|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-316 |
0e+00 |
|
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: 629.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 10 KAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLL 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 90 KEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIER 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 170 LLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAKHKKTTAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 250 IRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPETVNMEEFPYDAEY 316
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-306 |
2.03e-157 |
|
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: 441.82 E-value: 2.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 7 LSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKE-KAVRREDLFIVSKLWPTCFE 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 86 KKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHF 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 166 QIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAKHKKTT 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 246 AQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPETVN 306
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVPMITVD 299
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-316 |
2.83e-149 |
|
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: 421.29 E-value: 2.83e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKE 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 92 AFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 172 NKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGspdrprAKPDDPSLLQDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27465603 252 FHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPETVNMEEFPYDAEY 316
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-297 |
2.04e-128 |
|
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: 368.48 E-value: 2.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 3 TFVELSTKAKMPIVGLGTWKS--MP-NQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKL 79
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPeeVPkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 WPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGV 159
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 160 SNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPR-AKPDDPSLLQDPKIKEIA 238
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEwVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27465603 239 AKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
4.31e-124 |
|
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: 355.25 E-value: 4.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIkekaVRREDLFIVSKLWPTCFEKKLLKEA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 93 FQKTLTDLKLDYLDLYLIHWPQGFQAGkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEG-------------GSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 173 KPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPrakpddpsLLQDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 27465603 253 HIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
12-299 |
2.79e-123 |
|
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: 355.05 E-value: 2.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQ-VKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLK 90
Cdd:cd19116 10 EIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 91 EAFQKTLTDLKLDYLDLYLIHWPQGFqagKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERL 170
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPVAF---KENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 171 LNkpGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrPRAKPDDPSLLQDPKIKEIAAKHKKTTAQVLI 250
Cdd:cd19116 167 LS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLV-PRGQTNPPPRLDDPTLVAIAKKYGKTTAQIVL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27465603 251 RFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRAC 299
Cdd:cd19116 244 RYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-312 |
2.14e-119 |
|
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: 345.63 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTW----KSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKL 88
Cdd:cd19109 4 IPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHPPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 89 LKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIE 168
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRRQLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 169 RLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPR-AKPDDPSLLQDPKIKEIAAKHKKTTAQ 247
Cdd:cd19109 164 LILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwVNVSSPPLLEDPLLNSIGKKYNKTAAQ 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27465603 248 VLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPETVNMEEFPY 312
Cdd:cd19109 244 VVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
11-303 |
2.10e-115 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 333.56 E-value: 2.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 11 AKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCFEKKLLK 90
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDDTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 91 EAFQKTltdlkldyldlylIHWPqgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERL 170
Cdd:COG0656 79 AAFEESlerlgldyldlylIHWP--------------------GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 171 LNKPGlkHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrprakpddpsLLQDPKIKEIAAKHKKTTAQVLI 250
Cdd:COG0656 139 LAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQVVL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27465603 251 RFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPE 303
Cdd:COG0656 207 RWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-297 |
7.06e-114 |
|
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: 331.30 E-value: 7.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 1 MATFvELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLW 80
Cdd:cd19123 1 MKTL-PLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 81 PTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKeLFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVS 160
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGV-GFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRA--KPDDPSLLQDPKIKEIA 238
Cdd:cd19123 159 NFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmkAEGEPVLLEDPVINKIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27465603 239 AKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19123 237 EKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-300 |
6.17e-110 |
|
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: 321.28 E-value: 6.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 2 ATFVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWP 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 82 TCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 162 FNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDD-----PSLLQDPKIKE 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27465603 237 IAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACL 300
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLFL 302
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
3-287 |
7.12e-103 |
|
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: 302.73 E-value: 7.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 3 TFVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPT 82
Cdd:cd19125 1 RFFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 CFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKelfPKDEQGNVLPSKTTflEAWEGMEELVDQGLVKALGVSNF 162
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVLPPDIP--STWKAMEKLVDSGKVRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 163 NHFQIERLLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDdpsLLQDPKIKEIAAKHK 242
Cdd:cd19125 156 SVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLG 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27465603 243 KTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMA 287
Cdd:cd19125 231 KTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFA 275
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-299 |
6.66e-96 |
|
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: 285.96 E-value: 6.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 4 FVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTC 83
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 FEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQaGKEL--FPKDEQGNVLPSKTT-FLEAWEGMEELVDQGLVKALGVS 160
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSL-SKEDdsGKLDPTGEHKQDYTTdLLDIWKAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKP-------DDPSLLQDPK 233
Cdd:cd19155 162 NFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 234 IKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRAC 299
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-289 |
4.34e-92 |
|
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: 275.53 E-value: 4.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 7 LSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWptCFEK 86
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLW--CTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 87 KLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAG--KELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNH 164
Cdd:cd19117 82 RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNFSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 165 FQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPrakpddpsLLQDPKIKEIAAKHKKT 244
Cdd:cd19117 162 KNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27465603 245 TAQVLIRFHIQRNVVVIPKSVTPARIQENIQVfdFQLSDQEMATI 289
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-297 |
1.87e-91 |
|
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: 273.99 E-value: 1.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKE 91
Cdd:cd19111 3 PMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 92 AFQKTLTDLKLDYLDLYLIHWPQGFQAgkelfpKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPCGFVN------KKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 172 NKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPR--AKPDDPSLLQDPKIKEIAAKHKKTTAQVL 249
Cdd:cd19111 157 AYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANqsLWPDQPDLLEDPTVLAIAKELDKTPAQVL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 27465603 250 IRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19111 235 LRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
2.46e-89 |
|
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: 268.12 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 7 LSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEK-AVRREDLFIVSKLWPTCFE 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 86 KKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPK----DEQGNV-LPSKTTFLEAWEGMEELVDQGLVKALGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavpTNGGEVdLDLSVSLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSpDRPRAkpddPSLLQDPKIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-NLAGL----PLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27465603 241 HKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDfqLSDQEMATI 289
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAV 280
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-289 |
1.52e-86 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 260.38 E-value: 1.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCF 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 85 EKKLLKEAFQKTLTDLKLDYLDLYLIHWPQgfqagkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFNH 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPV------------------PAQDKYVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPdrprakpddpSLLQDPKIKEIAAKHKKT 244
Cdd:cd19131 140 EHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27465603 245 TAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAI 252
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-289 |
7.38e-86 |
|
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: 259.38 E-value: 7.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 14 PIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKEAF 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 94 QKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 174 pgLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSpdrpRAKPDDPSLLQDPKIKEIAAKHKKTTAQVLIRFH 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGG----SYGDGNLTFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 27465603 254 IQR---NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-297 |
6.68e-85 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 257.80 E-value: 6.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTcf 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 85 EKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQ---AGKELFPKDEQGNVLPSKTTFLEA-WEGMEELVDQGLVKALGVS 160
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgVGTTGSALGEDGVLDIDVTISLETtWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAK 240
