|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-308 |
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: 663.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 6 QKMELNDGHSIPVLGFGTYATEENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKL 85
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 WSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 166 SNFNRRQLEKILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPVLLDDPILCTMA 245
Cdd:cd19108 161 SNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEWVDQNSPVLLEDPVLCALA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709623 246 KKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFPA 308
Cdd:cd19108 241 KKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRYLPA 303
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-319 |
2.65e-161 |
|
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: 452.33 E-value: 2.65e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYA-TEENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHR 91
Cdd:cd19109 1 GNSIPIIGLGTYSePKTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 92 PELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 172 QLEKILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPVLLDDPILCTMAKKYKRT 251
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 252 PALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFPANMFKAHPNFPF 319
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
13-323 |
1.43e-129 |
|
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: 371.75 E-value: 1.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRP 92
Cdd:cd19107 1 GAKMPILGLGTWKSPPG---QVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 93 ELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19107 78 GLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 173 LEKILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDtPVLLDDPILCTMAKKYKRTP 252
Cdd:cd19107 158 IERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPED-PSLLEDPKIKEIAAKHNKTT 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709623 253 ALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFPANMFKAHPNFPFSDEY 323
Cdd:cd19107 237 AQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAEY 307
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-306 |
2.59e-128 |
|
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: 367.76 E-value: 2.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 7 KMELNDGHSIPVLGFGTYATEENlrKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLW 86
Cdd:cd19116 2 TIKLNDGNEIPAIALGTWKLKDD--EGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 87 STSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDEllpQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19116 80 NSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENND---SESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 167 NFNRRQLEKILNkpGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGtqRYKYCINEDTPVLLDDPILCTMAK 246
Cdd:cd19116 157 NFNSEQINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFG--RLVPRGQTNPPPRLDDPTLVAIAK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 247 KYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19116 233 KYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
10-306 |
3.89e-127 |
|
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: 365.55 E-value: 3.89e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKksmESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKI-EDGTVKREDIFYTSKLWST 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVK---AAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVgPGKAVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYcINEDTPVLLDDPILCTMAKKY 248
Cdd:cd19106 158 NSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPW-AKPDEPVLLEEPKVKALAKKY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19106 235 NKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
16-297 |
3.90e-119 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 342.92 E-value: 3.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTY-ATEENLRkksmESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIedgtVKREDIFYTSKLWSTSHRPEL 94
Cdd:cd19071 1 MPLIGLGTYkLKPEETA----EAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 95 VRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDellpqdehgnlilDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLE 174
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 175 KILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKycinedtpvLLDDPILCTMAKKYKRTPAL 254
Cdd:cd19071 140 ELLAAARIK--PAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP---------LLDDPVLKEIAKKYGKTPAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1709623 255 IALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19071 209 VLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-323 |
4.22e-115 |
|
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: 335.00 E-value: 4.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRPELV 95
Cdd:cd19110 4 IPAVGLGTWKASPG---EVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 96 RPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19110 81 KTACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 176 ILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQrykyciNEDTPvLLDDPILCTMAKKYKRTPALI 255
Cdd:cd19110 161 LLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGS------CEGVD-LIDDPVIQRIAKKHGKSPAQI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 256 ALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFPANMFKAHPNFPFSDEY 323
Cdd:cd19110 234 LIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIEY 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-307 |
6.38e-115 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 332.79 E-value: 6.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 12 DGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTSHR 91
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRT---ALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 92 PELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildtVDLCDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:COG0656 74 YDDTLAAFEESLERLGLDYLDLYLIHWPGP--------------------GPYVETWRALEELYEEGLIRAIGVSNFDPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 172 QLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYKRT 251
Cdd:COG0656 134 HLEELLAETGVK--PAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK-----------LLDDPVLAEIAEKHGKT 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 252 PALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFP 307
Cdd:COG0656 201 PAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERLGP 256
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-306 |
3.26e-113 |
|
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: 330.14 E-value: 3.26e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 9 ELNDGHSIPVLGFGTYATEENLRKKSMestKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWST 88
Cdd:cd19154 5 TLSNGVKMPLIGLGTWQSKGAEGITAV---RTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALG----TQRYKYCINEDTPVLLDDPILCTM 244
Cdd:cd19154 162 NNDQIQRILDNARVK--PHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgrANFTKSTGVSPAPNLLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709623 245 AKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
10-306 |
2.14e-112 |
|
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: 327.83 E-value: 2.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19123 6 LSNGDLIPALGLGTWKSKPG---EVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGdELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19123 83 HAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG-VGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGT-QRYKYCINEDTPVLLDDPILCTMAKKY 248
Cdd:cd19123 162 VKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSgDRPAAMKAEGEPVLLEDPVINKIAEKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19123 240 GASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-304 |
1.20e-105 |
|
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: 310.05 E-value: 1.20e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 9 ELNDGHSIPVLGFGTYATEENLRKKSMestKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWST 88
Cdd:cd19125 4 KLNTGAKIPAVGLGTWQADPGVVGNAV---KTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDellPQDEHGNLIldTVDLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19125 81 DHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVL--PPDIPSTWKAMEKLVDSGKVRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCinedTPVLLDDPILCTMAKKY 248
Cdd:cd19125 156 SVKKLEDLLAVARVP--PAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWV----KKNVLKDPIVTKVAEKL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLR 304
Cdd:cd19125 230 GKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRR 285
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
12-299 |
2.99e-95 |
|
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: 283.39 E-value: 2.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 12 DGHSIPVLGFGTYATEENlRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVK-REDIFYTSKLWSTSH 90
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS-PEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 91 RPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILdtvDLCDTWEAMEKCKDAGLAKSIGVSNFNR 170
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPF---DIKGVWEAMEECQRLGLTKAIGVSNFSC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 171 RQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYcineDTPVLLDDPILCTMAKKYKR 250
Cdd:cd19124 157 KKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKW----GSNAVMESDVLKEIAAAKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1709623 251 TPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19124 231 TVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-306 |
1.87e-92 |
|
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: 277.48 E-value: 1.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19155 6 FNNGEKMPVVGLGTWQSSPEEIETAVDT---ALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPV-SLKPGDELLPQDEHGNLILD-TVDLCDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19155 83 NRREKVEKFLLKSLEKLQLDYVDLYLIHFPVgSLSKEDDSGKLDPTGEHKQDyTTDLLDIWKAMEAQVDQGLTRSIGLSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 168 FNRRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQ-RYKY-----CINEDTPVLLDDPIL 241
Cdd:cd19155 163 FNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPgAAHFspgtgSPSGSSPDLLQDPVV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 242 CTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19155 241 KAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-306 |
6.83e-92 |
|
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: 275.15 E-value: 6.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTY-ATEENLRkksmESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHR 91
Cdd:cd19111 1 GFPMPVIGLGTYqSPPEEVR----AAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 92 PELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgdellPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPCGFV------NKKDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 172 QLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGT-QRYKYCINEDTPVLLDDPILCTMAKKYKR 250
Cdd:cd19111 151 QINKILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpGRANQSLWPDQPDLLEDPTVLAIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 251 TPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYF 306
Cdd:cd19111 229 TPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKYF 284
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
10-299 |
7.02e-92 |
|
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: 275.06 E-value: 7.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKKSMestKIAIDVGFRHIDCSHLYQNEEEIGQAIV-SKIEDGTVKREDIFYTSKLWST 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAV---KIALKAGYRHLDLAKVYQNQHEVGQALKeLLKEEPGVKREDLFITSKLWNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLP----QDEHGNLILDT-VDLCDTWEAMEKCKDAGLAKSI 163
Cdd:cd19118 78 SHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPltavPTNGGEVDLDLsVSLVDTWKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNKPGLkhRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinEDTPVLLDDPILCT 243
Cdd:cd19118 158 GVSNFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNL------AGLPLLVQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 244 MAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDfqLASDDMEILDNL 299
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
11-305 |
6.07e-90 |
|
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: 270.48 E-value: 6.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 11 NDGHSIPVLGFGTyATEENLRKKsmESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSH 90
Cdd:cd19129 1 NGSGAIPALGFGT-LIPDPSATR--NAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 91 RPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDT-VDLCDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGtqrykyciNEDTPVLLDDPILCTMAKKYK 249
Cdd:cd19129 158 LEKLREIFEAARIK--PAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLG--------HGMEPKLLEDPVITAIARRVN 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 250 RTPALIALRYQLERGIVTLVKSFNEERIRENlqvFDFQ-LASDDM-EILDNLDRNLRY 305
Cdd:cd19129 228 KTPAQVLLAWAIQRGTALLTTSKTPSRIREN---FDIStLPEDAMrEINEGIKTRYRF 282
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
16-297 |
3.01e-85 |
|
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: 256.81 E-value: 3.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYateENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTSHRPELV 95
Cdd:cd19073 1 IPALGLGTW---QLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAI----AESGVPREDLFITTKVWRDHLRPEDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 96 RPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK 175
Cdd:cd19073 74 KKSVDRSLEKLGTDYVDLLLIHWPNP-------------------TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 176 ILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYKRTPALI 255
Cdd:cd19073 135 ALDISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE-----------VLRDPVIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1709623 256 ALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
8-314 |
2.99e-84 |
|
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: 256.64 E-value: 2.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 8 MELNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWS 87
