIKSNIDIFD--FTLTDDDMNLLNDL 299
Cdd:COG1453 203 -LANPPeKLVELLC-PPLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-299 |
5.33e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 99.67 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGTW-------------QAKSEEIETVvITALECGYRHIDTAANY---NNEDAIGKALKKWfekggsREELFITTKL 77
Cdd:cd19102 3 TIGLGTWaiggggwgggwgpQDDRDSIAAI-RAALDLGINWIDTAAVYglgHSEEVVGRALKGL------RDRPIVATKC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 ---------PHFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMEN 148
Cdd:cd19102 76 gllwdeegrIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWP----------------------DPDEPIEEAWGALAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 149 QVKSGRTRSIGLSNFNEEQISLIwenAQIKP-SNLQVELHAYMQ--QKSIRELCKKYNIVITGYSPLGS----------- 214
Cdd:cd19102 134 LKEEGKVRAIGVSNFSVDQMKRC---QAIHPiASLQPPYSLLRRgiEAEILPFCAEHGIGVIVYSPMQSglltgkmtper 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 215 ----PGAKVH-----FQTKYNYTTEAFPDLLnhsvvQNIAERHKKSTAQVLLRHLLQLGIVI--IPKSASPERIKSNIDI 283
Cdd:cd19102 211 vaslPADDWRrrspfFQEPNLARNLALVDAL-----RPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQIDETVGA 285
|
330
....*....|....*.
gi 1153814477 284 FDFTLTDDDMNLLNDL 299
Cdd:cd19102 286 ADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
16-289 |
8.29e-24 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 98.78 E-value: 8.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 16 GLGTWQAKSEEIETVVITALECGYRHIDTA---ANYNNEDAIGKALKKWfekGGSREELFITTK---LPHFGNRPSDVEK 89
Cdd:cd19092 15 RLADWGESAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALALN---PGLREKIEIQTKcgiRLGDDPRPGRIKH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 90 F----------IKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRSIG 159
Cdd:cd19092 92 YdtskehilasVEGSLKRLGTDYLDLLLLHRP----------------------DPLMDPEEVAEAFDELVKSGKVRYFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 160 LSNFNEEQISL--------IWENaQIKPSNlqveLHAYMQQKSIRELCKKYNIVITGYSPLGspGAKVhfqtkYNYTTEA 231
Cdd:cd19092 150 VSNFTPSQIELlqsyldqpLVTN-QIELSL----LHTEAIDDGTLDYCQLLDITPMAWSPLG--GGRL-----FGGFDER 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 232 FPDLLNhsVVQNIAERHKKSTAQVLLRHLLQL--GIVIIPKSASPERIKSNIDIFDFTLT 289
Cdd:cd19092 218 FQRLRA--ALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-297 |
1.19e-22 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 96.11 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGT----------WQAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKKWfekgGSREELFIT 74
Cdd:cd19079 8 SGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEF----APRDEVVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 75 TKL-PHFGNRPSD-------VEKFIKLSLDKLGLDYLDMYLVHMpfafkldeatcaaathedgsyiLDFDTdPVlvwKE- 145
Cdd:cd19079 84 TKVyFPMGDGPNGrglsrkhIMAEVDASLKRLGTDYIDLYQIHR----------------------WDYET-PI---EEt 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 146 ME---NQVKSGRTRSIGLSNFNEEQIsliwENAQ--------IKPSNLQvELHAYMQQKSIRE---LCKKYNIVITGYSP 211
Cdd:cd19079 138 LEalhDVVKSGKVRYIGASSMYAWQF----AKALhlaekngwTKFVSMQ-NHYNLLYREEEREmipLCEEEGIGVIPWSP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 212 LGS--------PGAKVHFQT------KYNYTTEAFPDLLNhsVVQNIAERHKKSTAQVLLRHLLQLGIVIIP--KSASPE 275
Cdd:cd19079 213 LARgrlarpwgDTTERRRSTtdtaklKYDYFTEADKEIVD--RVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLE 290
|
330 340
....*....|....*....|..
gi 1153814477 276 RIKSNIDIFDFTLTDDDMNLLN 297
Cdd:cd19079 291 HLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
8-299 |
1.36e-21 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 92.87 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQA---------KSEEIETVVITALECGYRHIDTAANY---NNEDAIGKALKkwfekGGSREELFITT 75
Cdd:cd19083 7 SDIDVNPIGLGTNAVgghnlypnlDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK-----EYNRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 76 KLPH--------FGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaatheDGSYILDfdtDPVLVWKEME 147
Cdd:cd19083 82 KGAHkfggdgsvLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP----------------DGETPKA---EAVGALQELK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 148 nqvKSGRTRSIGLSNFNEEQIsliweNAQIKPSNLQVELHAY--MQQ---KSIRELCKKYNIVITGYSPLGSP--GAKVH 220
Cdd:cd19083 143 ---DEGKIRAIGVSNFSLEQL-----KEANKDGYVDVLQGEYnlLQReaeEDILPYCVENNISFIPYFPLASGllAGKYT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 221 FQTKYN----------YTTEAFPDLLnHSV--VQNIAERHKKSTAQVLLRHLL-QLGI-VIIPKSASPERIKSNIDIFDF 286
Cdd:cd19083 215 KDTKFPdndlrndkplFKGERFSENL-DKVdkLKSIADEKGVTVAHLALAWYLtRPAIdVVIPGAKRAEQVIDNLKALDV 293
|
330
....*....|...
gi 1153814477 287 TLTDDDMNLLNDL 299
Cdd:cd19083 294 TLTEEEIAFIDAL 306
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
15-293 |
1.37e-21 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 92.76 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 15 VGLGTWQA---------KSEEIETVViTALECGYRHIDTAANYN---NEDAIGKALKKwfekGGSREELFITTKL----- 77
Cdd:cd19148 7 IALGTWAIggwmwggtdEKEAIETIH-KALDLGINLIDTAPVYGfglSEEIVGKALKE----YGKRDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 ----PHFGNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATCAAATHEdgsyildfdtdpvlvwkEMENQVKSG 153
Cdd:cd19148 82 eggeVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWP-----DPLVPIEETAE-----------------ALKELLDEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 154 RTRSIGLSNFNEEQISLIWENAQIK----PSNLqVELHAymqQKSIRELCKKYNIVITGYSPL--GSPGAKVHFQTKYN- 226
Cdd:cd19148 140 KIRAIGVSNFSPEQMETFRKVAPLHtvqpPYNL-FEREI---EKDVLPYARKHNIVTLAYGALcrGLLSGKMTKDTKFEg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 227 ---------YTTEAFPDLLnhSVVQNI----AERHKKSTAQVLLRHLL-QLGIVIIPKSA-SPERIKSNIDIFDFTLTDD 291
Cdd:cd19148 216 ddlrrtdpkFQEPRFSQYL--AAVEELdklaQERYGKSVIHLAVRWLLdQPGVSIALWGArKPEQLDAVDEVFGWSLNDE 293
|
..