Cdd:cd19112 161 NYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWFGSVSPLDDPVLKDLAKK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 241 HKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19112 239 YGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-291 |
2.04e-83 |
|
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: 252.55 E-value: 2.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWK-SMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKE 91
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 92 AFQKTLTDLKLDYLDLYLIHWPqgfqaGKELFPKDEQGNvlpsKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWP-----GVQGLKPSDPRN----AELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 172 NKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrprakpddPSLLQDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19136 152 KYCEVP--PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD--------LRLLEDPTVLAIAKKYGRTPAQVLLR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27465603 252 FHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILS 291
Cdd:cd19136 222 WALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-292 |
3.44e-83 |
|
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: 251.86 E-value: 3.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 4 FVELSTKAKMPIVGLGTWKSmPNQVKEAVKAAI-DAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHS-GGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 CFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKElfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGVSNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN------------VKETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 163 NHFQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLgspdrprAKPddpSLLQDPKIKEIAAKHK 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-------AKG---KALEEPTVTELAKKYQ 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27465603 243 KTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSF 292
Cdd:cd19135 215 KTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
5-293 |
7.52e-82 |
|
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: 248.26 E-value: 7.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWK-SMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTC 83
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 FEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGfqagkelfpkDEQGnvlpskttfleAWEGMEELVDQGLVKALGVSNFN 163
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 164 HFQIERLLnkPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGspdrpRAKPDdpsLLQDPKIKEIAAKHKK 243
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA-----EGRNN---LFENPVLTEIAEKYGK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27465603 244 TTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFN 293
Cdd:cd19133 206 SVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
1.50e-81 |
|
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: 249.26 E-value: 1.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 1 MATFVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 81 PTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfQAGKELFP--------KDEQGNVLPSKTTFLEAWEGMEELVDQG 152
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFP---IALKYVDPavryppgwFYDGKKVEFSNAPIQETWTAMEKLVDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 153 LVKALGVSNFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGsP------DRPRAKpDDP 226
Cdd:cd19115 158 LARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTP 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 227 SLLQDPKIKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19115 234 PLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
2-286 |
2.52e-81 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 247.83 E-value: 2.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 2 ATFVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIkEKAVRREDLFIVSKLWP 81
Cdd:cd19121 1 MTSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 82 TCFEKklLKEAFQKTLTDLKLDYLDLYLIHWPQGFQ--AGKELFPKDEQG--NVLPSKtTFLEAWEGMEELVDQGLVKAL 157
Cdd:cd19121 80 TYHRR--VELCLDRSLKSLGLDYVDLYLVHWPVLLNpnGNHDLFPTLPDGsrDLDWDW-NHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 158 GVSNFNHFQIERLLnkPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPrakpddpsLLQDPKIKEI 237
Cdd:cd19121 157 GVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27465603 238 AAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFqlSDQEM 286
Cdd:cd19121 227 AKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDM 273
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
3.02e-81 |
|
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: 246.03 E-value: 3.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCFEKKLLKEA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 93 FQKTLTDLKLDYLDLYLIHWPQgfqagkelfPKDEQGNVLpskttfleawEGMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN---------PTVPLEETL----------GALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 173 KPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrprakpddpsLLQDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE----------VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 27465603 253 HIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-293 |
1.11e-80 |
|
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: 245.04 E-value: 1.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKsMP--NQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPT 82
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQ-TPdgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 CFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGVSNF 162
Cdd:cd19126 76 DQRARRTEDAFQESLDRLGLDYVDLYLIHWP--------------------GKDKFIDTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 163 NHFQIERLLnkpglKH---KPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPdrprakpddpSLLQDPKIKEIAA 239
Cdd:cd19126 136 QEHHLEELL-----AHadvVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGE 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27465603 240 KHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFN 293
Cdd:cd19126 201 KYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-297 |
1.61e-79 |
|
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: 242.68 E-value: 1.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 4 FVELSTKAKMPIVGLGTWKSMP-NQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPT 82
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 --CFEKKLlkEAFQKTLTDLKLDYLDLYLIHWPQgfqagkelfpkdeqgnvlpsKTTFLEAWEGMEELVDQGLVKALGVS 160
Cdd:cd19157 77 dqGYDSTL--KAFEASLERLGLDYLDLYLIHWPV--------------------KGKYKETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrprakpddpsLLQDPKIKEIAAK 240
Cdd:cd19157 135 NFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEK 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 241 HKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19157 203 YNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLR 259
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
5.94e-79 |
|
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: 242.74 E-value: 5.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKsMPNQV-KEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTC 83
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWK-LDNATaADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 FEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQagkeLFPKDEQ----------GNVLPSKTTFLEAWEGMEELVDQGL 153
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFK----FVPIEEKyppgfycgdgDNFVYEDVPILDTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 154 VKALGVSNFNHFQIERLLNkpGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSP-----DRPRAKpDDPSL 228
Cdd:cd19113 158 IKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27465603 229 LQDPKIKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19113 235 FEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-289 |
4.21e-77 |
|
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: 236.01 E-value: 4.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCFEKKLLKE 91
Cdd:cd19132 6 QIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 92 AFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWP------------------NPSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 172 NKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRprakpddpsLLQDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19132 144 DETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPAQVVLR 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 27465603 252 FHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19132 213 WHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
5-289 |
1.43e-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: 1.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCF 84
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGI----RRSGVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 85 EKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvlpSKTTF---LEAWEGMEELVDQGLVKALGVSN 161
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWP--------------------VPNDFdrtIQAYKALEKLLAEGRVRAIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 162 FNHFQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSP--DRPRAKPDDPSLLQDPKIKEIAA 239
Cdd:cd19127 137 FTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVmrYGASGPTGPGDVLQDPTITGLAE 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27465603 240 KHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19127 215 KYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-289 |
2.97e-76 |
|
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: 233.69 E-value: 2.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 11 AKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAiqekIKEKAVRREDLFIVSKLWPTCFEKKLLK 90
Cdd:cd19140 6 VRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 91 EAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERL 170
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 171 LNKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGspdrpRAKpddpsLLQDPKIKEIAAKHKKTTAQVLI 250
Cdd:cd19140 143 VELSEA--PLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA-----RGE-----VLKDPVLQEIGRKHGKTPAQVAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27465603 251 RFHIQR-NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19140 211 RWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-297 |
4.04e-75 |
|
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: 231.64 E-value: 4.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPNQVKE-AVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPT- 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVGQGI----RESGVPREEVFVTTKLWNSd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 -CFEKKLlkEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGVSN 161
Cdd:cd19156 77 qGYESTL--AAFEESLEKLGLDYVDLYLIHWP--------------------VKGKFKDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 162 FNHFQIERLLNKpgLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDrprakpddpsLLQDPKIKEIAAKH 241
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 242 KKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-276 |
5.10e-75 |
|
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: 232.35 E-value: 5.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKEA 92
Cdd:cd19129 6 IPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVKPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 93 FQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSK-TTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL 171
Cdd:cd19129 86 FEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 172 NKPGLkhKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRakpddpsLLQDPKIKEIAAKHKKTTAQVLIR 251
Cdd:cd19129 166 EAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPK-------LLEDPVITAIARRVNKTPAQVLLA 236
|
250 260
....*....|....*....|....*
gi 27465603 252 FHIQRNVVVIPKSVTPARIQENIQV 276
Cdd:cd19129 237 WAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-285 |
1.94e-74 |
|
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: 230.85 E-value: 1.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPN--QVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPT 82
Cdd:cd19119 4 FKLNTGASIPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 CFEKklLKEAFQKTLTDLKLDYLDLYLIHWPQGFQA-----GKELFPKDEQGNVLPSKTT-FLEAWEGMEELVDQGLVKA 156
Cdd:cd19119 84 FYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEKdsddsGKPFTPVNDDGKTRYAASGdHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 157 LGVSNFNHFQIERLLNKpgLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPrakpddpsLLQDPKIKE 236
Cdd:cd19119 162 IGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVKK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27465603 237 IAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQE 285
Cdd:cd19119 232 IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQ 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-289 |
2.23e-74 |
|
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: 229.85 E-value: 2.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 11 AKMPIVGLGTWKSM--PNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVR-REDLFIVSKLWPTCFEKK 87
Cdd:cd19124 3 QTMPVIGMGTASDPpsPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 88 LLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEqGNVLPskTTFLEAWEGMEELVDQGLVKALGVSNFNHFQI 167