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILN---AIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 TSHrpELVRPSLENSLRKLNLDYVDLYLIHFPVSLK------PGDELlpqDEHGNLILD-TVDLCDTWEAMEKCKDAGLA 160
Cdd:cd19112 80 SDH--GHVIEACKDSLKKLQLDYLDLYLVHFPVATKhtgvgtTGSAL---GEDGVLDIDvTISLETTWHAMEKLVSAGLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 161 KSIGVSNFNRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALG-----TQRYKYCinedTPvl 235
Cdd:cd19112 155 RSIGISNYDIFLTRDCLAYSKIK--PAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaanAEWFGSV----SP-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 236 LDDPILCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRY-FPANMFKAH 314
Cdd:cd19112 227 LDDPVLKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTnQPAKFWGID 306
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-299 |
3.29e-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: 252.83 E-value: 3.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTYATEENLRKksmESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRPELVR 96
Cdd:cd19128 2 PRLGFGTYKITESESK---EAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 97 PSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQDEHGNLILDTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKI 176
Cdd:cd19128 79 EQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 177 LNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGtQRYKYcineDTPVLLDDPILCTMAKKYKRTPALIA 256
Cdd:cd19128 159 LNYCKIK--PFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLG-GSYGD----GNLTFLNDSELKALATKYNTTPPQVI 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1709623 257 LRYQLERGIVT---LVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19128 232 IAWHLQKWPKNysvIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
16-299 |
3.92e-83 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 251.78 E-value: 3.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYAT--EENLRKksmeSTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRPE 93
Cdd:cd19136 1 MPILGLGTFRLrgEEEVRQ----AVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 94 LVRPSLENSLRKLNLDYVDLYLIHFpvslkPGDELLPQDEHGNLILDTvdlcDTWEAMEKCKDAGLAKSIGVSNFNRRQL 173
Cdd:cd19136 77 KARAACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNAELRR----ESWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 174 EKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQrykycinedTPVLLDDPILCTMAKKYKRTPA 253
Cdd:cd19136 148 EELLKYCEVP--PAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG---------DLRLLEDPTVLAIAKKYGRTPA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1709623 254 LIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19136 217 QVLLRWALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-297 |
5.02e-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: 251.77 E-value: 5.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGT-----YATEENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLws 87
Cdd:cd19120 1 GSKIPAIAFGTgtawyKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEAL----KESGVPREDLFITTKV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 tSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDellpqdehgnlildtVDLCDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19120 75 -SPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGG---------------PTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 168 FNRRQLEKILNKPglKHRPVCNQVECHLYLN--QSKLLAYCKMNDIVLVAYGALGTQRYKycinEDTPVlldDPILCTMA 245
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRD----AGGPL---DPVLEKIA 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1709623 246 KKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19120 210 EKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-299 |
2.84e-82 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 250.49 E-value: 2.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 3 SKIQKmeLNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYT 82
Cdd:cd19117 3 SKTFK--LNTGAEIPAVGLGTWQSKPNEVAKAVEA---ALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 83 SKLWSTSHRPelVRPSLENSLRKLNLDYVDLYLIHFPVSLKP-GDELLPQDEHGNLILDT-VDLCDTWEAMEKCKDAGLA 160
Cdd:cd19117 74 TKLWCTWHRR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPdGNDFLFKKDDGTKDHEPdWDFIKTWELMQKLPATGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 161 KSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQrykycineDTPvLLDDPI 240
Cdd:cd19117 152 KAIGVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGST--------NAP-LLKEPV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709623 241 LCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVfdFQLASDDMEILDNL 299
Cdd:cd19117 223 IIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-300 |
6.00e-82 |
|
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: 248.83 E-value: 6.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19131 4 LNDGNTIPQLGLGVWQVSND---EAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVslkPGdellpQDEHgnlildtvdlCDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19131 77 QGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PA-----QDKY----------VETWKALIELKKEGRVKSIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYK 249
Cdd:cd19131 139 IEHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-----------LLSDPVIGEIAEKHG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1709623 250 RTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:cd19131 206 KTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-307 |
1.08e-80 |
|
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: 245.76 E-value: 1.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 9 ELNDGHSIPVLGFGTYATEENlrKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWST 88
Cdd:cd19157 3 TLNNGVKMPWLGLGVFKVEEG--SEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgdellpqdehgnlildtvdLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGK--------------------YKETWKALEKLYKDGRVRAIGVSNF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKY 248
Cdd:cd19157 137 QVHHLEDLLADAEIV--PMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-----------LLDNPVLKEIAEKY 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFP 307
Cdd:cd19157 204 NKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRVGP 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
10-305 |
2.94e-80 |
|
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: 246.20 E-value: 2.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEenlRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19113 5 LNSGYKMPSVGFGCWKLD---NATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLK--PGDELLPQD----EHGNLILDTVDLCDTWEAMEKCKDAGLAKSI 163
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvPIEEKYPPGfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNkpGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINE---DTPVLLDDPI 240
Cdd:cd19113 162 GVSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQGralNTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 241 LCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRY 305
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRF 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
13-299 |
4.92e-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: 243.71 E-value: 4.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYateeNLR-KKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTSHR 91
Cdd:cd19140 5 GVRIPALGLGTY----PLTgEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAI----AASGVPRDELFLTTKVWPDNYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 92 PELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRR 171
Cdd:cd19140 77 PDDFLASVEESLRKLRTDYVDLLLLHWPNK-------------------DVPLAETLGALNEAQEAGLARHIGVSNFTVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 172 QLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYKRT 251
Cdd:cd19140 138 LLREAVELSEAP--LFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGE-----------VLKDPVLQEIGRKHGKT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1709623 252 PALIALRYQLER-GIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19140 205 PAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-300 |
1.02e-79 |
|
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: 242.87 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYatEENLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19133 3 LNNGVEMPILGFGVF--QIPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqDEHGnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------DVYG-----------AWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILnkPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGtqrykycinEDTPVLLDDPILCTMAKKYK 249
Cdd:cd19133 136 PDRLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFA---------EGRNNLFENPVLTEIAEKYG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1709623 250 RTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:cd19133 205 KSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-301 |
7.29e-79 |
|
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: 241.02 E-value: 7.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVA---ALQAGYRLLDTAFNYENEGAVGEAV----RRSGVPREELFVTTKLPGRH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgdelLPqdehgnlildTVDL-CDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19132 74 HGYEEALRTIEESLYRLGLDYVDLYLIHWP---------NP----------SRDLyVEAWQALIEAREEGLVRSIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTqrykyciNEDtpvLLDDPILCTMAKKY 248
Cdd:cd19132 135 LPEHLDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGR-------GSG---LLDEPVIKAIAEKH 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDR 301
Cdd:cd19132 203 GKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
8-300 |
1.58e-78 |
|
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: 240.03 E-value: 1.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 8 MELNDGHSIPVLGFGTYATEENlrKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSkiedGTVKREDIFYTSKLWS 87
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDG--DETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRE----SGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 TSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgdellpqdehgnlildtvdLCDTWEAMEKCKDAGLAKSIGVSN 167
Cdd:cd19126 75 DDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK--------------------FIDTWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 168 FNRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKK 247
Cdd:cd19126 135 FQEHHLEELLAHADVV--PAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-----------LLSNPVLAAIGEK 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1709623 248 YKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:cd19126 202 YGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
6-305 |
3.06e-78 |
|
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: 241.17 E-value: 3.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 6 QKMELNDGHSIPVLGFGTYATEenlrkKSMESTKI--AIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTS 83
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGLWKVN-----NDTCADQVynAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 84 KLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLK---PGDELLP--QDEHGNLILDTVDLCDTWEAMEKCKDAG 158
Cdd:cd19115 78 KLWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 159 LAKSIGVSNFNRRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCIN---EDTPVL 235
Cdd:cd19115 158 LARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDLpgaKDTPPL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 236 LDDPILCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRY 305
Cdd:cd19115 236 FEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRF 305
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-299 |
4.55e-77 |
|
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: 237.04 E-value: 4.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIVSKIeDGTVKREDIFYTSKLWSTS 89
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAH---ALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 H-RPELvrpSLENSLRKLNLDYVDLYLIHFPVSLKP--GDELLPQDEHGNLILD-TVDLCDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19121 82 HrRVEL---CLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTLPDGSRDLDwDWNHVDTWKQMEKVLKTGKTKAIGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 166 SNFNRRQLEKILnkPGLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQrykycineDTPVLLDDPILcTMA 245
Cdd:cd19121 159 SNYSIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGST--------GSPLISDEPVV-EIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1709623 246 KKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQlaSDDMEILDNL 299
Cdd:cd19121 228 KKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-299 |
1.67e-74 |
|
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: 229.90 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 4 KIQKMELNDGHSIPVLGFGTyateENLRKKSMESTKIAI-DVGFRHIDCSHLYQNEEEIGQAIVskiEDGtVKREDIFYT 82
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGT----SHSGGYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAIK---ESG-VPREDLFLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 83 SKLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGD---ELLPqdehgnlildtvdlcDTWEAMEKCKDAGL 159
Cdd:cd19135 73 TKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKnvkETRA---------------ETWRALEELYDEGL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 160 AKSIGVSNFNRRQLEKILNKPGLkhRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYkycinedtpvlLDDP 239
Cdd:cd19135 138 CRAIGVSNFLIEHLEQLLEDCSV--VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKA-----------LEEP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 240 ILCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19135 205 TVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-307 |
1.76e-72 |
|
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: 225.09 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 9 ELNDGHSIPVLGFGTYATEENlrKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKiedgTVKREDIFYTSKLWST 88
Cdd:cd19156 2 KLANGVEMPRLGLGVWRVQDG--AEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgdellpqdehgnlildtvdLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19156 76 DQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKpgLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKY 248
Cdd:cd19156 136 HEHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK-----------LLSNPVLKAIGKKY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFP 307
Cdd:cd19156 203 GKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRYGP 261