gi 1153814477 292 DM 293
Cdd:cd19148 294 DM 295
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
14-297 |
1.98e-21 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 92.30 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLG----TWQAKSEEIET---VVITALECGYRHIDTAANYNNEDAIG--KALKKWFEK-GGSREELFITTK------- 76
Cdd:cd19077 7 PIGLGlmglTWRPNPTPDEEafeTMKAALDAGSNLWNGGEFYGPPDPHAnlKLLARFFRKyPEYADKVVLSVKggldpdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 77 LPHFGnRPSDVEKFIKLSLDKLG-LDYLDMYlvhmpfafkldeaTCAAathedgsyiLDFDTDPVLVWKEMENQVKSGRT 155
Cdd:cd19077 87 LRPDG-SPEAVRKSIENILRALGgTKKIDIF-------------EPAR---------VDPNVPIEETIKALKELVKEGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 156 RSIGLSNFNEEQISLIwenAQIKP-SNLQVELHAYMQ---QKSIRELCKKYNIVITGYSPLGS--------------PGA 217
Cdd:cd19077 144 RGIGLSEVSAETIRRA---HAVHPiAAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRglltgriksladipEGD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 218 KVHFQTKYNytteafPDLLNH-----SVVQNIAERHKKSTAQVLLRHLLQLG---IVIIPKSASPERIKSNIDIFDFTLT 289
Cdd:cd19077 221 FRRHLDRFN------GENFEKnlklvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELT 294
|
....*...
gi 1153814477 290 DDDMNLLN 297
Cdd:cd19077 295 DEELKEIN 302
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-291 |
3.32e-21 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 91.50 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGTW-----QAKSEEIETVVITALECGYRHIDTAANYNNEDA---IGKALKKWfekggSREELFITTKLpHFGNRPS 85
Cdd:cd19074 6 ELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAeevLGKALKGW-----PRESYVISTKV-FWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 86 DVEK---------FIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTR 156
Cdd:cd19074 80 PNDRglsrkhifeSIHASLKRLQLDYVDIYYCHRY----------------------DPETPLEETVRAMDDLIRQGKIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 157 SIGLSNFNEEQI----SLIWENAQIKPSNLQVELHaYMQQKS---IRELCKKYNIVITGYSPL-----------GSP--- 215
Cdd:cd19074 138 YWGTSEWSAEQIaeahDLARQFGLIPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLaqglltgkyrdGIPpps 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 216 -GAKVHFQTKY---NYTTEAFPDLLNHsvVQNIAERHKKSTAQVLLRHLLQ---LGIVIIPKSaSPERIKSNIDIFDFTL 288
Cdd:cd19074 217 rSRATDEDNRDkkrRLLTDENLEKVKK--LKPIADELGLTLAQLALAWCLRnpaVSSAIIGAS-RPEQLEENVKASGVKL 293
|
...
gi 1153814477 289 TDD 291
Cdd:cd19074 294 SPE 296
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
8-296 |
3.95e-21 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 91.51 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLG----TW---QAKSEEIETVVITALECGYRHIDTA---ANYNNEDAIGKALKKWfekggsREELFITTKl 77
Cdd:cd19076 8 QGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTAdmyGPGTNEELLGKALKDR------RDEVVIATK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 phFG-------------NRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATCAAAThedgsyildfdtdpvlvWK 144
Cdd:cd19076 81 --FGivrdpgsgfrgvdGRPEYVRAACEASLKRLGTDVIDLYYQHRV-----DPNVPIEET-----------------VG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 145 EMENQVKSGRTRSIGLSNFNEEQISliwENAQIKP-SNLQVELHAYMQ--QKSIRELCKKYNIVITGYSPLG-------- 213
Cdd:cd19076 137 AMAELVEEGKVRYIGLSEASADTIR---RAHAVHPiTAVQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLGrgfltgai 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 214 SPGAKVH----FQTKYNYTTEAFP-DLLNHSVVQNIAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKSNIDIFDF 286
Cdd:cd19076 214 KSPEDLPeddfRRNNPRFQGENFDkNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDV 293
|
330
....*....|
gi 1153814477 287 TLTDDDMNLL 296
Cdd:cd19076 294 VLTPEELAEI 303
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
15-289 |
1.70e-20 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 88.81 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 15 VGLGTWQ----------AKSEEIETVVITALECGYRHIDTAANYN---NEDAIGKALKKWfekggsREELFITTKLPHF- 80
Cdd:cd19088 4 LGYGAMRltgpgiwgppADREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPY------PDDVVIATKGGLVr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 81 --------GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPFAFkldeatcaaathedgsyiLDFDtDPVLVWKEMENQvks 152
Cdd:cd19088 78 tgpgwwgpDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPK------------------VPFE-EQLGALAELQDE--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 153 GRTRSIGLSNFNEEQIsliwENAQIKPSNLQVELH---AYMQQKSIRELCKKYNIVITGYSPLGSpgakvhfqtkynytt 229
Cdd:cd19088 136 GLIRHIGLSNVTVAQI----EEARAIVRIVSVQNRynlANRDDEGVLDYCEAAGIAFIPWFPLGG--------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 230 eaFPDLLNHSVVQNIAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKSNIDIFDFTLT 289
Cdd:cd19088 197 --GDLAQPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
23-298 |
1.19e-19 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 87.29 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 23 KSEEIEtVVITALECGYRHIDTAANY---NNEDAIGKALKkwfekgGSREELFITTKL-PHFGN----------RPSDVE 88
Cdd:cd19078 24 KEEMIE-LIRKAVELGITFFDTAEVYgpyTNEELVGEALK------PFRDQVVIATKFgFKIDGgkpgplgldsRPEHIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 89 KFIKLSLDKLGLDYLDMYLVHMpfafkldeatcaaathedgsyiLDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQI 168
Cdd:cd19078 97 KAVEGSLKRLQTDYIDLYYQHR----------------------VDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 169 sliwENA-QIKP-SNLQVELH--AYMQQKSIRELCKKYNIVITGYSPLGSP--GAKVHFQTKYN----------YTTEAF 232
Cdd:cd19078 155 ----RRAhAVCPvTAVQSEYSmmWREPEKEVLPTLEELGIGFVPFSPLGKGflTGKIDENTKFDegddraslprFTPEAL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 233 P------DLLNHsvvqnIAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKSNIDIFDFTLTDDDMNLLND 298
Cdd:cd19078 231 EanqalvDLLKE-----FAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
8-296 |
1.63e-19 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 87.33 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQA----------KSEEIETVVItALECGYRHIDTAANYNN---EDAIGKALKK-------------- 60
Cdd:cd19149 7 SGIEASVIGLGTWAIgggpwwggsdDNESIRTIHA-ALDLGINLIDTAPAYGFghsEEIVGKAIKGrrdkvvlatkcglr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 61 WFEKGGSreELFITTKLPHFGN-RPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATCAAAThedgsyildfdtdp 139
Cdd:cd19149 86 WDREGGS--FFFVRDGVTVYKNlSPESIREEVEQSLKRLGTDYIDLYQTHWQ-----DVETPIEET-------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 140 vlvWKEMENQVKSGRTRSIGLSNFNEEQISlIWENA------QIKPSNLQVELhaymqQKSIRELCKKYNIVITGYSPL- 212
Cdd:cd19149 145 ---MEALEELKRQGKIRAIGASNVSVEQIK-EYVKAgqldiiQEKYSMLDRGI-----EKELLPYCKKNNIAFQAYSPLe 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 213 -----GSPGAKVHFQTKYNYTTEAFPDLLNHSVVQN-------IAERHKKSTAQVLLRHLL-QLGIVIIPKSA-SPERIK 278
Cdd:cd19149 216 qglltGKITPDREFDAGDARSGIPWFSPENREKVLAllekwkpLCEKYGCTLAQLVIAWTLaQPGITSALCGArKPEQAE 295
|
330
....*....|....*...
