|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
6-294 |
0e+00 |
|
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: 514.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFESD-AYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGG 84
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 85 IHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNA 164
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 165 AQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQW--PPFLYDEHAQNLAKKYGRTTAQ 242
Cdd:cd19116 161 EQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTnpPPRLDDPTLVAIAKKYGKTTAQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 20129731 243 ICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTV 294
Cdd:cd19116 241 IVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-282 |
9.16e-128 |
|
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: 364.50 E-value: 9.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIaegvVTREEVFVTTKLGGIHHDPALVERA 95
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 96 CRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhgtLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCR 175
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGK----------EGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 176 IRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPqparqWPPFLYDEHAQNLAKKYGRTTAQICLRYLVQLGVVP 255
Cdd:cd19071 147 IKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRG-----RRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVV 221
|
250 260
....*....|....*....|....*..
gi 20129731 256 LPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19071 222 IPKSSNPERIKENLDVFDFELSEEDMA 248
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
5-292 |
5.13e-125 |
|
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: 359.42 E-value: 5.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 5 APTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGG 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 85 IHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDS---NVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGEsgtMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 162 FNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARP------QPARQWPP--FLYDEHAQNLA 233
Cdd:cd19154 161 FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPgranftKSTGVSPApnLLQDPIVKAIA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129731 234 KKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19154 241 EKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-295 |
3.23e-123 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 353.21 E-value: 3.23e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIHHDPAL 91
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 92 VERACRLSLSNLGLEYVDLYLMHMPVgqkfhndsnvhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVL 171
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPG-----------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 172 ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLRYLVQL 251
Cdd:COG0656 140 AETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-------LLDDPVLAEIAEKHGKTPAQVVLRWHLQR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 20129731 252 GVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVP 295
Cdd:COG0656 213 GVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGP 256
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-292 |
1.17e-121 |
|
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: 350.92 E-value: 1.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 10 LNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEG-VVTREEVFVTTKLGGIHHD 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVERACRLSLSNLGLEYVDLYLMHMPVG-----QKFHNDSNvhGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFN 163
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAfergdNPFPKNPD--GTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 164 AAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQpaRQW-----PPFLYDEHAQNLAKKYGR 238
Cdd:cd19106 159 SRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPD--RPWakpdePVLLEEPKVKALAKKYNK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 20129731 239 TTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19106 237 SPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWR 290
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-311 |
1.06e-105 |
|
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: 310.50 E-value: 1.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALV 92
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 93 ERACRLSLSNLGLEYVDLYLMHMPVGQK-----FHNDSNvhGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQT 167
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKpgkelFPLDES--GNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 168 ERVL--ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQpaRQW-----PPFLYDEHAQNLAKKYGRTT 240
Cdd:cd19107 159 ERILnkPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPD--RPWakpedPSLLEDPKIKEIAAKHNKTT 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129731 241 AQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVPFSGMSGHKYYPFNDEF 311
Cdd:cd19107 237 AQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-280 |
6.25e-105 |
|
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: 308.39 E-value: 6.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFE---SDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKL 82
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 GGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHND---SNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGL 159
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEElfpKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 160 SNFNAAQTERVL--ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArPQPARQW-----PPFLYDEHAQNL 232
Cdd:cd19108 161 SNFNRRQLEMILnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALG-SQRDKEWvdqnsPVLLEDPVLCAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20129731 233 AKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDD 280
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSED 287
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
10-286 |
1.12e-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: 1.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 10 LNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDP 89
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 90 ALVERACRLSLSNLGLEYVDLYLMHMPVGQKfhNDSNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTER 169
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIHWPVRLK--KGAHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 170 VLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQWPPFLYDEHAQNLAKKYGRTTAQICLRYLV 249
Cdd:cd19125 163 LLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 20129731 250 QLGVVPLPKSSNKARIEENFRVFDFELSPDD---VAGMEQ 286
Cdd:cd19125 243 QRGTSVLPKSTNEERIKENIDVFDWSIPEEDfakFSSIEQ 282
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-292 |
2.17e-100 |
|
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: 296.33 E-value: 2.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALV 92
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 93 ERACRLSLSNLGLEYVDLYLMHMPVGqkfHNDSNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLA 172
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCG---FVNKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 173 NCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQ--WPP---FLYDEHAQNLAKKYGRTTAQICLRY 247
Cdd:cd19111 158 YAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQslWPDqpdLLEDPTVLAIAKELDKTPAQVLLRF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 20129731 248 LVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19111 238 VLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
8-296 |
3.87e-100 |
|
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: 296.36 E-value: 3.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHH 87
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 88 DPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVH----GTLEL-TDVDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKldptGEHKQdYTTDLLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARP----------QPARQWPPFLYDEHAQNL 232
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPgaahfspgtgSPSGSSPDLLQDPVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 233 AKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVPF 296
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGRTF 307
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
7-294 |
1.85e-97 |
|
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: 289.31 E-value: 1.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 7 TIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIH 86
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPV----GQKFHNDSNVHgtLELTDVDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19123 83 HAPEDVLPALEKTLADLQLDYLDLYLMHWPValkkGVGFPESGEDL--LSLSPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQW-----PPFLYDEHAQNLAKKYG 237
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMkaegePVLLEDPVINKIAEKHG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 20129731 238 RTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTV 294
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-307 |
7.99e-94 |
|
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: 280.53 E-value: 7.99e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTW----KSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHD 88
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVERACRLSLSNLGLEYVDLYLMHMPVGQK-----FHNDSNvhGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFN 163
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKpgdeiYPRDEN--GKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 164 AAQTERVL--ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQpARQW-----PPFLYDEHAQNLAKKY 236
Cdd:cd19109 159 RRQLELILnkPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCR-DPIWvnvssPPLLEDPLLNSIGKKY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129731 237 GRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVPFSGMSGHKYYPF 307
Cdd:cd19109 238 NKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
8-286 |
5.14e-92 |
|
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: 273.68 E-value: 5.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWK-SFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIaegvVTREEVFVTTKL---- 82
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLwiqd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 GGIHHDPALVERacrlSLSNLGLEYVDLYLMHMPVGqkfhndsnvhgtleltdvDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19133 77 AGYEKAKKAFER----SLKRLGLDYLDLYLIHQPFG------------------DVYGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPArqwppFLYDEHAQNLAKKYGRTTAQ 242
Cdd:cd19133 135 YPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN-----LFENPVLTEIAEKYGKSVAQ 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 20129731 243 ICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDvagMEQ 286
Cdd:cd19133 210 VILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDED---MEA 250
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-282 |
5.30e-92 |
|
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: 274.12 E-value: 5.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWK-SFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALVER 94
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 95 ACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVHGTLEltdvdyLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANC 174
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELR------RESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 175 RIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPArqwppFLYDEHAQNLAKKYGRTTAQICLRYLVQLGVV 254
Cdd:cd19136 155 EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR-----LLEDPTVLAIAKKYGRTPAQVLLRWALQQGIG 229
|
250 260
....*....|....*....|....*...
gi 20129731 255 PLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19136 230 VIPKSTNPERIAENIKVFDFELSEEDMA 257
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-288 |
4.16e-91 |
|
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: 271.89 E-value: 4.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKS--FESDAyhsTRHAL-DVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKL 82
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTSHSggYSHEA---VVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 GGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQkfhndSNVHGTLELTDvdylDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19135 76 WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCP-----SSGKNVKETRA----ETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQParqwppfLYDEHAQNLAKKYGRTTAQ 242
Cdd:cd19135 147 LIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKA-------LEEPTVTELAKKYQKTPAQ 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 20129731 243 ICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYH 288
Cdd:cd19135 220 ILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSLH 265
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-286 |
1.15e-90 |
|
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: 270.40 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 7 TIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIH 86
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHndsnvhgtleltdvdYLDTWREMEKLVDLGLTRSIGLSNFNAAQ 166
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDK---------------YVETWKALIELKKEGRVKSIGVSNFTIEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 167 TERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLR 246
Cdd:cd19131 142 LQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-------LLSDPVIGEIAEKHGKTPAQVVIR 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 20129731 247 YLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQ 286
Cdd:cd19131 215 WHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAG 254
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-280 |
1.53e-90 |
|
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: 271.06 E-value: 1.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSFES--DAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVV-TREEVFVTTKLGGIHHD 88
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSpeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVkSRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTE 168
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 169 RVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArpQPARQWPPFLYDEHA--QNLAKKYGRTTAQICLR 246
Cdd:cd19124 161 ELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLG--APGTKWGSNAVMESDvlKEIAAAKGKTVAQVSLR 238
|
250 260 270
....*....|....*....|....*....|....
gi 20129731 247 YLVQLGVVPLPKSSNKARIEENFRVFDFELSPDD 280
Cdd:cd19124 239 WVYEQGVSLVVKSFNKERMKQNLDIFDWELTEED 272
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-285 |
4.59e-90 |
|
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: 268.37 E-value: 4.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIHHDPALVERA 95
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 96 CRLSLSNLGLEYVDLYLMHMPVgqkfhndsnvhgtlelTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCR 175
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN----------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 176 IRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARqwppflyDEHAQNLAKKYGRTTAQICLRYLVQLGVVP 255
Cdd:cd19073 141 LPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGEVLR-------DPVIQEIAEKYDKTPAQVALRWLVQKGIVV 213
|
250 260 270
....*....|....*....|....*....|
gi 20129731 256 LPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19073 214 IPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
15-311 |
2.19e-88 |
|
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: 266.44 E-value: 2.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 15 EMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALVER 94
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 95 ACRLSLSNLGLEYVDLYLMHMPVGQK-FHNDSNV--HGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKpGEPDLPLdrSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 172 --ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArpqPARQWPPFLYDEHAQNLAKKYGRTTAQICLRYLV 249
Cdd:cd19110 163 nkPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG---GSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129731 250 QLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVPFSGMSGHKYYPFNDEF 311
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
6-293 |
8.56e-87 |
|
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: 262.42 E-value: 8.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGI 85
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHdpALVERACRLSLSNLGLEYVDLYLMHMPVGQKfHN-----DSNV--HGTLEL-TDVDYLDTWREMEKLVDLGLTRSI 157
Cdd:cd19112 81 DH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATK-HTgvgttGSALgeDGVLDIdVTISLETTWHAMEKLVSAGLVRSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 158 GLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQWppF-----LYDEHAQNL 232
Cdd:cd19112 158 GISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEW--FgsvspLDDPVLKDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129731 233 AKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRT 293
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRT 296
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-282 |
1.58e-86 |
|
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: 259.89 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 10 LNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIHHDP 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 90 ALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsnvhgtleLTDVD-YLDTWREMEKLVDLGLTRSIGLSNFNAAQTE 168
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWP----------------NPSRDlYVEAWQALIEAREEGLVRSIGVSNFLPEHLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 169 RVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQParqwppfLYDEHA-QNLAKKYGRTTAQICLRY 247
Cdd:cd19132 141 RLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG-------LLDEPViKAIAEKHGKTPAQVVLRW 213
|
250 260 270
....*....|....*....|....*....|....*
gi 20129731 248 LVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19132 214 HVQLGVVPIPKSANPERQRENLAIFDFELSDEDMA 248
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
12-282 |
1.36e-85 |
|
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: 257.57 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIHHDPAL 91
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYSPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 92 VERACRLSLSNLGLEYVDLYLMHMPvgqkfhNDsnvhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVL 171
Cdd:cd19140 80 FLASVEESLRKLRTDYVDLLLLHWP------NK----------DVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 172 ANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARqwppflyDEHAQNLAKKYGRTTAQICLRYLV-Q 250
Cdd:cd19140 144 ELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLK-------DPVLQEIGRKHGKTPAQVALRWLLqQ 216
|
250 260 270
....*....|....*....|....*....|..