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-300 |
1.44e-71 |
|
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: 222.67 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPE---ETADAVATALADGYRLIDTAAAYGNEREVGEGI----RRSGVDRSDIFVTTKLWISD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgNLILDTVDlcdTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19127 76 YGYDKALRGFDASLRRLGLDYVDLYLLHWPVP--------------NDFDRTIQ---AYKALEKLLAEGRVRAIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALG-TQRYKYCINEDTPVLLDDPILCTMAKKY 248
Cdd:cd19127 139 PEHLERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgVMRYGASGPTGPGDVLQDPTITGLAEKY 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:cd19127 217 GKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
13-305 |
3.56e-70 |
|
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: 220.12 E-value: 3.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYATEENlrkKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTSHRP 92
Cdd:cd19114 1 GDKMPLVGFGTAKIKAN---ETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 93 ELVRPSLENSLRKLNLDYVDLYLIHFPVSLK---PGDELLPQDEHGNLI---LDTVDLCDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKkfpLEQSPMQECWREMEKLVDAGLVRNIGIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 167 NFNRRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINED---TPvLLDDPILCT 243
Cdd:cd19114 158 NFNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLkhfTN-LLEHPVVKK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709623 244 MAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRY 305
Cdd:cd19114 235 LADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-300 |
2.28e-66 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 209.00 E-value: 2.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEEnlrKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAI-VSKIedgtvKREDIFYTSKLWST 88
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPP---ADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIaASGI-----PRDELFVTTKLWND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgdellpqdehGNLIldtvdlcDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19130 76 RHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTPAA-----------GNYV-------HTWEAMIELRAAGRTRSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKY 248
Cdd:cd19130 138 LPPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-----------LLGDPPVGAIAAAH 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1709623 249 KRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:cd19130 205 GKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
10-301 |
2.91e-66 |
|
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: 210.05 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENlRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKIEDGTVKREDIFYTSKLWSTS 89
Cdd:cd19119 6 LNTGASIPALGLGTASPHED-RAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPelVRPSLENSLRKLNLDYVDLYLIHFPVSLK-----PGDELLPQDEHGNLIL-DTVDLCDTWEAMEKCKDAGLAKSI 163
Cdd:cd19119 85 YDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYaASGDHITTYKQLEKIYLDGRAKAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNKpgLKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKycinedtpvLLDDPILCT 243
Cdd:cd19119 163 GVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP---------NLKNPLVKK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 244 MAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVfdFQLASDDMEILDNLDR 301
Cdd:cd19119 232 IAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDDIGE 287
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
16-299 |
5.15e-65 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 205.28 E-value: 5.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYateenlRKKS---MESTKIAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWSTSHRP 92
Cdd:cd19139 1 IPAFGLGTF------RLKDdvvIDSVRTALELGYRHIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIDNLSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 93 ELVRPSLENSLRKLNLDYVDLYLIHFPVslkpgdellPQDEhgnlildtVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQ 172
Cdd:cd19139 71 DKLLPSLEESLEKLRTDYVDLTLIHWPS---------PNDE--------VPVEEYIGALAEAKEQGLTRHIGVSNFTIAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 173 LEKILNKPGlKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYKRTP 252
Cdd:cd19139 134 LDEAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGK-----------VLDDPVLAAIAERHGATP 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1709623 253 ALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNL 299
Cdd:cd19139 202 AQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
10-294 |
2.91e-64 |
|
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: 204.78 E-value: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEeNLRKKSMESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVSKI-EDGTVKREDIFYTSKLWST 88
Cdd:cd19122 3 LNNGVKIPAVGFGTFANE-GAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLkENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQ-DEHGNLILDTvDLCD----TWEAMEKCKDAGLAKSI 163
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDQRSPKlGPDGKYVILK-DLTEnpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNKPglKHRPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPvllDDPILCT 243
Cdd:cd19122 161 GVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS---ENPTLNE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1709623 244 MAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDfqLASDDME 294
Cdd:cd19122 236 VAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFE 284
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
10-307 |
5.29e-64 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 203.38 E-value: 5.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTY-ATEENLRKKSMEstkiAIDVGFRHIDCSHLYQNEEEIGQAIvskiEDGTVKREDIFYTSKLWST 88
Cdd:PRK11565 9 LQDGNVMPQLGLGVWqASNEEVITAIHK----ALEVGYRSIDTAAIYKNEEGVGKAL----KEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPelVRPSLENSLRKLNLDYVDLYLIHFPVslkpgdellPQDEHgnlildtvdLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:PRK11565 81 DHKR--PREALEESLKKLQLDYVDLYLMHWPV---------PAIDH---------YVEAWKGMIELQKEGLIKSIGVCNF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVL-----VAYGALGtqrykycinedtpvLLDDPILCT 243
Cdd:PRK11565 141 QIHHLQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTeswspLAQGGKG--------------VFDQKVIRD 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709623 244 MAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRYFP 307
Cdd:PRK11565 205 LADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQGKRLGP 268
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-305 |
1.38e-63 |
|
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: 202.01 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEENLRKKSMEStkiAIDVGFRHIDCSHLYQNEEEIGQAIVSKiedgTVKREDIFYTSKLWSTS 89
Cdd:cd19134 5 LNDDNTMPVIGLGVGELSDDEAERSVSA---ALEAGYRLIDTAAAYGNEAAVGRAIAAS----GIPRGELFVTTKLATPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlilDTVDLCDTWEAMEKCKDAGLAKSIGVSNFN 169
Cdd:cd19134 78 QGFTASQAACRASLERLGLDYVDLYLIHWPAG------------------REGKYVDSWGGLMKLREEGLARSIGVSNFT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 170 RRQLEKILNKPGLKhrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYK 249
Cdd:cd19134 140 AEHLENLIDLTFFT--PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGR-----------LLDNPAVTAIAAAHG 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 250 RTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLRY 305
Cdd:cd19134 207 RTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
13-297 |
1.54e-63 |
|
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: 202.07 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYATEENL------RKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVskiedgTVKREDIFYTS 83
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdysdDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 84 KLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVslkpgdellpqdehgnlilDTVDLCDTWEAMEKCKDAGLAKSI 163
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNKPGlKHRPVCNQVECHLYLN--QSKLLAYCKMNDIVLVAYGALgtQRYKYCINEDTPVLLDdpil 241
Cdd:cd19072 136 GVSNFSLEELEEAQSYLK-KGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPL--EKGKLSNAKGSPLLDE---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1709623 242 ctMAKKYKRTPALIALRYQLER-GIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19072 209 --IAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
19-300 |
1.58e-62 |
|
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: 200.23 E-value: 1.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 19 LGFGTYATEENLRKKSMEST----KIAIDVGFRHIDCSHLY---QNEEEIGQAIVSKiedgTVKREDIFYTSKL------ 85
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEAlealRAALEAGINFIDTAEVYgdgKSEELLGEALKDY----PVKRDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 WSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgdellpqDEhgnlildTVDLCDTWEAMEKCKDAGLAKSIGV 165
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWP------------DP-------DTPIEETWDALEELKKEGKIRAIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 166 SNFNRRQLEKILNKPglKHRPVCNQVECHLY--LNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPV--------- 234
Cdd:pfam00248 138 SNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKgpgerrrll 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 235 -------LLDDPILCTMAKKYKRTPALIALRY--QLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLD 300
Cdd:pfam00248 216 kkgtplnLEALEALEEIAKEHGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
14-304 |
1.09e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 179.45 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 14 HSIPVLGFGTYateenlRKKS---MESTKIAIDVGFRHIDCSHLYQNEEEIGQAIVskiEDGtVKREDIFYTSKLWSTSH 90
Cdd:PRK11172 1 MSIPAFGLGTF------RLKDqvvIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKIWIDNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 91 RPELVRPSLENSLRKLNLDYVDLYLIHFPvslKPGDEllpqdehgnlildtVDLCDTWEAMEKCKDAGLAKSIGVSNFNR 170
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWP---SPNDE--------------VSVEEFMQALLEAKKQGLTREIGISNFTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 171 RQLEKILNKPGLKHrPVCNQVECHLYLNQSKLLAYCKMNDIVLVAYGALGTQRykycinedtpvLLDDPILCTMAKKYKR 250
Cdd:PRK11172 134 ALMKQAIAAVGAEN-IATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGK-----------VLKDPVIARIAAKHNA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1709623 251 TPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILDNLDRNLR 304
Cdd:PRK11172 202 TPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-297 |
8.32e-50 |
|
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: 166.59 E-value: 8.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGT-----YATEENLRKKSM-ESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIVSkiedgtVKREDIFYTS 83
Cdd:cd19137 1 GEKIPALGLGTwgiggFLTPDYSRDEEMvELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 84 KLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDEllpqdehgnlildtvdlcdTWEAMEKCKDAGLAKSI 163
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEE-------------------TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 164 GVSNFNRRQLEKILNKpgLKHRPVCNQVECHLY---LNQSKLLAYCKMNDIVLVAYGALgtqrykycineDTPVLLDDPI 240
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-----------RRGLEKTNRT 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1709623 241 LCTMAKKYKRTPALIALRYQLER-GIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19137 203 LEEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
10-297 |
6.05e-48 |
|
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: 161.65 E-value: 6.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 10 LNDGHSIPVLGFGTYATEEN--LRKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvkREDIFYTSK 84
Cdd:cd19138 5 LPDGTKVPALGQGTWYMGEDpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 LWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildtVDLCDTWEAMEKCKDAGLAKSIG 164
Cdd:cd19138 78 VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG--------------------VPLAETVAAMEELKKEGKIRAWG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 165 VSNFNRRQLEKILNKPGLKHrPVCNQVECHLylnQSK-----LLAYCKMNDIVLVAYGALGTQRykycinEDTPVLLDDP 239
Cdd:cd19138 138 VSNFDTDDMEELWAVPGGGN-CAANQVLYNL---GSRgieydLLPWCREHGVPVMAYSPLAQGG------LLRRGLLENP 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1709623 240 ILCTMAKKYKRTPALIALRYQLERGIVTLV-KSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19138 208 TLKEIAARHGATPAQVALAWVLRDGNVIAIpKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
16-297 |
2.11e-41 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 145.45 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGT--------YATEENLRKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIvskieDGTVKREDIFYTSK 84
Cdd:cd19093 2 VSPLGLGTwqwgdrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFL-----KELGDRDEVVIATK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 LWSTSHR--PELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLpqdehgnlildtvdlcdtWEAMEKCKDAGLAKS 162
Cdd:cd19093 77 FAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 163 IGVSNFNRRQLEKILNKpgLKHR---PVCNQVECHL---YLNQSKLLAYCKMNDIVLVAYGALG----TQRYK------- 225
Cdd:cd19093 139 VGVSNYSADQLRRAHKA--LKERgvpLASNQVEYSLlyrDPEQNGLLPACDELGITLIAYSPLAqgllTGKYSpenpppg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709623 226 --YCINEDTPVLLDDPILCTM---AKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19093 217 grRRLFGRKNLEKVQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
16-303 |
6.19e-39 |
|
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: 138.87 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGT------YATEENLRKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvkREDIFYTSKLW 86
Cdd:cd19085 1 VSRLGLGCwqfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 87 STSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildTVDLCDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS-------------------DVPLEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 167 NFNRRQLEKILnKPGlkhRPVCNQVECHLyLNQSK---LLAYCKMNDIVLVAYGAL------GtqryKYCINEDTP---- 233
Cdd:cd19085 135 NFGPAQLEEAL-DAG---RIDSNQLPYNL-LWRAIeyeILPFCREHGIGVLAYSPLaqglltG----KFSSAEDFPpgda 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 234 ----VLLDDPI-----------LCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDFQLASDDMEIL 296
Cdd:cd19085 206 rtrlFRHFEPGaeeetfealekLKEIADELGVTMAQLALAWVLQQPGVTsvIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
....*..