gi 1153814477 279 SNIDIFDFTLTDDDMNLL 296
Cdd:cd19149 296 ENAKAGDIRLSAEDIATM 313
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
9-292 |
2.06e-19 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 87.11 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTW-------QAKSEEIETVVIT-ALECGYRHIDTAANY-NNEDAIGKalkkWFEKG-GSREELFITTKlp 78
Cdd:cd19144 10 GPSVPALGFGAMglsafygPPKPDEERFAVLDaAFELGCTFWDTADIYgDSEELIGR----WFKQNpGKREKIFLATK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 79 hFGNR-------------PSDVEKFIKLSLDKLGLDYLDMYLVHmpfafKLDEATcaaathedgsyildfdtdPV-LVWK 144
Cdd:cd19144 84 -FGIEknvetgeysvdgsPEYVKKACETSLKRLGVDYIDLYYQH-----RVDGKT------------------PIeKTVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 145 EMENQVKSGRTRSIGLSNFNEEQISliwENAQIKP-SNLQVE-----LHAYMQQKSIRELCKKYNIVITGYSPLG----- 213
Cdd:cd19144 140 AMAELVQEGKIKHIGLSECSAETLR---RAHAVHPiAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLGrgflt 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 214 ----SPG--AKVHFQTKY-NYTTEAFPDllNHSVV---QNIAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKSNI 281
Cdd:cd19144 217 gairSPDdfEEGDFRRMApRFQAENFPK--NLELVdkiKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENL 294
|
330
....*....|.
gi 1153814477 282 DIFDFTLTDDD 292
Cdd:cd19144 295 GALKVKLTEEE 305
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-161 |
2.29e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 85.71 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGTWQAKSEEIEtVVITALECGYRHIDTAANY---NNEDAIGKALKkwfekGGSREELFITTK--LPHFGNR 83
Cdd:cd19105 10 GLKVSRLGFGGGGLPRESPE-LLRRALDLGINYFDTAEGYgngNSEEIIGEALK-----GLRRDKVFLATKasPRLDKKD 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 84 PSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathEDGSYILDFdtDPVLvwKEMENQVKSGRTRSIGLS 161
Cdd:cd19105 84 KAELLKSVEESLKRLQTDYIDIYQLHGV---------------DTPEERLLN--EELL--EALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
8-297 |
1.59e-18 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 84.19 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGT----WQAKSEEIETVVITALECGYRHIDTAANYNN----------EDAIGKalkkWFEKGGSREELFI 73
Cdd:cd19081 5 TGLSVSPLCLGTmvfgWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnaggesETIIGR----WLKSRGKRDRVVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 74 TTKL--PHFGNRP----SDVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATCAAATHEdgsyildfdtdpvlvwkEME 147
Cdd:cd19081 81 ATKVgfPMGPNGPglsrKHIRRAVEASLRRLQTDYIDLYQAHWD-----DPATPLEETLG-----------------ALN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 148 NQVKSGRTRSIGLSNFNEEQISLIWENAQ----IKPSNLQVELHAYMQQ---KSIRELCKKYNIVITGYSPLGS------ 214
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEYNLVDREsfeGELLPLCREEGIGVIPYSPLAGgfltgk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 215 --PGAKVhfqTKYNYTTEAFPDLLN------HSVVQNIAERHKKSTAQVLLRHLLQ---LGIVIIpkSA-SPERIKSNID 282
Cdd:cd19081 219 yrSEADL---PGSTRRGEAAKRYLNerglriLDALDEVAAEHGATPAQVALAWLLArpgVTAPIA--GArTVEQLEDLLA 293
|
330
....*....|....*
gi 1153814477 283 IFDFTLTDDDMNLLN 297
Cdd:cd19081 294 AAGLRLTDEEVARLD 308
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-214 |
1.82e-18 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 82.91 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 15 VGLGTWQ--------AKSEEIETVVITALECGYRHIDTAANY---NNEDAIGKALKkwfekgGSREELFITTKLPHFGN- 82
Cdd:cd19086 6 IGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALK------GRRDKVVIATKFGNRFDg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 --------RPSDVEKFIKLSLDKLGLDYLDMYLVHMPFafkldeatcaaathedgsyILDFDTDPvlVWKEMENQVKSGR 154
Cdd:cd19086 80 gperpqdfSPEYIREAVEASLKRLGTDYIDLYQLHNPP-------------------DEVLDNDE--LFEALEKLKQEGK 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 155 TRSIGLSNFNEEQISLIWENAQIkpSNLQVELHAYMQQ--KSIRELCKKYNIVITGYSPLGS 214
Cdd:cd19086 139 IRAYGVSVGDPEEALAALRRGGI--DVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
34-161 |
3.29e-18 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 82.61 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 34 ALECGYRHIDTAANYNN---EDAIGKALKKwfekgGSREELFITTKLPHFG-NRPSDVEKFIKLSLDKLGLDYLDMYLVH 109
Cdd:cd19096 30 AIDAGINYFDTAYGYGGgksEEILGEALKE-----GPREKFYLATKLPPWSvKSAEDFRRILEESLKRLGVDYIDFYLLH 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 110 MpfafkLDEATCAAATHEDGsyildfdtdpvlVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19096 105 G-----LNSPEWLEKARKGG------------LLEFLEKAKKEGLIRHIGFS 139
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
14-297 |
4.59e-18 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 83.04 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGT---WQAKSEEIETVVITALECGYRHIDTAANYNNEDAiGKALKKWFEkgGSREELFITTKL--------PHF-G 81
Cdd:cd19080 17 TMTFGTewgWGADREEARAMFDAYVEAGGNFIDTANNYTNGTS-ERLLGEFIA--GNRDRIVLATKYtmnrrpgdPNAgG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19080 94 NHRKNLRRSVEASLRRLQTDYIDLLYVHAW----------------------DFTTPVEEVMRALDDLVRAGKVLYVGIS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 162 NFNEEQISLIWENAQIK----PSNLQVELHayMQQKSI-REL---CKKYNIVITGYSPLGSpGAkvhFQTKYN------- 226
Cdd:cd19080 152 DTPAWVVARANTLAELRgwspFVALQIEYS--LLERTPeRELlpmARALGLGVTPWSPLGG-GL---LTGKYQrgeegra 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 227 ----YTTEAFPDLLNHS-----VVQNIAERHKKSTAQVLLRHLLQLGIVIIP--KSASPERIKSNIDIFDFTLTDDDMNL 295
Cdd:cd19080 226 geakGVTVGFGKLTERNwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLAR 305
|
..