gi 20129731 251 LGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19140 217 EGVAAIPKATNPERLEENLDIFDFTLSDEEMA 248
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
7-295 |
1.52e-85 |
|
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: 257.70 E-value: 1.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 7 TIRLNNGREMPTLGLGTWKSFE-SDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGI 85
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HH--DPALveRACRLSLSNLGLEYVDLYLMHMPVGQKFHndsnvhgtleltdvdylDTWREMEKLVDLGLTRSIGLSNFN 163
Cdd:cd19157 77 DQgyDSTL--KAFEASLERLGLDYLDLYLIHWPVKGKYK-----------------ETWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 164 AAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQI 243
Cdd:cd19157 138 VHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-------LLDNPVLKEIAEKYNKSVAQV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 20129731 244 CLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVP 295
Cdd:cd19157 211 ILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVGP 262
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-282 |
2.57e-83 |
|
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: 251.59 E-value: 2.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFESD-AYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIH 86
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDeTERAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFhndsnvhgtleltdvdyLDTWREMEKLVDLGLTRSIGLSNFNAAQ 166
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKF-----------------IDTWKALEKLYASGKVKAIGVSNFQEHH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 167 TERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLR 246
Cdd:cd19126 140 LEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-------LLSNPVLAAIGEKYGKSAAQVVLR 212
|
250 260 270
....*....|....*....|....*....|....*.
gi 20129731 247 YLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19126 213 WDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMT 248
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-295 |
1.32e-82 |
|
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: 250.51 E-value: 1.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFE-SDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIH 86
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhgtleltdvdYLDTWREMEKLVDLGLTRSIGLSNFNAAQ 166
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK-----------------FKDTWKAFEKLYKEKKVRAIGVSNFHEHH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 167 TERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLR 246
Cdd:cd19156 140 LEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-------LLSNPVLKAIGKKYGKSAAQVIIR 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 20129731 247 YLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVP 295
Cdd:cd19156 213 WDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRYGP 261
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
6-292 |
9.47e-82 |
|
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: 249.67 E-value: 9.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGI 85
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKF-------------HNDSNVHgtleLTDVDYLDTWREMEKLVDLG 152
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFvpieekyppgfycGDGDNFV----YEDVPILDTWKALEKLVDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 153 LTRSIGLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArPQP--------ARQWPPFL 224
Cdd:cd19113 157 KIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFG-PQSfvelnqgrALNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129731 225 YDEHAQNLAKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-295 |
1.90e-81 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 247.68 E-value: 1.90e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 1 MTNlAPTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEkiaeGVVTREEVFVTT 80
Cdd:PRK11565 1 MAN-PTVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KL-GGIHHDP--ALVEracrlSLSNLGLEYVDLYLMHMPVGQKFHndsnvhgtleltdvdYLDTWREMEKLVDLGLTRSI 157
Cdd:PRK11565 76 KLwNDDHKRPreALEE-----SLKKLQLDYVDLYLMHWPVPAIDH---------------YVEAWKGMIELQKEGLIKSI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 158 GLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArpqparQWPPFLYDEHA-QNLAKKY 236
Cdd:PRK11565 136 GVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLA------QGGKGVFDQKViRDLADKY 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 20129731 237 GRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTVP 295
Cdd:PRK11565 210 GKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRLGP 268
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-288 |
4.94e-81 |
|
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: 246.38 E-value: 4.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGT---WK-----SFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGG 84
Cdd:cd19120 1 GSKIPAIAFGTgtaWYksgddDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 85 IHHDPalvERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVhgtleltdvdylDTWREMEKLVDLGLTRSIGLSNFNA 164
Cdd:cd19120 77 GIKDP---REALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLA------------EAWAELEALKDAGLVRSIGVSNFRI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 165 AQTERVLANCRIRPVVNQVECHP--GFQQRQLREHAKRHGLVICAYCPLArpqPARQWPPFLYDEHAQNLAKKYGRTTAQ 242
Cdd:cd19120 142 EDLEELLDTAKIKPAVNQIEFHPylYPQQPALLEYCREHGIVVSAYSPLS---PLTRDAGGPLDPVLEKIAEKYGVTPAQ 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 20129731 243 ICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDV-----AGmEQYH 288
Cdd:cd19120 219 VLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVeeidkAG-KQKH 268
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-288 |
9.19e-81 |
|
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: 246.26 E-value: 9.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 7 TIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISekiAEGvVTREEVFVTTKLGGI- 85
Cdd:cd19117 5 TFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKLWCTw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPalvERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVH----GTLE-LTDVDYLDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19117 81 HRRV---EEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFkkddGTKDhEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLA--NCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwPPFLYDEHAQNLAKKYGR 238
Cdd:cd19117 158 NFSIKNLEKLLAspSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN-----APLLKEPVIIKIAKKHGK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 20129731 239 TTAQICLRYLVQLGVVPLPKSSNKARIEENFRVfdFELSPDDVAGMEQYH 288
Cdd:cd19117 233 TPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELH 280
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-282 |
1.05e-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: 246.17 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 10 LNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAE-GVVTREEVFVTTKLGGIHHD 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSN----VHGTLELTDVD----YLDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNpltaVPTNGGEVDLDlsvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArpQPARQWPPFLYDEHAQNLAKKYGRTT 240
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLG--NNLAGLPLLVQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 20129731 241 AQICLRYLVQLGVVPLPKSSNKARIEENFRvfDFELSPDDVA 282
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFN 278
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
5-292 |
2.42e-80 |
|
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: 246.18 E-value: 2.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 5 APTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGG 84
Cdd:cd19115 2 SPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 85 IHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFhNDSNVH---------GTLELTDVDYLDTWREMEKLVDLGLTR 155
Cdd:cd19115 82 TFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKY-VDPAVRyppgwfydgKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 156 SIGLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLArPQP--------ARQWPPFLYDE 227
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PQSfleldlpgAKDTPPLFEHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129731 228 HAQNLAKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19115 240 VIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-292 |
5.41e-80 |
|
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: 243.61 E-value: 5.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGI 85
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhGTleltdvdYLDTWREMEKLVDLGLTRSIGLSNFNAA 165
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAGRE--------GK-------YVDSWGGLMKLREEGLARSIGVSNFTAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 166 QTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICL 245
Cdd:cd19134 142 HLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-------LLDNPAVTAIAAAHGRTPAQVLL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 20129731 246 RYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19134 215 RWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTR 261
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
8-282 |
1.07e-76 |
|
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: 235.38 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKiaegVVTREEVFVTTKL----- 82
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLwisdy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 GgihHDPALveRACRLSLSNLGLEYVDLYLMHMPVGQKFHndsnvhgtleltdvDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19127 77 G---YDKAL--RGFDASLRRLGLDYVDLYLLHWPVPNDFD--------------RTIQAYKALEKLLAEGRVRAIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLA----RPQPARQWPP-FLYDEHAQNLAKKYG 237
Cdd:cd19127 138 TPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrYGASGPTGPGdVLQDPTITGLAEKYG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 20129731 238 RTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19127 218 KTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMA 262
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-292 |
3.49e-75 |
|
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: 232.83 E-value: 3.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALV 92
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 93 ERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVHGT---------LELTDVDYLDTWREMEKLVDLGLTRSIGLSNFN 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPFlwkdkelkkFPLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 164 AAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLAR------PQPARQWPPFLYDEHAQNLAKKYG 237
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNavytkvTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 20129731 238 RTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQR 292
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-287 |
1.07e-74 |
|
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: 230.50 E-value: 1.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 9 RLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAeGVVTREEVFVTTKLGGIHHD 88
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIA-GGVKREDLFVTTKLWSTYHR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PalVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNVHGTLE------LTDVDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19121 84 R--VELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPdgsrdlDWDWNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwPPFLYDEHAQNLAKKYGRTTAQ 242
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG-----SPLISDEPVVEIAKKHNVGPGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 20129731 243 ICLRYLVQLGVVPLPKSSNKARIEENFRVFDFElsPDDVAGMEQY 287
Cdd:cd19121 237 VLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-281 |
2.40e-72 |
|
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: 224.71 E-value: 2.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPALVERAC 96
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 97 RLSLSNLGLEYVDLYLMHMPVgQKFHND----SNVHGTLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLA 172
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPL-AFDMDTdgdpRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 173 NCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQ--PARQwppFLYDEHAQNLAKKYGRTTAQICL----- 245
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYgdGNLT---FLNDSELKALATKYNTTPPQVIIawhlq 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 20129731 246 RYLVQLGVVplPKSSNKARIEENFRVFDFELSPDDV 281
Cdd:cd19128 238 KWPKNYSVI--PKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
8-285 |
4.02e-72 |
|
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: 223.25 E-value: 4.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAIsekiAEGVVTREEVFVTTKLGGIHH 87
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDRH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 88 DPALVERACRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhgtleltdVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQT 167
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA---------------GNYVHTWEAMIELRAAGRTRSIGVSNFLPPHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 168 ERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLRY 247
Cdd:cd19130 143 ERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-------LLGDPPVGAIAAAHGKTPAQIVLRW 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 20129731 248 LVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19130 216 HLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-293 |
2.02e-70 |
|
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: 220.41 E-value: 2.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHDPA 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 91 LVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDS---NVHGTLELTD-VDYLDTWREMEKLVDLGLTRSIGLSNFNAAQ 166
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQdprDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 167 TERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLA---RPQParqwppfLYDEHAQNLAKKYGRTTAQI 243
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGhgmEPKL-------LEDPVITAIARRVNKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 20129731 244 CLRYLVQLGVVPLPKSSNKARIEENfrvFDFELSPDDvaGMEQYHTGQRT 293
Cdd:cd19129 234 LLAWAIQRGTALLTTSKTPSRIREN---FDISTLPED--AMREINEGIKT 278
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-268 |
5.40e-69 |
|
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: 216.59 E-value: 5.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRLNNGREMPTLGLGTWKSFE--SDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEGVVTREEVFVTTKLGGI 85
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHEdrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPalVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDS--------NVHG-TLELTDVDYLDTWREMEKLVDLGLTRS 156
Cdd:cd19119 84 FYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpftpvNDDGkTRYAASGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 157 IGLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwPPFLYDEHAQNLAKKY 236
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHG-----APNLKNPLVKKIAEKY 236
|
250 260 270
....*....|....*....|....*....|..
gi 20129731 237 GRTTAQICLRYLVQLGVVPLPKSSNKARIEEN 268
Cdd:cd19119 237 NVSTGDILISYHVRQGVIVLPKSLKPVRIVSN 268
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-282 |
2.16e-65 |
|
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: 205.67 E-value: 2.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAisekIAEGVVTREEVFVTTKLGGIHHDPALVERA 95
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 96 CRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCR 175
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPND--------------EVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 176 IRPVV-NQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYGRTTAQICLRYLVQLGVV 254
Cdd:cd19139 143 AGAIAtNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-------VLDDPVLAAIAERHGATPAQIALAWAMARGYA 215
|
250 260
....*....|....*....|....*...
