|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
15-322 |
0e+00 |
|
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: 648.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYGNPQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHP 94
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSNFNKR 174
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 175 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDASWVNLKCPPLLEDELLASIAKKYKKT 254
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 255 TAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFVELLMWSDHPEYPF 322
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
8-309 |
0e+00 |
|
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: 531.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 8 HSIPLSDGNTIPLIGLGTYGnPQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGK 87
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYA-PEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 LWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIG 167
Cdd:cd19108 80 LWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 168 VSNFNKRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDASWVNLKCPPLLEDELLASI 247
Cdd:cd19108 160 VSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308422931 248 AKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFV 309
Cdd:cd19108 240 AKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYL 301
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
15-326 |
9.06e-149 |
|
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: 420.67 E-value: 9.06e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHP 94
Cdd:cd19107 1 GAKMPILGLGTW----KSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSNFNKR 174
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 175 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtSRDASWVNLKCPPLLEDELLASIAKKYKKT 254
Cdd:cd19107 157 QIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLG-SPDRPWAKPEDPSLLEDPKIKEIAAKHNKT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308422931 255 TAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFVELLMWSDHPEYPFHDDY 326
Cdd:cd19107 236 TAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
12-309 |
5.52e-139 |
|
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: 395.60 E-value: 5.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKI-ADGTVKREDIFYCGKLWN 90
Cdd:cd19106 1 LHTGQKMPLIGLGTW----KSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSN 170
Cdd:cd19106 77 TKHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtSRDASWVNLKCPPLLEDELLASIAKK 250
Cdd:cd19106 157 FNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLG-SPDRPWAKPDEPVLLEEPKVKALAKK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFV 309
Cdd:cd19106 234 YNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-309 |
4.04e-127 |
|
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: 365.07 E-value: 4.04e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGNpqeTPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKL---KDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYpkdENGKHIYHETDLCATWEALEACKDAGLVKSIGV 168
Cdd:cd19116 79 WNSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSE---SNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNkpGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtsRDASWVNLKCPPLLEDELLASIA 248
Cdd:cd19116 156 SNFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFG--RLVPRGQTNPPPRLDDPTLVAIA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFV 309
Cdd:cd19116 232 KKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
18-300 |
3.22e-126 |
|
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: 361.03 E-value: 3.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYGnpqeTPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIadgtVKREDIFYCGKLWNTFHPPEL 97
Cdd:cd19071 1 MPLIGLGTYK----LKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 98 VRPALEKTLQTLQLDYVDLYIIELPTAFKPGDtfypkdengkhiyHETDLCATWEALEACKDAGLVKSIGVSNFNKRQLE 177
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 178 LILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDaswvnlkcpPLLEDELLASIAKKYKKTTAQ 257
Cdd:cd19071 140 ELLAAA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRR---------PLLDDPVLKEIAKKYGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1308422931 258 VCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19071 209 VLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
18-326 |
1.25e-121 |
|
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: 351.57 E-value: 1.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYgnpQETPkGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHPPEL 97
Cdd:cd19110 4 IPAVGLGTW---KASP-GEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 98 VRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSNFNKRQLE 177
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 178 LILNKPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDASwvnlkcpPLLEDELLASIAKKYKKTTAQ 257
Cdd:cd19110 160 RLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGV-------DLIDDPVIQRIAKKHGKSPAQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 258 VCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFVELLMWSDHPEYPFHDDY 326
Cdd:cd19110 233 ILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-307 |
3.43e-120 |
|
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: 347.86 E-value: 3.43e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTY-GNPQEtpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGK 87
Cdd:cd19154 3 SITLSNGVKMPLIGLGTWqSKGAE-----GITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 LWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIG 167
Cdd:cd19154 78 LWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 168 VSNFNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLG----TSRDASWVNLKCPPLLEDEL 243
Cdd:cd19154 158 VSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgrANFTKSTGVSPAPNLLQDPI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 244 LASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIR 307
Cdd:cd19154 236 VKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
14-308 |
9.08e-118 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 340.11 E-value: 9.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 14 DGNTIPLIGLGTYGNPQETpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREkiADgtVKREDIFYCGKLWNTFH 93
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEE----AAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAA--SG--VPREELFVTTKVWNDNH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 PPELVRPALEKTLQTLQLDYVDLYIIelptafkpgdtfypkdengkhiyH---ETDLCATWEALEACKDAGLVKSIGVSN 170
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLI-----------------------HwpgPGPYVETWRALEELYEEGLIRAIGVSN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKPGlkHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKK 250
Cdd:COG0656 130 FDPEHLEELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEK 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:COG0656 197 HGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
9-309 |
2.00e-117 |
|
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: 340.54 E-value: 2.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGnpqeTPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19123 3 TLPLSNGDLIPALGLGTWK----SKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGdTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGV 168
Cdd:cd19123 79 WNNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGT-SRDASWVNLKCPPLLEDELLASI 247
Cdd:cd19123 158 SNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308422931 248 AKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFV 309
Cdd:cd19123 236 AEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-299 |
5.41e-108 |
|
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: 316.21 E-value: 5.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 11 PLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWN 90
Cdd:cd19125 4 KLNTGAKIPAVGLGTW----QADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFyPKDENgkhiYHETDLCATWEALEACKDAGLVKSIGVSN 170
Cdd:cd19125 80 TDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAHM-PEPEE----VLPPDIPSTWKAMEKLVDSGKVRAIGVSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtSRDASWVNlkcPPLLEDELLASIAKK 250
Cdd:cd19125 155 FSVKKLEDLLAVARV--PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLG-SPGTTWVK---KNVLKDPIVTKVAEK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAI 299
Cdd:cd19125 229 LGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
12-302 |
4.06e-103 |
|
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: 303.95 E-value: 4.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYgnpQETPkGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIAD-GTVKREDIFYCGKLWN 90
Cdd:cd19118 1 LNTGNKIPAIGLGTW---QAEP-GEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPG-----DTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKS 165
Cdd:cd19118 77 NSHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdlnpLTAVPTNGGEVDLDLSVSLVDTWKAMVELKKTGKVKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 166 IGVSNFNKRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnLKCPPLLEDELLA 245
Cdd:cd19118 157 IGVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEVK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308422931 246 SIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEifDFSLSDAEMTAIEGL 302
Cdd:cd19118 229 AIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-314 |
4.43e-96 |
|
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: 287.03 E-value: 4.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCW----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFK---------PGdtFYPKDENgKHIYHETDLCATWEALEACKD 159
Cdd:cd19113 78 WNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekypPG--FYCGDGD-NFVYEDVPILDTWKALEKLVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 160 AGLVKSIGVSNFNKRQLELILNkpGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSrdaSWVNL------ 233
Cdd:cd19113 155 AGKIKSIGVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQ---SFVELnqgral 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 234 KCPPLLEDELLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFVELLM 313
Cdd:cd19113 230 NTPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDPWD 309
|
.
gi 1308422931 314 W 314
Cdd:cd19113 310 W 310
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
15-308 |
6.34e-95 |
|
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: 283.23 E-value: 6.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYGNPQETpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHP 94
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEE----VRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYIIELPTAFKpgdtfyPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSNFNKR 174
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 175 QLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDA---SWVNLkcPPLLEDELLASIAKKY 251
Cdd:cd19111 151 QINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqsLWPDQ--PDLLEDPTVLAIAKEL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308422931 252 KKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19111 227 DKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-307 |
1.31e-94 |
|
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: 282.88 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTY-GNPQETPKgtaceSVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGK 87
Cdd:cd19155 3 CVTFNNGEKMPVVGLGTWqSSPEEIET-----AVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 LWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFK-PGDTFYPKDENGKH-IYHETDLCATWEALEACKDAGLVKS 165
Cdd:cd19155 78 LPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHkQDYTTDLLDIWKAMEAQVDQGLTRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 166 IGVSNFNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGT------SRDASWVNLKCPPLL 239
Cdd:cd19155 158 IGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfSPGTGSPSGSSPDLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 240 EDELLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIR 307
Cdd:cd19155 236 QDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-302 |
1.40e-94 |
|
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: 281.85 E-value: 1.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 14 DGNTIPLIGLGTYGNPQEtpKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVK-REDIFYCGKLWNTF 92
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS--PEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 93 HPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDEngkHIYHETDLCATWEALEACKDAGLVKSIGVSNFN 172
Cdd:cd19124 79 AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE---EDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 173 KRQLELIL---NKPglkhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdASWVNlkcPPLLEDELLASIAK 249
Cdd:cd19124 156 CKKLQELLsfaTIP-----PAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPG-TKWGS---NAVMESDVLKEIAA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1308422931 250 KYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19124 227 AKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-303 |
1.32e-91 |
|
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: 273.48 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGNPQETpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIRekiaDGTVKREDIFYCGKL 88
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDE----AASAVREALEVGYRSIDTAAIYGNEEGVGKAIR----ASGVPREELFITTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfyPKdengKHIYHETdlcatWEALEACKDAGLVKSIGV 168