gi 1153814477 296 LN 297
Cdd:cd19080 306 LD 307
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-261 |
5.06e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 83.14 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGTWQ-----AKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKKWFEKGG-SREELFITTK---LPHFG 81
Cdd:cd19099 5 SLGLGTYRgdsddETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGiKRDEVVIVTKagyIPGDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKF------------------------------IKLSLDKLGLDYLDMYLVHMPFAFKLdeatcaaatHEDGSY 131
Cdd:cd19099 85 DEPLRPLKYleeklgrglidvadsaglrhcispayledqIERSLKRLGLDTIDLYLLHNPEEQLL---------ELGEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 132 ILDFDTDpvlVWKEMENQVKSGRTRSIGLS-------------NFNEEQISLIWENAQIKPSNL---QVELHAYMQQ--- 192
Cdd:cd19099 156 FYDRLEE---AFEALEEAVAEGKIRYYGIStwdgfrappalpgHLSLEKLVAAAEEVGGDNHHFkviQLPLNLLEPEalt 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153814477 193 ---------KSIRELCKKYNIVITGYSPLGspgakvhfqtkynytteAFPDLLNHSVVQNIAERHKKSTAQVLLRHLL 261
Cdd:cd19099 233 ekntvkgeaLSLLEAAKELGLGVIASRPLN-----------------QGQLLGELRLADLLALPGGATLAQRALQFAR 293
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-297 |
7.85e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 82.26 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQ--------AKSEEIETVVITALECGYRHIDTAANYNN-EDAIGKALKKWFEKGGSREELFITTKLPHFGN 82
Cdd:cd19101 2 ISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKRLRRERDAADDVQIHTKWVPDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 83 R----PSDVEKFIKLSLDKLGLDYLDMYLVHMpfafkldeatcaaATHEDGSYiLDfdtdpVLVWkeMENQVKSGRTRSI 158
Cdd:cd19101 82 EltmtRAYVEAAIDRSLKRLGVDRLDLVQFHW-------------WDYSDPGY-LD-----AAKH--LAELQEEGKIRHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 159 GLSNFNEEQISLIWEnAQIKPSNLQVELHAYMQ--QKSIRELCKKYNIVITGYSPLG------------SPGAKVHF--- 221
Cdd:cd19101 141 GLTNFDTERLREILD-AGVPIVSNQVQYSLLDRrpENGMAALCEDHGIKLLAYGTLAggllsekylgvpEPTGPALEtrs 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 222 QTKYNYTTEA------FPDLLnhSVVQNIAERHKKSTAQVLLRHLLQ---LGIVIIPKSASpERIKSNIDIFDFTLTDDD 292
Cdd:cd19101 220 LQKYKLMIDEwggwdlFQELL--RTLKAIADKHGVSIANVAVRWVLDqpgVAGVIVGARNS-EHIDDNVRAFSFRLDDED 296
|
....*
gi 1153814477 293 MNLLN 297
Cdd:cd19101 297 RAAID 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
25-299 |
1.04e-16 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 79.19 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 25 EEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELFITTKlphFGNRPSD-----------VEKF 90
Cdd:cd19091 39 EEADRLVDIALDAGINFFDTADVYSEgesEEILGKALK------GRRDDVLIATK---VRGRMGEgpndvglsrhhIIRA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 91 IKLSLDKLGLDYLDMYLVHmpfAFklDEATcaaathedgsyildfdtdPVL-VWKEMENQVKSGRTRSIGLSNFNEEQI- 168
Cdd:cd19091 110 VEASLKRLGTDYIDLYQLH---GF--DALT------------------PLEeTLRALDDLVRQGKVRYIGVSNFSAWQIm 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 169 ---SLIWENAQIKPSNLQV--ELHAYMQQKSIRELCKKYNIVITGYSPLG--------SPGAKVHFQTKYNYTTEAFPDL 235
Cdd:cd19091 167 kalGISERRGLARFVALQAyySLLGRDLEHELMPLALDQGVGLLVWSPLAggllsgkyRRGQPAPEGSRLRRTGFDFPPV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 236 ---LNHSVV---QNIAERHKKSTAQVLLRHLLQ---LGIVIIPKSaSPERIKSNIDIFDFTLTDDDMNLLNDL 299
Cdd:cd19091 247 dreRGYDVVdalREIAKETGATPAQVALAWLLSrptVSSVIIGAR-NEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-161 |
2.24e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 77.14 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGT---WQAKSEEIETVVITALECGYRHIDTAANYNN-EDAIGKALKkwfekgGSREELFITTKlphFGNRPSD-V 87
Cdd:cd19100 12 SRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALK------GRRDKVFLATK---TGARDYEgA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 88 EKFIKLSLDKLGLDYLDMYLVHMPfafkLDEATCAAATHEDGsyildfdtdpvlVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLHAV----DTEEDLDQVFGPGG------------ALEALLEAKEEGKIRFIGIS 140
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
13-166 |
2.43e-16 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 77.28 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQAKS-------EEIETVVITALECGYRHIDTAANY-NNEDAIGKALKkwfekGGSREELFITTKL-PHFGNR 83
Cdd:cd19095 1 SVLGLGTSGIGRvwgvpseAEAARLLNTALDLGINLIDTAPAYgRSEERLGRALA-----GLRRDDLFIATKVgTHGEGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 84 -------PSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyILDFDTDPVLvwKEMENQVKSGRTR 156
Cdd:cd19095 76 rdrkdfsPAAIRASIERSLRRLGTDYIDLLQLHGP--------------------SDDELTGEVL--ETLEDLKAAGKVR 133
|
170
....*....|
gi 1153814477 157 SIGLSNFNEE 166
Cdd:cd19095 134 YIGVSGDGEE 143
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-299 |
2.84e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 77.76 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 12 MPTVGLGTWQAKS---------------EEIETVVITALECGYRHIDTAANY---NNEDAIGKALKKWfekggSREELFI 73
Cdd:cd19103 4 LPKIALGTWSWGSggaggdqvfgnhldeDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKRY-----PREDYII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 74 TTKL-PHF-GNRPSDVEKFIKLSLDKLGLDYLDMYLVHMPfafkldeatcaaathedgsyildfdTDpVLVW-KEMENQV 150
Cdd:cd19103 79 STKFtPQIaGQSADPVADMLEGSLARLGTDYIDIYWIHNP-------------------------AD-VERWtPELIPLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 151 KSGRTRSIGLSNFNEEQISL---IWENAQIKPSNLQVE---LHAYMQQKSIRELCKKYNIVITGYS-------------- 210
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHyslLYRSSEEAGILDYCKENGITFFAYMvleqgalsgkydtk 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 211 ---PLGSPGAKvhfqtKYNYTTEAFPDLLNhsVVQNIAERHKKSTAQVLLRHLLQLGIVIIPKSASPERIKSNIDIFDFT 287
Cdd:cd19103 213 hplPEGSGRAE-----TYNPLLPQLEELTA--VMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASIT 285
|
330
....*....|..