gi 20129731 255 PLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19139 216 VIPSSTKREHLRSNLLALDLTLDADDMA 243
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-282 |
1.24e-60 |
|
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: 194.84 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTWKSF-------ESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAIsekiAEGVVTREEVFVTTKLGG---- 84
Cdd:pfam00248 1 IGLGTWQLGggwgpisKEEALEALRAALEAGINFIDTAEVYgdgKSEELLGEAL----KDYPVKRDKVVIATKVPDgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 85 --IHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGqkfhndsnvhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:pfam00248 77 wpSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDP----------------DTPIEETWDALEELKKEGKIRAIGVSNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCRIRPVVNQVECHP--GFQQRQLREHAKRHGLVICAYCPLA-------------------RPQPARQWP 221
Cdd:pfam00248 141 DAEQIEKALTKGKIPIVAVQVEYNLlrRRQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpgerRRLLKKGTP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 222 PFL-YDEHAQNLAKKYGRTTAQICLRYLVQ--LGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:pfam00248 221 LNLeALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVA 284
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-280 |
1.88e-60 |
|
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: 193.60 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWK---------SFESDAYHSTRHALDVGYRHLDTAFVY-ENEAE--VGQAISEkiaegvVTREEVFVTT 80
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYgGGHAEelVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KLGGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsNVHGTLEltdvdylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP---------NPSIPIE-------ETLRAMEELVEEGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLAN-CRIRPVVNQVECHPGFQ--QRQLREHAKRHGLVICAYCPLARPQPARQWPPFLYDEhaqnLAKKYG 237
Cdd:cd19072 139 NFSLEELEEAQSYlKKGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPLLDE----IAKKYG 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 20129731 238 RTTAQICLRYLVQL-GVVPLPKSSNKARIEENFRVFDFELSPDD 280
Cdd:cd19072 215 KTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-286 |
2.50e-55 |
|
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: 181.28 E-value: 2.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 10 LNNGREMPTLGLGTWKSFES--DAYHSTRHALDVGYRHLDTAFVYENEAEVGQAISEKIAEG-VVTREEVFVTTKLGGIH 86
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPVGQ--------KFHNDSNVHGTLELTDvDYLDTWREMEKLVDLGLTRSIG 158
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspKLGPDGKYVILKDLTE-NPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 159 LSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREHAKRHGLVICAYCPLARPQPARQWPPFLYDEHAQN-LAKKYG 237
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVSENPTLNeVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 20129731 238 RTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVfdFELSPDDVAGMEQ 286
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQ 288
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
16-294 |
2.00e-51 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 170.59 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWKSFESDAYHSTRHALDVGYRHLDTAFVYENEAEVGQAisekIAEGVVTREEVFVTTKLGGIHHDPALVERA 95
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 96 CRLSLSNLGLEYVDLYLMHMPVGQKfhndsnvhgtlELTDVDYldtwreMEKLVD---LGLTRSIGLSNFNAAQTERVLA 172
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPSPND-----------EVSVEEF------MQALLEakkQGLTREIGISNFTIALMKQAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 173 ncrirpVV-------NQVECHPGFQQRQLREHAKRHGLVICAYCPLArpqparqWPPFLYDEHAQNLAKKYGRTTAQICL 245
Cdd:PRK11172 142 ------AVgaeniatNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-------YGKVLKDPVIARIAAKHNATPAQVIL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 20129731 246 RYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGMEQYHTGQRTV 294
Cdd:PRK11172 209 AWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-282 |
1.13e-47 |
|
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: 160.88 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRLNNGREMPTLGLGTWKSFESDAYHST-----RHALDVGYRHLDTAFVYEN---EAEVGQAISEKiaegvvtREEVF 77
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQeiealRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 78 VTTKLGGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHndsnvhgtleltdvdylDTWREMEKLVDLGLTRSI 157
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLA-----------------ETVAAMEELKKEGKIRAW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 158 GLSNFNAAQTERVLA-----NCrirpVVNQVECHPGfqQR----QLREHAKRHGLVICAYCPLARPQPARQwpPFLYDEH 228
Cdd:cd19138 137 GVSNFDTDDMEELWAvpgggNC----AANQVLYNLG--SRgieyDLLPWCREHGVPVMAYSPLAQGGLLRR--GLLENPT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 20129731 229 AQNLAKKYGRTTAQICLRYLV-QLGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19138 209 LKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLA 263
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
15-285 |
2.66e-45 |
|
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: 155.46 E-value: 2.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 15 EMPTLGLGTWK------------SFES--DAYhstRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIAegvvtREEVF 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeyGDEDlqAAF---DAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 78 VTTKLGGIHHD--PALVERACRLSLSNLGLEYVDLYLMHMPvgqkFHNDSNVHGTleltdvdyldtWREMEKLVDLGLTR 155
Cdd:cd19093 73 IATKFAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWP----GPWYSQIEAL-----------MDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 156 SIGLSNFNAAQTERV---LANCRIRPVVNQVE---CHPGFQQRQLREHAKRHGLVICAYCPLA------------RPQPA 217
Cdd:cd19093 138 AVGVSNYSADQLRRAhkaLKERGVPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspenPPPGG 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129731 218 RQWPPFLYD--------EHAQNLAKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19093 218 RRRLFGRKNlekvqpllDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
6-282 |
6.90e-45 |
|
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: 154.95 E-value: 6.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRL-NNGREMPTLGLGTWkSFeSDAYHST---------RHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvT 72
Cdd:COG0667 2 EYRRLgRSGLKVSRLGLGTM-TF-GGPWGGVdeaeaiailDAALDAGINFFDTADVYgpgRSEELLGEALKGR------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 73 REEVFVTTKLG--------GIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDsnvhgtlelTDVDYLDTWRE 144
Cdd:COG0667 74 RDDVVIATKVGrrmgpgpnGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP-------D---------PDTPIEETLGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 145 MEKLVDLGLTRSIGLSNFNAAQTERVLANCR--IRPVVNQVECHPGFQQ--RQLREHAKRHGLVICAYCPLAR------- 213
Cdd:COG0667 138 LDELVREGKIRYIGVSNYSAEQLRRALAIAEglPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGglltgky 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 ------PQPARQ----WPPFLYDEHA------QNLAKKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEENFRVFDFE 275
Cdd:COG0667 218 rrgatfPEGDRAatnfVQGYLTERNLalvdalRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLE 297
|
....*..
gi 20129731 276 LSPDDVA 282
Cdd:COG0667 298 LSAEDLA 304
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-280 |
1.33e-39 |
|
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: 139.63 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWK---------SFESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEkiaegvVTREEVFVTT 80
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KLGGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsNVHGTLEltdvdylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP---------NPNIPLE-------ETLSAMAEGVRQGLIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLANCRIRPVVNQVECH---PGFQQRQLREHAKRHGLVICAYCPLARPQparqwppFLYDEHAQNLAKKYG 237
Cdd:cd19137 139 NFNRRLLEEAISKSQTPIVCNQVKYNledRDPERDGLLEYCQKNGITVVAYSPLRRGL-------EKTNRTLEEIAKNYG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 20129731 238 RTTAQICLRYLVQL-GVVPLPKSSNKARIEENFRVFDFELSPDD 280
Cdd:cd19137 212 KTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-270 |
1.49e-38 |
|
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: 136.11 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGTWkSF-----ESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIAegvvtREEVFVTTKLG----- 83
Cdd:cd06660 1 SRLGLGTM-TFggdgdEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-----RDDVVIATKGGhppgg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 ---GIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNvhgtlelTDVDylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd06660 75 dpsRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD-------DPS-------TPVE--ETLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLANCR----IRPVVNQVE---CHPGFQQRQLREHAKRHGLVICAYCPLARpqparqwppflydehaqnla 233
Cdd:cd06660 139 NWSAERLAEALAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR-------------------- 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 20129731 234 kkyGRttAQICLRYLVQ--LGVVPLPKSSNKARIEENFR 270
Cdd:cd06660 199 ---GP--AQLALAWLLSqpFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
17-286 |
1.06e-36 |
|
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: 132.71 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGTWkSF----------ESDAYHSTRHALDVGYRHLDTAFVYEN-EAE--VGQAISEKiaegvvtREEVFVTTKLG 83
Cdd:cd19085 2 SRLGLGCW-QFgggywwgdqdDEESIATIHAALDAGINFFDTAEAYGDgHSEevLGKALKGR-------RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 GIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsnvhgtleLTDVDYLDTWREMEKLVDLGLTRSIGLSNFN 163
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP----------------SSDVPLEETMEALEKLKEEGKIRAIGVSNFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 164 AAQTERVLANCRIrpVVNQVECHPGFQQ--RQLREHAKRHGLVICAYCPLA------RPQPARQWPP-------FLY--D 226
Cdd:cd19085 138 PAQLEEALDAGRI--DSNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLAqglltgKFSSAEDFPPgdartrlFRHfeP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129731 227 EHAQN----------LAKKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEENFRVFDFELSPDDVAGMEQ 286
Cdd:cd19085 216 GAEEEtfealeklkeIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
6-282 |
2.90e-34 |
|
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: 126.56 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRL-NNGREMPTLGLG----TW---KSFESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvtRE 74
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 75 EVFVTTKLG----------GIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNVhgTLEltdvdylDTWRE 144
Cdd:cd19076 74 EVVIATKFGivrdpgsgfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV-------DPNV--PIE-------ETVGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 145 MEKLVDLGLTRSIGLSNFNAAQTERvlANcRIRPVVN-QVECHPgfQQRQLREH----AKRHGLVICAYCPLAR------ 213
Cdd:cd19076 138 MAELVEEGKVRYIGLSEASADTIRR--AH-AVHPITAvQSEYSL--WTRDIEDEvlptCRELGIGFVAYSPLGRgfltga 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 --------PQPARQWPPFLYDEHAQN----------LAKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENFRVFD 273
Cdd:cd19076 213 ikspedlpEDDFRRNNPRFQGENFDKnlklvekleaIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALD 292
|
....*....
gi 20129731 274 FELSPDDVA 282
Cdd:cd19076 293 VVLTPEELA 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-286 |
4.78e-33 |
|
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: 123.55 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 18 TLGLGTWKSF------------ESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvtREEVFVTTKL 82
Cdd:cd19102 3 TIGLGTWAIGgggwgggwgpqdDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 G---------GIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGqkfhndsnvhgtleltDVDYLDTWREMEKLVDLGL 153
Cdd:cd19102 76 GllwdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP----------------DEPIEEAWGALAELKEEGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 154 TRSIGLSNFNAAQTERVLAncrIRPV-VNQVE---CHPGFQQRQLReHAKRHGLVICAYCPLAR-------------PQP 216
Cdd:cd19102 140 VRAIGVSNFSVDQMKRCQA---IHPIaSLQPPyslLRRGIEAEILP-FCAEHGIGVIVYSPMQSglltgkmtpervaSLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 217 ARQWPP----FLYDEHAQNL---------AKKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEENFRVFDFELSPDDV 281
Cdd:cd19102 216 ADDWRRrspfFQEPNLARNLalvdalrpiAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLRLTPEEL 295
|
....*
gi 20129731 282 AGMEQ 286
Cdd:cd19102 296 AEIEA 300
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
15-285 |
2.77e-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: 121.09 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 15 EMPTLGLGTW--------KSFESDAYHSTRHALDVGYRHLDTAFVYEN-EAE--VGQAISEKiaegvvtREEVFVTTKLG 83
Cdd:cd19084 3 KVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFgHSEeiLGKALKGR-------RDDVVIATKCG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 -------GIHHD--PALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNvhgtlelTDVDylDTWREMEKLVDLGLT 154
Cdd:cd19084 76 lrwdggkGVTKDlsPESIRKEVEQSLRRLQTDYIDLYQIHWP-------DPN-------TPIE--ETAEALEKLKKEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 155 RSIGLSNFNAAQTERVLANCRIrpVVNQVECHPGFQQ--RQLREHAKRHGLVICAYCPLAR--------------PQPAR 218
Cdd:cd19084 140 RYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQglltgkykkeptfpPDDRR 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129731 219 QWPPFLYDEHAQN----------LAKKYGRTTAQICLRYLV-QLGV-VPLPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19084 218 SRFPFFRGENFEKnleivdklkeIAEKYGKSLAQLAIAWTLaQPGVtSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
36-277 |
1.04e-28 |
|
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: 110.77 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVYeneaevGQAISEK-IAEGVVTR-EEVFVTTKLG---------GIHHDPALVERACRLSLSNLG 104
Cdd:cd19088 31 RRALELGVNFIDTADSY------GPDVNERlIAEALHPYpDDVVIATKGGlvrtgpgwwGPDGSPEYLRQAVEASLRRLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 105 LEYVDLYLMHMPvgqkfhnDsnvhgtlelTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCRIRPVVNQVe 184
Cdd:cd19088 105 LDRIDLYQLHRI-------D---------PKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRIVSVQNRY- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 185 chpGFQQRQ---LREHAKRHGLVICAYCPLARPQPARQWPPFlydehaQNLAKKYGRTTAQICLRYLVQLG--VVPLPKS 259
Cdd:cd19088 168 ---NLANRDdegVLDYCEAAGIAFIPWFPLGGGDLAQPGGLL------AEVAARLGATPAQVALAWLLARSpvMLPIPGT 238
|
250
....*....|....*...