Cdd:cd19131 73 WNSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---------PA----QDKYVET-----WKALIELKKEGRVKSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIA 248
Cdd:cd19131 135 SNFTIEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19131 202 EKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
12-304 |
4.14e-91 |
|
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: 273.22 E-value: 4.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYgnpQETPkGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIRekiaDGTVKREDIFYCGKLWNT 91
Cdd:cd19117 8 LNTGAEIPAVGLGTW---QSKP-NEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLWCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHppELVRPALEKTLQTLQLDYVDLYIIELPTAFKP-GDTFYPKDENG-KHIYHETDLCATWEALEACKDAGLVKSIGVS 169
Cdd:cd19117 80 WH--RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGtKDHEPDWDFIKTWELMQKLPATGKVKAIGVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 170 NFNKRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSrDAswvnlkcpPLLEDELLASIAK 249
Cdd:cd19117 158 NFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST-NA--------PLLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1308422931 250 KYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIfdFSLSDAEMTAIEGLNK 304
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHK 281
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-303 |
7.44e-91 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 271.37 E-value: 7.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 10 IPLSDGNTIPLIGLGTYgnpQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIadgtVKREDIFYCGKLW 89
Cdd:cd19133 1 VTLNNGVEMPILGFGVF---QIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpGDtfypkdengkhiYHETdlcatWEALEACKDAGLVKSIGVS 169
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPF----GD------------VYGA-----WRAMEELYKEGKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 170 NFNKRQL-ELILNKpglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDAswvnlkcppLLEDELLASIA 248
Cdd:cd19133 133 NFYPDRLvDLILHN---EVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNN---------LFENPVLTEIA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19133 201 EKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
9-308 |
1.31e-90 |
|
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: 272.76 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19115 4 TVKLNSGYDMPLVGFGLW----KVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGD--TFYP---KDENGKHIYHETDLCATWEALEACKDAGLV 163
Cdd:cd19115 80 WNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDpaVRYPpgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 164 KSIGVSNFNKrQLELILNKPGlKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTsrdASWVNL------KCPP 237
Cdd:cd19115 160 RSIGVSNFSA-QLLMDLLRYA-RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGP---QSFLELdlpgakDTPP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308422931 238 LLEDELLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19115 235 LFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
13-308 |
9.46e-89 |
|
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: 267.79 E-value: 9.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 13 SDGNTIPLIGLGT-YGNPQETPkgtacESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNT 91
Cdd:cd19129 1 NGSGAIPALGFGTlIPDPSATR-----NAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHE-TDLCATWEALEACKDAGLVKSIGVSN 170
Cdd:cd19129 76 NHRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKPGLkhKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDaswvnlkcPPLLEDELLASIAKK 250
Cdd:cd19129 156 VSLEKLREIFEAARI--KPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME--------PKLLEDPVITAIARR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIfdFSLSDAEMTAI-EGLNKNIRF 308
Cdd:cd19129 226 VNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREInEGIKTRYRF 282
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
18-302 |
2.63e-87 |
|
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: 262.57 E-value: 2.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYgnpQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHPPEL 97
Cdd:cd19136 1 MPILGLGTF---RLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 98 VRPALEKTLQTLQLDYVDLYIIELPTAFKpgdtFYPKDENGKHIYHETdlcatWEALEACKDAGLVKSIGVSNFNKRQLE 177
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVQG----LKPSDPRNAELRRES-----WRALEDLYKEGKLRAIGVSNYTVRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 178 LILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcPPLLEDELLASIAKKYKKTTAQ 257
Cdd:cd19136 149 ELLKYCEVP--PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD---------LRLLEDPTVLAIAKKYGRTPAQ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1308422931 258 VCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19136 218 VLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
12-303 |
4.35e-87 |
|
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: 261.82 E-value: 4.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYgnpqeTPKGTA-CESVKVAIEKGYRHIDGALVYFNEHEVGQAIREkiadGTVKREDIFYCGKLWN 90
Cdd:cd19132 1 LNDGTQIPAIGFGTY-----PLKGDEgVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfyPKdeNGKHIyhetdlcATWEALEACKDAGLVKSIGVSN 170
Cdd:cd19132 72 RHHGYEEALRTIEESLYRLGLDYVDLYLIHWPN---------PS--RDLYV-------EAWQALIEAREEGLVRSIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtsRDASwvnlkcppLLEDELLASIAKK 250
Cdd:cd19132 134 FLPEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLG--RGSG--------LLDEPVIKAIAEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19132 202 HGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-303 |
2.05e-86 |
|
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: 260.06 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 10 IPLSDGNTIPLIGLGTYgnpqETPKG-TACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREkiadGTVKREDIFYCGKL 88
Cdd:cd19126 1 VTLNNGTRMPWLGLGVF----QTPDGdETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTfypkdengkhiyhetdlcatWEALEACKDAGLVKSIGV 168
Cdd:cd19126 73 WNDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDT--------------------WKALEKLYASGKVKAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILnkpglKH---KPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLA 245
Cdd:cd19126 133 SNFQEHHLEELL-----AHadvVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 246 SIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19126 197 AIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-308 |
2.75e-86 |
|
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: 260.40 E-value: 2.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGNPQETpkgTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREkiadGTVKREDIFYCGKL 88
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEEGS---EVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKE----SGIPREELFITSKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPtafkpgdtfypkdenGKHIYHETdlcatWEALEACKDAGLVKSIGV 168
Cdd:cd19157 74 WNADQGYDSTLKAFEASLERLGLDYLDLYLIHWP---------------VKGKYKET-----WKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIA 248
Cdd:cd19157 134 SNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19157 201 EKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-307 |
3.91e-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: 258.95 E-value: 3.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19112 2 TITLNSGHKMPVIGLGVW----RMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHppELVRPALEKTLQTLQLDYVDLYIIELPTAFKP---GDTFYPKDENGK-HIYHETDLCATWEALEACKDAGLVK 164
Cdd:cd19112 78 WNSDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVlDIDVTISLETTWHAMEKLVSAGLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFnkrqlELILNKPGL---KHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLG-TSRDASWVNLKCPplLE 240
Cdd:cd19112 156 SIGISNY-----DIFLTRDCLaysKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgAAANAEWFGSVSP--LD 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308422931 241 DELLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIR 307
Cdd:cd19112 229 DPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-302 |
1.47e-84 |
|
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: 256.30 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGtVKREDIFYCGKL 88
Cdd:cd19121 3 SFKLNTGASIPAVGLGTW----QAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHP-PELvrpALEKTLQTLQLDYVDLYIIELPTAFKP--GDTFYPKDENGKH-IYHETDLCATWEALEACKDAGLVK 164
Cdd:cd19121 78 WSTYHRrVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRdLDWDWNHVDTWKQMEKVLKTGKTK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNKRQLELILnkPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDaswvnlkcpPLLEDELL 244
Cdd:cd19121 155 AIGVSNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGS---------PLISDEPV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 245 ASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFslSDAEMTAIEGL 302
Cdd:cd19121 224 VEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
15-308 |
1.81e-83 |
|
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: 253.31 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGT----YGNPQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIadgtVKREDIFYCGKLW- 89
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTFHPPElvrpALEKTLQTLQLDYVDLYIIELPTAFKPGDTfypkdengkhiyhetDLCATWEALEACKDAGLVKSIGVS 169
Cdd:cd19120 77 GIKDPRE----ALRKSLAKLGVDYVDLYLIHSPFFAKEGGP---------------TLAEAWAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 170 NFNKRQLELILNKPglKHKPVSNQVECHPYFT--QPKLLDYCRQKDIVIVGYSPLgtsrdASWVNLKCPPLleDELLASI 247
Cdd:cd19120 138 NFRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPL-----SPLTRDAGGPL--DPVLEKI 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308422931 248 AKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19120 209 AEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
18-300 |
1.83e-83 |
|
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: 252.19 E-value: 1.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYGNpqetpKGTAC-ESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKiadgTVKREDIFYCGKLWNTFHPPE 96
Cdd:cd19073 1 IPALGLGTWQL-----RGDDCaNAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 97 LVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyHETDLCATWEALEACKDAGLVKSIGVSNFNKRQL 176
Cdd:cd19073 72 DLKKSVDRSLEKLGTDYVDLLLIHWPN-------------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 177 ELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKKYKKTTA 256
Cdd:cd19073 133 EEALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE-----------VLRDPVIQEIAEKYDKTPA 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1308422931 257 QVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19073 200 QVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
19-302 |
9.80e-83 |
|
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: 251.67 E-value: 9.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 19 PLIGLGTYGNPQETPKgtacESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHPPELV 98
Cdd:cd19128 2 PRLGFGTYKITESESK----EAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 99 RPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKDENGKHIYHETDLCATWEALEACKDAGLVKSIGVSNFNKRQLEL 178
Cdd:cd19128 78 KEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 179 ILNKpgLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTS-RDASWVNLKCPPLLEdellasIAKKYKKTTAQ 257
Cdd:cd19128 158 LLNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSyGDGNLTFLNDSELKA------LATKYNTTPPQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1308422931 258 VCLRFNVQR---GVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19128 230 VIIAWHLQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-302 |
1.97e-81 |
|
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: 248.01 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 10 IPLSDGNTIPLIGLGT--YGnpqetpkGTACESVKVAIEK-GYRHIDGALVYFNEHEVGQAIREkiadGTVKREDIFYCG 86
Cdd:cd19135 5 VRLSNGVEMPILGLGTshSG-------GYSHEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKE----SGVPREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 KLWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDtfypkdeNGKHIYHETdlcatWEALEACKDAGLVKSI 166
Cdd:cd19135 74 KLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGK-------NVKETRAET-----WRALEELYDEGLCRAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLgtsrdASWvnlkcpPLLEDELLAS 246
Cdd:cd19135 142 GVSNFLIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-----AKG------KALEEPTVTE 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308422931 247 IAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19135 209 LAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
15-302 |
2.18e-80 |
|
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: 244.86 E-value: 2.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYGNPQETpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIrekiADGTVKREDIFYCGKLWNTFHP 94
Cdd:cd19140 5 GVRIPALGLGTYPLTGEE----CTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyHETDLCATWEALEACKDAGLVKSIGVSNFNKR 174
Cdd:cd19140 77 PDDFLASVEESLRKLRTDYVDLLLLHWPN-------------------KDVPLAETLGALNEAQEAGLARHIGVSNFTVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 175 QLELILNKPGLKHkpVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKKYKKT 254
Cdd:cd19140 138 LLREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1308422931 255 TAQVCLRFNVQR-GVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19140 205 PAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
15-314 |
3.35e-79 |
|
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: 243.62 E-value: 3.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYgnpQETPKGTAcESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKLWNTFHP 94