gi 1709623 297 DNLDRNL 303
Cdd:cd19085 286 DEISDPL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
11-299 |
3.57e-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: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 11 NDGHSIPVLGFGT-------YATEENlrkksmESTKI---AIDVGFRHIDCSHLY---QNEEEIGQAIvskiedGTVKRE 77
Cdd:COG0667 8 RSGLKVSRLGLGTmtfggpwGGVDEA------EAIAIldaALDAGINFFDTADVYgpgRSEELLGEAL------KGRPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 78 DIFYTSKL--------WSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgdellpqDehgnlilDTVDLCDTWE 149
Cdd:COG0667 76 DVVIATKVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP------------D-------PDTPIEETLG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 150 AMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHLyLNQS---KLLAYCKMNDIVLVAYGALG----TQ 222
Cdd:COG0667 137 ALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSL-LDRSaeeELLPAARELGVGVLAYSPLAggllTG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 223 RYK----------YCINEDTPVLLDDPI-----LCTMAKKYKRTPALIALRYQLERGIVTLV----KSfnEERIRENLQV 283
Cdd:COG0667 216 KYRrgatfpegdrAATNFVQGYLTERNLalvdaLRAIAAEHGVTPAQLALAWLLAQPGVTSVipgaRS--PEQLEENLAA 293
|
330
....*....|....*.
gi 1709623 284 FDFQLASDDMEILDNL 299
Cdd:COG0667 294 ADLELSAEDLAALDAA 309
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
13-297 |
1.47e-37 |
|
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: 135.35 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYA--------TEEnlrKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvkREDIFY 81
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwwgeVDD---QESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 82 TSK---LWSTSH------RPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPqdehgnlildtvdLCDTWEAME 152
Cdd:cd19084 71 ATKcglRWDGGKgvtkdlSPESIRKEVEQSLRRLQTDYIDLYQIHWP------DPNTP-------------IEETAEALE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 153 KCKDAGLAKSIGVSNFNRRQLEKIlnkpgLKHRP-VCNQVECHLyLNQ---SKLLAYCKMNDIVLVAYGALG----TQRY 224
Cdd:cd19084 132 KLKKEGKIRYIGVSNFSVEQLEEA-----RKYGPiVSLQPPYSM-LEReieEELLPYCRENGIGVLPYGPLAqgllTGKY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 225 KYCIN-EDTPVLLDDP---------------ILCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDF 286
Cdd:cd19084 206 KKEPTfPPDDRRSRFPffrgenfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQPGVTsaIVGAKNPEQLEENAGALDW 285
|
330
....*....|.
gi 1709623 287 QLASDDMEILD 297
Cdd:cd19084 286 ELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-282 |
1.06e-31 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 118.39 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTYA-TEENLRKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIVSKiedgtVKREDIFYTSK-----LWS 87
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKgghppGGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 TSHR---PELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIG 164
Cdd:cd06660 76 PSRSrlsPEHIRRDLEESLRRLGTDYIDLYYLHRD------DPSTPVEE-------------TLEALNELVREGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 165 VSNFNRRQLEKILN--KPGLKHRPVCNQVECHLYLNQ---SKLLAYCKMNDIVLVAYGALGtqrykycinedtpvllddp 239
Cdd:cd06660 137 VSNWSAERLAEALAyaKAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLA------------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1709623 240 ilctmakkykRTPALIALRYQLERGIVT--LVKSFNEERIRENLQ 282
Cdd:cd06660 198 ----------RGPAQLALAWLLSQPFVTvpIVGARSPEQLEENLA 232
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
41-288 |
2.31e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 105.62 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVG---FRHIDCSHLYQNEEEIGQA------------IVSK--IE------DGTVKREDifytsklWSTSHrpelVRP 97
Cdd:COG4989 40 ALELGittFDHADIYGGYTCEALFGEAlklspslrekieLQTKcgIRlpsearDNRVKHYD-------TSKEH----IIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 98 SLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFNRRQLEkIL 177
Cdd:COG4989 109 SVEGSLRRLGTDYLDLLLLHRP------DPLMDPEE-------------VAEAFDELKASGKVRHFGVSNFTPSQFE-LL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 178 NKpGLKHRPVCNQVECHLyLNQSKL----LAYCKMNDIVLVAYGALGTQRYKYCINEDTPVLLDdpILCTMAKKYKRTPA 253
Cdd:COG4989 169 QS-ALDQPLVTNQIELSL-LHTDAFddgtLDYCQLNGITPMAWSPLAGGRLFGGFDEQFPRLRA--ALDELAEKYGVSPE 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 1709623 254 LIALRYqLER---GIVTLVKSFNEERIRENLQVFDFQL 288
Cdd:COG4989 245 AIALAW-LLRhpaGIQPVIGTTNPERIKAAAAALDIEL 281
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
19-299 |
1.61e-25 |
|
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: 103.65 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 19 LGFGTYATE-ENLRKKSMEST-----KIAIDVGFRHIDCSHLY---QNEEEIGQAIVSKiedgtvKREDIFYTSK---LW 86
Cdd:cd19083 14 IGLGTNAVGgHNLYPNLDEEEgkdlvREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKgahKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 87 ST-----SHRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEHGNlildtvdlcdtweAMEKCKDAGLAK 161
Cdd:cd19083 88 GGdgsvlNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFP------DGETPKAEAVG-------------ALQELKDEGKIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 162 SIGVSNFNRRQLeKILNKPGLkhrpvCNQVE-CHLYLNQ---SKLLAYCKMNDIVLVAYGAL--GTQRYKYciNEDTpVL 235
Cdd:cd19083 149 AIGVSNFSLEQL-KEANKDGY-----VDVLQgEYNLLQReaeEDILPYCVENNISFIPYFPLasGLLAGKY--TKDT-KF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 236 LDDPI---------------------LCTMAKKYKRTPALIALRYQLERGIVTLV--KSFNEERIRENLQVFDFQLASDD 292
Cdd:cd19083 220 PDNDLrndkplfkgerfsenldkvdkLKSIADEKGVTVAHLALAWYLTRPAIDVVipGAKRAEQVIDNLKALDVTLTEEE 299
|
....*..
gi 1709623 293 MEILDNL 299
Cdd:cd19083 300 IAFIDAL 306
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
41-288 |
1.20e-24 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 100.71 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgTVKREDIFYTSK----------LWSTSH---RPELVRPSLENSLR 104
Cdd:cd19092 33 ALELGITTFDHADIYGGgkcEELFGEALALN----PGLREKIEIQTKcgirlgddprPGRIKHydtSKEHILASVEGSLK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 105 KLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFNRRQLEkILNKpGLKH 184
Cdd:cd19092 109 RLGTDYLDLLLLHRP------DPLMDPEE-------------VAEAFDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLDQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 185 RPVCNQVEC---HLYLNQSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTPVLLDdpILCTMAKKYKRTPALIALRYqL 261
Cdd:cd19092 168 PLVTNQIELsllHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFDERFQRLRA--ALEELAEEYGVTIEAIALAW-L 244
|
250 260 270
....*....|....*....|....*....|
gi 1709623 262 ER---GIVTLVKSFNEERIRENLQVFDFQL 288
Cdd:cd19092 245 LRhpaRIQPILGTTNPERIRSAVKALDIEL 274
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-299 |
2.09e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 100.44 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYA-----------TEENlrKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIvskiedgTVKREDIFY 81
Cdd:cd19102 1 LTTIGLGTWAiggggwgggwgPQDD--RDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRAL-------KGLRDRPIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 82 TSK---LW------STSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellpqdehgnlildTVDLCDTWEAME 152
Cdd:cd19102 72 ATKcglLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-------------------DEPIEEAWGALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 153 KCKDAGLAKSIGVSNFNRRQLEKIL-------NKPG--LKHRPVcnqvechlylnQSKLLAYCKMNDIVLVAY------- 216
Cdd:cd19102 133 ELKEEGKVRAIGVSNFSVDQMKRCQaihpiasLQPPysLLRRGI-----------EAEILPFCAEHGIGVIVYspmqsgl 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 217 --GALGTQRYKYCINEDTPV---------------LLDdpILCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERI 277
Cdd:cd19102 202 ltGKMTPERVASLPADDWRRrspffqepnlarnlaLVD--ALRPIAERHGRTVAQLAIAWVLRRPEVTsaIVGARRPDQI 279
|
330 340
....*....|....*....|..
gi 1709623 278 RENLQVFDFQLASDDMEILDNL 299
Cdd:cd19102 280 DETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-180 |
4.57e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 97.94 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYAteeNLRKKSMESTKI---AIDVGFRHIDCSHLYQN-EEEIGQAIVSKiedgtvkREDIFYTSKLWST 88
Cdd:cd19100 8 GLKVSRLGFGGGP---LGRLSQEEAAAIirrALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 ShrPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKpgDELLPQDEHGnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19100 78 D--YEGAKRDLERSLKRLGTDYIDLYQLHAVDTEE--DLDQVFGPGG-----------ALEALLEAKEEGKIRFIGISGH 142
|
170
....*....|..