gi 1153814477 288 LTDDDMNLLNDL 299
Cdd:cd19103 286 LTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-182 |
2.00e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 74.87 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 16 GLGTWQ-------AKS------EEIETVVITALECGYRHIDTAANYNN-EDAIGKALKKWfekggsrEELFITTKLPHFG 81
Cdd:cd19097 4 ALGTAQfgldygiANKsgkpseKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL-------DKFKIITKLPPLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 82 NRPSDVEKFIKL----SLDKLGLDYLDMYLVHmpfafkldeatcaaatheDGSYILDFDTDpvlVWKEMENQVKSGRTRS 157
Cdd:cd19097 77 EDKKEDEAAIEAsveaSLKRLKVDSLDGLLLH------------------NPDDLLKHGGK---LVEALLELKKEGLIRK 135
|
170 180
....*....|....*....|....*....
gi 1153814477 158 IGLSNFNEEQISLIWENAQIK----PSNL 182
Cdd:cd19097 136 IGVSVYSPEELEKALESFKIDiiqlPFNI 164
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-282 |
3.98e-14 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 71.82 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGTWQAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKAL--KKWFEkggsreelfITTKLPHF---GNRPS 85
Cdd:cd19075 9 TFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELGlgERGFK---------IDTKANPGvggGLSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 86 DVEKFIKLSLDKLGLDYLDMYLVHMPfafklDEATcaaathedgsyildfdtdPVLVW-KEMENQVKSGRTRSIGLSNFN 164
Cdd:cd19075 80 NVRKQLETSLKRLKVDKVDVFYLHAP-----DRST------------------PLEETlAAIDELYKEGKFKEFGLSNYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 165 EEQISLIW----ENAQIKPS------NL---QVElhaymqqksiREL---CKKYNIVITGYSPLG--------------- 213
Cdd:cd19075 137 AWEVAEIVeickENGWVLPTvyqgmyNAitrQVE----------TELfpcLRKLGIRFYAYSPLAggfltgkykysedka 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 214 --------SPGAKVhFQTKYNytTEAFPDLLNhsVVQNIAERHKKSTAQVLLRHLL-------QLGIVIIPKSASPERIK 278
Cdd:cd19075 207 gggrfdpnNALGKL-YRDRYW--KPSYFEALE--KVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLE 281
|
....
gi 1153814477 279 SNID 282
Cdd:cd19075 282 ENLA 285
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
13-161 |
2.21e-13 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 69.12 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGT------WQAKS-EEIETVVITALECGYRHIDTAANYNN-EDAIGKALKKWfekggSREELFITTKLphfGNRP 84
Cdd:cd19090 1 SALGLGTaglggvFGGVDdDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAEL-----PREPLVLSTKV---GRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 85 SDVEKF--------IKLSLDKLGLDYLDMYLVHMPFAFKLDEAtcaaathedgsyildFDTDPVLvwKEMENQVKSGRTR 156
Cdd:cd19090 73 EDTADYsadrvrrsVEESLERLGRDRIDLLMIHDPERVPWVDI---------------LAPGGAL--EALLELKEEGLIK 135
|
....*
gi 1153814477 157 SIGLS 161
Cdd:cd19090 136 HIGLG 140
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
33-281 |
7.43e-13 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 67.96 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 33 TALECGYRHIDTAANYNNEDAIG---KALKKWFEKGGSREELFITTKLPHFG------NR--PSDVEKFIKLSLDKLGLD 101
Cdd:cd19082 25 AFVELGGNFIDTARVYGDWVERGaseRVIGEWLKSRGNRDKVVIATKGGHPDledmsrSRlsPEDIRADLEESLERLGTD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 102 YLDMYLVHMpfafklDEATCAAathedgSYILDfdtdpvlvwkEMENQVKSGRTRSIGLSNFNEEQI------------- 168
Cdd:cd19082 105 YIDLYFLHR------DDPSVPV------GEIVD----------TLNELVRAGKIRAFGASNWSTERIaeanayakahglp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 169 -----SLIWENAQIKPSNLQVELHAYMQQKSiRELCKKYNIVITGYSPLGS--------PGAKVHFQTKYNYTTEAfpdl 235
Cdd:cd19082 163 gfaasSPQWSLARPNEPPWPGPTLVAMDEEM-RAWHEENQLPVFAYSSQARgffskraaGGAEDDSELRRVYYSEE---- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1153814477 236 lNH---SVVQNIAERHKKSTAQVLLRHLLQLGIVIIP--KSASPERIKSNI 281
Cdd:cd19082 238 -NFerlERAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSL 287
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
34-213 |
2.10e-12 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 66.83 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 34 ALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELFITTKLpHF--GNRPSD-----------VEKfiklSLDK 97
Cdd:cd19087 39 ALDAGINFFDTADVYGGgrsEEIIGRWIA------GRRDDIVLATKV-FGpmGDDPNDrglsrrhirraVEA----SLRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 98 LGLDYLDMYLVHMPFAF-KLDEatcaaathedgsyildfdtdpvlVWKEMENQVKSGRTRSIGLSNFNEEQISLIWENAQ 176
Cdd:cd19087 108 LQTDYIDLYQMHHFDRDtPLEE-----------------------TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1153814477 177 ---------IKPS-NL---QVELHaymqqksIRELCKKYNIVITGYSPLG 213
Cdd:cd19087 165 rrgllrfvsEQPMyNLlkrQAELE-------ILPAARAYGLGVIPYSPLA 207
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-161 |
4.49e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 65.75 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 18 GTW-QAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfekgGSREELFITTK----LPHFGNRPSDVEK 89
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALK------GLPAGPYITTKvrldPDDLGDIGGQIER 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1153814477 90 FIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAATHEDgsyILDFDTdpvlVWKEMENQVKSGRTRSIGLS 161