Cdd:cd19114 1 GDKMPLVGFGTA---KIKANETE-EVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGD--TFYP----KDENGKHIYHETDLCATWEALEACKDAGLVKSIGV 168
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDpaENYPflwkDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNkrqLELILN-KPGLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSR--DASWVNLKCPPLLEDELLA 245
Cdd:cd19114 157 ANFN---VQLILDlLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytKVTKHLKHFTNLLEHPVVK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 246 SIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFVELLMW 314
Cdd:cd19114 234 KLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPVVY 302
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-308 |
1.91e-77 |
|
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: 238.94 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYgNPQETPKGTAcESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADGTVKREDIFYCGKL 88
Cdd:cd19119 3 SFKLNTGASIPALGLGTA-SPHEDRAEVK-EAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHppELVRPALEKTLQTLQLDYVDLYIIELPTAFK-----PGDTFYPKDENGKHIYHET-DLCATWEALEACKDAGL 162
Cdd:cd19119 81 WPTFY--DEVERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 163 VKSIGVSNFNKRQLELILNKpgLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcPPLLEDE 242
Cdd:cd19119 159 AKAIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHG---------APNLKNP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308422931 243 LLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19119 228 LVKKIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIGEKYPVRF 293
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-303 |
2.79e-77 |
|
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: 237.30 E-value: 2.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 10 IPLSDGNTIPLIGLGTYgnpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKiadgTVKREDIFYCGKLW 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVF----QTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengKHIYHETdlCATWEALEACKDAGLVKSIGVS 169
Cdd:cd19127 73 ISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV---------------PNDFDRT--IQAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 170 NFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLG--TSRDASWvNLKCPPLLEDELLASI 247
Cdd:cd19127 136 NFTPEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvMRYGASG-PTGPGDVLQDPTITGL 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308422931 248 AKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19127 213 AEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-308 |
9.85e-77 |
|
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: 235.88 E-value: 9.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYgnpqETPKGT-ACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKiadgTVKREDIFYCGKLWN 90
Cdd:cd19156 3 LANGVEMPRLGLGVW----RVQDGAeAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTfypkdengkhiyhetdlcatWEALEACKDAGLVKSIGVSN 170
Cdd:cd19156 75 SDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDT--------------------WKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILNKpgLKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKK 250
Cdd:cd19156 135 FHEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 251 YKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19156 202 YGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-303 |
2.25e-72 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 224.40 E-value: 2.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGNPqetPKGTAcESVKVAIEKGYRHIDGALVYFNEHEVGQAIrekiADGTVKREDIFYCGKL 88
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVP---PADTQ-RAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKpgdtfypkdengkhiyheTDLCATWEALEACKDAGLVKSIGV 168
Cdd:cd19130 73 WNDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA------------------GNYVHTWEAMIELRAAGRTRSIGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIA 248
Cdd:cd19130 135 SNFLPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:cd19130 202 AAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
18-302 |
2.53e-67 |
|
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: 211.06 E-value: 2.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYGnpqetPKGTAC-ESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKiadgTVKREDIFYCGKLW-NTFHPP 95
Cdd:cd19139 1 IPAFGLGTFR-----LKDDVViDSVRTALELGYRHIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWiDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 96 ELVrPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhIYHETDLCATWEALEACKDAGLVKSIGVSNFNKRQ 175
Cdd:cd19139 72 KLL-PSLEESLEKLRTDYVDLTLIHWPS-----------------PNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 176 LELILNKPGlKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKKYKKTT 255
Cdd:cd19139 134 LDEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATP 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1308422931 256 AQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGL 302
Cdd:cd19139 202 AQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
12-304 |
4.05e-67 |
|
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: 212.10 E-value: 4.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 12 LSDGNTIPLIGLGTYGNpqETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREKIADG-TVKREDIFYCGKLWN 90
Cdd:cd19122 3 LNNGVKIPAVGFGTFAN--EGAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPK-DENGKHIYHEtDLC----ATWEALEACKDAGLVKS 165
Cdd:cd19122 81 HLHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILK-DLTenpePTWRAMEEIYESGKAKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 166 IGVSNFNKRQLELILNKPglKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDASWVNLKcppLLEDELLA 245
Cdd:cd19122 160 IGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGER---VSENPTLN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 246 SIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDfsLSDAEMTAIEGLNK 304
Cdd:cd19122 235 EVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-307 |
1.74e-66 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 209.93 E-value: 1.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 10 IPLSDGNTIPLIGLGTY--GNPQetpkgtACESVKVAIEKGYRHIDGALVYFNEHEVGQAIREkiadGTVKREDIFYCGK 87
Cdd:PRK11565 7 IKLQDGNVMPQLGLGVWqaSNEE------VITAIHKALEVGYRSIDTAAIYKNEEGVGKALKE----ASVAREELFITTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 LWNTFHppELVRPALEKTLQTLQLDYVDLYIIELPTAFKpgDTFypkdengkhiyhetdlCATWEALEACKDAGLVKSIG 167
Cdd:PRK11565 77 LWNDDH--KRPREALEESLKKLQLDYVDLYLMHWPVPAI--DHY----------------VEAWKGMIELQKEGLIKSIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 168 VSNFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRDAswvnlkcppLLEDELLASI 247
Cdd:PRK11565 137 VCNFQIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG---------VFDQKVIRDL 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 248 AKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIR 307
Cdd:PRK11565 206 ADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
9-308 |
2.93e-66 |
|
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: 208.94 E-value: 2.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 9 SIPLSDGNTIPLIGLGTYGNPQETPKGtaceSVKVAIEKGYRHIDGALVYFNEHEVGQAIRekiADGtVKREDIFYCGKL 88
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAER----SVSAALEAGYRLIDTAAAYGNEAAVGRAIA---ASG-IPRGELFVTTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAfkpgdtfypkdENGKHIyhetdlcATWEALEACKDAGLVKSIGV 168
Cdd:cd19134 74 ATPDQGFTASQAACRASLERLGLDYVDLYLIHWPAG-----------REGKYV-------DSWGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIA 248
Cdd:cd19134 136 SNFTAEHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIA 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 249 KKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRF 308
Cdd:cd19134 203 AAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
15-300 |
2.43e-61 |
|
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: 196.30 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTY--GNPQETPKGT---ACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREkiadgtVKREDIFYCG 86
Cdd:cd19072 1 GEEVPVLGLGTWgiGGGMSKDYSDdkkAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 KLWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyHETDLCATWEALEACKDAGLVKSI 166
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLELILNKPGlKHKPVSNQVECHPYFTQP--KLLDYCRQKDIVIVGYSPLG---TSRDAswvnlkcppllED 241
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYNLFDREEesGLLPYCQKNGIAIIAYSPLEkgkLSNAK-----------GS 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 242 ELLASIAKKYKKTTAQVCLRFNVQR-GVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19072 204 PLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
21-303 |
6.26e-61 |
|
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: 196.38 E-value: 6.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTY---GNPQETPKGTACESVKVAIEKGYRHIDGALVYF---NEHEVGQAIREKiadgTVKREDIFYCGKLWNTFHP 94
Cdd:pfam00248 1 IGLGTWqlgGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDY----PVKRDKVVIATKVPDGDGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 ------PELVRPALEKTLQTLQLDYVDLYIIelptafkpgdtfypkdengkH-IYHETDLCATWEALEACKDAGLVKSIG 167
Cdd:pfam00248 77 wpsggsKENIRKSLEESLKRLGTDYIDLYYL--------------------HwPDPDTPIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 168 VSNFNKRQLELILNKPglKHKPVSNQVECHPYF--TQPKLLDYCRQKDIVIVGYSPLG----------------TSRDAS 229
Cdd:pfam00248 137 VSNFDAEQIEKALTKG--KIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGgglltgkytrdpdkgpGERRRL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308422931 230 WVNLKCPPLLEDELLASIAKKYKKTTAQVCLRF--NVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:pfam00248 215 LKKGTPLNLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
17-309 |
4.40e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 177.91 E-value: 4.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 17 TIPLIGLGTYgnpqeTPKG-TACESVKVAIEKGYRHIDGALVYFNEHEVGQAIrekiADGTVKREDIFYCGKLWNTFHPP 95
Cdd:PRK11172 2 SIPAFGLGTF-----RLKDqVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 96 ELVRPALEKTLQTLQLDYVDLYIIELPTafkPGDtfypkdengkhiyhETDLCATWEALEACKDAGLVKSIGVSNFNKRQ 175
Cdd:PRK11172 73 DKLIPSLKESLQKLRTDYVDLTLIHWPS---PND--------------EVSVEEFMQALLEAKKQGLTREIGISNFTIAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 176 LELILNKPGlKHKPVSNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLEDELLASIAKKYKKTT 255
Cdd:PRK11172 136 MKQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNATP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 256 AQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKNIRFV 309
Cdd:PRK11172 204 AQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
15-300 |
4.37e-44 |
|
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: 151.95 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYG-----NPQETPKGTACESVKVAIEKGYRHIDGALVYFNEHE---VGQAIREkiadgtVKREDIFYCG 86
Cdd:cd19137 1 GEKIPALGLGTWGiggflTPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTeelVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 KLWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAfkpgdtfypkdengkhiyhETDLCATWEALEACKDAGLVKSI 166
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP-------------------NIPLEETLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLELILNKpgLKHKPVSNQVECHPYFTQPK---LLDYCRQKDIVIVGYSPLgtSRDAswvnlkcppLLEDEL 243
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEDRDPErdgLLEYCQKNGITVVAYSPL--RRGL---------EKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 244 LASIAKKYKKTTAQVCLRFNVQR-GVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-300 |
1.47e-43 |
|
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: 150.48 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 8 HSIPLSDGNTIPLIGLGTY--GNPQETPKgTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKiadgtvkREDI 82
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWymGEDPAKRA-QEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 83 FYCGKLWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAfkpgdtfYPKDEngkhiyhetdlcaTWEALEACKDAGL 162
Cdd:cd19138 73 FLVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-------VPLAE-------------TVAAMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 163 VKSIGVSNFNKRQLELILNKPGlKHKPVSNQVECH-----PYFTqpkLLDYCRQKDIVIVGYSPLGTSRDASWVnlkcpp 237
Cdd:cd19138 133 IRAWGVSNFDTDDMEELWAVPG-GGNCAANQVLYNlgsrgIEYD---LLPWCREHGVPVMAYSPLAQGGLLRRG------ 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 238 LLEDELLASIAKKYKKTTAQVCLRFNV-QRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19138 203 LLENPTLKEIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
18-300 |
5.85e-43 |
|
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: 149.69 E-value: 5.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGT-------YGNPQETPKGTACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREkiadgTVKREDIFYCGK 87
Cdd:cd19093 2 VSPLGLGTwqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKE-----LGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 ---LWNTFHPPELVRpALEKTLQTLQLDYVDLYIIELPTAFKPGDtfypkdengkhiyhetdlCATWEALEACKDAGLVK 164
Cdd:cd19093 77 fapLPWRLTRRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQI------------------EALMDGLADAVEEGLVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNKRQLELI---LNKPGlkHKPVSNQVE---CHPYFTQPKLLDYCRQKDIVIVGYSPLGTSR------------ 226
Cdd:cd19093 138 AVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGLltgkyspenppp 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 227 --------DASWVNLKcpPLLEdeLLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLSDAEMTA 298
Cdd:cd19093 216 ggrrrlfgRKNLEKVQ--PLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAE 291
|
..