gi 1709623 169 NRRQLEKILNKP 180
Cdd:cd19100 143 SPEVLLRALETG 154
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
13-304 |
7.58e-23 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 97.20 E-value: 7.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTyateENLRKKSMEST----KIAIDVGFRHIDCSHLYQNEEE-IGQAIvSKIedgtvkREDIFYTSKLWS 87
Cdd:COG1453 10 GLEVSVLGFGG----MRLPRKDEEEAealiRRAIDNGINYIDTARGYGDSEEfLGKAL-KGP------RDKVILATKLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 TSHRPELVRPSLENSLRKLNLDYVDLYLIHFpvslkpgdelLPQDEHGNLILDTVDLcdtWEAMEKCKDAGLAKSIGVSN 167
Cdd:COG1453 79 WVRDPEDMRKDLEESLKRLQTDYIDLYLIHG----------LNTEEDLEKVLKPGGA---LEALEKAKAEGKIRHIGFST 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 168 FNRRQ-LEKILNKpglkhrpvcNQVE---CHL-YLNQS-----KLLAYCKMNDIVLVAYGALGTQRykycINEDTPVLLD 237
Cdd:COG1453 146 HGSLEvIKEAIDT---------GDFDfvqLQYnYLDQDnqageEALEAAAEKGIGVIIMKPLKGGR----LANPPEKLVE 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709623 238 dpILCTmakkyKRTPALIALRYQLERGIVTLVKS--FNEERIRENLQVFD--FQLASDDMEILDNLDRNLR 304
Cdd:COG1453 213 --LLCP-----PLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
16-288 |
4.76e-21 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 90.35 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGT-------YATEENLRKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQA---------IVSKIedGTVKR 76
Cdd:cd19088 1 VSRLGYGAmrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEAlhpypddvvIATKG--GLVRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 77 EDifytsKLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgdellpqDehgnlilDTVDLCDTWEAMEKCKD 156
Cdd:cd19088 79 GP-----GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI------------D-------PKVPFEEQLGALAELQD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 157 AGLAKSIGVSNFNRRQLEKILNKPGLkhrpVCNQVECHLYLNQS-KLLAYCKMNDIVLVAYGALGTQrykycinedtPVL 235
Cdd:cd19088 135 EGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDDeGVLDYCEAAGIAFIPWFPLGGG----------DLA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 236 LDDPILCTMAKKYKRTPALIALRYQLERG--IVTLVKSFNEERIRENLQVFDFQL 288
Cdd:cd19088 201 QPGGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRL 255
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
20-297 |
9.27e-21 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 90.44 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 20 GFGTYA--------TEEnlrKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIVskiedGTVKREDIFYTSKL--- 85
Cdd:cd19148 8 ALGTWAiggwmwggTDE---KEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVgle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 WSTSH------RPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGL 159
Cdd:cd19148 80 WDEGGevvrnsSPARIRKEVEDSLRRLQTDYIDLYQVHWP------DPLVPIEE-------------TAEALKELLDEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 160 AKSIGVSNFNRRQLEkILNKPGLKH--RPVCNQVECHLylnQSKLLAYCKMNDIVLVAYGALgtqrykyC-------INE 230
Cdd:cd19148 141 IRAIGVSNFSPEQME-TFRKVAPLHtvQPPYNLFEREI---EKDVLPYARKHNIVTLAYGAL-------CrgllsgkMTK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 231 DTPVLLDD-----PI---------------LCTMAKK-YKRTPALIALRYQLERGIVTLV--KSFNEERIRENLQVFDFQ 287
Cdd:cd19148 210 DTKFEGDDlrrtdPKfqeprfsqylaaveeLDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWS 289
|
330
....*....|
gi 1709623 288 LASDDMEILD 297
Cdd:cd19148 290 LNDEDMKEID 299
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-169 |
1.85e-20 |
|
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: 88.83 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTYATEENLRKKSMESTKI----AIDVGFRHIDCSHLYQNEEE-IGQAIvskiedGTVKREDIFYTSKLWSTS-- 89
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAARllntALDLGINLIDTAPAYGRSEErLGRAL------AGLRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 ------HRPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLpqdehgnlildtvdlcdtwEAMEKCKDAGLAKSI 163
Cdd:cd19095 75 grdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVL-------------------ETLEDLKAAGKVRYI 135
|
....*.
gi 1709623 164 GVSNFN 169
Cdd:cd19095 136 GVSGDG 141
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
17-285 |
4.55e-20 |
|
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: 87.62 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTY-ATEENLRKKSMESTK--I--AIDVGFRHIDCSHLY---QNEEEIGQAIVskiedgTVKREDIFYTSKL-WS 87
Cdd:cd19096 1 SVLGFGTMrLPESDDDSIDEEKAIemIryAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 88 TSHRPELVRPSLENSLRKLNLDYVDLYLIHFPVSlkpgDELLPQDEHGNLildtvdlcdtWEAMEKCKDAGLAKSIGVSn 167
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS----PEWLEKARKGGL----------LEFLEKAKKEGLIRHIGFS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 168 F--NRRQLEKILNkpglkhrpvCNQVEC---HL-YLNQ-----SKLLAYCKMNDIVLVAYGALGTQRykycINEDTPVLL 236
Cdd:cd19096 140 FhdSPELLKEILD---------SYDFDFvqlQYnYLDQenqagRPGIEYAAKKGMGVIIMEPLKGGG----LANNPPEAL 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1709623 237 DdpILCtmakKYKRTPALIALRYQLERGIVTLVKS--FNEERIRENLQVFD 285
Cdd:cd19096 207 A--ILC----GAPLSPAEWALRFLLSHPEVTTVLSgmSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-283 |
2.33e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 85.71 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYATeenlrkkSMESTKI---AIDVGFRHIDCSHLYQN---EEEIGQAIvskiedGTVKREDIFYTSK-- 84
Cdd:cd19105 10 GLKVSRLGFGGGGL-------PRESPELlrrALDLGINYFDTAEGYGNgnsEEIIGEAL------KGLRRDKVFLATKas 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 LWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHfpvSLKPGDELLpqdEHGNLIldtvdlcdtwEAMEKCKDAGLAKSIG 164
Cdd:cd19105 77 PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLH---GVDTPEERL---LNEELL----------EALEKLKKEGKVRFIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 165 VS--NFNRRQLEKILNKPGLKhrpVCnQVeCHLYLNQS----KLLAYCKMNDIVLVAYgalGTQRYKYCINEDTPVLLdd 238
Cdd:cd19105 141 FSthDNMAEVLQAAIESGWFD---VI-MV-AYNFLNQPaeleEALAAAAEKGIGVVAM---KTLAGGYLQPALLSVLK-- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1709623 239 pilctmAKKYKRTPAliALRYQL-ERGIVTLVKSF-NEERIRENLQV 283
Cdd:cd19105 211 ------AKGFSLPQA--ALKWVLsNPRVDTVVPGMrNFAELEENLAA 249
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-297 |
1.51e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 84.18 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 31 RKKSMESTKIAIDVGFRHIDCSHLYQNEEEI-GQAIVSKIEDGTVKREDIFYT------SKLWSTshrPELVRPSLENSL 103
Cdd:cd19101 22 EDAAVRAMAAYVDAGLTTFDCADIYGPAEELiGEFRKRLRRERDAADDVQIHTkwvpdpGELTMT---RAYVEAAIDRSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 104 RKLNLDYVDLYLIHFpvslkpgdellpQDEHGNLILDTVdlcdtwEAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGlk 183
Cdd:cd19101 99 KRLGVDRLDLVQFHW------------WDYSDPGYLDAA------KHLAELQEEGKIRHLGLTNFDTERLREILDAGV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 184 hRPVCNQVECHLyLNQ---SKLLAYCKMNDIVLVAYGALG----TQRYkYCINEDTPVLLDDPILC-------------- 242
Cdd:cd19101 159 -PIVSNQVQYSL-LDRrpeNGMAALCEDHGIKLLAYGTLAggllSEKY-LGVPEPTGPALETRSLQkyklmidewggwdl 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 243 ---------TMAKKYKRTPALIALRYQLERGIV--TLVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19101 236 fqellrtlkAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
13-291 |
4.15e-18 |
|
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: 83.02 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYAT--EENLRKKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIvskiedGTVKREDIFYTSKL-W 86
Cdd:cd19074 1 GLKVSELSLGTWLTfgGQVDDEDAKACVRKAYDLGINFFDTADVYaagQAEEVLGKAL------KGWPRESYVISTKVfW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 87 STSHRPE---LVRP----SLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGL 159
Cdd:cd19074 75 PTGPGPNdrgLSRKhifeSIHASLKRLQLDYVDIYYCHRY------DPETPLEE-------------TVRAMDDLIRQGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 160 AKSIGVSNFNRRQLEKILN--KPGLKHRPVCNQVECHLyLNQSK---LLAYCKMNDIVLVAYGALG----TQRYKYCINE 230
Cdd:cd19074 136 ILYWGTSEWSAEQIAEAHDlaRQFGLIPPVVEQPQYNM-LWREIeeeVIPLCEKNGIGLVVWSPLAqgllTGKYRDGIPP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 231 D-----TPVLLDDPI--------------LCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDFQLA 289
Cdd:cd19074 215 PsrsraTDEDNRDKKrrlltdenlekvkkLKPIADELGLTLAQLALAWCLRNPAVSsaIIGASRPEQLEENVKASGVKLS 294
|
..
gi 1709623 290 SD 291
Cdd:cd19074 295 PE 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-297 |
5.54e-18 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 82.65 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 42 IDVGFRHIDCSHLY----------QNEEEIGQAIVSKiedgtVKREDIFYTSKL--WSTSHRPEL----VRPSLENSLRK 105
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSR-----GKRDRVVIATKVgfPMGPNGPGLsrkhIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 106 LNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILN---KPGL 182
Cdd:cd19081 111 LQTDYIDLYQAHWD------DPATPLEE-------------TLGALNDLIRQGKVRYIGASNYSAWRLQEALElsrQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 183 KhRPVCNQVECHLYLNQS---KLLAYCKMNDIVLVAYGALGT--------------------QRYKYCINEDTPVLLDdp 239
Cdd:cd19081 172 P-RYVSLQPEYNLVDRESfegELLPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrrgEAAKRYLNERGLRILD-- 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 240 ILCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19081 249 ALDEVAAEHGATPAQVALAWLLARPGVTapIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
7-292 |
7.97e-18 |
|
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: 82.32 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 7 KMEL-NDGHSIPVLGFGTYA---------TEENlrkKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgt 73
Cdd:cd19149 1 YRKLgKSGIEASVIGLGTWAigggpwwggSDDN---ESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 74 vkREDIFYTSK---LWS---TSH-------------RPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDEllpqdeh 134
Cdd:cd19149 73 --RDKVVLATKcglRWDregGSFffvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEE------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 135 gnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILNkpglkhrpvCNQVEchlyLNQSK-----------LL 203
Cdd:cd19149 144 ------------TMEALEELKRQGKIRAIGASNVSVEQIKEYVK---------AGQLD----IIQEKysmldrgiekeLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 204 AYCKMNDIVLVAYGAL-----------------GTQRYKYCI----NEDTPVLLDDPILcTMAKKYKRTPALIALRYQL- 261
Cdd:cd19149 199 PYCKKNNIAFQAYSPLeqglltgkitpdrefdaGDARSGIPWfspeNREKVLALLEKWK-PLCEKYGCTLAQLVIAWTLa 277
|
330 340 350
....*....|....*....|....*....|..