Cdd:cd19104 98 SVEKSLKRLKRDSVDLLQLHNRIGDERDKPVGGTLSTTD---VLGLGG----VADAFERLRSEGKIRFIGIT 162
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
25-293 |
8.80e-12 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 64.76 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 25 EEIETVVITALECGYRHIDTAANY---NNEDAIGKALKkwfekGGSREELFITTKlphFGNR------------PSDVEK 89
Cdd:cd19145 33 EEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK-----DGPREKVQLATK---FGIHeiggsgvevrgdPAYVRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 90 FIKLSLDKLGLDYLDMYLVHmpfafKLDEatcaaathedgsyildfdTDPVLV-WKEMENQVKSGRTRSIGLSnfnEEQI 168
Cdd:cd19145 105 ACEASLKRLDVDYIDLYYQH-----RIDT------------------TVPIEItMGELKKLVEEGKIKYIGLS---EASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 169 SLIWENAQIKP-SNLQVELHAYMQ--QKSIRELCKKYNIVITGYSPLG----SPGAKVHFQTKYNYTTEAFPDLLNHSVV 241
Cdd:cd19145 159 DTIRRAHAVHPiTAVQLEWSLWTRdiEEEIIPTCRELGIGIVPYSPLGrgffAGKAKLEELLENSDVRKSHPRFQGENLE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1153814477 242 QN---------IAERHKKSTAQVLLRHLLQLG--IVIIPKSASPERIKSNIDIFDFTLTDDDM 293
Cdd:cd19145 239 KNkvlyerveaLAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDL 301
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
8-232 |
1.10e-11 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 64.79 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQAKSEEI-----ETVVITALECGYRHIDTAANYNNEDA---IGKALKKwfeKGGSREELFITTKLpH 79
Cdd:cd19142 9 SGLRVSNVGLGTWSTFSTAIseeqaEEIVTLAYENGINYFDTSDAFTSGQAeteLGRILKK---KGWKRSSYIVSTKI-Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 80 FGNRPSD---VEKFI----KLSLDKLGLDYLDMYLVHmpfafKLDeATCAAAThedgsyildfdtdpvlVWKEMENQVKS 152
Cdd:cd19142 85 WSYGSEErglSRKHIiesvRASLRRLQLDYIDIVIIH-----KAD-PMCPMEE----------------VVRAMSYLIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 153 GRTRSIGLSNFNEEQISLIWENAQ----IKPSNLQVELHAYMQQK---SIRELCKKYNIVITGYSPLG---SPGakVHFQ 222
Cdd:cd19142 143 GLIMYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHMFCREKmelYMPELYNKVGVGLITWSPLSlglDPG--ISEE 220
|
250
....*....|
gi 1153814477 223 TKYNYTTEAF 232
Cdd:cd19142 221 TRRLVTKLSF 230
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-301 |
6.13e-11 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 62.58 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 14 TVGLGT--WQAKSEEIETVVI--TALECGYRHIDTAANY----------NNEDAIGKalkkWFEKGGSREELFITTK--- 76
Cdd:cd19094 3 EICLGTmtWGEQNTEAEAHEQldYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGS----WLKKKGNRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 77 ----LPHFGNRPSDVEKF-IKLSLDK----LGLDYLDMYLVHMPfafklDEATcaaaTHEDGSYILDFDTDPVLVwkEME 147
Cdd:cd19094 79 pgegITWPRGGGTRLDREnIREAVEGslkrLGTDYIDLYQLHWP-----DRYT----PLFGGGYYTEPSEEEDSV--SFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 148 NQ-------VKSGRTRSIGLSN--------FNEEQISLIWEnaqiKPSNLQ----------VELHAymqqksirELCKKY 202
Cdd:cd19094 148 EQlealgelVKAGKIRHIGLSNetpwgvmkFLELAEQLGLP----RIVSIQnpysllnrnfEEGLA--------EACHRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 203 NIVITGYSPLG--------------SPGAKV----HFQTKYN--YTTEAFPDLlnhsvvQNIAERHKKSTAQVLLRHLLQ 262
Cdd:cd19094 216 NVGLLAYSPLAggvltgkyldgaarPEGGRLnlfpGYMARYRspQALEAVAEY------VKLARKHGLSPAQLALAWVRS 289
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1153814477 263 ---LGIVIIPKSaSPERIKSNIDIFDFTLTDDdmnLLNDLDK 301
Cdd:cd19094 290 rpfVTSTIIGAT-TLEQLKENIDAFDVPLSDE---LLAEIDA 327
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-213 |
1.17e-10 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 61.41 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 9 GYDMPTVGLGT-------WQAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfekGGSREELFITTKLP 78
Cdd:cd19163 10 GLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALK-----GIPRDSYYLATKVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 79 HFGNRPSD--------VEKFIKLSLDKLGLDYLDMYLVH-MPFAFKLDEatcaaathedgsyILDfDTDPVLvwkemENQ 149
Cdd:cd19163 85 RYGLDPDKmfdfsaerITKSVEESLKRLGLDYIDIIQVHdIEFAPSLDQ-------------ILN-ETLPAL-----QKL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 150 VKSGRTRSIGLSNFNEEQISLIWENAQIKpsnLQVEL---HAYMQQKSIREL---CKKYNIVITGYSPLG 213
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLERSPVK---IDTVLsycHYTLNDTSLLELlpfFKEKGVGVINASPLS 212
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-168 |
1.50e-10 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 61.12 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQ-----AKSEEIETVVITALECGYRHIDTAANY-----NNEDAIGKALKKwfEKGGSREELFITTK- 76
Cdd:cd19089 7 SGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKR--DLRPYRDELVISTKa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 77 ------LP--HFGNRpsdveKFIKLSLD----KLGLDYLDMYLVH-----MPfafkLDEATCAAAthedgsYIldfdtdp 139
Cdd:cd19089 85 gygmwpGPygDGGSR-----KYLLASLDqslkRMGLDYVDIFYHHrydpdTP----LEETMTALA------DA------- 142
|
170 180
....*....|....*....|....*....