gi 1308422931 299 IE 300
Cdd:cd19093 292 LD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-300 |
3.47e-38 |
|
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: 137.62 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGT--YGNPQ-ETPKGTACESVKVAIEKGYRHIDGALVYF---NEHEVGQAIREKiadgtvKREDIFYCGKL 88
Cdd:COG0667 10 GLKVSRLGLGTmtFGGPWgGVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGR------PRDDVVIATKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHP--------PELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyHETDLCATWEALEACKDA 160
Cdd:COG0667 84 GRRMGPgpngrglsREHIRRAVEASLRRLGTDYIDLYQLHRPD-------------------PDTPIEETLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 161 GLVKSIGVSNFNKRQLELILNKPGLKHKPVSNQVECHPYFTQP--KLLDYCRQKDIVIVGYSPLG--------------- 223
Cdd:COG0667 145 GKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSLLDRSAeeELLPAARELGVGVLAYSPLAgglltgkyrrgatfp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 224 -TSRDASwvNLKCPPLLED-----ELLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFDFSLSDAE 295
Cdd:COG0667 225 eGDRAAT--NFVQGYLTERnlalvDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAED 302
|
....*
gi 1308422931 296 MTAIE 300
Cdd:COG0667 303 LAALD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
21-306 |
1.10e-33 |
|
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: 125.39 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT-------YGNPQEtpKGTACESVKVAIEKGYRHIDGALVYFNEHE---VGQAIREKiadgtvkREDIFYCGKLWN 90
Cdd:cd19085 4 LGLGCwqfgggyWWGDQD--DEESIATIHAALDAGINFFDTAEAYGDGHSeevLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFHPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyHETDLCATWEALEACKDAGLVKSIGVSN 170
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPS-------------------SDVPLEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 171 FNKRQLELILnKPGlkhKPVSNQVECHPYFTQPK--LLDYCRQKDIVIVGYSPLG--------TSRDASWVN-------- 232
Cdd:cd19085 136 FGPAQLEEAL-DAG---RIDSNQLPYNLLWRAIEyeILPFCREHGIGVLAYSPLAqglltgkfSSAEDFPPGdartrlfr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 233 LKCPPLLED-----ELLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLNKN 305
Cdd:cd19085 212 HFEPGAEEEtfealEKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDP 291
|
.
gi 1308422931 306 I 306
Cdd:cd19085 292 L 292
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
21-300 |
2.40e-33 |
|
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: 124.56 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYG----NPQETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKiadgtvkREDIFY---CGKLWN 90
Cdd:cd19084 7 IGLGTWAiggtWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIatkCGLRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 TFH------PPELVRPALEKTLQTLQLDYVDLYIIELPtafkpgdtfypkDENgkhiyheTDLCATWEALEACKDAGLVK 164
Cdd:cd19084 80 GGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------------DPN-------TPIEETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNKRQLELILNkpglKHKPVSNQVECHPYFTQP--KLLDYCRQKDIVIVGYSPLG--------------TSRD- 227
Cdd:cd19084 141 YIGVSNFSVEQLEEARK----YGPIVSLQPPYSMLEREIeeELLPYCRENGIGVLPYGPLAqglltgkykkeptfPPDDr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 228 -ASWVNLKcPPLLEDEL-----LASIAKKYKKTTAQVCLRFNVQR-GV-VVIPKSFNPDRIKENFEIFDFSLSDAEMTAI 299
Cdd:cd19084 217 rSRFPFFR-GENFEKNLeivdkLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
.
gi 1308422931 300 E 300
Cdd:cd19084 296 D 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-223 |
1.19e-26 |
|
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: 104.91 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYGNPQETPKGTACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKiadgtVKREDIFYCGKLWNTFHP--- 94
Cdd:cd06660 3 LGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGGHPPGGdps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 -----PELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVKSIGVS 169
Cdd:cd06660 78 rsrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIGVS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308422931 170 NFNKRQLELILNKPGLKHK--PVSNQVE---CHPYFTQPKLLDYCRQKDIVIVGYSPLG 223
Cdd:cd06660 139 NWSAERLAEALAYAKAHGLpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLA 197
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-302 |
1.50e-25 |
|
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: 103.52 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYG----------NPQETPKGTACesVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKiadgtvkREDIFY--- 84
Cdd:cd19102 4 IGLGTWAiggggwgggwGPQDDRDSIAA--IRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVatk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 85 CGKLWN------TFHPPELVRPALEKTLQTLQLDYVDLYIIELPtafkpgdtfypkdengkhiYHETDLCATWEALEACK 158
Cdd:cd19102 75 CGLLWDeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWP-------------------DPDEPIEEAWGALAELK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 159 DAGLVKSIGVSNFNKRQLELIL-------NKPG--LKHKPVSNQVechpyftqpklLDYCRQKDIVIVGYSPLGT----- 224
Cdd:cd19102 136 EEGKVRAIGVSNFSVDQMKRCQaihpiasLQPPysLLRRGIEAEI-----------LPFCAEHGIGVIVYSPMQSglltg 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 225 ----SRDAS-----WVNlKCPPLLEDEL---------LASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENF 284
Cdd:cd19102 205 kmtpERVASlpaddWRR-RSPFFQEPNLarnlalvdaLRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETV 283
|
330
....*....|....*...
gi 1308422931 285 EIFDFSLSDAEMTAIEGL 302
Cdd:cd19102 284 GAADLRLTPEELAEIEAL 301
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
41-299 |
4.34e-25 |
|
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: 102.25 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 41 VKVAIEKGYRHIDGALVYFN---EHEVGQAIREKiadgTVKREDIFY---CG-KLWNTFHP---------PELVRPALEK 104
Cdd:cd19092 30 IEAALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIqtkCGiRLGDDPRPgrikhydtsKEHILASVEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 105 TLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVKSIGVSNFNKRQLELiLNKpG 184
Cdd:cd19092 106 SLKRLGTDYLDLLLLHRP------DPLMDPEE-------------VAEAFDELVKSGKVRYFGVSNFTPSQIEL-LQS-Y 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 185 LKHKPVSNQVECHPYFTQP---KLLDYCRQKDIVIVGYSPLGTSRDASWVNLKCPPLLedELLASIAKKYKKTTAQVCLR 261
Cdd:cd19092 165 LDQPLVTNQIELSLLHTEAiddGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLR--AALEELAEEYGVTIEAIALA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1308422931 262 FnVQR---GVVVIPKSFNPDRIKENFEIFDFSLSDAEMTAI 299
Cdd:cd19092 243 W-LLRhpaRIQPILGTTNPERIRSAVKALDIELTREEWYEI 282
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
21-302 |
1.08e-23 |
|
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: 98.65 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT--------YGNPQETpkgTACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKiadgtvKREDIFYCGKLW 89
Cdd:cd19083 14 IGLGTnavgghnlYPNLDEE---EGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTF--------HPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpGDTfyPKDEngkhiyhetdlcaTWEALEACKDAG 161
Cdd:cd19083 85 HKFggdgsvlnNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPD----GET--PKAE-------------AVGALQELKDEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 162 LVKSIGVSNFNKRQLELiLNKPGL------KHKPVSNQVECHpyftqpkLLDYCRQKDIVIVGYSPLG------------ 223
Cdd:cd19083 146 KIRAIGVSNFSLEQLKE-ANKDGYvdvlqgEYNLLQREAEED-------ILPYCVENNISFIPYFPLAsgllagkytkdt 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 224 TSRDASWVNLKcpPLLEDEL----------LASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFDFSL 291
Cdd:cd19083 218 KFPDNDLRNDK--PLFKGERfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTL 295
|
330
....*....|.
gi 1308422931 292 SDAEMTAIEGL 302
Cdd:cd19083 296 TEEEIAFIDAL 306
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
103-295 |
1.40e-23 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 98.30 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 103 EKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVKSIGVSNFNKRQLELiLNK 182
Cdd:COG4989 111 EGSLRRLGTDYLDLLLLHRP------DPLMDPEE-------------VAEAFDELKASGKVRHFGVSNFTPSQFEL-LQS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 183 pGLKHKPVSNQVECHPYFTQP---KLLDYCRQKDIVIVGYSPLGTSRDASWVNLKCPPLleDELLASIAKKYKKTTAQVC 259
Cdd:COG4989 171 -ALDQPLVTNQIELSLLHTDAfddGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRL--RAALDELAEKYGVSPEAIA 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 1308422931 260 LRFnVQR---GVVVIPKSFNPDRIKENFEIFDFSLSDAE 295
Cdd:COG4989 248 LAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
17-292 |
7.77e-23 |
|
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: 95.36 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 17 TIPLIGLGTYGNPQetPKGTACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKIAD-------GTVKREDifycg 86
Cdd:cd19088 8 AMRLTGPGIWGPPA--DREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHPYPDDvviatkgGLVRTGP----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 klwNTFHP---PELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLV 163
Cdd:cd19088 81 ---GWWGPdgsPEYLRQAVEASLRRLGLDRIDLYQLHRI------DPKVPFEE-------------QLGALAELQDEGLI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 164 KSIGVSNFNKRQLELILNKPGLkhkpVSNQVECHPYFTQP-KLLDYCRQKDIVIVGYSPLGTSRDASwvnlkcppllEDE 242
Cdd:cd19088 139 RHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGGDLAQ----------PGG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1308422931 243 LLASIAKKYKKTTAQVCLRFNVQRG--VVVIPKSFNPDRIKENFEIFDFSLS 292
Cdd:cd19088 205 LLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
14-305 |
3.08e-22 |
|
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: 94.82 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 14 DGNTIPLIGLGT------YGNPQetPKGTACESVKVAIEKGYRHIDGALVY-FNEHEVGQAIreKIADGtvKREDIFYCG 86
Cdd:cd19144 9 NGPSVPALGFGAmglsafYGPPK--PDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWF--KQNPG--KREKIFLAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 KLWNTFHP----------PELVRPALEKTLQTLQLDYVDLYiielptafkpgdtfYPKDENGKhiyheTDLCATWEALEA 156
Cdd:cd19144 83 KFGIEKNVetgeysvdgsPEYVKKACETSLKRLGVDYIDLY--------------YQHRVDGK-----TPIEKTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 157 CKDAGLVKSIGVSNFNKRQLelilnKPGLKHKPVSN-QVECHPYFT-----QPKLLDYCRQKDIVIVGYSPLG------- 223
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETL-----RRAHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrgfltga 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 224 -TSRD---ASWVNLKCPPLLED------EL---LASIAKKYKKTTAQVCLRFNVQRG--VVVIPKSFNPDRIKENFEIFD 288
Cdd:cd19144 219 iRSPDdfeEGDFRRMAPRFQAEnfpknlELvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALK 298
|
330
....*....|....*..