gi 1709623 262 ERGIVT-LVKSFNEERIRENLQVFDFQLASDD 292
Cdd:cd19149 278 QPGITSaLCGARKPEQAEENAKAGDIRLSAED 309
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
13-297 |
2.92e-17 |
|
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: 80.74 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHS---IPVLGFGTyAT--EENLRKKSMEST---------KIAIDVGFRHIDCSHLY---QNEEEIGQAIVSKiedgtvk 75
Cdd:cd19091 7 GRSglkVSELALGT-MTfgGGGGFFGAWGGVdqeeadrlvDIALDAGINFFDTADVYsegESEEILGKALKGR------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 76 REDIFYTSKLWST---------SHRPELVRpSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLpqdehgnlildtvdlcd 146
Cdd:cd19091 79 RDDVLIATKVRGRmgegpndvgLSRHHIIR-AVEASLKRLGTDYIDLYQLHGFDALTPLEETL----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 147 twEAMEKCKDAGLAKSIGVSNFNRRQLEKIL---NKPGLKhRPVCNQVECHLyLNQS---KLLAYCKMNDIVLVAYGALG 220
Cdd:cd19091 141 --RALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQAYYSL-LGRDlehELMPLALDQGVGLLVWSPLA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 221 TQRY--KYCINEDTP-----------------VLLDDPI--LCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERI 277
Cdd:cd19091 217 GGLLsgKYRRGQPAPegsrlrrtgfdfppvdrERGYDVVdaLREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQL 296
|
330 340
....*....|....*....|
gi 1709623 278 RENLQVFDFQLASDDMEILD 297
Cdd:cd19091 297 EDNLGAAGLSLTPEEIARLD 316
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
73-299 |
3.78e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 77.37 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 73 TVKREDIFYTSKLWST--SHRPELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgdelLPQDEHGNLiLDTVDLcdtwea 150
Cdd:cd19103 70 RYPREDYIISTKFTPQiaGQSADPVADMLEGSLARLGTDYIDIYWIH-----------NPADVERWT-PELIPL------ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 151 mekcKDAGLAKSIGVSNFNRRQLEK---ILNKPGLKHRPVCNqvecH---LYLN--QSKLLAYCKMNDIVLVAY-----G 217
Cdd:cd19103 132 ----LKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQN----HyslLYRSseEAGILDYCKENGITFFAYmvleqG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 218 AL------------GTQRYK-YciNEDTPVLLD-DPILCTMAKKYKRTPALIALRYQLERGIVTLVKSFNEERIRENLQV 283
Cdd:cd19103 204 ALsgkydtkhplpeGSGRAEtY--NPLLPQLEElTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARA 281
|
250
....*....|....*.
gi 1709623 284 FDFQLASDDMEILDNL 299
Cdd:cd19103 282 ASITLTDDEIKELEQL 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-291 |
4.00e-16 |
|
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: 76.82 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTYATEENLRKKSMESTKI----AIDVGFRHIDCSHLYQNEEE-IGQAIvskiedGTVKREDIFYTSKL------ 85
Cdd:cd19090 1 SALGLGTAGLGGVFGGVDDDEAVAtiraALDLGINYIDTAPAYGDSEErLGLAL------AELPREPLVLSTKVgrlped 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 -WSTShrPELVRPSLENSLRKLNLDYVDLYLIHFPVSLKPGDELLPQdehGNLildtvdlcdtwEAMEKCKDAGLAKSIG 164
Cdd:cd19090 75 tADYS--ADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPG---GAL-----------EALLELKEEGLIKHIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 165 VSnfnrrqlekiLNKPGLkHRPVCNQ-----VECHLY---LNQS---KLLAYCKMNDI-VLVA----YGALGTQRYKYCI 228
Cdd:cd19090 139 LG----------GGPPDL-LRRAIETgdfdvVLTANRytlLDQSaadELLPAAARHGVgVINAsplgMGLLAGRPPERVR 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 229 NEdtpvllDDPILCTMAKKYKRTPAL----------IALRYQL--ERGIVTLVKSFNEERIRENLQVFDFQLASD 291
Cdd:cd19090 208 YT------YRWLSPELLDRAKRLYELcdehgvplpaLALRFLLrdPRISTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
15-166 |
6.92e-16 |
|
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: 75.59 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 15 SIPVLGFGTYA-----TEENLRKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQA---------IVSKIedGTVkre 77
Cdd:cd19086 2 EVSEIGFGTWGlggdwWGDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKAlkgrrdkvvIATKF--GNR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 78 diFYTSKLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIHfpvslKPGDELLPQDEHgnlildtvdlcdtWEAMEKCKDA 157
Cdd:cd19086 77 --FDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLH-----NPPDEVLDNDEL-------------FEALEKLKQE 136
|
....*....
gi 1709623 158 GLAKSIGVS 166
Cdd:cd19086 137 GKIRAYGVS 145
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-166 |
1.08e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 76.20 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 19 LGFGTY--ATEENLRKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIVSKIEDGTVKREDIFYTSK--------- 84
Cdd:cd19099 6 LGLGTYrgDSDDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 -------------------------LWSTSHrPELVRPSLENSLRKLNLDYVDLYLIHFPVslkpgdELLPQDEHGNLiL 139
Cdd:cd19099 86 eplrplkyleeklgrglidvadsagLRHCIS-PAYLEDQIERSLKRLGLDTIDLYLLHNPE------EQLLELGEEEF-Y 157
|
170 180
....*....|....*....|....*..
gi 1709623 140 DTVDlcDTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19099 158 DRLE--EAFEALEEAVAEGKIRYYGIS 182
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
27-294 |
8.38e-15 |
|
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: 73.75 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 27 EENLRKKSMESTKIAIDVGFRHIDCSHLY----------QNEEEIGQAIVSKiedgtVKREDIF-------YTSKLW--- 86
Cdd:cd19094 13 EQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKK-----GNRDKVVlatkvagPGEGITwpr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 87 --STSHRPELVRPSLENSLRKLNLDYVDLYLIHFP---VSLKPGDELLPQDEHGnlilDTVDLCDTWEAMEKCKDAGLAK 161
Cdd:cd19094 88 ggGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPdryTPLFGGGYYTEPSEEE----DSVSFEEQLEALGELVKAGKIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 162 SIGVSN--------FNRrqLEKILNKPglkhRPVCNQVECHLyLNQSKL--LA-YCKMNDIVLVAYGAL--GTQRYKYCI 228
Cdd:cd19094 164 HIGLSNetpwgvmkFLE--LAEQLGLP----RIVSIQNPYSL-LNRNFEegLAeACHRENVGLLAYSPLagGVLTGKYLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 229 NEDTP-------------------------VLLDdpilctMAKKYKRTPALIALRYQLERGIV--TLVKSFNEERIRENL 281
Cdd:cd19094 237 GAARPeggrlnlfpgymaryrspqaleavaEYVK------LARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENI 310
|
330
....*....|...
gi 1709623 282 QVFDFQLaSDDME 294
Cdd:cd19094 311 DAFDVPL-SDELL 322
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
36-297 |
5.48e-14 |
|
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: 71.46 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 36 ESTKI---AIDVGFRHIDCSHLYQN---EEEIGQAIvskieDGTVKREDIFYTSKLW-STSHRP-------ELVRPSLEN 101
Cdd:cd19079 36 ESRPIikrALDLGINFFDTANVYSGgasEEILGRAL-----KEFAPRDEVVIATKVYfPMGDGPngrglsrKHIMAEVDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 102 SLRKLNLDYVDLYLIHFPvslkpgdellpqDEHgnlildtVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILN--- 178
Cdd:cd19079 111 SLKRLGTDYIDLYQIHRW------------DYE-------TPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHlae 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 179 KPGLkHRPVCNQvechLYLN------QSKLLAYCKMNDIVLVAYGALGTQR----------------------YKYCINE 230
Cdd:cd19079 172 KNGW-TKFVSMQ----NHYNllyreeEREMIPLCEEEGIGVIPWSPLARGRlarpwgdtterrrsttdtaklkYDYFTEA 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709623 231 DTPVLLDdpiLCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDFQLASDDMEILD 297
Cdd:cd19079 247 DKEIVDR---VEEVAKERGVSMAQVALAWLLSKPGVTapIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
11-292 |
1.73e-13 |
|
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: 69.78 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 11 NDGHSIPVLGFGT------YAT--EENLRKKSMEStkiAIDVGFRHIDCSHLYQ-NEEEIGQAIvsKIEDGtvKREDIFY 81
Cdd:cd19144 8 RNGPSVPALGFGAmglsafYGPpkPDEERFAVLDA---AFELGCTFWDTADIYGdSEELIGRWF--KQNPG--KREKIFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 82 TSKL----------WSTSHRPELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgdellpqdehgnLILDTVDLCDTWEAM 151
Cdd:cd19144 81 ATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH-------------------RVDGKTPIEKTVAAM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 152 EKCKDAGLAKSIGVSNFNRRQLEKI-----LNKPGLKHRPVCNQVEchlyLNQSKLLAYCKMNDIVLVAYGALG----TQ 222
Cdd:cd19144 142 AELVQEGKIKHIGLSECSAETLRRAhavhpIAAVQIEYSPFSLDIE----RPEIGVLDTCRELGVAIVAYSPLGrgflTG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 223 RYKYciNEDTP--------------------VLLDDpiLCTMAKKYKRTPALIALRYQLERG--IVTLVKSFNEERIREN 280
Cdd:cd19144 218 AIRS--PDDFEegdfrrmaprfqaenfpknlELVDK--IKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEEN 293
|
330
....*....|..