gi 20129731 260 SNKARIEENFRVFDFELS 277
Cdd:cd19088 239 SSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
6-287 |
2.21e-27 |
|
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: 108.68 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRL-NNGREMPTLGLGTW--------KSFESDAYHSTRHALDVGYRHLDTAFVY-ENEAEVGQAIseKIAEGvvTREE 75
Cdd:cd19144 2 PTRTLgRNGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 76 VFVTTKLGG----------IHHDPALVERACRLSLSNLGLEYVDLYLMHmpvgqkfhndsNVHGTLELTdvdylDTWREM 145
Cdd:cd19144 78 IFLATKFGIeknvetgeysVDGSPEYVKKACETSLKRLGVDYIDLYYQH-----------RVDGKTPIE-----KTVAAM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 146 EKLVDLGLTRSIGLSNFNAAQTERVlanCRIRPVVN-QVECHPgFQ------QRQLREHAKRHGLVICAYCPLAR----- 213
Cdd:cd19144 142 AELVQEGKIKHIGLSECSAETLRRA---HAVHPIAAvQIEYSP-FSldierpEIGVLDTCRELGVAIVAYSPLGRgfltg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 ---------PQPARQWPP-FLYDEHAQNL---------AKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENFRVF 272
Cdd:cd19144 218 airspddfeEGDFRRMAPrFQAENFPKNLelvdkikaiAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|....*
gi 20129731 273 DFELSPDDVAGMEQY 287
Cdd:cd19144 298 KVKLTEEEEKEIREI 312
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
18-279 |
4.33e-24 |
|
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: 99.20 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 18 TLGLGTWKSF-----ESDAYHSTRHALDVGYRHLDTAFVYEN---EAEVGQAISEkiaegvVTREEVFVTTKL----GGI 85
Cdd:cd19074 6 ELSLGTWLTFggqvdDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfwptGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPAL-----VErACRLSLSNLGLEYVDLYLMHMPvgqkfhnDsnvhgtlELTDVDylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19074 80 PNDRGLsrkhiFE-SIHASLKRLQLDYVDIYYCHRY-------D-------PETPLE--ETVRAMDDLIRQGKILYWGTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAQTERVLANCR----IRPVVNQVECHPGFQQR--QLREHAKRHGLVICAYCPLA-----------RPQPAR----- 218
Cdd:cd19074 143 EWSAEQIAEAHDLARqfglIPPVVEQPQYNMLWREIeeEVIPLCEKNGIGLVVWSPLAqglltgkyrdgIPPPSRsratd 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129731 219 -QWPPF----LYDEHA------QNLAKKYGRTTAQI----CLRylvQLGVV-PLPKSSNKARIEENFRVFDFELSPD 279
Cdd:cd19074 223 eDNRDKkrrlLTDENLekvkklKPIADELGLTLAQLalawCLR---NPAVSsAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-285 |
9.06e-24 |
|
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: 98.81 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 8 IRL-NNGREMPTLGLGTWkSFESDAYHS-----------TRHALDVGYRHLDTAFVYEN-EAE--VGQAISEkiaegVVT 72
Cdd:cd19079 3 VRLgNSGLKVSRLCLGCM-SFGDPKWRPwvldeeesrpiIKRALDLGINFFDTANVYSGgASEeiLGRALKE-----FAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 73 REEVFVTTKLGG-IHHDP-------ALVERACRLSLSNLGLEYVDLYLMHMpvgqkFHNDSNVHGTLE-LTDVdyldtwr 143
Cdd:cd19079 77 RDEVVIATKVYFpMGDGPngrglsrKHIMAEVDASLKRLGTDYIDLYQIHR-----WDYETPIEETLEaLHDV------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 144 emeklVDLGLTRSIGLSNFNAAQTERVL----ANCRIRPVVNQvechpGF-------QQRQLREHAKRHGLVICAYCPLA 212
Cdd:cd19079 145 -----VKSGKVRYIGASSMYAWQFAKALhlaeKNGWTKFVSMQ-----NHynllyreEEREMIPLCEEEGIGVIPWSPLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 213 RPQPARQWPP---------------FLYDEHA--------QNLAKKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEE 267
Cdd:cd19079 215 RGRLARPWGDtterrrsttdtaklkYDYFTEAdkeivdrvEEVAKERGVSMAQVALAWLLSKPGVtaPIVGATKLEHLED 294
|
330
....*....|....*...
gi 20129731 268 NFRVFDFELSPDDVAGME 285
Cdd:cd19079 295 AVAALDIKLSEEEIKYLE 312
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
38-286 |
4.58e-23 |
|
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: 96.91 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 38 ALDVGYRHLDTAFVYEN-EAEV--GQAISEKiaegvvtREEVFVTTKLGGI------------HHdpalVERACRLSLSN 102
Cdd:cd19091 48 ALDAGINFFDTADVYSEgESEEilGKALKGR-------RDDVLIATKVRGRmgegpndvglsrHH----IIRAVEASLKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 103 LGLEYVDLYLMHMPvgqkfhnDSnvhgtleLTDVDylDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCR----IRP 178
Cdd:cd19091 117 LGTDYIDLYQLHGF-------DA-------LTPLE--ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 179 VVNQVecHPGFQQRQLrEH-----AKRHGLVICAYCPLA---------RPQPA-------RQWPPFLY--DEHAQNL--- 232
Cdd:cd19091 181 VALQA--YYSLLGRDL-EHelmplALDQGVGLLVWSPLAggllsgkyrRGQPApegsrlrRTGFDFPPvdRERGYDVvda 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 233 ----AKKYGRTTAQICLRYLVQLGVVplpkSS------NKARIEENFRVFDFELSPDDVAGMEQ 286
Cdd:cd19091 258 lreiAKETGATPAQVALAWLLSRPTV----SSviigarNEEQLEDNLGAAGLSLTPEEIARLDK 317
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-277 |
9.46e-23 |
|
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: 95.32 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTW---KSFESD--AYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIAEgvvtREEVFVTTKl 82
Cdd:cd19092 1 PEGLEVSRLVLGCMrlaDWGESAeeLLSLIEAALELGITTFDHADIYgggKCEELFGEALALNPGL----REKIEIQTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 GGI------------HHD--PALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsnvhgtleltdvDYL----DTWRE 144
Cdd:cd19092 76 CGIrlgddprpgrikHYDtsKEHILASVEGSLKRLGTDYLDLLLLHRP--------------------DPLmdpeEVAEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 145 MEKLVDLGLTRSIGLSNFNAAQTERVLANCRIRPVVNQVE----CHPGFQQRQLrEHAKRHGLVICAYCPLA-----RPQ 215
Cdd:cd19092 136 FDELVKSGKVRYFGVSNFTPSQIELLQSYLDQPLVTNQIElsllHTEAIDDGTL-DYCQLLDITPMAWSPLGggrlfGGF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 216 PARQwpPFLYDEhAQNLAKKYGRTTAQICLRYLVQL--GVVPLPKSSNKARIEENFRVFDFELS 277
Cdd:cd19092 215 DERF--QRLRAA-LEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
18-248 |
1.79e-22 |
|
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: 95.08 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 18 TLGLGTWK---SFESDAYH--STRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIAEGVVTREEVFVTTKLGGIHHD- 88
Cdd:cd19099 5 SLGLGTYRgdsDDETDEEYreALKAALDSGINVIDTAINYrggRSERLIGKALRELIEKGGIKRDEVVIVTKAGYIPGDg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 --------------------------------PALVERACRLSLSNLGLEYVDLYLMHMPVGQKFHNDSNvhgtleltdv 136
Cdd:cd19099 85 deplrplkyleeklgrglidvadsaglrhcisPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEE---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 137 DYLDTWRE----MEKLVDLGLTRSIGLSNFN------------------AAQTERVLANCRIRPVvnQVECHPGFQQRQL 194
Cdd:cd19099 155 EFYDRLEEafeaLEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKVI--QLPLNLLEPEALT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129731 195 R------------EHAKRHGLVICAYCPLARPQPARQWPPflydehAQNLAKKYGRTTAQICLRYL 248
Cdd:cd19099 233 EkntvkgealsllEAAKELGLGVIASRPLNQGQLLGELRL------ADLLALPGGATLAQRALQFA 292
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
6-284 |
1.26e-20 |
|
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: 89.80 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRL-NNGREMPTLGLG---------TWKSfESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIaegvvt 72
Cdd:cd19145 1 PRVKLgSQGLEVSAQGLGcmglsgdygAPKP-EEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 73 REEVFVTTKLG---------GIHHDPALVERACRLSLSNLGLEYVDLYLMHmpvgqkfHNDsnvhgtlelTDVDYLDTWR 143
Cdd:cd19145 74 REKVQLATKFGiheiggsgvEVRGDPAYVRAACEASLKRLDVDYIDLYYQH-------RID---------TTVPIEITMG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 144 EMEKLVDLGLTRSIGLSNFNAAQTERVLAncrIRPvVNQVECHPGFQQRQLREH----AKRHGLVICAYCPLAR----PQ 215
Cdd:cd19145 138 ELKKLVEEGKIKYIGLSEASADTIRRAHA---VHP-ITAVQLEWSLWTRDIEEEiiptCRELGIGIVPYSPLGRgffaGK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 216 PA-----------RQWPPF----------LYdEHAQNLAKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENFRVF 272
Cdd:cd19145 214 AKleellensdvrKSHPRFqgenleknkvLY-ERVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGAL 292
|
330
....*....|..