gi 1308422931 289 FSLSDAEMTAIEGLNKN 305
Cdd:cd19144 299 VKLTEEEEKEIREIAEE 315
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
21-294 |
9.01e-19 |
|
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: 84.53 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTY---GNPQETPKGTACESVKVAIEKGYRHIDGALVYFN-EHEVGQAIREkiadgtVKREDIFYCGKL-----WNT 91
Cdd:cd19090 3 LGLGTAglgGVFGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFKPGDTFYPKdengkhiyhetdlcATWEALEACKDAGLVKSIGVSNf 171
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPG--------------GALEALLELKEEGLIKHIGLGG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 172 nkRQLELilnkpglkHKPV--SNQVEC---HPYFT---QP---KLLDYCRQKDIVIVGYSPLG----TSRDASWVNLKCP 236
Cdd:cd19090 142 --GPPDL--------LRRAieTGDFDVvltANRYTlldQSaadELLPAAARHGVGVINASPLGmgllAGRPPERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308422931 237 PLLEDEL-----LASIAKKYKKTTAQVCLRFNVQ----RGVVVIPKsfNPDRIKENFEIFDFSLSDA 294
Cdd:cd19090 212 WLSPELLdrakrLYELCDEHGVPLPALALRFLLRdpriSTVLVGAS--SPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
21-283 |
3.38e-18 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 82.14 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTY--GNPQETP--KGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKiadgtvkREDIFYCGKLWNTFH 93
Cdd:cd19086 6 IGFGTWglGGDWWGDvdDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 P---------PELVRPALEKTLQTLQLDYVDLYIIELPTafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVK 164
Cdd:cd19086 79 GgperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNPP-----DEVLDNDE-------------LFEALEKLKQEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNKRQLELILNKPGLkhkpVSNQVECHPYFTQP--KLLDYCRQKDIVIVGYSPL--GtsrdaswvnlkcppLLE 240
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGGI----DVVQVIYNLLDQRPeeELFPLAEEHGVGVIARVPLasG--------------LLT 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1308422931 241 DELlasiakkykkttAQVCLRFNVQRGVV--VIPKSFNPDRIKEN 283
Cdd:cd19086 203 GKL------------AQAALRFILSHPAVstVIPGARSPEQVEEN 235
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
21-300 |
1.12e-17 |
|
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: 81.90 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYG---NPQETPKGTACESVKVAIEKGYRHIDGALVY------FNEHEVGQAIREKIADgtvkREDIFYC---GKL 88
Cdd:cd19077 8 IGLGLMGltwRPNPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEY----ADKVVLSvkgGLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNTFHP---PELVRPALEKTLQTL-QLDYVDLYIielPTAFKPgdtfypkdengkHIYHETdlcaTWEALEACKDAGLVK 164
Cdd:cd19077 84 PDTLRPdgsPEAVRKSIENILRALgGTKKIDIFE---PARVDP------------NVPIEE----TIKALKELVKEGKIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNKRQLELILNKpglkHKPVSNQVECHPYFTQPK---LLDYCRQKDIVIVGYSPLG----TSRDASWVNLK--- 234
Cdd:cd19077 145 GIGLSEVSAETIRRAHAV----HPIAAVEVEYSLFSREIEengVLETCAELGIPIIAYSPLGrgllTGRIKSLADIPegd 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 235 ---CPPLLEDE----------LLASIAKKYKKTTAQVCLRFNVQRG---VVVIPKSFNPDRIKENFEIFDFSLSDAEMTA 298
Cdd:cd19077 221 frrHLDRFNGEnfeknlklvdALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKE 300
|
..
gi 1308422931 299 IE 300
Cdd:cd19077 301 IN 302
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-285 |
1.89e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 79.83 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYGNPQETPKGTAcESVKVAIEKGYRHIDGALVYFNEHE-VGQAIREKiadgtvkREDIFYCGKLWNtfH 93
Cdd:cd19100 8 GLKVSRLGFGGGPLGRLSQEEAA-AIIRRALDLGINYFDTAPSYGDSEEkIGKALKGR-------RDKVFLATKTGA--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 PPELVRPALEKTLQTLQLDYVDLYII-ELPTAFKPGDTFypkDENGkhiyhetdlcaTWEALEACKDAGLVKSIGVSNFN 172
Cdd:cd19100 78 DYEGAKRDLERSLKRLGTDYIDLYQLhAVDTEEDLDQVF---GPGG-----------ALEALLEAKEEGKIRFIGISGHS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 173 KRQLELILNKPGLK--HKPVsNQVECHPYFTQPKLLDYCRQKDIVIVGYSPLGtsrdaswvnlkcpplledellASIAKK 250
Cdd:cd19100 144 PEVLLRALETGEFDvvLFPI-NPAGDHIDSFREELLPLAREKGVGVIAMKVLA---------------------GGRLLS 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 1308422931 251 YKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFE 285
Cdd:cd19100 202 GDPLDPEQALRYALSLPPVdvVIVGMDSPEELDENLA 238
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-300 |
2.19e-17 |
|
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: 81.16 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNT---IPLIGLGTYGNPQETPKGTACESVKV-----AIEKGYRHIDGALVY-FNEHE--VGQAIREKiadgtvkREDIF 83
Cdd:cd19149 5 GKSgieASVIGLGTWAIGGGPWWGGSDDNESIrtihaALDLGINLIDTAPAYgFGHSEeiVGKAIKGR-------RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 84 Y---CGKLWN---TFHP-------------PELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhe 144
Cdd:cd19149 78 LatkCGLRWDregGSFFfvrdgvtvyknlsPESIREEVEQSLKRLGTDYIDLYQTHWQ------DVETPIEE-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 145 tdlcaTWEALEACKDAGLVKSIGVSNFNKRQLelilnKPGLKHKPVS-NQVechPY-----FTQPKLLDYCRQKDIVIVG 218
Cdd:cd19149 144 -----TMEALEELKRQGKIRAIGASNVSVEQI-----KEYVKAGQLDiIQE---KYsmldrGIEKELLPYCKKNNIAFQA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 219 YSPL-----------------GTSRdaSWVNLKCPPLLE-----DELLASIAKKYKKTTAQVCLRFNVQRG--VVVIPKS 274
Cdd:cd19149 211 YSPLeqglltgkitpdrefdaGDAR--SGIPWFSPENREkvlalLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGA 288
|
330 340
....*....|....*....|....*.
gi 1308422931 275 FNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19149 289 RKPEQAEENAKAGDIRLSAEDIATMR 314
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
21-300 |
1.48e-16 |
|
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: 78.78 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLG--TYGNPQETP----KGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKIadgtvKREDIFYCGKLWNT 91
Cdd:cd19079 15 LCLGcmSFGDPKWRPwvldEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-----PRDEVVIATKVYFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHPP--------ELVRPALEKTLQTLQLDYVDLYIIelptafkpgdtfypkdengkHIY-HETDLCATWEALEACKDAGL 162
Cdd:cd19079 90 MGDGpngrglsrKHIMAEVDASLKRLGTDYIDLYQI--------------------HRWdYETPIEETLEALHDVVKSGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 163 VKSIGVSNFNKRQLELILN---KPGLkHKPVSNQvechPYFT------QPKLLDYCRQKDIVIVGYSPL---------GT 224
Cdd:cd19079 150 VRYIGASSMYAWQFAKALHlaeKNGW-TKFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLargrlarpwGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 225 SRDASWVNLKCPPLLED----------ELLASIAKKYKKTTAQVCLRFNVQRGVVVIP-----KsfnPDRIKENFEIFDF 289
Cdd:cd19079 225 TTERRRSTTDTAKLKYDyfteadkeivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivgatK---LEHLEDAVAALDI 301
|
330
....*....|.