gi 1153814477 140 vlvwkemenqVKSGRTRSIGLSNFNEEQI 168
Cdd:cd19089 143 ----------VRSGKALYVGISNYPGAKA 161
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-282 |
3.07e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 60.04 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 35 LECGYRHIDTAANYN----------NEDAIGKalkkWFEKGGSREELFITTKL------PHFGNR------PSDVEKFIK 92
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvggeSERLIGR----WLKDRGNRDDVVIATKVgagprdPDGGPEspeglsAETIEQEID 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 93 LSLDKLGLDYLDMYLVHmpfafkldeatcaaathedgsyILDFDTDPVLVWKEMENQVKSGRTRSIGLSNFNEEQISLI- 171
Cdd:cd19752 103 KSLRRLGTDYIDLYYAH----------------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERAr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 172 -------WEnaqiKPSNLQvELHAYMQQKSIRELCKKYNI--------------VITGYSPL-----GSPGAKVhfqtKY 225
Cdd:cd19752 161 qiarqqgWA----EFSAIQ-QRHSYLRPRPGADFGVQRIVtdelldyassrpdlTLLAYSPLlsgayTRPDRPL----PE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1153814477 226 NYTTEAFPDLLnhSVVQNIAERHKKSTAQVLLRHLLQLGIVIIP--KSASPERIKSNID 282
Cdd:cd19752 232 QYDGPDSDARL--AVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVEQLEENLA 288
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
13-291 |
3.68e-09 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 56.85 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGT-------WQAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfekGGSREELFITTKL----- 77
Cdd:cd19152 1 PKLGFGTaplgnlyEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALR-----ELGREDYVISTKVgrllv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 -----------PHFGNRPSD---------VEKFIKLSLDKLGLDYLDMYLVHMP---FAFKLDEATCAAATheDGSYild 134
Cdd:cd19152 76 plqeveptfepGFWNPLPFDavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPdedLAGAESDEHFAQAI--KGAF--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 135 fdtdpvlvwKEMENQVKSGRTRSIGLSnFNEEQISL-IWENAQIKPSNLQVELHAYMQQKSIR--ELCKKYNI-VITGyS 210
Cdd:cd19152 151 ---------RALEELREEGVIKAIGLG-VNDWEVILrILEEADLDWVMLAGRYTLLDHSAAREllPECEKRGVkVVNA-G 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 211 PLGSpGAKV---HFqtKYNYTTEAFPDLLNHSV-VQNIAERHKKSTAQVLLRHLLQLGIV--IIPKSASPERIKSNIDIF 284
Cdd:cd19152 220 PFNS-GFLAggdNF--DYYEYGPAPPELIARRDrIEALCEQHGVSLAAAALQFALAPPAVasVAPGASSPERVEENVALL 296
|
....*..
gi 1153814477 285 DFTLTDD 291
Cdd:cd19152 297 ATEIPAA 303
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
8-167 |
6.15e-09 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 56.26 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQ-----AKSEEIETVVITALECGYRHIDTAANY-----NNEDAIGKALKKWFEkgGSREELFITTKL 77
Cdd:cd19151 8 SGLKLPAISLGLWHnfgdvDRYENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLK--PYRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 PH---------FGNRpsdveKFIKLSLD----KLGLDYLDMYLVHMPfafkldeatcaaathedgsyilDFDTDPVLVWK 144
Cdd:cd19151 86 GYtmwpgpygdWGSK-----KYLIASLDqslkRMGLDYVDIFYHHRP----------------------DPETPLEETMG 138
|
170 180
....*....|....*....|...
gi 1153814477 145 EMENQVKSGRTRSIGLSNFNEEQ 167
Cdd:cd19151 139 ALDQIVRQGKALYVGISNYPPEE 161
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
8-281 |
8.37e-09 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 56.15 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQAKS-----EEIETVVITALECGYRHIDTAANY-----NNEDAIGKALKKWFekGGSREELFITTKL 77
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDF--AAYRDELIISTKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 PH------FGNRPSdvEKFIKLSLD----KLGLDYLDMYLVHmpfafKLDEATCAAATHEdgsyildfdtdpvlvwkEME 147
Cdd:PRK09912 99 GYdmwpgpYGSGGS--RKYLLASLDqslkRMGLEYVDIFYSH-----RVDENTPMEETAS-----------------ALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 148 NQVKSGRTRSIGLSNFNEEQISLI------WENAQI--KPS-NLqveLHAYMQQKSIRELCKKYNIVITGYSPL------ 212
Cdd:PRK09912 155 HAVQSGKALYVGISSYSPERTQKMvellreWKIPLLihQPSyNL---LNRWVDKSGLLDTLQNNGVGCIAFTPLaqgllt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 213 -----GSP-GAKVHFQTK------YNYTTEAfpDLLNHSVVQNIAERHKKSTAQVLLRHLLQLGIV--IIPKSASPERIK 278
Cdd:PRK09912 232 gkylnGIPqDSRMHREGNkvrgltPKMLTEA--NLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLE 309
|
...
gi 1153814477 279 SNI 281
Cdd:PRK09912 310 ENV 312
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
15-109 |
2.48e-08 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 54.46 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 15 VGLGT------WQAKSEEIETVVI--TALECGYRHIDTAANYNN---EDAIGKALKKwfeKGGSREELFITTKLPHFGNR 83
Cdd:cd19153 15 VGLGTaalggvYGDGLEQDEAVAIvaEAFAAGINHFDTSPYYGAessEAVLGKALAA---LQVPRSSYTVATKVGRYRDS 91
|
90 100 110
....*....|....*....|....*....|.
gi 1153814477 84 PSD-----VEKFIKLSLDKLGLDYLDMYLVH 109
Cdd:cd19153 92 EFDysaerVRASVATSLERLHTTYLDVVYLH 122
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
8-126 |
5.93e-08 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 53.22 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTW-----QAKSEEIETVVITALECGYRHIDTAANYNNEDA---IGKALKKwfeKGGSREELFITTKLpH 79
Cdd:cd19141 8 SGLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGKAeivLGKILKK---KGWRRSSYVITTKI-F 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1153814477 80 FGNRpSDVEKF---------IKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAATH 126
Cdd:cd19141 84 WGGK-AETERGlsrkhiiegLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTH 138
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
8-293 |
8.31e-08 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 52.84 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTWQ--AKSEEIET---VVITALECGYRHIDTAANY-----NNEDAIGKALKKWFEkgGSREELFITTKL 77
Cdd:cd19150 8 SGLKLPALSLGLWHnfGDDTPLETqraILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFA--GYRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 -------PH--FGNRpsdveKFIKLSLD----KLGLDYLDMYLVHmpfafKLDEATCAAATHedgsyildfdtdpvlvwK 144
Cdd:cd19150 86 gydmwpgPYgeWGSR-----KYLLASLDqslkRMGLDYVDIFYSH-----RFDPDTPLEETM-----------------G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 145 EMENQVKSGRTRSIGLSNFNEEQISliwENAQI-----------KPS-NLqveLHAYMQQKSIRELCKKYNIVITGYSPL 212
Cdd:cd19150 139 ALDHAVRSGKALYVGISSYSPERTR---EAAAIlrelgtpllihQPSyNM---LNRWVEESGLLDTLQELGVGCIAFTPL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 213 -----------GSP-GAKVHFQTKYNYTTEAFPDLLNHSVVQNIAERHKKSTAQVLLRHLLQLGIV--IIPKSASPERIK 278
Cdd:cd19150 213 aqglltdkylnGIPeGSRASKERSLSPKMLTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLE 292
|
330
....*....|....*.
gi 1153814477 279 SNIDIFD-FTLTDDDM 293
Cdd:cd19150 293 ENVGALDnLTFSADEL 308
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-162 |
1.01e-07 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 1 MHFVRL-LSGYDMPTVGLGTW----QAKSEEIETVVITALECGYRHIDTAANYN----------NEDAIGKalkkWFEKG 65
Cdd:PRK10625 1 MQYHRIpHSSLEVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGN----WLAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 66 GSREELFITTKL--PHFGN----RPSDV--EKFIKLSLD----KLGLDYLDMYLVHMPfafkLDEATCAAAThedgSYIL 133
Cdd:PRK10625 77 GSREKLIIASKVsgPSRNNdkgiRPNQAldRKNIREALHdslkRLQTDYLDLYQVHWP----QRPTNCFGKL----GYSW 148
|
170 180 190
....*....|....*....|....*....|..