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE-EDFLP--FDIKGVWEAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 168 ERLL---NKPglkhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSpdrPRAKPDDPSLLQDPKIKEIAAKHKKT 244
Cdd:cd19124 160 QELLsfaTIP-----PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGA---PGTKWGSNAVMESDVLKEIAAAKGKT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27465603 245 TAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19124 232 VAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
12-297 |
9.43e-74 |
|
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: 229.37 E-value: 9.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKE 91
Cdd:cd19114 3 KMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHVRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 92 AFQKTLTDLKLDYLDLYLIHWP--QGFQAGKELFP---KDEQGNVLP-SKTTFLEAWEGMEELVDQGLVKALGVSNFNHF 165
Cdd:cd19114 83 AFDRQLKDYGLDYIDLYLIHFPipAAYVDPAENYPflwKDKELKKFPlEQSPMQECWREMEKLVDAGLVRNIGIANFNVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 166 QIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSP---DRPRAKPDDPSLLQDPKIKEIAAKHK 242
Cdd:cd19114 163 LILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27465603 243 KTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
12-289 |
5.84e-70 |
|
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: 218.26 E-value: 5.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGT----WKSMPNQVK----EAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTc 83
Cdd:cd19120 3 KIPAIAFGTgtawYKSGDDDIQrdlvDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKVSPG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 feKKLLKEAFQKTLTDLKLDYLDLYLIHwpqgfqagkelFPKDEQgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFN 163
Cdd:cd19120 78 --IKDPREALRKSLAKLGVDYVDLYLIH-----------SPFFAK----EGGPTLAEAWAELEALKDAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 164 HFQIERLLNKPglKHKPVTNQVECHPYLT--QEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLlqdpkiKEIAAKH 241
Cdd:cd19120 141 IEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVL------EKIAEKY 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 27465603 242 KKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19120 213 GVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-289 |
6.05e-68 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 213.40 E-value: 6.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 3 TFVELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKikekAVRREDLFIVSKLWPT 82
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 cfEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvLPSKTTFLEAWEGMEELVDQGLVKALGVSNF 162
Cdd:PRK11565 81 --DHKRPREALEESLKKLQLDYVDLYLMHWP------------------VPAIDHYVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 163 NHFQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRprakpddpSLLQDPKIKEIAAKHK 242
Cdd:PRK11565 141 QIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYG 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27465603 243 KTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:PRK11565 211 KTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEI 257
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
13-293 |
1.18e-66 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 209.38 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCFEKKLLKEA 92
Cdd:cd19130 10 IPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDRHDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 93 FQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19130 86 FAESLAKLGLDQVDLYLVHWP------------------TPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 173 KPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPdrprakpddpSLLQDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19130 148 ATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGKTPAQIVLRW 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 27465603 253 HIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFN 293
Cdd:cd19130 216 HLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-289 |
4.61e-61 |
|
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: 194.88 E-value: 4.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKikekAVRREDLFIVSKLWPTCFEKKLLKEA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 93 FQKTLTDLKLDYLDLYLIHWPQgfqagkelfPKDEQgnvlpSKTTFLEAwegMEELVDQGLVKALGVSNFNHFQIERLLN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPS---------PNDEV-----PVEEYIGA---LAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 173 KPGlKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGspdrpRAKpddpsLLQDPKIKEIAAKHKKTTAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 27465603 253 HIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
4.41e-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: 193.68 E-value: 4.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTW-------KSMPNQVKEAVKAAIDAGYRHIDCAYAYC---NENEVGEAIqekiKEKAVRREDLFIVSKL------ 79
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEAL----KDYPVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 WPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelFPKdeqgnvlpskTTFLEAWEGMEELVDQGLVKALGV 159
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP---------DPD----------TPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 160 SNFNHFQIERLLNKPglKHKPVTNQVECHPY--LTQEKLIQYCHSKGIVVTAYSPLGS---------------PDRPRAK 222
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpGERRRLL 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 223 PDDPSLLQD--PKIKEIAAKHKKTTAQVLIRFHIQ--RNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:pfam00248 216 KKGTPLNLEalEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-289 |
7.78e-60 |
|
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: 193.22 E-value: 7.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 7 LSTKAKMPIVGLGTWKS--MPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEK-AVRREDLFIVSKLWPTC 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 FEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPK---DEQGNVLPSKTTFLE-AWEGMEELVDQGLVKALGV 159
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlgpDGKYVILKDLTENPEpTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 160 SNFNHFQIERLLNKPglKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSllQDPKIKEIAA 239
Cdd:cd19122 163 SNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENPTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27465603 240 KHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDfqLSDQEMATI 289
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAI 286
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
5-289 |
5.08e-58 |
|
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: 187.37 E-value: 5.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIqekiKEKAVRREDLFIVSKLWPTCF 84
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 85 EKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNH 164
Cdd:cd19134 79 GFTASQAACRASLERLGLDYVDLYLIHWP------------------AGREGKYVDSWGGLMKLREEGLARSIGVSNFTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 165 FQIERLLNKPGLKhkPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPdrprakpddpSLLQDPKIKEIAAKHKKT 244
Cdd:cd19134 141 EHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27465603 245 TAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
5.48e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 177.14 E-value: 5.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKikekAVRREDLFIVSKLWPTCFEK-KL-- 88
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIDNLAKdKLip 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 89 -LKEAFQKtltdLKLDYLDLYLIHWPQgfqagkelfPKDEqgnvlpskttfLEAWEGMEELVD---QGLVKALGVSNFNH 164
Cdd:PRK11172 78 sLKESLQK----LRTDYVDLTLIHWPS---------PNDE-----------VSVEEFMQALLEakkQGLTREIGISNFTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 165 FQIERLLNKPGlKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPdrprakpddpSLLQDPKIKEIAAKHKKT 244
Cdd:PRK11172 134 ALMKQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYG----------KVLKDPVIARIAAKHNAT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27465603 245 TAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWR 297
Cdd:PRK11172 203 PAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
5.07e-53 |
|
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: 174.72 E-value: 5.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 10 KAKMPIVGLGTWK---------SMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIqekikeKAVRREDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI------KGFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 78 KLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqGNVLPSKTTfleaWEGMEELVDQGLVKAL 157
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP---------------NPSIPIEET----LRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 158 GVSNFNHFQIERLLNKPGlKHKPVTNQVECHpYLTQE---KLIQYCHSKGIVVTAYSPLGSPDRPRAKpddpsllQDPKI 234
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAK-------GSPLL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 235 KEIAAKHKKTTAQVLIRFHIQR-NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19072 207 DEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
5-289 |
2.13e-52 |
|
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: 173.20 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 5 VELSTKAKMPIVGLGTW-----KSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekavRREDLFIV 76
Cdd:cd19138 3 VTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRG-------RRDKVFLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 77 SKLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqGNVlPSKTTFleawEGMEELVDQGLVKA 156
Cdd:cd19138 76 SKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWR---------------GGV-PLAETV----AAMEELKKEGKIRA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 157 LGVSNFNHFQIERLLNKPGlKHKPVTNQVECHpyLTQE----KLIQYCHSKGIVVTAYSPLGSPDRPRAkpddpSLLQDP 232
Cdd:cd19138 136 WGVSNFDTDDMEELWAVPG-GGNCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLLRR-----GLLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27465603 233 KIKEIAAKHKKTTAQVLIRFHI-QRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-289 |
1.19e-48 |
|
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: 163.13 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWK---------SMPNQVKEAVKAAIDAGYRHIDCAYAYC---NENEVGEAIqekikeKAVRREDLFIVSKL 79
Cdd:cd19137 3 KIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKAI------KDFPREDLFIVTKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 WPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGV 159
Cdd:cd19137 77 WPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN-------------------PNIPLEETLSAMAEGVRQGLIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 160 SNFNHFQIERLLNKpgLKHKPVTNQVECHPY---LTQEKLIQYCHSKGIVVTAYSPLgspdrprakpDDPSLLQDPKIKE 236
Cdd:cd19137 138 SNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL----------RRGLEKTNRTLEE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27465603 237 IAAKHKKTTAQVLIRFHIQR-NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19137 206 IAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-287 |
3.09e-40 |
|
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: 142.37 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWK-----------SMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEKIKekavrREDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELGD-----RDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 78 KLWPTC--FEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKElfpkdeqgnvlpskttflEAWEGMEELVDQGLVK 155
Cdd:cd19093 76 KFAPLPwrLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIE------------------ALMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 156 ALGVSNFNHFQIER---LLNKPGlkHKPVTNQVE---CHPYLTQEKLIQYCHSKGIVVTAYSPLG--------SPDRPRA 221
Cdd:cd19093 138 AVGVSNYSADQLRRahkALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPPP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 222 KPD-----------DPSLLQdpKIKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMA 287
Cdd:cd19093 216 GGRrrlfgrknlekVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVA 290
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
16-289 |
4.75e-35 |
|
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: 129.14 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTW-------KSMPNQVKEAVKAAIDAGYRHIDCAYAYCN-ENE--VGEAIqekikeKAVRREDLFIVSKL------ 79
Cdd:COG0667 16 LGLGTMtfggpwgGVDEAEAIAILDAALDAGINFFDTADVYGPgRSEelLGEAL------KGRPRDDVVIATKVgrrmgp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 --WPTCFEKKLLKEA---------------FQktltdlkldyldlylIHWPqgfqagkelfpkdeqgnvlPSKTTFLEAW 142
Cdd:COG0667 90 gpNGRGLSREHIRRAveaslrrlgtdyidlYQ---------------LHRP-------------------DPDTPIEETL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 143 EGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVEchpY--LTQ---EKLIQYCHSKGIVVTAYSPLGS-- 215
Cdd:COG0667 136 GALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGgl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 216 -----------PDRPRAKPDDPSLLQDPK-------IKEIAAKHKKTTAQVLIRFHIQR--NVVVIPKSVTPARIQENIQ 275
Cdd:COG0667 213 ltgkyrrgatfPEGDRAATNFVQGYLTERnlalvdaLRAIAAEHGVTPAQLALAWLLAQpgVTSVIPGARSPEQLEENLA 292
|
330
....*....|....