gi 1308422931 290 SLSDAEMTAIE 300
Cdd:cd19079 302 KLSEEEIKYLE 312
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
21-300 |
2.04e-16 |
|
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: 78.12 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTY-------GNPQETpkgTACESVKVAIEKGYRHIDGALVY-FNEHE--VGQAIREKiadgtVKREDIFY---CGK 87
Cdd:cd19148 7 IALGTWaiggwmwGGTDEK---EAIETIHKALDLGINLIDTAPVYgFGLSEeiVGKALKEY-----GKRDRVVIatkVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 LWNTFHP------PELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAG 161
Cdd:cd19148 79 EWDEGGEvvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWP------DPLVPIEE-------------TAEALKELLDEG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 162 LVKSIGVSNFNKRQLELIlnkpgLKHKPVS-NQVechPY--FTQ---PKLLDYCRQKDIVIVGYSPLgtsrdaswvnlkC 235
Cdd:cd19148 140 KIRAIGVSNFSPEQMETF-----RKVAPLHtVQP---PYnlFEReieKDVLPYARKHNIVTLAYGAL------------C 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 236 PPLL-----------EDEL---------------------LASIAKK-YKKTTAQVCLRFNVQRGVVVIP--KSFNPDRI 280
Cdd:cd19148 200 RGLLsgkmtkdtkfeGDDLrrtdpkfqeprfsqylaaveeLDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQL 279
|
330 340
....*....|....*....|
gi 1308422931 281 KENFEIFDFSLSDAEMTAIE 300
Cdd:cd19148 280 DAVDEVFGWSLNDEDMKEID 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-268 |
4.47e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 77.36 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTY-GNPQETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKIADGTVKREDIFYCGK--------- 87
Cdd:cd19099 6 LGLGTYrGDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 88 -------------------------LWNTFHPPELVRpALEKTLQTLQLDYVDLYIIELPTAFKPgdtfypkDENGKHIY 142
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRHCISPAYLED-QIERSLKRLGLDTIDLYLLHNPEEQLL-------ELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 143 HEtdLCATWEALEACKDAGLVKSIGVSNFN------------------KRQLELILNKPGLKHkpVsnQVECHPYFTQ-- 202
Cdd:cd19099 158 DR--LEEAFEALEEAVAEGKIRYYGISTWDgfrappalpghlsleklvAAAEEVGGDNHHFKV--I--QLPLNLLEPEal 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 203 ----------PKLLDYCRQKDIVIVGYSPLGTsrdaswvnlkcPPLLEDELLASI-AKKYKKTTAQVCLRFNV-QRGV 268
Cdd:cd19099 232 tekntvkgeaLSLLEAAKELGLGVIASRPLNQ-----------GQLLGELRLADLlALPGGATLAQRALQFARsTPGV 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-302 |
5.55e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.99 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 17 TIPLIGLGT--YGNPQETPKG---------TACESVKVAIEKGYRHIDGALVYfnehevGQAIREKIAdGTV----KRED 81
Cdd:cd19103 3 KLPKIALGTwsWGSGGAGGDQvfgnhldedTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKIL-GEFlkryPRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 82 IFYCGKlwntFHP------PELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfypkdengkhiyhetDLCATWEALE 155
Cdd:cd19103 76 YIISTK----FTPqiagqsADPVADMLEGSLARLGTDYIDIYWIHNPA----------------------DVERWTPELI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 156 ACKDAGLVKSIGVSNFNKRQLEL---ILNKPGLKHKPVSNQVE-CHPYFTQPKLLDYCRQKDIVIVGYS----------- 220
Cdd:cd19103 130 PLLKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHYSlLYRSSEEAGILDYCKENGITFFAYMvleqgalsgky 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 221 ------PLGTSRDASWVNLKcpPLLED--ELLASIAKKYKKTTAQVCLRFNVQRGVVVIPKSFNPDRIKENFEIFDFSLS 292
Cdd:cd19103 210 dtkhplPEGSGRAETYNPLL--PQLEEltAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLT 287
|
330
....*....|
gi 1308422931 293 DAEMTAIEGL 302
Cdd:cd19103 288 DDEIKELEQL 297
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-302 |
4.47e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 72.16 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNTIPLIGLGTYGNPQETPKgTACESVKVAIEKGYRHIDGALVYFN-EHEVGQAIREKiadgtvkREDIFYCGKLWNTFH 93
Cdd:COG1453 10 GLEVSVLGFGGMRLPRKDEE-EAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPWVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 PPELVRPALEKTLQTLQLDYVDLYII-------ELPTAFKPGDTFypkdengkhiyhetdlcatwEALEACKDAGLVKSI 166
Cdd:COG1453 82 DPEDMRKDLEESLKRLQTDYIDLYLIhglnteeDLEKVLKPGGAL--------------------EALEKAKAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQ-LELILNkpglkhkpvSNQVEC-----HPYFTQP----KLLDYCRQKDIVIVGYSPLG----TSRDASWVN 232
Cdd:COG1453 142 GFSTHGSLEvIKEAID---------TGDFDFvqlqyNYLDQDNqageEALEAAAEKGIGVIIMKPLKggrlANPPEKLVE 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 233 LKCPPLledellasiakkykkTTAQVCLRF--NVQRGVVVIPKSFNPDRIKENFEIFD--FSLSDAEMTAIEGL 302
Cdd:COG1453 213 LLCPPL---------------SPAEWALRFllSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
41-300 |
8.42e-14 |
|
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: 70.72 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 41 VKVAIEKGYRHIDGALVY-FNEHEV--GQAIREKiadgtvkREDIFYCGKLwnTFHPPE-----------LVRpALEKTL 106
Cdd:cd19091 45 VDIALDAGINFFDTADVYsEGESEEilGKALKGR-------RDDVLIATKV--RGRMGEgpndvglsrhhIIR-AVEASL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 107 QTLQLDYVDLYIIelptafkpgdtfypkdengkHIY-HETDLCATWEALEACKDAGLVKSIGVSNFNKRQLELIL---NK 182
Cdd:cd19091 115 KRLGTDYIDLYQL--------------------HGFdALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 183 PGLKhKPVSNQVechpYFT------QPKLLDYCRQKDIVIVGYSPLG----------------TSRDASwVNLKCPPLLE 240
Cdd:cd19091 175 RGLA-RFVALQA----YYSllgrdlEHELMPLALDQGVGLLVWSPLAggllsgkyrrgqpapeGSRLRR-TGFDFPPVDR 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 241 D------ELLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19091 249 ErgydvvDALREIAKETGATPAQVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARLD 316
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
21-293 |
1.20e-13 |
|
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: 70.31 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLG---TYGNpqETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREkiadgtVKREDIFYCGKL-WNTFH 93
Cdd:cd19074 7 LSLGtwlTFGG--QVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 PPE---LVRP----ALEKTLQTLQLDYVDLYIIelpTAFKPgdtfypkdengkhiyhETDLCATWEALEACKDAGLVKSI 166
Cdd:cd19074 79 GPNdrgLSRKhifeSIHASLKRLQLDYVDIYYC---HRYDP----------------ETPLEETVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLE--LILNKPGLKHKPVSNQVECHPYFTQ--PKLLDYCRQKDIVIVGYSPLG--------------TSRDA 228
Cdd:cd19074 140 GTSEWSAEQIAeaHDLARQFGLIPPVVEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPLAqglltgkyrdgippPSRSR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 229 ---SWVNLKCPPLLEDELLA------SIAKKYKKTTAQV----CLRfnvQRGV--VVIPKSfNPDRIKENFEIFDFSLSD 293
Cdd:cd19074 220 atdEDNRDKKRRLLTDENLEkvkklkPIADELGLTLAQLalawCLR---NPAVssAIIGAS-RPEQLEENVKASGVKLSP 295
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-286 |
2.00e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 68.77 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 15 GNT---IPLIGLGTYGNPQETPkgtacESVKVAIEKGYRHIDGALVYFN---EHEVGQAIRekiadgTVKREDIFYCGKL 88
Cdd:cd19105 7 GKTglkVSRLGFGGGGLPRESP-----ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK------GLRRDKVFLATKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 WNT--FHPPELVRPALEKTLQTLQLDYVDLYIIelptafkPGDTFYPKDENGKHIYhetdlcatwEALEACKDAGLVKSI 166
Cdd:cd19105 76 SPRldKKDKAELLKSVEESLKRLQTDYIDIYQL-------HGVDTPEERLLNEELL---------EALEKLKKEGKVRFI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNfnkrqlelilnkpglkHKPVSNQ----VECHPY---------FTQP----KLLDYCRQKDIVIVGYSPL--GTSRD 227
Cdd:cd19105 140 GFST----------------HDNMAEVlqaaIESGWFdvimvaynfLNQPaeleEALAAAAEKGIGVVAMKTLagGYLQP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308422931 228 ASWVNLKCPPLledellasiakkykkTTAQVCLRFNVQ-RGV-VVIPKSFNPDRIKENFEI 286
Cdd:cd19105 204 ALLSVLKAKGF---------------SLPQAALKWVLSnPRVdTVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
21-300 |
1.05e-12 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 67.64 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLG------TYGNPQETPKGTacESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKiadgtvkREDIFYCGKLWNT 91
Cdd:cd19078 7 IGLGcmgmshGYGPPPDKEEMI--ELIRKAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFGFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHP-----------PELVRPALEKTLQTLQLDYVDLYIIelptafkpgdtfypkdengkhiyHETDLCATWEAL-EACKD 159
Cdd:cd19078 78 IDGgkpgplgldsrPEHIRKAVEGSLKRLQTDYIDLYYQ-----------------------HRVDPNVPIEEVaGTMKE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 160 ---AGLVKSIGVSNFNKRQLElilnkpgLKHK--PVSN-QVECHPYFTQP--KLLDYCRQKDIVIVGYSPLG-------- 223
Cdd:cd19078 135 likEGKIRHWGLSEAGVETIR-------RAHAvcPVTAvQSEYSMMWREPekEVLPTLEELGIGFVPFSPLGkgfltgki 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 224 -------TSRDASWV----------NLkcpPLLedELLASIAKKYKKTTAQVCLRF--NVQRGVVVIPKSFNPDRIKENF 284
Cdd:cd19078 208 dentkfdEGDDRASLprftpealeaNQ---ALV--DLLKEFAEEKGATPAQIALAWllAKKPWIVPIPGTTKLSRLEENI 282
|
330
....*....|....*.
gi 1308422931 285 EIFDFSLSDAEMTAIE 300
Cdd:cd19078 283 GAADIELTPEELREIE 298
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
154-300 |
1.08e-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: 67.62 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 154 LEACKDAGLVKSIGVSNFNKRQLELILNKPGlkhKPVSNQVECHPYFTQP--KLLDYCRQKDIVIVGYSPLG----TSRd 227
Cdd:cd19101 128 LAELQEEGKIRHLGLTNFDTERLREILDAGV---PIVSNQVQYSLLDRRPenGMAALCEDHGIKLLAYGTLAggllSEK- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 228 asWVNLKCPP---------------------------LLedELLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPD 278
Cdd:cd19101 204 --YLGVPEPTgpaletrslqkyklmidewggwdlfqeLL--RTLKAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSE 279
|
170 180
....*....|....*....|..