gi 20129731 273 DFELSPDDVAGM 284
Cdd:cd19145 293 SVKLTKEDLKEI 304
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
30-273 |
2.86e-20 |
|
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: 88.76 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 30 DAYhstrhaLDVGYRHLDTAFVYENEAEVGQaiSEKI------AEGVvtREEVFVTTKlGGIHH---------DPALVER 94
Cdd:cd19082 24 DAF------VELGGNFIDTARVYGDWVERGA--SERVigewlkSRGN--RDKVVIATK-GGHPDledmsrsrlSPEDIRA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 95 ACRLSLSNLGLEYVDLYLMH-----MPVGqkfhndsnvhgtlELTDVdyldtwreMEKLVDLGLTRSIGLSNFNaaqTER 169
Cdd:cd19082 93 DLEESLERLGTDYIDLYFLHrddpsVPVG-------------EIVDT--------LNELVRAGKIRAFGASNWS---TER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 170 VLA-------NCRIRPVVNQV---------ECHPG----FQQRQLREHAKRHGLVICAYCPLAR---------PQPARQW 220
Cdd:cd19082 149 IAEanayakaHGLPGFAASSPqwslarpnePPWPGptlvAMDEEMRAWHEENQLPVFAYSSQARgffskraagGAEDDSE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129731 221 PPFLYD--------EHAQNLAKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENFRVFD 273
Cdd:cd19082 229 LRRVYYseenferlERAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-212 |
5.45e-20 |
|
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: 86.76 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTWkSFESDAYHST---------RHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvtREEVFVTTKLGGIH 86
Cdd:cd19086 6 IGFGTW-GLGGDWWGDVddaeairalRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 87 H---------DPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsnvhgTLELTDVDylDTWREMEKLVDLGLTRSI 157
Cdd:cd19086 78 DggperpqdfSPEYIREAVEASLKRLGTDYIDLYQLHNP-------------PDEVLDND--ELFEALEKLKQEGKIRAY 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 20129731 158 GLSNFNAAQTERVLANCRIRPVvnQVECHPgFQQR---QLREHAKRHGLVICAYCPLA 212
Cdd:cd19086 143 GVSVGDPEEALAALRRGGIDVV--QVIYNL-LDQRpeeELFPLAEEHGVGVIARVPLA 197
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-271 |
1.77e-19 |
|
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: 85.75 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGTWKSF-------ESDAYHSTRHALDVGYRHLDTAFVYEN-EAEVGQAISEkiaegvVTREEVFVTTKLG----- 83
Cdd:cd19095 1 SVLGLGTSGIGrvwgvpsEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGthgeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 -GIHHD--PALVERACRLSLSNLGLEYVDLYLmhmpvgqkFHNDSNVhgtlELTDvdylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19095 75 gRDRKDfsPAAIRASIERSLRRLGTDYIDLLQ--------LHGPSDD----ELTG----EVLETLEDLKAAGKVRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 NFNAAqTERVLANCRIRPVvnQVECHPGFQ-QRQLREHAKRHGLVICAYCPLAR---PQPARQWPPFLYDEHAQNLAKKY 236
Cdd:cd19095 139 GDGEE-LEAAIASGVFDVV--QLPYNVLDReEEELLPLAAEAGLGVIVNRPLANgrlRRRVRRRPLYADYARRPEFAAEI 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 20129731 237 G-RTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRV 271
Cdd:cd19095 216 GgATWAQAALRFVLSHPGVSsaIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
20-213 |
3.00e-19 |
|
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: 85.82 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 20 GLGTWK--------SFESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvVTREEVFVTTKLGGIHHD 88
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEY-----GKRDRVVIATKVGLEWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVERACRL---------SLSNLGLEYVDLYLMHMPvgqkfhnDsnvhgtlELTDVDylDTWREMEKLVDLGLTRSIGL 159
Cdd:cd19148 83 GGEVVRNSSParirkevedSLRRLQTDYIDLYQVHWP-------D-------PLVPIE--ETAEALKELLDEGKIRAIGV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 20129731 160 SNFNAAQTERVLANCRI---RPVVNQVEchPGFQQRQLReHAKRHGLVICAYCPLAR 213
Cdd:cd19148 147 SNFSPEQMETFRKVAPLhtvQPPYNLFE--REIEKDVLP-YARKHNIVTLAYGALCR 200
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
11-282 |
5.13e-19 |
|
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: 85.34 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTWkSFESDAYHSTRHAL-----DVGYRHLDTAFVY----------ENEAEVGQAISEKIAegvvtREE 75
Cdd:cd19081 4 RTGLSVSPLCLGTM-VFGWTADEETSFALldafvDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRGK-----RDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 76 VFVTTKLG--------GIHhdPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNVHgtLEltdvdylDTWREMEK 147
Cdd:cd19081 78 VVIATKVGfpmgpngpGLS--RKHIRRAVEASLRRLQTDYIDLYQAHWD-------DPATP--LE-------ETLGALND 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 148 LVDLGLTRSIGLSNFNAAQTERVLANCR----IRPVVNQVE----CHPGFQQRqLREHAKRHGLVICAYCPLA------- 212
Cdd:cd19081 140 LIRQGKVRYIGASNYSAWRLQEALELSRqhglPRYVSLQPEynlvDRESFEGE-LLPLCREEGIGVIPYSPLAggfltgk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 213 --RPQP------ARQWPPFLYDEHA-------QNLAKKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEENFRVFDFE 275
Cdd:cd19081 219 yrSEADlpgstrRGEAAKRYLNERGlrildalDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLR 298
|
....*..
gi 20129731 276 LSPDDVA 282
Cdd:cd19081 299 LTDEEVA 305
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
11-286 |
5.38e-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: 85.40 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTW---------KSFESDAYHSTRHALDVGYRHLDTAFVYEN---EAEVGQAISEKiaegvvtREEVFV 78
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 79 TTKLGGIHHD-------------------PALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNvhgtlelTDVDyl 139
Cdd:cd19149 79 ATKCGLRWDReggsfffvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQ-------DVE-------TPIE-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 140 DTWREMEKLVDLGLTRSIGLSNFNAAQTErvlANCRIRPV-VNQVE---CHPGFQQRQLrEHAKRHGLVICAYCPLAR-- 213
Cdd:cd19149 143 ETMEALEELKRQGKIRAIGASNVSVEQIK---EYVKAGQLdIIQEKysmLDRGIEKELL-PYCKKNNIAFQAYSPLEQgl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 ------------PQPARQWPPFL----------YDEHAQNLAKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENF 269
Cdd:cd19149 219 ltgkitpdrefdAGDARSGIPWFspenrekvlaLLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENA 298
|
330
....*....|....*..
gi 20129731 270 RVFDFELSPDDVAGMEQ 286
Cdd:cd19149 299 KAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
36-285 |
9.43e-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: 84.59 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvtREEVFVTTKLgGIHHD------------PALVERACRLSL 100
Cdd:cd19078 32 RKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKF-GFKIDggkpgplgldsrPEHIRKAVEGSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 101 SNLGLEYVDLYLMH-----MPVGQkfhndsnVHGTleltdvdyldtwreMEKLVDLGLTRSIGLSNFNAAQTERVLANCr 175
Cdd:cd19078 104 KRLQTDYIDLYYQHrvdpnVPIEE-------VAGT--------------MKELIKEGKIRHWGLSEAGVETIRRAHAVC- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 176 irPVVN-QVECHPGFqqrqlREHAKRH---------GLVicAYCPLAR--------------PQPARQWPPFLYDEH-AQ 230
Cdd:cd19078 162 --PVTAvQSEYSMMW-----REPEKEVlptleelgiGFV--PFSPLGKgfltgkidentkfdEGDDRASLPRFTPEAlEA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129731 231 N---------LAKKYGRTTAQICLRYLVQLG--VVPLPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19078 233 NqalvdllkeFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-160 |
2.88e-17 |
|
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: 80.77 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVY-ENEAEV--GQAISEKiaegvvtREEVFVTTKlGGIHHDPAL-----VERACRLSLSNLGLEY 107
Cdd:cd19104 39 RRALDLGINFFDTAPSYgDGKSEEnlGRALKGL-------PAGPYITTK-VRLDPDDLGdiggqIERSVEKSLKRLKRDS 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 20129731 108 VDLYLMHMPVGQKfhNDSNVHGTLELTDVDYLD-TWREMEKLVDLGLTRSIGLS 160
Cdd:cd19104 111 VDLLQLHNRIGDE--RDKPVGGTLSTTDVLGLGgVADAFERLRSEGKIRFIGIT 162
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-160 |
6.03e-17 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 80.25 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTWKSFESDAYHST---RHALDVGYRHLDTAFVYEN-EAEVGQAISEkiaegvvTREEVFVTTKLGGIH 86
Cdd:COG1453 8 KTGLEVSVLGFGGMRLPRKDEEEAEaliRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKLPPWV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 87 HDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsNVHGTLELTDVDyLDTWREMEKLVDLGLTRSIGLS 160
Cdd:COG1453 81 RDPEDMRKDLEESLKRLQTDYIDLYLIHGL---------NTEEDLEKVLKP-GGALEALEKAKAEGKIRHIGFS 144
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-270 |
1.52e-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: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGT----WKSFEsDAYHSTRHALDVGYRHLDTAFVYEN-EAEVGQAISEKiaegvvtREEVFVTTKLGGihH 87
Cdd:cd19100 8 GLKVSRLGFGGgplgRLSQE-EAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGA--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 88 DPALVERACRLSLSNLGLEYVDLYLMHmpvgqkfhndsnvhgtleltDVDYLDTWRE----------MEKLVDLGLTRSI 157
Cdd:cd19100 78 DYEGAKRDLERSLKRLGTDYIDLYQLH--------------------AVDTEEDLDQvfgpggaleaLLEAKEEGKIRFI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 158 GLSNFNAAQTERVLancRIRPV------VNQVECHPGFQQRQLREHAKRHGLVICAYCPLArpqpARQWPpflydehaqn 231
Cdd:cd19100 138 GISGHSPEVLLRAL---ETGEFdvvlfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLA----GGRLL---------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 20129731 232 lakKYGRTTAQICLRYLVQLGVV--PLPKSSNKARIEENFR 270
Cdd:cd19100 201 ---SGDPLDPEQALRYALSLPPVdvVIVGMDSPEELDENLA 238
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
36-285 |
5.30e-16 |
|
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: 77.07 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvTREEVFVTTKLG--------GIHHDPALVERACRLSLSNLG 104
Cdd:cd19083 40 REALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAhkfggdgsVLNNSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 105 LEYVDLYLMHMPVGQKFHNDSnvHGTLeltdvdyldtwremEKLVDLGLTRSIGLSNFNAAQTERVLANcrirPVVNQVE 184
Cdd:cd19083 114 TDYIDLYYIHFPDGETPKAEA--VGAL--------------QELKDEGKIRAIGVSNFSLEQLKEANKD----GYVDVLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 185 CHPGFQQRQLREH----AKRHGLVICAYCPLA--------------RPQPARQ-WPPFLYDEHAQNL---------AKKY 236
Cdd:cd19083 174 GEYNLLQREAEEDilpyCVENNISFIPYFPLAsgllagkytkdtkfPDNDLRNdKPLFKGERFSENLdkvdklksiADEK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 20129731 237 GRTTAQICLR-YLVQLGV-VPLPKSSNKARIEENFRVFDFELSPDDVAGME 285
Cdd:cd19083 254 GVTVAHLALAwYLTRPAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFID 304
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-160 |
5.76e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 75.70 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 6 PTIRL-NNGREMPTLGLGTwkSFESDAYHST-RHALDVGYRHLDTAFVY---ENEAEVGQAISEkiaegvVTREEVFVTT 80
Cdd:cd19105 2 PYRTLgKTGLKVSRLGFGG--GGLPRESPELlRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 K--LGGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVGQKFH-NDSNVHgtleltdvdyldtwREMEKLVDLGLTRSI 157
Cdd:cd19105 74 KasPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERlLNEELL--------------EALEKLKKEGKVRFI 139
|
...