gi 27465603 276 VFDFQLSDQEMATI 289
Cdd:COG0667 293 AADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
2.17e-30 |
|
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: 116.15 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 14 PIVGLGTW---------KSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekavRREDLFIVSKLWP 81
Cdd:cd19085 2 SRLGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 82 TCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSN 161
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP-------------------SSDVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 162 FNHFQIERLLnKPGlkhKPVTNQVECHPYLTQ-EK-LIQYCHSKGIVVTAYSPLGS--------------PDRPRAK--- 222
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLAQglltgkfssaedfpPGDARTRlfr 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 223 PDDP-------SLLQdpKIKEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19085 212 HFEPgaeeetfEALE--KLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-289 |
8.88e-29 |
|
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: 111.85 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTW--------KSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekavRREDLFIVSK-- 78
Cdd:cd19084 3 KVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKcg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 79 -LWPT------CFEKKLLKEA---------------FQktltdlkldyldlylIHWPQGfqagkelfpkdeqgnvlpsKT 136
Cdd:cd19084 76 lRWDGgkgvtkDLSPESIRKEveqslrrlqtdyidlYQ---------------IHWPDP-------------------NT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 137 TFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNkpglKHKPVTNQVechPY--LTQ---EKLIQYCHSKGIVVTAYS 211
Cdd:cd19084 122 PIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK----YGPIVSLQP---PYsmLEReieEELLPYCRENGIGVLPYG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 212 PLGS-------PDRPRAKPDD----PSLLQDP----------KIKEIAAKHKKTTAQVLIRFHIQRN--VVVIPKSVTPA 268
Cdd:cd19084 195 PLAQglltgkyKKEPTFPPDDrrsrFPFFRGEnfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQPgvTSAIVGAKNPE 274
|
330 340
....*....|....*....|.
gi 27465603 269 RIQENIQVFDFQLSDQEMATI 289
Cdd:cd19084 275 QLEENAGALDWELTEEELKEI 295
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
16-285 |
9.94e-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: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTWKSM-----PNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIqekiKEKAVRREDLFIVSKlwptCFekk 87
Cdd:cd19092 9 LVLGCMRLAdwgesAEELLSLIEAALELGITTFDHADIYGGgkcEELFGEAL----ALNPGLREKIEIQTK----CG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 88 lLKEAFQKTLtdlkldyldlyliHWPQGFQAGKElfpkdeqgNVLPS--------KTTFL------------EAWE---G 144
Cdd:cd19092 78 -IRLGDDPRP-------------GRIKHYDTSKE--------HILASvegslkrlGTDYLdllllhrpdplmDPEEvaeA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 145 MEELVDQGLVKALGVSNFNHFQIErLLNKpGLKHKPVTNQVEC---HPYLTQEKLIQYCHSKGIVVTAYSPLG-----SP 216
Cdd:cd19092 136 FDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGggrlfGG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27465603 217 DRPRakpdDPSLLQdpKIKEIAAKHKKTTAQVLIRFhIQR---NVVVIPKSVTPARIQENIQVFDFQLSDQE 285
Cdd:cd19092 214 FDER----FQRLRA--ALEELAEEYGVTIEAIALAW-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-282 |
1.08e-21 |
|
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: 91.90 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 13 MPIVGLGTWKSMPN--QVKEAVKAAIDAGYRHIDCAYAYC---NENEVGEAIqekikekAVRREDLFIVSKL-------- 79
Cdd:cd19088 9 MRLTGPGIWGPPADreEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEAL-------HPYPDDVVIATKGglvrtgpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 -WPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALG 158
Cdd:cd19088 82 wWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRID-------------------PKVPFEEQLGALAELQDEGLIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 159 VSNFNHFQIERLLNKPGLkhkpVTNQVECHPYLTQ-EKLIQYCHSKGIVVTAYSPLGSpdRPRAKPddpsllqDPKIKEI 237
Cdd:cd19088 143 LSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLAQP-------GGLLAEV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27465603 238 AAKHKKTTAQVLIRFHIQR--NVVVIPKSVTPARIQENIQVFDFQLS 282
Cdd:cd19088 210 AARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-289 |
2.01e-21 |
|
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: 91.97 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTWKS------MP------NQVKEAVKAAIDAGYRHIDCAYAYC---NENEVGEAIQEkikekavRREDLFIVSK-- 78
Cdd:cd19102 4 IGLGTWAIggggwgGGwgpqddRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVGRALKG-------LRDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 79 -LW------PTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGfqagkelfpkDEQgnvlpskttFLEAWEGMEELVDQ 151
Cdd:cd19102 77 lLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP----------DEP---------IEEAWGALAELKEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 152 GLVKALGVSNFNHFQIERLlnkpgLKHKPVT-NQVechPY--LTQE---KLIQYCHSKGIVVTAYSPLGS--------PD 217
Cdd:cd19102 138 GKVRAIGVSNFSVDQMKRC-----QAIHPIAsLQP---PYslLRRGieaEILPFCAEHGIGVIVYSPMQSglltgkmtPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 218 RPRAKPDD-----------PSLLQDPKI----KEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDFQ 280
Cdd:cd19102 210 RVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADLR 289
|
....*....
gi 27465603 281 LSDQEMATI 289
Cdd:cd19102 290 LTPEELAEI 298
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-285 |
2.32e-21 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 91.75 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 17 GLGTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIqekiKEKAVRREDLFIVSKlwptC---------- 83
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYGGytcEALFGEAL----KLSPSLREKIELQTK----Cgirlpseard 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 -------FEKK-------------------LLkeafqktltdlkldyldlyLIHWPqgfqagkelfpkDeqgnvlpsktT 137
Cdd:COG4989 94 nrvkhydTSKEhiiasvegslrrlgtdyldLL-------------------LLHRP------------D----------P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 138 FLEAWE---GMEELVDQGLVKALGVSNFNHFQIErLLNKpGLKHKPVTNQVECHPYLTQ---EKLIQYCHSKGIVVTAYS 211
Cdd:COG4989 133 LMDPEEvaeAFDELKASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 212 PLG-----SPDRPRAKPddpslLQDpKIKEIAAKHKKTTAQVLIRFhIQR---NVVVIPKSVTPARIQENIQVFDFQLSD 283
Cdd:COG4989 211 PLAggrlfGGFDEQFPR-----LRA-ALDELAEKYGVSPEAIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTR 283
|
..