gi 1308422931 279 RIKENFEIFDFSLSDAEMTAIE 300
Cdd:cd19101 280 HIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
21-283 |
1.60e-12 |
|
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: 66.49 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT---YGNPQETPKGTACESVKVAIEKGYRHIDGALVYFN-EHEVGQAIREkiadgtVKREDIFYCGKLWNTF---- 92
Cdd:cd19095 3 LGLGTsgiGRVWGVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGeggr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 93 ----HPPELVRPALEKTLQTLQLDYVDLYIIELPTafkpgdtfyPKDENGKHIyhetdlcatwEALEACKDAGLVKSIGV 168
Cdd:cd19095 77 drkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPS---------DDELTGEVL----------ETLEDLKAAGKVRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 169 SNFNKRQLELIlnkpglkhkpVSNQVEC--HPY----FTQPKLLDYCRQKDIVIVGYSPLGTSRDASWVNLKCPPLLEDE 242
Cdd:cd19095 138 SGDGEELEAAI----------ASGVFDVvqLPYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1308422931 243 LLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKEN 283
Cdd:cd19095 208 RPEFAAEIGGATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
41-288 |
5.01e-12 |
|
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: 64.89 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 41 VKVAIEKGYRHIDGALVYFN---EHEVGQAIREkiadgtVKREDIFYCGKL-WNTFHPPELVRPALEKTLQTLQLDYVDL 116
Cdd:cd19096 27 IRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLpPWSVKSAEDFRRILEESLKRLGVDYIDF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 117 YII------ELPTAFKPGDTFypkdengkhiyhetdlcatwEALEACKDAGLVKSIGVS------NFNKrqlelILNkpg 184
Cdd:cd19096 101 YLLhglnspEWLEKARKGGLL--------------------EFLEKAKKEGLIRHIGFSfhdspeLLKE-----ILD--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 185 lkhkpvSNQVEC----HPYFTQP-----KLLDYCRQKDIVIVGYSPLGTSRdaswvnlkcppLLED-ELLASIAKKYKKT 254
Cdd:cd19096 153 ------SYDFDFvqlqYNYLDQEnqagrPGIEYAAKKGMGVIIMEPLKGGG-----------LANNpPEALAILCGAPLS 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 1308422931 255 TAQVCLRFNV-QRGVVVIPKSF-NPDRIKENFEIFD 288
Cdd:cd19096 216 PAEWALRFLLsHPEVTTVLSGMsTPEQLDENIAAAD 251
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
98-299 |
5.19e-12 |
|
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: 65.31 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 98 VRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVKSIGVSNFNKRQLE 177
Cdd:cd19081 100 IRRAVEASLRRLQTDYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 178 LILN---KPGLKhKPVSNQVEchpY------FTQPKLLDYCRQKDIVIVGYSPL----------------GTSRDASWVN 232
Cdd:cd19081 161 EALElsrQHGLP-RYVSLQPE---YnlvdreSFEGELLPLCREEGIGVIPYSPLaggfltgkyrseadlpGSTRRGEAAK 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308422931 233 LKCPP----LLedELLASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFDFSLSDAEMTAI 299
Cdd:cd19081 237 RYLNErglrIL--DALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
21-300 |
1.40e-10 |
|
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: 61.43 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT--YGNpQETpKGTACESVKVAIEKGYRHIDGALVY-FNEHEVGQAIREKIA----DGTVKREDIFYCGKL----W 89
Cdd:cd19094 4 ICLGTmtWGE-QNT-EAEAHEQLDYAFDEGVNFIDTAEMYpVPPSPETQGRTEEIIgswlKKKGNRDKVVLATKVagpgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTFHP--------PELVRPALEKTLQTLQLDYVDLYIIELPTAFKP-GDTFYPKDENGKHIYheTDLCATWEALEACKDA 160
Cdd:cd19094 82 GITWPrgggtrldRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlFGGGYYTEPSEEEDS--VSFEEQLEALGELVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 161 GLVKSIGVSN--------FNK--RQLELilnkPglkhKPVSNQvecHPYftqpKLLD---------YCRQKDIVIVGYSP 221
Cdd:cd19094 160 GKIRHIGLSNetpwgvmkFLElaEQLGL----P----RIVSIQ---NPY----SLLNrnfeeglaeACHRENVGLLAYSP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 222 LG----------------TSRdaswVNL--------KCPPLLE--DElLASIAKKYKKTTAQVCLRFnvqrgvvVIPKSF 275
Cdd:cd19094 225 LAggvltgkyldgaarpeGGR----LNLfpgymaryRSPQALEavAE-YVKLARKHGLSPAQLALAW-------VRSRPF 292
|
330 340 350
....*....|....*....|....*....|....
gi 1308422931 276 NPDRI---------KENFEIFDFSLSDAEMTAIE 300
Cdd:cd19094 293 VTSTIigattleqlKENIDAFDVPLSDELLAEID 326
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-262 |
2.57e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 57.15 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT------YG--NPQETPKGTACES-VKVAIEKGYRHIDGALVYFNEHEV-GQAIREKiadgtvkrEDIFYCGKL-- 88
Cdd:cd19097 3 LALGTaqfgldYGiaNKSGKPSEKEAKKiLEYALKAGINTLDTAPAYGDSEKVlGKFLKRL--------DKFKIITKLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 89 --WNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPTAFkpgdtfypkDENGKHIyhetdlcatWEALEACKDAGLVKSI 166
Cdd:cd19097 75 lkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDL---------LKHGGKL---------VEALLELKKEGLIRKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLELILNKPGLKHkpVsnQVECHPY---FTQPKLLDYCRQKDIVIVGYSP------LGTSRDASWVNLKCPP 237
Cdd:cd19097 137 GVSVYSPEELEKALESFKIDI--I--QLPFNILdqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAPAKP 212
|
250 260
....*....|....*....|....*
gi 1308422931 238 LLEDelLASIAKKYKKTTAQVCLRF 262
Cdd:cd19097 213 LLKK--LHELAKKLGLSPLELALGF 235
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
95-272 |
2.79e-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: 57.34 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 95 PELVRPALEKTLQTLQLDYVDLYiielptafkpgdtfYpkdengKHIY-HETDLCATWEALEACKDAGLVKSIGVSNFNK 173
Cdd:cd19752 94 AETIEQEIDKSLRRLGTDYIDLY--------------Y------AHVDdRDTPLEETLEAFNELVKAGKVRAIGASNFAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 174 RQLEL---ILNKPGLkHKPVSNQVEcHPYFtQPK--------------LLDYCRQ-KDIVIVGYSP-LGTSRDASWVNLK 234
Cdd:cd19752 154 WRLERarqIARQQGW-AEFSAIQQR-HSYL-RPRpgadfgvqrivtdeLLDYASSrPDLTLLAYSPlLSGAYTRPDRPLP 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1308422931 235 CPPLLED-----ELLASIAKKYKKTTAQVCLRFNVQRGVVVIP 272
Cdd:cd19752 231 EQYDGPDsdarlAVLEEVAGELGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
13-299 |
2.42e-08 |
|
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: 54.36 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 13 SDGNTIPLIGLG------TYGNPQETPKGTACesVKVAIEKGYRHIDGALVY---FNEHEVGQAI----REKIADGTvkR 79
Cdd:cd19145 7 SQGLEVSAQGLGcmglsgDYGAPKPEEEGIAL--IHHAFNSGVTFLDTSDIYgpnTNEVLLGKALkdgpREKVQLAT--K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 80 EDIFYCGKLWNTFH-PPELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACK 158
Cdd:cd19145 83 FGIHEIGGSGVEVRgDPAYVRAACEASLKRLDVDYIDLYYQHRI------DTTVPIEI-------------TMGELKKLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 159 DAGLVKSIGVSNFNK---RQLELIlnkpglkHKPVSNQVECHPYF--TQPKLLDYCRQKDIVIVGYSPLG---------- 223
Cdd:cd19145 144 EEGKIKYIGLSEASAdtiRRAHAV-------HPITAVQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLGrgffagkakl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 224 -TSRDASWVNLKCPPLLEDEL---------LASIAKKYKKTTAQVCLRFNVQRG--VVVIPKSFNPDRIKENFEIFDFSL 291
Cdd:cd19145 217 eELLENSDVRKSHPRFQGENLeknkvlyerVEALAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKL 296
|
....*...
gi 1308422931 292 SDAEMTAI 299
Cdd:cd19145 297 TKEDLKEI 304
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
8-170 |
6.20e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 53.32 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 8 HSIPLSDGNtIPLIGLGTYGNPQETPKGTACESVKVAIEKGYRHIDGALVY----------FNEHEVGQAI-----REKI 72
Cdd:PRK10625 4 HRIPHSSLE-VSTLGLGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpetqgLTETYIGNWLakrgsREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 73 -----ADGTVKREDifycgklwNTFHPPEL-----VRPALEKTLQTLQLDYVDLYIIELPTafKPGDTFypkdenGKHIY 142
Cdd:PRK10625 83 iiaskVSGPSRNND--------KGIRPNQAldrknIREALHDSLKRLQTDYLDLYQVHWPQ--RPTNCF------GKLGY 146
|
170 180 190
....*....|....*....|....*....|....
gi 1308422931 143 HETD------LCATWEALEACKDAGLVKSIGVSN 170
Cdd:PRK10625 147 SWTDsapavsLLETLDALAEQQRAGKIRYIGVSN 180
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
20-303 |
8.64e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 52.66 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 20 LIGLGTYGNPQEtpKGTACESVKVAIEKGYRHIDGALVYfNEHEVGQAIRE-------------KIadGTVKREDifycg 86
Cdd:PRK10376 27 LAGPGVFGPPKD--RDAAIAVLREAVALGVNHIDTSDFY-GPHVTNQLIREalhpypddltivtKV--GARRGED----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 87 KLWNTFHPPELVRPALEKTLQTLQLDYVDLYIIELPtafkpGDTFYPKdengkhiyhETDLCATWEALEACKDAGLVKSI 166
Cdd:PRK10376 97 GSWLPAFSPAELRRAVHDNLRNLGLDVLDVVNLRLM-----GDGHGPA---------EGSIEEPLTVLAELQRQGLVRHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 167 GVSNFNKRQLE---------LILNKPGLKHKpvsnqvechpyfTQPKLLDYCRQKDIVIVGYSPLG--TSrdaswvnlkc 235
Cdd:PRK10376 163 GLSNVTPTQVAearkiaeivCVQNHYNLAHR------------ADDALIDALARDGIAYVPFFPLGgfTP---------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 236 pplLEDELLASIAKKYKKTTAQVCLRFNVQRG--VVVIPKSFNPDRIKENFEIFDFSLSDAEMTAIEGLN 303
Cdd:PRK10376 221 ---LQSSTLSDVAASLGATPMQVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
23-223 |
1.18e-07 |
|
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: 52.57 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 23 LGT--YGNpqETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKiadgtvkREDIFYCGKLwntFHPP-- 95
Cdd:cd19087 18 LGTmnFGG--RTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKV---FGPMgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 96 ---------ELVRPALEKTLQTLQLDYVDLYIIElptafkpgdtfypkdengkHIYHETDLCATWEALEACKDAGLVKSI 166
Cdd:cd19087 86 dpndrglsrRHIRRAVEASLRRLQTDYIDLYQMH-------------------HFDRDTPLEETLRALDDLVRQGKIRYI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 167 GVSNFNKRQLELILNKPGLKH--KPVSNQvecHPY---FTQPKL--LDYCRQKDIVIVGYSPLG 223
Cdd:cd19087 147 GVSNFAAWQIAKAQGIAARRGllRFVSEQ---PMYnllKRQAELeiLPAARAYGLGVIPYSPLA 207
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-302 |
5.97e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 50.34 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYGNPQ---ETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIRE---------KIADGTVKREDIfyc 85
Cdd:cd19104 15 LTFGGGGIGGlmgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGlpagpyittKVRLDPDDLGDI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 86 gklwntfhpPELVRPALEKTLQTLQLDYVDLYIIE---LPTAFKPGDTFYPKDEngkhiYHETDlcATWEALEACKDAGL 162
Cdd:cd19104 92 ---------GGQIERSVEKSLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTD-----VLGLG--GVADAFERLRSEGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 163 VKSIGVS---------------NFNKRQLELILNKPGLKHKPVSNqvecHPYFTQPKLLDYCRQKDIVIVGYSPLGTSRD 227
Cdd:cd19104 156 IRFIGITglgnppairelldsgKFDAVQVYYNLLNPSAAEARPRG----WSAQDYGGIIDAAAEHGVGVMGIRVLAAGAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 228 ASWVNLKCPPLLEDELLASI----AKKYK-------KTTAQVCLRFNV-QRGVV-VIPKSFNPDRIKENFEIFDF-SLSD 293
Cdd:cd19104 232 TTSLDRGREAPPTSDSDVAIdfrrAAAFRalarewgETLAQLAHRFALsNPGVStVLVGVKNREELEEAVAAEAAgPLPA 311
|
....*....