gi 1709623 281 LQVFDFQLASDD 292
Cdd:cd19144 294 LGALKVKLTEEE 305
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
21-190 |
7.19e-13 |
|
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: 67.98 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 21 FGTYATEEnlrkksmESTKI---AIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvkREDIFYTSKLW-STSHRPE 93
Cdd:cd19087 23 FGGRTDEE-------TSFAImdrALDAGINFFDTADVYGGgrsEEIIGRWIAGR-------RDDIVLATKVFgPMGDDPN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 94 L-------VRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19087 89 DrglsrrhIRRAVEASLRRLQTDYIDLYQMHHF------DRDTPLEE-------------TLRALDDLVRQGKIRYIGVS 149
|
170 180
....*....|....*....|....*.
gi 1709623 167 NFNRRQLEKILNKPGLKH--RPVCNQ 190
Cdd:cd19087 150 NFAAWQIAKAQGIAARRGllRFVSEQ 175
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
16-288 |
1.16e-12 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 67.19 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 16 IPVLGFGTYATEENLR----KKSMESTKIAIDVGFRHIDCSHLY---QNEEEIGQAIVskiedgTVKREDIFYTSK---- 84
Cdd:cd19163 13 VSKLGFGASPLGGVFGpvdeEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATKvgry 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 --LWSTS--HRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgdellpqdEHGNLiLDTVdLCDTWEAMEKCKDAGLA 160
Cdd:cd19163 87 glDPDKMfdFSAERITKSVEESLKRLGLDYIDIIQVHDI-------------EFAPS-LDQI-LNETLPALQKLKEEGKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 161 KSIGVSNFNRRQLEKILNKpglkhrpVCNQVE-----CHLYLNQS---KLLAYCKMNDIVLVAYGALG----TQRYKYCI 228
Cdd:cd19163 152 RFIGITGYPLDVLKEVLER-------SPVKIDtvlsyCHYTLNDTsllELLPFFKEKGVGVINASPLSmgllTERGPPDW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 229 NEDTPVLLDdpiLCTMAKKYKRTP----ALIALRYQL--ERGIVTLVKSFNEERIRENLQVFDFQL 288
Cdd:cd19163 225 HPASPEIKE---ACAKAAAYCKSRgvdiSKLALQFALsnPDIATTLVGTASPENLRKNLEAAEEPL 287
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-180 |
9.14e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 64.09 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 39 KIAIDVGFRHIDCSHLYQNEEE-IGQAIVSKiedgtvkrEDIFYTSKL----WSTSHRPELVRPSLENSLRKLNLDYVDL 113
Cdd:cd19097 33 EYALKAGINTLDTAPAYGDSEKvLGKFLKRL--------DKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709623 114 YLIHfpvslKPGDELLpqdeHGNLIldtvdlcdtWEAMEKCKDAGLAKSIGVSNFNRRQLEKILNKP 180
Cdd:cd19097 105 LLLH-----NPDDLLK----HGGKL---------VEALLELKKEGLIRKIGVSVYSPEELEKALESF 153
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
11-166 |
3.56e-11 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 63.00 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 11 NDGHSIPVLGFGT------YATEEnlRKKSMESTKIAIDVGFRHIDCSHLYQ---NEEEIGQAIVSKiedgtvkREDIFY 81
Cdd:cd19076 7 TQGLEVSALGLGCmgmsafYGPAD--EEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 82 TSK---LWS-------TSHRPELVRPSLENSLRKLNLDYVDLYLIHFPvslkpgDellpqdehgnlilDTVDLCDTWEAM 151
Cdd:cd19076 78 ATKfgiVRDpgsgfrgVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV------D-------------PNVPIEETVGAM 138
|
170
....*....|....*
gi 1709623 152 EKCKDAGLAKSIGVS 166
Cdd:cd19076 139 AELVEEGKVRYIGLS 153
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-299 |
3.58e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 63.05 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVGFRHIDCSHLY---QNEEEIGQAIvskieDGtvKREDIFYTSK----LWSTSHRPELVRPSLENSLRKLNLDYVDL 113
Cdd:cd19104 41 ALDLGINFFDTAPSYgdgKSEENLGRAL-----KG--LPAGPYITTKvrldPDDLGDIGGQIERSVEKSLKRLKRDSVDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 114 YLIHfpvslkpgDELLPQDEHGNL----ILDTVDLCDTWEAMEKCKDAGLAKSIGVSnfnrrqlekilnkpGLKHRPVCN 189
Cdd:cd19104 114 LQLH--------NRIGDERDKPVGgtlsTTDVLGLGGVADAFERLRSEGKIRFIGIT--------------GLGNPPAIR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 190 QVECH--------LY--LNQS---------------KLLAYCKMND-----IVLVAYGALGTqrykyciNEDTPVLLDDP 239
Cdd:cd19104 172 ELLDSgkfdavqvYYnlLNPSaaearprgwsaqdygGIIDAAAEHGvgvmgIRVLAAGALTT-------SLDRGREAPPT 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709623 240 ILCTMAKKYKR-------------TPALIALRYQL-ERGIVTLVKSF-NEERIRENLQVFDF-QLASDDMEILDNL 299
Cdd:cd19104 245 SDSDVAIDFRRaaafralarewgeTLAQLAHRFALsNPGVSTVLVGVkNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
43-226 |
1.27e-10 |
|
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: 61.42 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 43 DVGFRHIDCSHLYQN---EEEIGQAIVSKiEDGTV--KredifyTSKLWSTSHRPELVRPSLENSLRKLNLDYVDLYLIH 117
Cdd:cd19075 31 ERGHTEIDTARVYPDgtsEELLGELGLGE-RGFKIdtK------ANPGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 118 FPvslkpgDEllpqdehgnlildTVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILN--------KP----GLkHR 185
Cdd:cd19075 104 AP------DR-------------STPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqGM-YN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1709623 186 PVCNQVEchlylnqSKLLAYCKMNDIVLVAYGALG----TQRYKY 226
Cdd:cd19075 164 AITRQVE-------TELFPCLRKLGIRFYAYSPLAggflTGKYKY 201
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
17-166 |
2.20e-10 |
|
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: 60.45 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTyATEENLRKKSMESTKIAI----DVGFRHIDCSHLY---QNEEEIGQAIVSKiedgtvKREDIFYTSKL---- 85
Cdd:cd19162 1 PRLGLGA-ASLGNLARAGEDEAAATLdaawDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVgrll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 ------WSTSHRPEL------VRPSLENSLRKLNLDYVDLYLIHFPvslkpgdellpqDEHGNLILDtvdlcDTWEAMEK 153
Cdd:cd19162 74 epgaagRPAGADRRFdfsadgIRRSIEASLERLGLDRLDLVFLHDP------------DRHLLQALT-----DAFPALEE 136
|
170
....*....|...
gi 1709623 154 CKDAGLAKSIGVS 166
Cdd:cd19162 137 LRAEGVVGAIGVG 149
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
20-298 |
8.70e-10 |
|
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: 58.78 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 20 GFGTYATEEnlrkksmESTKI---AIDVGFRHIDCSHLY---QNEEEIGQAIVSKiedgtvkREDIFYTSKL-WSTSH-- 90
Cdd:cd19078 17 GYGPPPDKE-------EMIELirkAVELGITFFDTAEVYgpyTNEELVGEALKPF-------RDQVVIATKFgFKIDGgk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 91 --------RPELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgdellpqdehgnLILDTVDLCDTWEAMEKCKDAGLAKS 162
Cdd:cd19078 83 pgplgldsRPEHIRKAVEGSLKRLQTDYIDLYYQH-------------------RVDPNVPIEEVAGTMKELIKEGKIRH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 163 IGVSNFNRRQLEKilnkpglKHRpVCN----QVECHLYLN--QSKLLAYCKMNDIVLVAYGALGTQRYKYCINEDTP--- 233
Cdd:cd19078 144 WGLSEAGVETIRR-------AHA-VCPvtavQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKfde 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 234 -------------------VLLDdpILCTMAKKYKRTPALIALRYQLERG--IVTLVKSFNEERIRENLQVFDFQLASDD 292
Cdd:cd19078 216 gddraslprftpealeanqALVD--LLKEFAEEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEE 293
|
....*.
gi 1709623 293 MEILDN 298
Cdd:cd19078 294 LREIED 299
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-308 |
1.92e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 57.94 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 14 HSIP-------VLGFGTYA-TEENLRKKSMESTKIAIDVGFRHIDCSHLYQ----------NEEEIGQAIVSKiedgtVK 75
Cdd:PRK10625 4 HRIPhsslevsTLGLGTMTfGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKR-----GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 76 REDIFYTSKLWSTSH------RPEL------VRPSLENSLRKLNLDYVDLYLIHFPVSlkpgdellPQDEHGNLILD--- 140
Cdd:PRK10625 79 REKLIIASKVSGPSRnndkgiRPNQaldrknIREALHDSLKRLQTDYLDLYQVHWPQR--------PTNCFGKLGYSwtd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 141 ---TVDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGlKH---RPVCNQVECHLyLNQS---KLLAYCKMNDI 211
Cdd:PRK10625 151 sapAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAE-KHdlpRIVTIQNPYSL-LNRSfevGLAEVSQYEGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 212 VLVAYGAL--GTQRYKYcINEDTPVLLDDPIL------------------CTMAKKYKRTPALIALRYQLERGIV--TLV 269
Cdd:PRK10625 229 ELLAYSCLafGTLTGKY-LNGAKPAGARNTLFsrftrysgeqtqkavaayVDIAKRHGLDPAQMALAFVRRQPFVasTLL 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1709623 270 KSFNEERIRENLQVFDFQLASDDMEILDNLDRnlRY-FPA 308
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ--VYtYPA 345
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
20-295 |
6.92e-09 |
|
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: 56.11 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 20 GFGTYATEENLRKKSMEstkiAIDVGFRHIDCSHLYQNEEEIGQAIVSKI--EDGTVKREDIFYTSK----LW-----ST 88
Cdd:cd19089 21 NFGDYTSPEEARELLRT----AFDLGITHFDLANNYGPPPGSAEENFGRIlkRDLRPYRDELVISTKagygMWpgpygDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPELVRpSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19089 97 GSRKYLLA-SLDQSLKRMGLDYVDIFYHHRY------DPDTPLEE-------------TMTALADAVRSGKALYVGISNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 169 NRRQLEK---ILNKpgLKHRPVCNQVECHLyLNQS---KLLAYCKMNDIVLVAYGALG----TQRYKYCINED------- 231
Cdd:cd19089 157 PGAKARRaiaLLRE--LGVPLIIHQPRYSL-LDRWaedGLLEVLEEAGIGFIAFSPLAqgllTDKYLNGIPPDsrraaes 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 232 ---TPVLLDDPI------LCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFDfQLASDDMEI 295
Cdd:cd19089 234 kflTEEALTPEKleqlrkLNKIAAKRGQSLAQLALSWVLRDPRVTsvLIGASSPSQLEDNVAALK-NLDFSEEEL 307
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
19-297 |
1.13e-08 |
|
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: 55.30 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 19 LGFGTYATEenlRKKSM---ESTKIA---IDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvkREDIFYTSKL-WST 88
Cdd:cd19080 15 LGTMTFGTE---WGWGAdreEARAMFdayVEAGGNFIDTANNYTNgtsERLLGEFIAGN-------RDRIVLATKYtMNR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 ---------SHRPELVRpSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlILDTVD------------LCDT 147
Cdd:cd19080 85 rpgdpnaggNHRKNLRR-SVEASLRRLQTDYIDLLYVHAW------DFTTPVEE----VMRALDdlvragkvlyvgISDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 148 --WEAmekCKDAGLAKSIGVSnfnrrqlekilnkpglkhRPVCNQVECHLyLNQS---KLLAYCKMNDIVLVAYGALGTQ 222
Cdd:cd19080 154 paWVV---ARANTLAELRGWS------------------PFVALQIEYSL-LERTperELLPMARALGLGVTPWSPLGGG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 223 RY--KYCINEDTPVLLDDPI-----------------LCTMAKKYKRTPALIALRYQLER--GIVTLVKSFNEERIRENL 281
Cdd:cd19080 212 LLtgKYQRGEEGRAGEAKGVtvgfgklternwaivdvVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNL 291
|
330
....*....|....*.