gi 27465603 284 QE 285
Cdd:COG4989 284 EE 285
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
16-275 |
4.71e-20 |
|
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: 86.80 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTWK-SMPNQVKEA---VKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEKIKekavrREDLFIVSKL--------W 80
Cdd:cd06660 3 LGLGTMTfGGDGDEEEAfalLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRGN-----RDDVVIATKGghppggdpS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 81 PTCFEKKLLKEAFQKTltdlkldyldlyLIHWPqgfqagkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVS 160
Cdd:cd06660 78 RSRLSPEHIRRDLEESlrrlgtdyidlyYLHRD-------------------DPSTPVEETLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNKPGLKHK--PVTNQVE---CHPYLTQEKLIQYCHSKGIVVTAYSPLGS-Pdrprakpddpsllqdpki 234
Cdd:cd06660 139 NWSAERLAEALAYAKAHGLpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARgP------------------ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 27465603 235 keiaakhkkttAQVLIRFHIQR--NVVVIPKSVTPARIQENIQ 275
Cdd:cd06660 201 -----------AQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
29-291 |
9.61e-18 |
|
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: 82.08 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 29 KEAVKAAIDAGYRHIDCAYAYC---NENEVGEAIQEKIKEKAV--------RREDLFIVSKlwptcfEKKLLKEAFQKTL 97
Cdd:cd19083 36 KDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYNRNEVViatkgahkFGGDGSVLNN------SPEFLRSAVEKSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 98 TDLKLDYLDLYLIHWPQGFQagkelfPKDEQGNVLpskttfleawegmEELVDQGLVKALGVSNFNHFQIERlLNKPGLk 177
Cdd:cd19083 110 KRLNTDYIDLYYIHFPDGET------PKAEAVGAL-------------QELKDEGKIRAIGVSNFSLEQLKE-ANKDGY- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 178 hkpvTNQVEcHPY-LTQ----EKLIQYCHSKGIVVTAYSPLGS--------PDrprAKPDDPSLLQD------------- 231
Cdd:cd19083 169 ----VDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytKD---TKFPDNDLRNDkplfkgerfsenl 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27465603 232 ---PKIKEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDFQLSDQEMATILS 291
Cdd:cd19083 241 dkvDKLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
143-289 |
7.69e-15 |
|
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: 73.43 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 143 EGMEELVDQGLVKALGVSNFNHFQIERLLNKpglkHKPVTNQVECHPyLTQEKL----IQYCHSKGIVVTAYSPLG---- 214
Cdd:cd19077 132 KALKELVKEGKIRGIGLSEVSAETIRRAHAV----HPIAAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLGrgll 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 215 ---SPDRPRAKPDDPSLLQD--------------PKIKEIAAKHKKTTAQVLIRFHIQRN---VVVIPKSVTPARIQENI 274
Cdd:cd19077 207 tgrIKSLADIPEGDFRRHLDrfngenfeknlklvDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENL 286
|
170
....*....|....*
gi 27465603 275 QVFDFQLSDQEMATI 289
Cdd:cd19077 287 KAANVELTDEELKEI 301
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
16-291 |
1.49e-13 |
|
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: 69.99 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTW---------KSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekavRREDLFIVSKlwptC 83
Cdd:cd19149 14 IGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATK----C 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 ---FEKKLLKEAFQktltdlkldyldlylihwPQGFQAGKELFPK---DE--------QGNVL-------PSKTTFL-EA 141
Cdd:cd19149 83 glrWDREGGSFFFV------------------RDGVTVYKNLSPEsirEEveqslkrlGTDYIdlyqthwQDVETPIeET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 142 WEGMEELVDQGLVKALGVSNFNHFQIERLlnkpgLKHKPV-TNQVechPY-----LTQEKLIQYCHSKGIVVTAYSPLGS 215
Cdd:cd19149 145 MEALEELKRQGKIRAIGASNVSVEQIKEY-----VKAGQLdIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSPLEQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 216 --------PDR-----------PRAKPDDPSLLQD--PKIKEIAAKHKKTTAQVLIRFHIQR--NVVVIPKSVTPARIQE 272
Cdd:cd19149 217 glltgkitPDRefdagdarsgiPWFSPENREKVLAllEKWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQAEE 296
|
330
....*....|....*....
gi 27465603 273 NIQVFDFQLSDQEMATILS 291
Cdd:cd19149 297 NAKAGDIRLSAEDIATMRS 315
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
19-289 |
2.05e-13 |
|
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: 69.54 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 19 GTWKSMPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEKIKekavrREDLFIVSKLWPTCFE--------KK 87
Cdd:cd19079 28 RPWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFAP-----RDEVVIATKVYFPMGDgpngrglsRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 88 LLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkDEQgnvlpskTTFLEAWEGMEELVDQGLVKALGVSNFNHFQI 167
Cdd:cd19079 103 HIMAEVDASLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 168 ERLLN---KPGLkHKPVTNQvecHPY--LTQE---KLIQYCHSKGIVVTAYSPL----------GSPDRPRAKPDDPSLL 229
Cdd:cd19079 164 AKALHlaeKNGW-TKFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrlarpwgDTTERRRSTTDTAKLK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27465603 230 QD----------PKIKEIAAKHKKTTAQVLIRFHIQRNVVVIP--KSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19079 240 YDyfteadkeivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
12-289 |
3.30e-13 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 69.46 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTwksMPNQVKEA------VKAAIDAGYRHIDCAYAYCN-ENEVGEAIQEkikekavRREDLFIVSKLWPTCF 84
Cdd:COG1453 12 EVSVLGFGG---MRLPRKDEeeaealIRRAIDNGINYIDTARGYGDsEEFLGKALKG-------PRDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 85 EKKLLKEAFQKTLTDLKLDYLDLYLIHWPQgfqaGKELFPKDEQGNvlpskttflEAWEGMEELVDQGLVKALGVSNFNH 164
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIHGLN----TEEDLEKVLKPG---------GALEALEKAKAEGKIRHIGFSTHGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 165 FQ-IERLLNkpglkhkpvTNQVEC---------HPYLTQEKLIQYCHSKGIVVTAYSPLGspdrprakpdDPSLLQDP-K 233
Cdd:COG1453 149 LEvIKEAID---------TGDFDFvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLK----------GGRLANPPeK 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 234 IKEIaAKHKKTTAQVLIRF--HIQRNVVVIPKSVTPARIQENIQVFD--FQLSDQEMATI 289
Cdd:COG1453 210 LVEL-LCPPLSPAEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAIL 268
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
16-289 |
2.39e-12 |
|
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: 66.18 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTWK---SM-----PNQVKEAVKAAIDAGYRHIDCAYAY---CNENEVGEAIQEKIKekavrREDLFIVSKL----- 79
Cdd:cd19148 7 IALGTWAiggWMwggtdEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYGK-----RDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 -----WPTCFEKKLLKEaFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkDEqgnvlpsKTTFLEAWEGMEELVDQGLV 154
Cdd:cd19148 82 eggevVRNSSPARIRKE-VEDSLRRLQTDYIDLYQVHWP------------DP-------LVPIEETAEALKELLDEGKI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 155 KALGVSNFNHFQIERLLNKPGLKhkpvTNQVechPY-----LTQEKLIQYCHSKGIVVTAYSPL------GSPDRPRAKP 223
Cdd:cd19148 142 RAIGVSNFSPEQMETFRKVAPLH----TVQP---PYnlferEIEKDVLPYARKHNIVTLAYGALcrgllsGKMTKDTKFE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 224 DDPSLLQDPKIKE------IAA----------KHKKTTAQVLIRFHIQRNVVVIP--KSVTPARIQENIQVFDFQLSDQE 285
Cdd:cd19148 215 GDDLRRTDPKFQEprfsqyLAAveeldklaqeRYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDED 294
|
....