gi 1308422931 294 AEMTAIEGL 302
Cdd:cd19104 312 ENLARLEAL 320
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
18-295 |
8.45e-07 |
|
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: 49.95 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 18 IPLIGLGTYGNP-QETPKGTACESVKVAIEKGYRHIDGALVY-----FNEHEVGQAIREkiaDGTVKREDIFYCGKLWNT 91
Cdd:cd19089 11 LPAISLGLWHNFgDYTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKR---DLRPYRDELVISTKAGYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 92 FHPPEL--------VRPALEKTLQTLQLDYVDLyiielptafkpgdtFYpkdengKHIY-HETDLCATWEALeackdAGL 162
Cdd:cd19089 88 MWPGPYgdggsrkyLLASLDQSLKRMGLDYVDI--------------FY------HHRYdPDTPLEETMTAL-----ADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 163 VKS-----IGVSNFNKRQLEL---ILNKpgLKHKPVSNQVECHPYFTQPK--LLDYCRQKDIVIVGYSPL---------- 222
Cdd:cd19089 143 VRSgkalyVGISNYPGAKARRaiaLLRE--LGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPLaqglltdkyl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 223 -----GTSRDASWVNLKCPPLLEDEL-----LASIAKKYKKTTAQVCLRFNVQRGVV--VIPKSFNPDRIKENFEIFD-F 289
Cdd:cd19089 221 ngippDSRRAAESKFLTEEALTPEKLeqlrkLNKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVAALKnL 300
|
....*.
gi 1308422931 290 SLSDAE 295
Cdd:cd19089 301 DFSEEE 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
21-170 |
3.61e-06 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 47.93 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGTYGNPQETPKGTACESVKVAIEKGYRHIDGALVYFNEHEVG---QAIREKIAdGTVKREDIFYCGK-----LWNTF 92
Cdd:cd19082 3 IVLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVERGaseRVIGEWLK-SRGNRDKVVIATKgghpdLEDMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 93 HP---PELVRPALEKTLQTLQLDYVDLYiielptafkpgdtfypkdengkhIYHETDLCAT----WEALEACKDAGLVKS 165
Cdd:cd19082 82 RSrlsPEDIRADLEESLERLGTDYIDLY-----------------------FLHRDDPSVPvgeiVDTLNELVRAGKIRA 138
|
....*
gi 1308422931 166 IGVSN 170
Cdd:cd19082 139 FGASN 143
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
25-301 |
4.84e-05 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 44.51 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 25 TYGNPQETPKGTACesVKVAIEKGYRHIDGALVYFN---EHEVGQAIREkiadGTVKREDIFYCGKL-WNTFHPPE---- 96
Cdd:cd19143 23 TFGNQVDVDEAKEC--MKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKE----LGWPRSDYVVSTKIfWGGGGPPPndrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 97 LVRP----ALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVKSIGVSNFN 172
Cdd:cd19143 97 LSRKhiveGTKASLKRLQLDYVDLVFCHRP------DPATPIEE-------------TVRAMNDLIDQGKAFYWGTSEWS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 173 KRQLE---LILNKPGLkHKPVSNQVECHpYFTQPKL-LDYCRQKDIVIVG---YSPLGT--------------SR----D 227
Cdd:cd19143 158 AQQIEeahEIADRLGL-IPPVMEQPQYN-LFHRERVeVEYAPLYEKYGLGtttWSPLASglltgkynngipegSRlalpG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 228 ASWVNLKCPPLLEDEL-----LASIAKKYKKTTAQV----CLRF-NVQrgvVVIPKSFNPDRIKENFEIFDF--SLSDAE 295
Cdd:cd19143 236 YEWLKDRKEELGQEKIekvrkLKPIAEELGCSLAQLaiawCLKNpNVS---TVITGATKVEQLEENLKALEVlpKLTPEV 312
|
....*.
gi 1308422931 296 MTAIEG 301
Cdd:cd19143 313 MEKIEA 318
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
19-167 |
6.35e-05 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 43.85 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 19 PLIGLGT--YGNP-QETPKGTACESVKVAIEKGYRHIDGALVYFN---EHEVGQAIREKIADGTV---KREDIFYCGKLW 89
Cdd:cd19161 1 SELGLGTagLGNLyTAVSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLREKPRDEFVlstKVGRLLKPAREG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 NTFHPPELVRP----------------ALEKTLQTLQLDYVD-LYIIELptafkpgDTFYPKDENGKHIYHETdLCATWE 152
Cdd:cd19161 81 SVPDPNGFVDPlpfeivydysydgimrSFEDSLQRLGLNRIDiLYVHDI-------GVYTHGDRKERHHFAQL-MSGGFK 152
|
170
....*....|....*
gi 1308422931 153 ALEACKDAGLVKSIG 167
Cdd:cd19161 153 ALEELKKAGVIKAFG 167
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-300 |
1.56e-04 |
|
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: 42.98 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 19 PLI-GLGTYGNP--QETPKGTACESVKVAIEKGYRHIDGALVYFNEH------EVGQAIREKIADGT-----VKREDIFY 84
Cdd:cd19080 12 PLAlGTMTFGTEwgWGADREEARAMFDAYVEAGGNFIDTANNYTNGTserllgEFIAGNRDRIVLATkytmnRRPGDPNA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 85 CGKlwntfHPPELVRpALEKTLQTLQLDYVDLYIIELPtafkpgDTFYPKDEngkhiyhetdlcaTWEALEACKDAGLVK 164
Cdd:cd19080 92 GGN-----HRKNLRR-SVEASLRRLQTDYIDLLYVHAW------DFTTPVEE-------------VMRALDDLVRAGKVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 165 SIGVSNFNK---RQLELILNKPGLKhKPVSNQVECHPYFTQPK--LLDYCRQKDIVIVGYSPLG--------------TS 225
Cdd:cd19080 147 YVGISDTPAwvvARANTLAELRGWS-PFVALQIEYSLLERTPEreLLPMARALGLGVTPWSPLGgglltgkyqrgeegRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 226 RDASWVNLKCPPLLEDEL-----LASIAKKYKKTTAQVCLRFNVQRGVVVIP--KSFNPDRIKENFEIFDFSLSDAEMTA 298
Cdd:cd19080 226 GEAKGVTVGFGKLTERNWaivdvVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLAR 305
|
..
gi 1308422931 299 IE 300
Cdd:cd19080 306 LD 307
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
22-223 |
2.74e-04 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 42.16 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 22 GLGTYGNPQETPKGTACesVKVAIEKGYRHIDGALVYFN-EHE--VGQA--------IREKIADGTVKRedifycgklwn 90
Cdd:cd19075 9 TFGSQGRFTTAEAAAEL--LDAFLERGHTEIDTARVYPDgTSEelLGELglgergfkIDTKANPGVGGG----------- 75
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 91 tfHPPELVRPALEKTLQTLQLDYVDLYIIELPtafkpgDtfypkdengkhiyHETDLCatwEALEACKD---AGLVKSIG 167
Cdd:cd19075 76 --LSPENVRKQLETSLKRLKVDKVDVFYLHAP------D-------------RSTPLE---ETLAAIDElykEGKFKEFG 131
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308422931 168 VSNFNKRQLELILN--------KP----GLkHKPVSNQVEchpyftqPKLLDYCRQKDIVIVGYSPLG 223
Cdd:cd19075 132 LSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRKLGIRFYAYSPLA 191
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| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
19-285 |
3.52e-04 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 41.58 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 19 PLIGLG--TYGNPQETPKGTACESVKVAIEKGYRHIDGALVY---FNEHEVGQAIREKiadgtvKREDIFYCGKLWNTFH 93
Cdd:cd19162 1 PRLGLGaaSLGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVGRLLE 74
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 94 PPELVRPA----------------LEKTLQTLQLDYVDLYIIELPtafkpgdtfypkDEngkhiYHETDLCATWEALEAC 157
Cdd:cd19162 75 PGAAGRPAgadrrfdfsadgirrsIEASLERLGLDRLDLVFLHDP------------DR-----HLLQALTDAFPALEEL 137
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 158 KDAGLVKSIGVSNFNKRQLELILNKPGLKHKPVSNQvecHPYFTQP---KLLDYCRQKDIVIVGYSPLGT----SRDASW 230
Cdd:cd19162 138 RAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLDRRaatELLPLCAAKGVAVVAAGVFNSgilaTDDPAG 214
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308422931 231 VNLKCPPLLEDEL-----LASIAKKYKKTTAQVCLRFNVQ----RGVVVIPKSfnPDRIKENFE 285
Cdd:cd19162 215 DRYDYRPATPEVLararrLAAVCRRYGVPLPAAALQFPLRhpavASVVVGAAS--PAELRDNLA 276
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| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
21-171 |
1.16e-03 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 40.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 21 IGLGT------YGNPQETPKgtACESVKVAIEKGYRHIDGALVYFNEHE---VGQAIREKiadgTVKREDIFYCGKLW-- 89
Cdd:cd19153 15 VGLGTaalggvYGDGLEQDE--AVAIVAEAFAAGINHFDTSPYYGAESSeavLGKALAAL----QVPRSSYTVATKVGry 88
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308422931 90 --NTF-HPPELVRPALEKTLQTLQLDYVD---LYIIELptafkpGDTFypkdengkhiyheTDLCATWEALEACKDAGLV 163
Cdd:cd19153 89 rdSEFdYSAERVRASVATSLERLHTTYLDvvyLHDIEF------VDYD-------------TLVDEALPALRTLKDEGVI 149
|
....*...
gi 1308422931 164 KSIGVSNF 171
Cdd:cd19153 150 KRIGIAGY 157
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