gi 20129731 158 GLS 160
Cdd:cd19105 140 GFS 142
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-286 |
1.59e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 75.32 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 28 ESDAYHSTRHALDVGYRHLDTAFVYEN-EAEVGQAIsEKIAEGVVTREEVFVTTKL----GGIHHDPALVERACRLSLSN 102
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFR-KRLRRERDAADDVQIHTKWvpdpGELTMTRAYVEAAIDRSLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 103 LGLEYVDLYLMHmpvgqkFHNDSnvhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANcRIRPVVNQ 182
Cdd:cd19101 101 LGVDRLDLVQFH------WWDYS---------DPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA-GVPIVSNQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 183 VEcHPGFQQR---QLREHAKRHGLVICAYCPLA----------RPQPARQ-------------------WPPFlydehaQ 230
Cdd:cd19101 165 VQ-YSLLDRRpenGMAALCEDHGIKLLAYGTLAggllsekylgVPEPTGPaletrslqkyklmidewggWDLF------Q 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129731 231 NL-------AKKYGRTTAQICLRYLVQ--------LGVvplpksSNKARIEENFRVFDFELSPDDVAGMEQ 286
Cdd:cd19101 238 ELlrtlkaiADKHGVSIANVAVRWVLDqpgvagviVGA------RNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
19-249 |
1.70e-15 |
|
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: 75.29 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTWKSFESDA-YHSTRHALDV----GYRHLDTAFVYENeaevGQaiSEK-IAEGVVTREEVFVTTK---LGGIHHDP 89
Cdd:cd19075 5 LGTMTFGSQGRFTtAEAAAELLDAflerGHTEIDTARVYPD----GT--SEElLGELGLGERGFKIDTKanpGVGGGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 90 ALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDsnvHGT-LEltdvdylDTWREMEKLVDLGLTRSIGLSNFNAAQTE 168
Cdd:cd19075 79 ENVRKQLETSLKRLKVDKVDVFYLHAP-------D---RSTpLE-------ETLAAIDELYKEGKFKEFGLSNYSAWEVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 169 RVLANCR----IRPVVNQ---------VE-----ChpgfqqrqLRehakRHGLVICAYCPLA------------------ 212
Cdd:cd19075 142 EIVEICKengwVLPTVYQgmynaitrqVEtelfpC--------LR----KLGIRFYAYSPLAggfltgkykysedkaggg 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20129731 213 RPQPARQWPPFLYD-----------EHAQNLAKKYGRTTAQICLRYLV 249
Cdd:cd19075 210 RFDPNNALGKLYRDrywkpsyfealEKVEEAAEKEGISLAEAALRWLY 257
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
19-213 |
3.01e-15 |
|
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: 74.92 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTwKSF-----ESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvtREEVFVTTKLGGIHHDPA 90
Cdd:cd19087 16 LCLGT-MNFggrtdEETSFAIMDRALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATKVFGPMGDDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 91 --------LVERACRLSLSNLGLEYVDLYLMHmpvgqkfHNDSNVHgtLEltdvdylDTWREMEKLVDLGLTRSIGLSNF 162
Cdd:cd19087 88 ndrglsrrHIRRAVEASLRRLQTDYIDLYQMH-------HFDRDTP--LE-------ETLRALDDLVRQGKIRYIGVSNF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 163 NAAQTERVLANCR---------IRPVVNQVECHPgfqQRQLREHAKRHGLVICAYCPLAR 213
Cdd:cd19087 152 AAWQIAKAQGIAArrgllrfvsEQPMYNLLKRQA---ELEILPAARAYGLGVIPYSPLAG 208
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-279 |
3.94e-15 |
|
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: 74.13 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGT------WKSFESDAYHST-RHALDVGYRHLDTAFVY-ENEAEVGQAISEkiaegvVTREEVFVTTKLG---GI 85
Cdd:cd19090 1 SALGLGTaglggvFGGVDDDEAVATiRAALDLGINYIDTAPAYgDSEERLGLALAE------LPREPLVLSTKVGrlpED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHD--PALVERACRLSLSNLGLEYVDLYLMHMP--VGQKFHNDSNvhGTLEltdvdyldtwrEMEKLVDLGLTRSIGLS- 160
Cdd:cd19090 75 TADysADRVRRSVEESLERLGRDRIDLLMIHDPerVPWVDILAPG--GALE-----------ALLELKEEGLIKHIGLGg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 161 -----NFNAAQTER---VLANCRIRPVvnqveCHPGFQqrQLREHAKRHGLVICAYCPLA----------RPQPARQWPP 222
Cdd:cd19090 142 gppdlLRRAIETGDfdvVLTANRYTLL-----DQSAAD--ELLPAAARHGVGVINASPLGmgllagrppeRVRYTYRWLS 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 223 FLYDEHAQ---NLAKKYGRTTAQICLRYLVQL----GVVPLPksSNKARIEENFRVFDFELSPD 279
Cdd:cd19090 215 PELLDRAKrlyELCDEHGVPLPALALRFLLRDprisTVLVGA--SSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-286 |
1.30e-14 |
|
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: 72.75 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 16 MPTLGLGTWkSFESDAY--------HSTR--------HALDVGYRHLDTAFVYeneaevGQAISEKIAEGVVT---REEV 76
Cdd:cd19103 4 LPKIALGTW-SWGSGGAggdqvfgnHLDEdtlkavfdKAMAAGLNLWDTAAVY------GMGASEKILGEFLKrypREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 77 FVTTKL--GGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPvgqkfhndsnvhgtlelTDVDyldtwREMEKLVDL--- 151
Cdd:cd19103 77 IISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP-----------------ADVE-----RWTPELIPLlks 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 152 GLTRSIGLSNFNAAQTERVL-----ANCRIRPVVNQVE-CHPGFQQRQLREHAKRHGLVICAYCPL-----------ARP 214
Cdd:cd19103 135 GKVKHVGVSNHNLAEIKRANeilakAGVSLSAVQNHYSlLYRSSEEAGILDYCKENGITFFAYMVLeqgalsgkydtKHP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 215 QPA---------RQWPPF--LYDEHAQnLAKKYGRTTAQICLRYLVQLGVVPLPKSSNKARIEENFRVFDFELSPDDVAG 283
Cdd:cd19103 215 LPEgsgraetynPLLPQLeeLTAVMAE-IGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKE 293
|
...
gi 20129731 284 MEQ 286
Cdd:cd19103 294 LEQ 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-251 |
1.45e-14 |
|
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: 72.17 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVYENeaevgqaiSEK-IAEGVVTREEVFVTTKL----GGIHHDPALVERACRLSLSNLGLEYVDL 110
Cdd:cd19097 33 EYALKAGINTLDTAPAYGD--------SEKvLGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 111 YLmhmpvgqkFHNDSNVhgtleltDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCRIRpVVnQVECHPgFQ 190
Cdd:cd19097 105 LL--------LHNPDDL-------LKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKID-II-QLPFNI-LD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129731 191 QRQLREH----AKRHGLVICA---YC-------PLARPQPARQWPPFLydEHAQNLAKKYGRTTAQICLRYLVQL 251
Cdd:cd19097 167 QRFLKSGllakLKKKGIEIHArsvFLqglllmePDKLPAKFAPAKPLL--KKLHELAKKLGLSPLELALGFVLSL 239
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-268 |
1.32e-13 |
|
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: 69.67 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 39 LDVGYRHLDTAFVY----------ENEAEVGQAISEKIAegvvtREEVFVTTKLGGIHHDPA------------LVERAC 96
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-----RDDVVIATKVGAGPRDPDggpespeglsaeTIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 97 RLSLSNLGLEYVDLYLMHmpvgqkfhndsnvhgtLELTDVDYLDTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCRI 176
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAH----------------VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 177 RPVvnqvechPGF---QQR--------------------QLREHAKRHG-LVICAYCPLARPQPARQWPPFLYDEHAQN- 231
Cdd:cd19752 166 QGW-------AEFsaiQQRhsylrprpgadfgvqrivtdELLDYASSRPdLTLLAYSPLLSGAYTRPDRPLPEQYDGPDs 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 20129731 232 ---------LAKKYGRTTAQICLRYLVQ--LGVVPLPKSSNKARIEEN 268
Cdd:cd19752 239 darlavleeVAGELGATPNQVVLAWLLHrtPAIIPLLGASTVEQLEEN 286
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
30-282 |
1.62e-13 |
|
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: 69.56 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 30 DAYhstrhaLDVGYRHLDTAFVYEN---EAEVGQAISEKiaegvvtREEVFVTTKLGGIHH--DP--------ALVeRAC 96
Cdd:cd19080 38 DAY------VEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYTMNRRpgDPnaggnhrkNLR-RSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 97 RLSLSNLGLEYVDLYLMHMPvgqkfhnDsnvhgtlELTDVDylDTWREMEKLVDLGLTRSIGLSNFNA-----AQTervL 171
Cdd:cd19080 104 EASLRRLQTDYIDLLYVHAW-------D-------FTTPVE--EVMRALDDLVRAGKVLYVGISDTPAwvvarANT---L 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 172 ANCR--IRPVVNQVECHpgFQQRQL-REH---AKRHGLVICAYCPLA----------------RPQPARQWPPFLYDEHA 229
Cdd:cd19080 165 AELRgwSPFVALQIEYS--LLERTPeRELlpmARALGLGVTPWSPLGgglltgkyqrgeegraGEAKGVTVGFGKLTERN 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129731 230 QNL-------AKKYGRTTAQICLRYLVQ--LGVVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:cd19080 243 WAIvdvvaavAEELGRSAAQVALAWVRQkpGVVIPIIGARTLEQLKDNLGALDLTLSPEQLA 304
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
36-273 |
1.74e-13 |
|
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: 68.74 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVY---ENEAEVGQAISEkiaegvVTREEVFVTTKLG-GIHHDPALVERACRLSLSNLGLEYVDLY 111
Cdd:cd19096 28 RYAIDAGINYFDTAYGYgggKSEEILGEALKE------GPREKFYLATKLPpWSVKSAEDFRRILEESLKRLGVDYIDFY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 112 LMHMPvgqkfhndsnVHGTLELTDVDYlDTWREMEKLVDLGLTRSIGLS------NFNAAQTERVLANCRIR-PVVNQve 184
Cdd:cd19096 102 LLHGL----------NSPEWLEKARKG-GLLEFLEKAKKEGLIRHIGFSfhdspeLLKEILDSYDFDFVQLQyNYLDQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 185 chPGFQQRQLREHAKRHGLVICAYCPLA---RPQPArqwppflydEHAQNLAKKYGRTTAQICLRYLVQLGVVPLPKS-- 259
Cdd:cd19096 169 --ENQAGRPGIEYAAKKGMGVIIMEPLKgggLANNP---------PEALAILCGAPLSPAEWALRFLLSHPEVTTVLSgm 237
|
250
....*....|....