gi 27465603 286 MATI 289
Cdd:cd19148 295 MKEI 298
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-283 |
4.54e-12 |
|
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: 65.31 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTWKSMPNQV-----KEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekaVRREDLFIVSKL-WPTCFE- 85
Cdd:cd19074 7 LSLGTWLTFGGQVddedaKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPGp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 86 ------KKLLKEAFQKTLTDLKLDYLDLYLIHWPqgfqagkelfpkDEQgnvlpskTTFLEAWEGMEELVDQGLVKALGV 159
Cdd:cd19074 81 ndrglsRKHIFESIHASLKRLQLDYVDIYYCHRY------------DPE-------TPLEETVRAMDDLIRQGKILYWGT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 160 SNFNHFQIE---RLLNKPGLkHKPVTNQVECHpYLTQEK---LIQYCHSKGIVVTAYSPLGS-------------PDRPR 220
Cdd:cd19074 142 SEWSAEQIAeahDLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgippPSRSR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 221 AKPDDP-----SLLQDP------KIKEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDFQLSD 283
Cdd:cd19074 220 ATDEDNrdkkrRLLTDEnlekvkKLKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
138-289 |
6.70e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 64.92 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 138 FLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGlkhKPVTNQVEC-----HPyltQEKLIQYCHSKGIVVTAYSP 212
Cdd:cd19101 121 YLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGV---PIVSNQVQYslldrRP---ENGMAALCEDHGIKLLAYGT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 213 ----------LGSPDRPRAKPDDPS-------------------LLQDpkIKEIAAKHKKTTAQVLIRFHIQRNVV--VI 261
Cdd:cd19101 195 laggllsekyLGVPEPTGPALETRSlqkyklmidewggwdlfqeLLRT--LKAIADKHGVSIANVAVRWVLDQPGVagVI 272
|
170 180 190
....*....|....*....|....*....|..
gi 27465603 262 pksvTPAR----IQENIQVFDFQLSDQEMATI 289
Cdd:cd19101 273 ----VGARnsehIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
144-289 |
1.94e-11 |
|
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: 63.62 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 144 GMEELVDQGLVKALGVSNFNHFQIERllnkpglKHK--PVTN-QVECHPYLT-----QEKLIQYCHSKGIVVTAYSPLG- 214
Cdd:cd19144 140 AMAELVQEGKIKHIGLSECSAETLRR-------AHAvhPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 215 --------SPD----------RPRAKPDD-PSLLQ--DpKIKEIAAKHKKTTAQVLIRFHIQR--NVVVIPKSVTPARIQ 271
Cdd:cd19144 213 gfltgairSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLE 291
|
170
....*....|....*...
gi 27465603 272 ENIQVFDFQLSDQEMATI 289
Cdd:cd19144 292 ENLGALKVKLTEEEEKEI 309
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-289 |
2.95e-11 |
|
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: 63.12 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWK-----SMPNQV----------KEAVKAAIDAGYRHIDCAYAY---CNENEVGEAIqekikeKAVRREDL 73
Cdd:cd19103 3 KLPKIALGTWSwgsggAGGDQVfgnhldedtlKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFL------KRYPREDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 74 FIVSKLWPTCFEKKL--LKEAFQKTLTDLKLDYLDLYLIHwpqgfqagkelfpkdeqgnvLPSKttfLEAW-EGMEELVD 150
Cdd:cd19103 77 IISTKFTPQIAGQSAdpVADMLEGSLARLGTDYIDIYWIH--------------------NPAD---VERWtPELIPLLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 151 QGLVKALGVSNFNHFQIER---LLNKPGLKHKPVTNqvecH---PYLTQEK--LIQYCHSKGIVVTAYSPL------GSP 216
Cdd:cd19103 134 SGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HyslLYRSSEEagILDYCKENGITFFAYMVLeqgalsGKY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 217 DRPRAKPDDPSLLQD-----PKI-------KEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQ 284
Cdd:cd19103 210 DTKHPLPEGSGRAETynpllPQLeeltavmAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDD 289
|
....*
gi 27465603 285 EMATI 289
Cdd:cd19103 290 EIKEL 294
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-276 |
6.95e-11 |
|
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: 61.48 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 14 PIVGLGTWK----SMPNQVKEAVK---AAIDAGYRHIDCAYAYCN-ENEVGEAIqekikeKAVRREDLFIVSKLWPTCFE 85
Cdd:cd19095 1 SVLGLGTSGigrvWGVPSEAEAARllnTALDLGINLIDTAPAYGRsEERLGRAL------AGLRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 86 KKLLKE-----------------------AFQktltdlkldyldlylIHWPQgfqagkelfPKDEQGNVLpskttfleaw 142
Cdd:cd19095 75 GRDRKDfspaairasierslrrlgtdyidLLQ---------------LHGPS---------DDELTGEVL---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 143 EGMEELVDQGLVKALGVSNFNHfQIERLLNKPGLKhkpvTNQVechPY----LTQEKLIQYCHSKGIVVTAYSPLGSPDR 218
Cdd:cd19095 121 ETLEDLKAAGKVRYIGVSGDGE-ELEAAIASGVFD----VVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRL 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 219 PRAKPDDPSLLQDPKIKEIAAKHK-KTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQV 276
Cdd:cd19095 193 RRRVRRRPLYADYARRPEFAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEENLAA 253
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
109-289 |
7.36e-11 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 62.20 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 109 LIHWP---QGFQAGKELFPKDEQGNVLPskttFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLN---KPGLKhKPVT 182
Cdd:cd19094 118 QLHWPdryTPLFGGGYYTEPSEEEDSVS----FEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLElaeQLGLP-RIVS 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 183 NQvecHPY--LTQ---EKLIQYCHSKGIVVTAYSPLG----------SPDRP-RAKPDD-----------PSLLQDPKIK 235
Cdd:cd19094 193 IQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAARPeGGRLNLfpgymaryrspQALEAVAEYV 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 236 EIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19094 270 KLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
147-289 |
9.93e-11 |
|
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: 61.46 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 147 ELVDQGLVKALGVSNFNHFQIERLLN---KPGLKhKPVTNQVEchpY------LTQEKLIQYCHSKGIVVTAYSPLGS-- 215
Cdd:cd19081 139 DLIRQGKVRYIGASNYSAWRLQEALElsrQHGLP-RYVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPLAGgf 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 216 -----------PDRPRAKPDDPSLLQDP------KIKEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQV 276
Cdd:cd19081 215 ltgkyrseadlPGSTRRGEAAKRYLNERglrildALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAA 294
|
170
....*....|...
gi 27465603 277 FDFQLSDQEMATI 289
Cdd:cd19081 295 AGLRLTDEEVARL 307
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
136-289 |
1.02e-10 |
|
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: 61.48 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 136 TTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLL---NKPGLKhKPVTNQV-----------ECHPYLTQEKLiqych 201
Cdd:cd19091 134 TPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQAyysllgrdlehELMPLALDQGV----- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 202 skGIVVtaYSPLG--------SPDRPRAK------------PDDPSLLQD--PKIKEIAAKHKKTTAQVLIRFHIQRNVV 259
Cdd:cd19091 208 --GLLV--WSPLAggllsgkyRRGQPAPEgsrlrrtgfdfpPVDRERGYDvvDALREIAKETGATPAQVALAWLLSRPTV 283
|
170 180 190
....*....|....*....|....*....|..