gi 1153814477 134 DFDTDPVLVWKEME---NQVKSGRTRSIGLSN 162
Cdd:PRK10625 149 TDSAPAVSLLETLDalaEQQRAGKIRYIGVSN 180
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
25-109 |
3.22e-07 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 51.12 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 25 EEIETV--VITALECGYRHIDTAANY-NNEDAIGKALKKWFEKgGSREELFITTKLPHFGNR-----PSDVEKFIKLSLD 96
Cdd:cd19164 32 ESIPPVdiVRRALELGIRAFDTSPYYgPSEIILGRALKALRDE-FPRDTYFIITKVGRYGPDdfdysPEWIRASVERSLR 110
|
90
....*....|...
gi 1153814477 97 KLGLDYLDMYLVH 109
Cdd:cd19164 111 RLHTDYLDLVYLH 123
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
13-111 |
5.25e-07 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 50.44 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGTWQ------AKSEEIETVVITALECGYRHIDTAANYN---NEDAIGKALKKWfekggSREELFITTKL-----P 78
Cdd:cd19162 1 PRLGLGAASlgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH-----PRAEYVVSTKVgrlleP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1153814477 79 HFGNRPSDVEKF-----------IKLSLDKLGLDYLDMYLVHMP 111
Cdd:cd19162 76 GAAGRPAGADRRfdfsadgirrsIEASLERLGLDRLDLVFLHDP 119
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
8-117 |
1.21e-06 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 49.60 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTW-----QAKSEEIETVVITALECGYRHIDTAANY---NNEDAIGKALKKwfeKGGSREELFITTKLPH 79
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKS---KGWRRSSYVVTTKIYW 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1153814477 80 FGNRPSD-------VEKFIKLSLDKLGLDYLDMYlvhmpFAFKLD 117
Cdd:cd19160 88 GGQAETErglsrkhIIEGLRGSLDRLQLEYVDIV-----FANRSD 127
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-214 |
2.29e-06 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 48.36 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 1 MHFVRL-LSGYDMPTVGLGTW-----QAKSEEIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfEKGGSREEL 71
Cdd:cd19143 1 MEYRRLgRSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIK---ELGWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 72 FITTKLpHFG-----------NRPSDVEKfIKLSLDKLGLDYLDMYLVHMPfafklDEATcaaathedgsyildfdtdPV 140
Cdd:cd19143 78 VVSTKI-FWGgggpppndrglSRKHIVEG-TKASLKRLQLDYVDLVFCHRP-----DPAT------------------PI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 141 --LVWKeMENQVKSGRTRSIGLSNFNEEQISLIWENAQ----IKPSNLQVELHAYMQQKSIRE---LCKKYNIVITGYSP 211
Cdd:cd19143 133 eeTVRA-MNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVMEQPQYNLFHRERVEVEyapLYEKYGLGTTTWSP 211
|
...
gi 1153814477 212 LGS 214
Cdd:cd19143 212 LAS 214
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
8-126 |
2.84e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 48.16 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 8 SGYDMPTVGLGTW-----QAKSEEIETVVITALECGYRHIDTAANY---NNEDAIGKALKKwfeKGGSREELFITTKLPH 79
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKK---KGWRRSSLVITTKIFW 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1153814477 80 FGNRPSD-------VEKFIKLSLDKLGLDYLDMYLVHMPFAFKLDEATCAAATH 126
Cdd:cd19158 86 GGKAETErglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTH 139
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
13-285 |
5.88e-06 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 47.32 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 13 PTVGLGT------WQAKSE-EIETVVITALECGYRHIDTAANYNN---EDAIGKALKkwfEKGgsREELFITTKL----- 77
Cdd:cd19161 1 SELGLGTaglgnlYTAVSNaDADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLR---EKP--RDEFVLSTKVgrllk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 78 PHFGNRPSDVEKF--------------------IKLSLDKLGLDYLDMYLVHmpfafkldeaTCAAATHEDGSYILDFDT 137
Cdd:cd19161 76 PAREGSVPDPNGFvdplpfeivydysydgimrsFEDSLQRLGLNRIDILYVH----------DIGVYTHGDRKERHHFAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 138 DPVLVWKEMENQVKSGRTRSIGLSnFNEEQISL-IWENAQIKPSNLQVElHAYMQQKSIREL---CKKYN--IVITGYSP 211
Cdd:cd19161 146 LMSGGFKALEELKKAGVIKAFGLG-VNEVQICLeALDEADLDCFLLAGR-YSLLDQSAEEEFlprCEQRGtsLVIGGVFN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1153814477 212 LGSPGAKVHFQTKYNYtTEAFPDLLNH-SVVQNIAERHKKSTAQVLLRHLLQLGIV--IIPKSASPERIKSNIDIFD 285
Cdd:cd19161 224 SGILATGTKSGAKFNY-GDAPAEIISRvMEIEKICDAYNVPLAAAALQFPLRHPAVasVLTGARNPAQLRQNVEAFQ 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
36-110 |
3.57e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 41.64 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 36 ECGYRHIDTAANYNNEDAiGKALKKWFEKGGSREELFITTKLPhFGNRPSDVEKF---------------IKLSLDKLGL 100
Cdd:cd19146 46 EQGGNFIDTANNYQGEES-ERWVGEWMASRGNRDEMVLATKYT-TGYRRGGPIKIksnyqgnhakslrlsVEASLKKLQT 123
|
90
....*....|
gi 1153814477 101 DYLDMYLVHM 110
Cdd:cd19146 124 SYIDILYVHW 133
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
36-109 |
5.06e-03 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 38.27 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 36 ECGYRHIDTAANYNNEDA---IGKalkkWFEKGGSREELFITTKLP---------------HFGNRPSDVEKFIKLSLDK 97
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGE----WMKSRKNRDQIVIATKFTtdykayevgkgkavnYCGNHKRSLHVSVRDSLRK 120
|
90
....*....|..
gi 1153814477 98 LGLDYLDMYLVH 109
Cdd:cd19147 121 LQTDWIDILYVH 132
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
34-109 |
7.72e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 37.45 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153814477 34 ALECGYRHIDTAANYNN---EDAIGKALKKwfeKGGSREELFITTKLPHFGN----RPSDVEKFIKLSLDKLGLDYLDMY 106
Cdd:PLN02587 40 AFRLGINFFDTSPYYGGtlsEKVLGKALKA---LGIPREKYVVSTKCGRYGEgfdfSAERVTKSVDESLARLQLDYVDIL 116
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...
gi 1153814477 107 LVH 109
Cdd:PLN02587 117 HCH 119
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