gi 20129731 260 SNKARIEENFRVFD 273
Cdd:cd19096 238 STPEQLDENIAAAD 251
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
11-282 |
2.20e-13 |
|
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: 69.21 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGTWKSFESDAYHST-----RHALDVGYRHLDTAFVY-----ENEAEVGQAISEKIAEgvvTREEVFVTT 80
Cdd:cd19089 6 RSGLHLPAISLGLWHNFGDYTSPEEarellRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KLG-GIHHDP-----------ALVERacrlSLSNLGLEYVDLYLMHMPvgqkfhnDSNVhgTLELTdvdyldtwreMEKL 148
Cdd:cd19089 83 KAGyGMWPGPygdggsrkyllASLDQ----SLKRMGLDYVDIFYHHRY-------DPDT--PLEET----------MTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 149 ---VDLGLTRSIGLSNFNAAQTERVLANCR---IRPVVNQVEcHPGFQQ---RQLREHAKRHGLVICAYCPLAR------ 213
Cdd:cd19089 140 adaVRSGKALYVGISNYPGAKARRAIALLRelgVPLIIHQPR-YSLLDRwaeDGLLEVLEEAGIGFIAFSPLAQglltdk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 ------PQPARQWPPFLYDEHAQN------------LAKKYGRTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRVFD 273
Cdd:cd19089 219 ylngipPDSRRAAESKFLTEEALTpekleqlrklnkIAAKRGQSLAQLALSWVLRDPRVTsvLIGASSPSQLEDNVAALK 298
|
330
....*....|
gi 20129731 274 -FELSPDDVA 282
Cdd:cd19089 299 nLDFSEEELA 308
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
18-279 |
1.80e-12 |
|
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: 66.82 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 18 TLGLGT--WKSF--ESDAYHSTRHALDVGYRHLDTAFVYE--NEAEvGQAISEKIA----EGVVTREEVFVTTKL----- 82
Cdd:cd19094 3 EICLGTmtWGEQntEAEAHEQLDYAFDEGVNFIDTAEMYPvpPSPE-TQGRTEEIIgswlKKKGNRDKVVLATKVagpge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 -------GGIHHDPALVERACRLSLSNLGLEYVDLYLMHMPVgqkfhNDSNVHGTLELTD-------VDYLDTWREMEKL 148
Cdd:cd19094 82 gitwprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPD-----RYTPLFGGGYYTEpseeedsVSFEEQLEALGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 149 VDLGLTRSIGLSNFNAAQTERVLANCRI----RPVVNQVE---CHPGFqQRQLREHAKRHGLVICAYCPLA--------- 212
Cdd:cd19094 157 VKAGKIRHIGLSNETPWGVMKFLELAEQlglpRIVSIQNPyslLNRNF-EEGLAEACHRENVGLLAYSPLAggvltgkyl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 213 ----RPQPAR-----QWPPFLYDEHAQ-------NLAKKYGRTTAQICLRYLVQlgvVPLPKS-----SNKARIEENFRV 271
Cdd:cd19094 236 dgaaRPEGGRlnlfpGYMARYRSPQALeavaeyvKLARKHGLSPAQLALAWVRS---RPFVTStiigaTTLEQLKENIDA 312
|
....*...
gi 20129731 272 FDFELSPD 279
Cdd:cd19094 313 FDVPLSDE 320
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
19-184 |
2.76e-12 |
|
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: 66.08 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTWKSF-----ESDAYHSTRHALDVGYRHLDTAFVYEN-EAEV--GQAISEkiaeGVVTREEVFVTTKL-----GGI 85
Cdd:cd19143 16 LSFGSWVTFgnqvdVDEAKECMKAAYDAGVNFFDNAEVYANgQSEEimGQAIKE----LGWPRSDYVVSTKIfwgggGPP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 86 HHDPAL-----VErACRLSLSNLGLEYVDLYLMHMPvgqkfhndsNVHGTLEltdvdylDTWREMEKLVDLGLTRSIGLS 160
Cdd:cd19143 92 PNDRGLsrkhiVE-GTKASLKRLQLDYVDLVFCHRP---------DPATPIE-------ETVRAMNDLIDQGKAFYWGTS 154
|
170 180
....*....|....*....|....*...
gi 20129731 161 NFNAAQTERVLANCR----IRPVVNQVE 184
Cdd:cd19143 155 EWSAQQIEEAHEIADrlglIPPVMEQPQ 182
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
12-282 |
6.84e-12 |
|
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: 64.95 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLG----TWKSFESD---AYHSTRHALDVGYRHLDTAFVY------ENEAEVGQAIsEKIAEgvvTREEVFV 78
Cdd:cd19077 1 NGKLVGPIGLGlmglTWRPNPTPdeeAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFF-RKYPE---YADKVVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 79 TTKLGGI------HHDPALVERACRLSLSNLG-LEYVDLYlmhmpvgqkfhndsnvhgtlELTDVD---YL-DTWREMEK 147
Cdd:cd19077 77 SVKGGLDpdtlrpDGSPEAVRKSIENILRALGgTKKIDIF--------------------EPARVDpnvPIeETIKALKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 148 LVDLGLTRSIGLSNFNAAQTERVLAncrIRPVV-NQVECHPGFQ---QRQLREHAKRHGLVICAYCPLARPQPARQW--- 220
Cdd:cd19077 137 LVKEGKIRGIGLSEVSAETIRRAHA---VHPIAaVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGRGLLTGRIksl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 221 ---PPFLYDEH---------AQNL---------AKKYGRTTAQICLRYLVQLG---VVPLPKSSNKARIEENFRVFDFEL 276
Cdd:cd19077 214 adiPEGDFRRHldrfngenfEKNLklvdalqelAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVEL 293
|
....*.
gi 20129731 277 SPDDVA 282
Cdd:cd19077 294 TDEELK 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
28-273 |
1.80e-11 |
|
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: 63.71 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 28 ESDAYHSTRHALDVGYRHLDTAFVYEN---EAEVGQAISekiAEGVvTREEVFVTTKLG-----GIHHDPALVERACRLS 99
Cdd:cd19153 32 QDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALA---ALQV-PRSSYTVATKVGryrdsEFDYSAERVRASVATS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 100 LSNLGLEYVDLYLMHmpvgqkfhndsnvhgTLELTDVDYL--DTWREMEKLVDLGLTRSIGLSNFNAAQTERVLANCRIR 177
Cdd:cd19153 108 LERLHTTYLDVVYLH---------------DIEFVDYDTLvdEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 178 PV-VNQVECHPGFQQRQL----REHAKRHGLVICAYCPLA----RPQPARQWPPF-----LYDEHAQNLAKKYGRTTAQI 243
Cdd:cd19153 173 SLdAVLSYCHLTLQDARLesdaPGLVRGAGPHVINASPLSmgllTSQGPPPWHPAsgelrHYAAAADAVCASVEASLPDL 252
|
250 260 270
....*....|....*....|....*....|...
gi 20129731 244 CLRYLV--QLGVVP-LPKSSNKARIEENFRVFD 273
Cdd:cd19153 253 ALQYSLaaHAGVGTvLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
11-279 |
7.95e-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: 58.72 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 11 NNGREMPTLGLGT-------WKSFESDAYHSTRHALDVGYRHLDTAFVYeneaevGQAISEKI---AEGVVTREEVFVTT 80
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWY------GQGRSETVlgkALKGIPRDSYYLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KLGGIHHDP--------ALVERACRLSLSNLGLEYVDLYLMHmpvgqkfhndsnvhgtleltDVDYLDTWRE-------- 144
Cdd:cd19163 82 KVGRYGLDPdkmfdfsaERITKSVEESLKRLGLDYIDIIQVH--------------------DIEFAPSLDQilnetlpa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 145 MEKLVDLGLTRSIGLSNFNAAQTERVLANCRIRPVVNQVECHPGFQQRQLREH---AKRHGL-VICAyCPLA----RPQP 216
Cdd:cd19163 142 LQKLKEEGKVRFIGITGYPLDVLKEVLERSPVKIDTVLSYCHYTLNDTSLLELlpfFKEKGVgVINA-SPLSmgllTERG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 217 ARQWPPFLYD-----EHAQNLAKKYGRTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRVFDFELSPD 279
Cdd:cd19163 221 PPDWHPASPEikeacAKAAAYCKSRGVDISKLALQFALSNPDIAttLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
15-289 |
1.08e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 58.71 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 15 EMPTLGLGTW----KSFESDAYHSTRHALDVGYRHLDTAFVYE----------NEAEVGQAISEKiaegvVTREEVFVTT 80
Cdd:PRK10625 12 EVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GSREKLIIAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 81 KLGG--------IHHDPAL----VERACRLSLSNLGLEYVDLYLMHMPVGQkfhndSNVHGTL--ELTD----VDYLDTW 142
Cdd:PRK10625 87 KVSGpsrnndkgIRPNQALdrknIREALHDSLKRLQTDYLDLYQVHWPQRP-----TNCFGKLgySWTDsapaVSLLETL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 143 REMEKLVDLGLTRSIGLSNFNAAQTERV--LANCRIRPVVNQVECHPGFQQRQ----LREHAKRHGLVICAYCPL----- 211
Cdd:PRK10625 162 DALAEQQRAGKIRYIGVSNETAFGVMRYlhLAEKHDLPRIVTIQNPYSLLNRSfevgLAEVSQYEGVELLAYSCLafgtl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 212 -------ARPQPARQ--WPPFL-YD-EHAQ-------NLAKKYGRTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRV 271
Cdd:PRK10625 242 tgkylngAKPAGARNtlFSRFTrYSgEQTQkavaayvDIAKRHGLDPAQMALAFVRRQPFVAstLLGATTMEQLKTNIES 321
|
330
....*....|....*...
gi 20129731 272 FDFELSPDDVAGMEQYHT 289
Cdd:PRK10625 322 LHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
13-282 |
2.21e-09 |
|
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: 57.46 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 13 GREMPTLGLGTWKSFESDAYHST-----RHALDVGYRHLDTAFVY-----ENEAEVGQAISEKIAEgvvTREEVFVTTKL 82
Cdd:cd19150 9 GLKLPALSLGLWHNFGDDTPLETqrailRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAG---YRDELIISTKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 G--------GIHHDPALVERACRLSLSNLGLEYVDLYLMHmpvgqKFHNDSnvhgTLEltdvdylDTWREMEKLVDLGLT 154
Cdd:cd19150 86 GydmwpgpyGEWGSRKYLLASLDQSLKRMGLDYVDIFYSH-----RFDPDT----PLE-------ETMGALDHAVRSGKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 155 RSIGLSNFNAAQTER---VLANCRIRPVVNQvechPGF-------QQRQLREHAKRHGLVICAYCPLAR----------- 213
Cdd:cd19150 150 LYVGISSYSPERTREaaaILRELGTPLLIHQ----PSYnmlnrwvEESGLLDTLQELGVGCIAFTPLAQglltdkylngi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 PQPARQW------PPFLYDEHAQNL------AKKYGRTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRVFD-FELSP 278
Cdd:cd19150 226 PEGSRASkerslsPKMLTEANLNSIralneiAQKRGQSLAQMALAWVLRDGRVTsaLIGASRPEQLEENVGALDnLTFSA 305
|
....
gi 20129731 279 DDVA 282
Cdd:cd19150 306 DELA 309
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-160 |
2.13e-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: 51.21 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGT------WKSFESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKiaegvvTREEVFVTTKLGGIHH 87
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 88 DPAL----------------VERACRLSLSNLGLEYVDLYLMHmpvgqkfhnDSNVHGTLELTdvdylDTWREMEKLVDL 151
Cdd:cd19162 75 PGAAgrpagadrrfdfsadgIRRSIEASLERLGLDRLDLVFLH---------DPDRHLLQALT-----DAFPALEELRAE 140
|
....*....