gi 27465603 260 --VIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19091 284 ssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
24-278 |
1.20e-10 |
|
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: 60.65 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 24 MPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIqekikeKAVRREDLFIVSKLWPTCFEK-----KLLKEAFQK 95
Cdd:cd19096 19 DEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEAL------KEGPREKFYLATKLPPWSVKSaedfrRILEESLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 96 TltdlKLDYLDLYLIHWPQgfqaGKELFPKDEQGNvlpskttfleAWEGMEELVDQGLVKALGVSnfnhF-----QIERL 170
Cdd:cd19096 93 L----GVDYIDFYLLHGLN----SPEWLEKARKGG----------LLEFLEKAKKEGLIRHIGFS----FhdspeLLKEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 171 LNkpglkhkpvTNQVEC----HPYLTQE-----KLIQYCHSKGIVVTAYSPLgspdrprakpDDPSLLQDPK-IKEIAAK 240
Cdd:cd19096 151 LD---------SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPL----------KGGGLANNPPeALAILCG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27465603 241 HKKTTAQVLIRFHI-QRNV-VVIPKSVTPARIQENIQVFD 278
Cdd:cd19096 212 APLSPAEWALRFLLsHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-276 |
1.42e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 60.68 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 9 TKAKMPIVGLGTWKSmPNQVKEAVKAAIDAGYRHIDCAYAYCN---ENEVGEAIqekikeKAVRREDLFIVSKLWPTcfE 85
Cdd:cd19105 9 TGLKVSRLGFGGGGL-PRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKASPR--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 86 KKLLKEAFQKTLTDLKLDYLD----LYLIHwpqGFQAGKELFPKDEqgnvlpskttFLEAwegMEELVDQGLVKALGVSn 161
Cdd:cd19105 80 DKKDKAELLKSVEESLKRLQTdyidIYQLH---GVDTPEERLLNEE----------LLEA---LEKLKKEGKVRFIGFS- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 162 fNHFQIERLLNKpglkhkpvtnQVECHPY---------LTQ----EKLIQYCHSKGIVVTAYSPLGSPdrprakpddpsL 228
Cdd:cd19105 143 -THDNMAEVLQA----------AIESGWFdvimvaynfLNQpaelEEALAAAAEKGIGVVAMKTLAGG-----------Y 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27465603 229 LQDPKIKEIAAKhKKTTAQVLIRFHIQ-RNV-VVIPKSVTPARIQENIQV 276
Cdd:cd19105 201 LQPALLSVLKAK-GFSLPQAALKWVLSnPRVdTVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-283 |
2.15e-10 |
|
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: 60.26 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 14 PIVGLGT--WKSMPNQV-----KEAVKAAIDAGYRHIDCAYAYCN-ENEVGEAIQEkikekaVRREDLFIVSKL-----W 80
Cdd:cd19090 1 SALGLGTagLGGVFGGVdddeaVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 81 PTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPkdeqGNVLpskttfleawEGMEELVDQGLVKALGVS 160
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP----GGAL----------EALLELKEEGLIKHIGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 161 NFNHFQIERLLNkpglkhkpvTNQVEC----HPY--LTQE---KLIQYCHSKGIVVTAYSPLGS-------PDRPRAKPD 224
Cdd:cd19090 141 GGPPDLLRRAIE---------TGDFDVvltaNRYtlLDQSaadELLPAAARHGVGVINASPLGMgllagrpPERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 225 DPSL-LQDP--KIKEIAAKHKKTTAQVLIRFhIQRN-----VVVIPKSvtPARIQENIQVFDFQLSD 283
Cdd:cd19090 212 WLSPeLLDRakRLYELCDEHGVPLPALALRF-LLRDpristVLVGASS--PEELEQNVAAAEGPLPE 275
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-276 |
1.34e-09 |
|
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: 57.49 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 16 VGLGTW-------KSM-PNQVKEAVKAAIDAGYRHIDCAYAY---CNENEVGEAIQEkikekavRREDLFIVSKL----- 79
Cdd:cd19086 6 IGFGTWglggdwwGDVdDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG-------RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 80 ----WPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIH-WPQgfqagkELFPKDeqgnvlpskttflEAWEGMEELVDQGLV 154
Cdd:cd19086 79 ggpeRPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPD------EVLDND-------------ELFEALEKLKQEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 155 KALGVSNFNHFQIERLLNKPGLkhkpVTNQV-----ECHPYltqEKLIQYCHSKGIVVTAYSPLGSpdrprakpddpSLL 229
Cdd:cd19086 140 RAYGVSVGDPEEALAALRRGGI----DVVQViynllDQRPE---EELFPLAEEHGVGVIARVPLAS-----------GLL 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27465603 230 qDPKIKEIAakhkkttaqvlIRFHIQRNVV--VIPKSVTPARIQENIQV 276
Cdd:cd19086 202 -TGKLAQAA-----------LRFILSHPAVstVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-226 |
4.47e-09 |
|
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: 55.95 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 8 STKAKMPIVGLGTWKSMPNQVKEAVK---AAIDAGYRHIDCAYAYCN-ENEVGEAIQEkikekavRREDLFIVSKLWPTc 83
Cdd:cd19100 6 RTGLKVSRLGFGGGPLGRLSQEEAAAiirRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 84 fEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQgfqagkelFPKDEQGNVLPSkttflEAWEGMEELVDQGLVKALGVSNFN 163
Cdd:cd19100 78 -DYEGAKRDLERSLKRLGTDYIDLYQLHAVD--------TEEDLDQVFGPG-----GALEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27465603 164 HFQIERLLNKPGLK--HKPVtNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDP 226
Cdd:cd19100 144 PEVLLRALETGEFDvvLFPI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
136-275 |
8.70e-09 |
|
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: 55.80 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 136 TTFLEAWEGMEELVDQGLVKALGVSNFNHFQIER---LLNKPGLkHKPVTNQVEcHPYL--------------TQEkLIQ 198
Cdd:cd19752 125 TPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGW-AEFSAIQQR-HSYLrprpgadfgvqrivTDE-LLD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 199 YCHSKG-IVVTAYSPL-----GSPDRPRAKPDD--PSLLQDPKIKEIAAKHKKTTAQVLIRFHIQRNVVVIP--KSVTPA 268
Cdd:cd19752 202 YASSRPdLTLLAYSPLlsgayTRPDRPLPEQYDgpDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTVE 281
|
....*..
gi 27465603 269 RIQENIQ 275
Cdd:cd19752 282 QLEENLA 288
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-289 |
1.20e-08 |
|
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: 55.30 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 35 AIDAGYRHIDCAYAY---CNENEVGEAIQEkikekavRREDLFIVSKlWPTCFEKK-----------LLKEAFQKTLTDL 100
Cdd:cd19076 41 ALELGVTFLDTADMYgpgTNEELLGKALKD-------RRDEVVIATK-FGIVRDPGsgfrgvdgrpeYVRAACEASLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 101 KLDYLDLYLIHWPqgfqagkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERllnkpglKHK- 179
Cdd:cd19076 113 GTDVIDLYYQHRV-------------------DPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRR-------AHAv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 180 -PVTN-QVECHPYLT--QEKLIQYCHSKGIVVTAYSPL------GSPDRPRAKPDDPSLLQDP---------------KI 234
Cdd:cd19076 167 hPITAvQSEYSLWTRdiEDEVLPTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPrfqgenfdknlklveKL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27465603 235 KEIAAKHKKTTAQVLIRFHIQR--NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19076 247 EAIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-289 |
1.21e-08 |
|
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: 55.35 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 31 AVKAAIDAGYRHIDCAYAY---CNENEVGEAIQEKikekavrREDLFIVSKL---------WPTCFEKKL---LK----- 90
Cdd:cd19104 37 AVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVrldpddlgdIGGQIERSVeksLKrlkrd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 91 --EAFQktltdlkldyldlylIHWPQGFQAGKELFPKdeqgnvlPSKTTFL---EAWEGMEELVDQGLVKALGVSNFNHF 165
Cdd:cd19104 110 svDLLQ---------------LHNRIGDERDKPVGGT-------LSTTDVLglgGVADAFERLRSEGKIRFIGITGLGNP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 166 Q-----IER-----------LLNKP-GLKHKPVtnqvecHPYLTQEKLIQYCHSKGIVVTAYSPL------GSPDRPRA- 221
Cdd:cd19104 168 PairelLDSgkfdavqvyynLLNPSaAEARPRG------WSAQDYGGIIDAAAEHGVGVMGIRVLaagaltTSLDRGREa 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 222 -----KPDDPSLLQDPKIKEIAAKHKKTTAQVLIRFHIQRNVV--VIPKSVTPARIQENIQVFDF-QLSDQEMATI 289
Cdd:cd19104 242 pptsdSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVstVLVGVKNREELEEAVAAEAAgPLPAENLARL 317
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-78 |
3.49e-08 |
|
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: 53.86 E-value: 3.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 16 VGLGTWKSMPN-----QVKEAVKAAIDAGYRHIDCAYAY-CNENE--VGEAIQEKIKEKAVRREDLFIVSK 78
Cdd:cd19099 6 LGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYrGGRSErlIGKALRELIEKGGIKRDEVVIVTK 76
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-252 |
5.46e-07 |
|
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: 49.83 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 25 PNQVKEAVKAAIDAGYRHIDCAYAYcnenevGEAiQEKIKEKAVRREDLFIVSKL----WPTCFEKKLLKEAFQKTLTDL 100
Cdd:cd19097 25 EKEAKKILEYALKAGINTLDTAPAY------GDS-EKVLGKFLKRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 101 KLDYLDLYLIHWPQgfqagkELFPKDEqgnvlpskttflEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHkp 180
Cdd:cd19097 98 KVDSLDGLLLHNPD------DLLKHGG------------KLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDI-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 181 VtnQVechPY------LTQEKLIQYCHSKGIVVTAYSP------LGSPDRPRAKPDDPSLLQDpKIKEIAAKHKKTTAQV 248
Cdd:cd19097 158 I--QL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPAKPLLK-KLHELAKKLGLSPLEL 231
|
....
gi 27465603 249 LIRF 252
Cdd:cd19097 232 ALGF 235
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
31-289 |
2.26e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.43 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 31 AV-KAAIDAGYRHIDCAYAYcnenevGEAIQEKIKEKAVR--REDLFIVSKL---------WPTCFEKKLLKEAFQKTLT 98
Cdd:PRK10376 44 AVlREAVALGVNHIDTSDFY------GPHVTNQLIREALHpyPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 99 DLKLDYLDLYLIHWPQGFQAgkelfpkdeqgnvlPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIER--------- 169
Cdd:PRK10376 118 NLGLDVLDVVNLRLMGDGHG--------------PAEGSIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEarkiaeivc 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 170 LLNKPGLKHKpvtnqvechpylTQEKLIQYCHSKGIVVTAYSPLG--SPdrprakpddpslLQDPKIKEIAAKHKKTTAQ 247
Cdd:PRK10376 184 VQNHYNLAHR------------ADDALIDALARDGIAYVPFFPLGgfTP------------LQSSTLSDVAASLGATPMQ 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 27465603 248 VLIRFHIQR--NVVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:PRK10376 240 VALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
144-289 |
7.20e-06 |
|
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: 46.83 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 144 GMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHK--PVTNQVECHpyLTQ----EKLIQYCHSKGIVVTAYSPLGS-- 215
Cdd:cd19080 135 ALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWspFVALQIEYS--LLErtpeRELLPMARALGLGVTPWSPLGGgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 216 -------PDRPRAKPDDPSLLQDPKI-----------KEIAAKHKKTTAQVLIRFHIQRNVVVIP--KSVTPARIQENIQ 275
Cdd:cd19080 213 ltgkyqrGEEGRAGEAKGVTVGFGKLternwaivdvvAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLG 292
|
170
....*....|....
gi 27465603 276 VFDFQLSDQEMATI 289
Cdd:cd19080 293 ALDLTLSPEQLARL 306
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
33-236 |
8.41e-05 |
|
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: 43.72 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 33 KAAIDAGYRHIDCAYAYCN---ENEVGEAIQEkikekavRREDLFIVSKlwptCFEK------------KLLKEAFQKTL 97
Cdd:cd19087 37 DRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATK----VFGPmgddpndrglsrRHIRRAVEASL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 98 TDLKLDYLDLYLIHWPQgfqagkelfpkdeqgnvlpSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLN---KP 174
Cdd:cd19087 106 RRLQTDYIDLYQMHHFD-------------------RDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 175 GLKH----KPVTNQVECHPYLtqeKLIQYCHSKGIVVTAYSPLGS-----PDRPRAKPDDPSLLQDPKIKE 236
Cdd:cd19087 167 GLLRfvseQPMYNLLKRQAEL---EILPAARAYGLGVIPYSPLAGglltgKYGKGKRPESGRLVERARYQA 234
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
133-287 |
1.55e-04 |
|
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: 42.63 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 133 PSKTTFLEawEGMEEL---VDQGlvKAL--GVSNFNHFQIER---LLNKpgLKHKPVTNQVechPY--LTQ---EKLIQY 199
Cdd:cd19089 126 YDPDTPLE--ETMTALadaVRSG--KALyvGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 200 CHSKGIVVTAYSPL-----------GSPDRPRAKPDDPSLLQD-------PKIK---EIAAKHKKTTAQVLIRFHIQRNV 258
Cdd:cd19089 197 LEEAGIGFIAFSPLaqglltdkylnGIPPDSRRAAESKFLTEEaltpeklEQLRklnKIAAKRGQSLAQLALSWVLRDPR 276
|
170 180 190
....*....|....*....|....*....|..
gi 27465603 259 V--VIPKSVTPARIQENIQVFD-FQLSDQEMA 287
Cdd:cd19089 277 VtsVLIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
12-213 |
2.81e-03 |
|
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: 38.98 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 12 KMPIVGLGTWKSMPNQVKEA-----VKAAIDAGYRHIDCAYAYCN---ENEVGeAIqekIKEKAVRREDLFIVSKL-WPT 82
Cdd:cd19142 12 RVSNVGLGTWSTFSTAISEEqaeeiVTLAYENGINYFDTSDAFTSgqaETELG-RI---LKKKGWKRSSYIVSTKIyWSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 83 CFE-----KKLLKEAFQKTLTDLKLDYLDLYLIHwpqgfqagkelfpkdeqgnVLPSKTTFLEAWEGMEELVDQGLVKAL 157
Cdd:cd19142 88 GSEerglsRKHIIESVRASLRRLQLDYIDIVIIH-------------------KADPMCPMEEVVRAMSYLIDNGLIMYW 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465603 158 GVSNFNH------FQIERLLNKPglkhKPVTNQVECHPyLTQEKLIQYC----HSKGIVVTAYSPL 213
Cdd:cd19142 149 GTSRWSPveimeaFSIARQFNCP----TPICEQSEYHM-FCREKMELYMpelyNKVGVGLITWSPL 209
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-289 |
5.86e-03 |
|
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: 37.80 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 17 GLGTWKSMPNQVKEA---VKAAIDAGYRHIDCAYAY---CNENEVGEAIQEKIKEKaVRREDLFIVSKLWPTCFEKK--- 87
Cdd:cd19145 21 GLSGDYGAPKPEEEGialIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPREK-VQLATKFGIHEIGGSGVEVRgdp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 88 -LLKEAFQKTLTDLKLDYLDLYLIHwpqgfqagkelfpkdEQGNVLPSKTTFLEawegMEELVDQGLVKALGVSNFNHFQ 166
Cdd:cd19145 100 aYVRAACEASLKRLDVDYIDLYYQH---------------RIDTTVPIEITMGE----LKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465603 167 IERllnkpglKH--KPVTN-QVECHPYL--TQEKLIQYCHSKGIVVTAYSPLG------SPDRPRAKPDDPSLLQDP--- 232
Cdd:cd19145 161 IRR-------AHavHPITAvQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgffagKAKLEELLENSDVRKSHPrfq 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465603 233 ------------KIKEIAAKHKKTTAQV-LIRFHIQRN-VVVIPKSVTPARIQENIQVFDFQLSDQEMATI 289
Cdd:cd19145 234 genleknkvlyeRVEALAKKKGCTPAQLaLAWVLHQGEdVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| |