gi 20129731 152 GLTRSIGLS 160
Cdd:cd19162 141 GVVGAIGVG 149
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
12-212 |
5.86e-07 |
|
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: 50.37 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSFESDAYHST-RHALDVGYRH----LDTAFVY---ENEAEVGQAISEKIAEgvvtREEVFVTTKL- 82
Cdd:cd19160 11 SGLRVSCLGLGTWVTFGSQISDETaEDLLTVAYEHgvnlFDTAEVYaagKAERTLGNILKSKGWR----RSSYVVTTKIy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 -GGihhdPALVER---------ACRLSLSNLGLEYVDLYlmhmpvgqkFHNDSNVHGTLEltdvdylDTWREMEKLVDLG 152
Cdd:cd19160 87 wGG----QAETERglsrkhiieGLRGSLDRLQLEYVDIV---------FANRSDPNSPME-------EIVRAMTYVINQG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129731 153 LTRSIGLSNFNAAQTERVLANCR----IRPVVNQVECHpgFQQR-----QLREHAKRHGLVICAYCPLA 212
Cdd:cd19160 147 MAMYWGTSRWSAMEIMEAYSVARqfnlIPPVCEQAEYH--LFQRekvemQLPELYHKIGVGSVTWSPLA 213
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
12-287 |
7.24e-07 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 49.99 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSF-ESDAYHSTR----HALDVGYRHLDTAFVY-----ENEAEVGQAISEKIAEgvvTREEVFVTTK 81
Cdd:PRK09912 21 SGLRLPALSLGLWHNFgHVNALESQRailrKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 82 LG--------GIHHDPALVERACRLSLSNLGLEYVDLYLMHmpvgqkfHNDSNVhgTLEltdvdylDTWREMEKLVDLGL 153
Cdd:PRK09912 98 AGydmwpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH-------RVDENT--PME-------ETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 154 TRSIGLSNFNAAQTER---VLANCRIRPVVNQvechPGF-------QQRQLREHAKRHGLVICAYCPLAR---------- 213
Cdd:PRK09912 162 ALYVGISSYSPERTQKmveLLREWKIPLLIHQ----PSYnllnrwvDKSGLLDTLQNNGVGCIAFTPLAQglltgkylng 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 214 -PQPARQW----------PPFLYDEHAQNL------AKKYGRTTAQICLRYLVQLGVVP--LPKSSNKARIEENFRVF-D 273
Cdd:PRK09912 238 iPQDSRMHregnkvrgltPKMLTEANLNSLrllnemAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnN 317
|
330
....*....|....
gi 20129731 274 FELSPDDVAGMEQY 287
Cdd:PRK09912 318 LTFSTEELAQIDQH 331
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
36-282 |
7.69e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.58 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 36 RHALDVGYRHLDTAFVY----ENeaevgQAISEKIAEGvvtREEVFVTTKLGGIH---------HDPALVERACRLSLSN 102
Cdd:PRK10376 47 REAVALGVNHIDTSDFYgphvTN-----QLIREALHPY---PDDLTIVTKVGARRgedgswlpaFSPAELRRAVHDNLRN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 103 LGLE---YVDLYLMHmpvgqkfhndsNVHGTLELTdvdyldTWREMEKLVDL---GLTRSIGLSNFNAAQTERVLancRI 176
Cdd:PRK10376 119 LGLDvldVVNLRLMG-----------DGHGPAEGS------IEEPLTVLAELqrqGLVRHIGLSNVTPTQVAEAR---KI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 177 RPVVNqVECHPGFQQRQ---LREHAKRHGLVICAYCPLARPQParqwppfLYDEHAQNLAKKYGRTTAQICLRYLVQLG- 252
Cdd:PRK10376 179 AEIVC-VQNHYNLAHRAddaLIDALARDGIAYVPFFPLGGFTP-------LQSSTLSDVAASLGATPMQVALAWLLQRSp 250
|
250 260 270
....*....|....*....|....*....|.
gi 20129731 253 -VVPLPKSSNKARIEENFRVFDFELSPDDVA 282
Cdd:PRK10376 251 nILLIPGTSSVAHLRENLAAAELVLSEEVLA 281
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
18-247 |
2.53e-06 |
|
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: 48.04 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 18 TLGLGTWKSFESDAYHST------RHALDVGYRHLDTAFVY-ENEAEVGQAISEKIAEgvVTREEVFVTTKLGGIHHD-- 88
Cdd:cd19164 17 IFGAATFSYQYTTDPESIppvdivRRALELGIRAFDTSPYYgPSEIILGRALKALRDE--FPRDTYFIITKVGRYGPDdf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 ---PALVERACRLSLSNLGLEYVDLYLMHmpvgqkfhndsnvhgtleltDVDY------LDTWREMEKLVDLGLTRSIGL 159
Cdd:cd19164 95 dysPEWIRASVERSLRRLHTDYLDLVYLH--------------------DVEFvadeevLEALKELFKLKDEGKIRNVGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 160 SNF---------NAAQTErvlancRIRPV-VNQVECHPGFQQRQL---REHAKRHGLV--ICAYCPLA----RPQPARQW 220
Cdd:cd19164 155 SGYplpvllrlaELARTT------AGRPLdAVLSYCHYTLQNTTLlayIPKFLAAAGVkvVLNASPLSmgllRSQGPPEW 228
|
250 260 270
....*....|....*....|....*....|..
gi 20129731 221 ---PPFLYD--EHAQNLAKKYGRTTAQICLRY 247
Cdd:cd19164 229 hpaSPELRAaaAKAAEYCQAKGTDLADVALRY 260
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
19-212 |
9.90e-06 |
|
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: 46.29 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 19 LGLGTWKSFESD-AYHSTRHALDVGYRH----LDTAFVYE-NEAEV--GQAISEKIAEgvvtREEVFVTTKL--GGihhd 88
Cdd:cd19141 15 LGLGTWVTFGSQiSDEVAEELVTLAYENginlFDTAEVYAaGKAEIvlGKILKKKGWR----RSSYVITTKIfwGG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 89 PALVER---------ACRLSLSNLGLEYVDLYlmhmpvgqkFHNDSNVHGTLEltdvdylDTWREMEKLVDLGLTRSIGL 159
Cdd:cd19141 87 KAETERglsrkhiieGLKASLERLQLEYVDIV---------FANRPDPNTPME-------EIVRAFTHVINQGMAMYWGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129731 160 SNFNAAQTERVLANCR----IRPVVNQVECHpgFQQR-----QLREHAKRHGLVICAYCPLA 212
Cdd:cd19141 151 SRWSAMEIMEAYSVARqfnlIPPIVEQAEYH--LFQRekvemQLPELFHKIGVGAMTWSPLA 210
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
28-247 |
2.30e-05 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 45.15 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 28 ESDAYHSTRHALDVGYRHLDTAFVYeneaevGQAISEKI------AEGVvTREEVFVTTKLG----GIHHDPALVERACR 97
Cdd:PLN02587 30 EEDAIASVREAFRLGINFFDTSPYY------GGTLSEKVlgkalkALGI-PREKYVVSTKCGrygeGFDFSAERVTKSVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 98 LSLSNLGLEYVDLYLMHmpvgqkfhndsnvhgTLELTDVDYL--DTWREMEKLVDLGLTRSIGLSNFNAAQTERVLAncR 175
Cdd:PLN02587 103 ESLARLQLDYVDILHCH---------------DIEFGSLDQIvnETIPALQKLKESGKVRFIGITGLPLAIFTYVLD--R 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 176 IRPVVNQV---ECHPGFQQRQLRE---HAKRHGLVICAYCPLAR--------PQ--PArqwPPFLYDEHAQNLA--KKYG 237
Cdd:PLN02587 166 VPPGTVDVilsYCHYSLNDSSLEDllpYLKSKGVGVISASPLAMglltengpPEwhPA---PPELKSACAAAAThcKEKG 242
|
250
....*....|
gi 20129731 238 RTTAQICLRY 247
Cdd:PLN02587 243 KNISKLALQY 252
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
12-212 |
3.08e-05 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 45.03 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSF-----ESDAYHSTRHALDVGYRHLDTAFVY-ENEAEV--GQAISEKIAEgvvtREEVFVTTKL- 82
Cdd:cd19159 9 SGLRVSCLGLGTWVTFggqisDEVAERLMTIAYESGVNLFDTAEVYaAGKAEVilGSIIKKKGWR----RSSLVITTKLy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 -GGihhdPALVER---------ACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNVhgTLEltdvdylDTWREMEKLVDLG 152
Cdd:cd19159 85 wGG----KAETERglsrkhiieGLKGSLQRLQLEYVDVVFANRP-------DSNT--PME-------EIVRAMTHVINQG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129731 153 LTRSIGLSNFNAAQTERVLANCR----IRPVVNQVECHPgFQQR----QLREHAKRHGLVICAYCPLA 212
Cdd:cd19159 145 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREkvevQLPELYHKIGVGAMTWSPLA 211
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-159 |
3.24e-05 |
|
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: 44.91 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 17 PTLGLGT------WKSFESDAYHSTRH-ALDVGYRHLDTAFVYEN---EAEVGQAISEKiaegvvTREEVFVTTKLG--- 83
Cdd:cd19152 1 PKLGFGTaplgnlYEAVSDEEAKATLVaAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVGrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 ----------------GIHHDPAL------VERACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNVHG--TLELTDVDYL 139
Cdd:cd19152 75 vplqeveptfepgfwnPLPFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP-------DEDLAGaeSDEHFAQAIK 147
|
170 180
....*....|....*....|
gi 20129731 140 DTWREMEKLVDLGLTRSIGL 159
Cdd:cd19152 148 GAFRALEELREEGVIKAIGL 167
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-187 |
5.65e-05 |
|
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: 43.99 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSF-----ESDAYHSTRHALDVGYRHLDTAFVYEN---EAEVGQAISEKIAEgvvtREEVFVTTKlg 83
Cdd:cd19142 9 SGLRVSNVGLGTWSTFstaisEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKKKGWK----RSSYIVSTK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 84 gIHHDPALVER---------ACRLSLSNLGLEYVDLYLMHmpvgqkfHNDSnvHGTLEltdvdylDTWREMEKLVDLGLT 154
Cdd:cd19142 83 -IYWSYGSEERglsrkhiieSVRASLRRLQLDYIDIVIIH-------KADP--MCPME-------EVVRAMSYLIDNGLI 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 20129731 155 RSIGLSNFNAAQTERVLANCR----IRPVVNQVECHP 187
Cdd:cd19142 146 MYWGTSRWSPVEIMEAFSIARqfncPTPICEQSEYHM 182
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
12-212 |
2.88e-04 |
|
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: 41.99 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 12 NGREMPTLGLGTWKSF-----ESDAYHSTRHALDVGYRHLDTAFVY---ENEAEVGQAISEKIAEgvvtREEVFVTTKL- 82
Cdd:cd19158 9 SGLRVSCLGLGTWVTFggqitDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWR----RSSLVITTKIf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129731 83 -GGIHHDPALVER-----ACRLSLSNLGLEYVDLYLMHMPvgqkfhnDSNVhgTLEltdvdylDTWREMEKLVDLGLTRS 156
Cdd:cd19158 85 wGGKAETERGLSRkhiieGLKASLERLQLEYVDVVFANRP-------DPNT--PME-------ETVRAMTHVINQGMAMY 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129731 157 IGLSNFNAAQTERVLANCR----IRPVVNQVECHPgFQQR----QLREHAKRHGLVICAYCPLA 212
Cdd:cd19158 149 WGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHM-FQREkvevQLPELFHKIGVGAMTWSPLA 211
|
|
| |