gi 1709623 282 QVFDFQLASDDMEILD 297
Cdd:cd19080 292 GALDLTLSPEQLARLD 307
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
18-167 |
2.82e-08 |
|
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: 54.10 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 18 VLG---FGTYATEEnlrkksmESTKI---AIDVGFRHIDCSHLYQNEEEIGQA--IVSKIEDGTVKREDIFYTSK----- 84
Cdd:cd19082 4 VLGtadFGTRIDEE-------EAFALldaFVELGGNFIDTARVYGDWVERGASerVIGEWLKSRGNRDKVVIATKgghpd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 85 LWSTS-HR--PELVRPSLENSLRKLNLDYVDLYLIH-----FPVslkpgDELLpqdehgnlildtvdlcdtwEAMEKCKD 156
Cdd:cd19082 77 LEDMSrSRlsPEDIRADLEESLERLGTDYIDLYFLHrddpsVPV-----GEIV-------------------DTLNELVR 132
|
170
....*....|.
gi 1709623 157 AGLAKSIGVSN 167
Cdd:cd19082 133 AGKIRAFGASN 143
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
41-297 |
3.21e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 54.23 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVGFRHIDCSHLY-----QNEEEIGQAIVskiEDGTVKREDIFYTSK----LW-----STSHRPELVrPSLENSLRKL 106
Cdd:PRK09912 52 AFDLGITHFDLANNYgpppgSAEENFGRLLR---EDFAAYRDELIISTKagydMWpgpygSGGSRKYLL-ASLDQSLKRM 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 107 NLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFNRRQLEKILNK------P 180
Cdd:PRK09912 128 GLEYVDIFYSHRV------DENTPMEE-------------TASALAHAVQSGKALYVGISSYSPERTQKMVELlrewkiP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 181 GLKHRPVCNQVecHLYLNQSKLLAYCKMNDIVLVAYGALG----TQRYKYCINED-------------TPVLLDDP---- 239
Cdd:PRK09912 189 LLIHQPSYNLL--NRWVDKSGLLDTLQNNGVGCIAFTPLAqgllTGKYLNGIPQDsrmhregnkvrglTPKMLTEAnlns 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709623 240 --ILCTMAKKYKRTPALIALRYQL--ERGIVTLVKSFNEERIRENLQVF-DFQLASDDMEILD 297
Cdd:PRK09912 267 lrLLNEMAQQRGQSMAQMALSWLLkdERVTSVLIGASRAEQLEENVQALnNLTFSTEELAQID 329
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
75-282 |
1.37e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 51.95 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 75 KREDIFYTSKL---------WSTSHR---PELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgdellpqdehgnlILD-T 141
Cdd:cd19752 65 NRDDVVIATKVgagprdpdgGPESPEglsAETIEQEIDKSLRRLGTDYIDLYYAH--------------------VDDrD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 142 VDLCDTWEAMEKCKDAGLAKSIGVSNFNRRQLEK---ILNKPGLkHRPVCNQVEcHLYL---------NQS----KLLAY 205
Cdd:cd19752 125 TPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGW-AEFSAIQQR-HSYLrprpgadfgVQRivtdELLDY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 206 CKMN-DIVLVAYGALGTQRY--------KYCINEDTPVLLDdpILCTMAKKYKRTPALIALRYQLER--GIVTLVKSFNE 274
Cdd:cd19752 203 ASSRpDLTLLAYSPLLSGAYtrpdrplpEQYDGPDSDARLA--VLEEVAGELGATPNQVVLAWLLHRtpAIIPLLGASTV 280
|
....*...
gi 1709623 275 ERIRENLQ 282
Cdd:cd19752 281 EQLEENLA 288
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
18-195 |
6.27e-07 |
|
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: 50.29 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 18 VLGFG---TYATE--ENLRKKSMestKIAIDVGFRHIDCSHLYQN---EEEIGQAIvskiEDGTVKREDIFYTSKL-WST 88
Cdd:cd19143 15 ALSFGswvTFGNQvdVDEAKECM---KAAYDAGVNFFDNAEVYANgqsEEIMGQAI----KELGWPRSDYVVSTKIfWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 89 SHRPE----LVRPSL----ENSLRKLNLDYVDLYLIHFPvslkpgDELLPqdehgnlILDTVdlcdtwEAMEKCKDAGLA 160
Cdd:cd19143 88 GGPPPndrgLSRKHIvegtKASLKRLQLDYVDLVFCHRP------DPATP-------IEETV------RAMNDLIDQGKA 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1709623 161 KSIGVSNFNRRQLEK---ILNKPGLkHRPVCNQVECHL 195
Cdd:cd19143 149 FYWGTSEWSAQQIEEaheIADRLGL-IPPVMEQPQYNL 185
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
17-165 |
1.71e-06 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 48.76 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 17 PVLGFGTyATEENLRKKSMESTKI-----AIDVGFRHIDCSHLYQN---EEEIGQAIVSKiedgtvKREDIFYTSKL--- 85
Cdd:cd19152 1 PKLGFGT-APLGNLYEAVSDEEAKatlvaAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 86 ---------------WSTS-HRPEL------VRPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEHGNlILDTvD 143
Cdd:cd19152 74 lvplqeveptfepgfWNPLpFDAVFdysydgILRSIEDSLQRLGLSRIDLLSIHDP------DEDLAGAESDE-HFAQ-A 145
|
170 180
....*....|....*....|..
gi 1709623 144 LCDTWEAMEKCKDAGLAKSIGV 165
Cdd:cd19152 146 IKGAFRALEELREEGVIKAIGL 167
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
39-166 |
4.25e-06 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 47.66 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 39 KIAIDVGFRHIDCSHLYQNEEEI-GQAIvSKIEDGtVKREDIFYTSK-----LWSTSHRPELVRPSLENSLRKLNLDYVD 112
Cdd:cd19164 41 RRALELGIRAFDTSPYYGPSEIIlGRAL-KALRDE-FPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTDYLD 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1709623 113 LYLIHfpvslkpgD-ELLPQDEhgnlILDTVdlcdtwEAMEKCKDAGLAKSIGVS 166
Cdd:cd19164 119 LVYLH--------DvEFVADEE----VLEAL------KELFKLKDEGKIRNVGIS 155
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
20-203 |
5.66e-05 |
|
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: 44.06 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 20 GFGTYATEENLRKKSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIvSKIEdgtVKREDIFYTSKL-------WSTS 89
Cdd:cd19153 21 ALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKAL-AALQ---VPRSSYTVATKVgryrdseFDYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 90 HrpELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgD-ELLPQDEhgnlildtvDLCDTWEAMEKCKDAGLAKSIGVSNF 168
Cdd:cd19153 97 A--ERVRASVATSLERLHTTYLDVVYLH--------DiEFVDYDT---------LVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1709623 169 NRRQLEKILNKPGLKHRPVCnQVECHLYLNQSKLL 203
Cdd:cd19153 158 PLDTLTRATRRCSPGSLDAV-LSYCHLTLQDARLE 191
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
21-285 |
8.68e-05 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 43.55 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 21 FGTYATEENLRkksmESTKIAIDVGFRHIDCSHLY-----QNEEEIGQAIVskiEDGTVKREDIFYTSK----LWSTSH- 90
Cdd:cd19151 23 FGDVDRYENSR----AMLRRAFDLGITHFDLANNYgpppgSAEENFGRILK---EDLKPYRDELIISTKagytMWPGPYg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 91 ----RPELVrPSLENSLRKLNLDYVDLYLIHFPvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVS 166
Cdd:cd19151 96 dwgsKKYLI-ASLDQSLKRMGLDYVDIFYHHRP------DPETPLEE-------------TMGALDQIVRQGKALYVGIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 167 NFN---RRQLEKILNK---PGLKHRPVCNQVECHlylNQSKLLAYCKMNDIVLVAYGALG----TQRYKYCINED----- 231
Cdd:cd19151 156 NYPpeeAREAAAILKDlgtPCLIHQPKYSMFNRW---VEEGLLDVLEEEGIGCIAFSPLAqgllTDRYLNGIPEDsraak 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709623 232 ----------TPVLLDD-PILCTMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFD 285
Cdd:cd19151 233 gssflkpeqiTEEKLAKvRRLNEIAQARGQKLAQMALAWVLRNKRVTsvLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
41-117 |
1.13e-04 |
|
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: 43.19 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVGFRHIDCSHLY---QNEEEIGQAIVS----KIEDGTVKREDIFYTSKLWSTSHrPELVRPSLENSLRKLNLDYVDL 113
Cdd:cd19145 42 AFNSGVTFLDTSDIYgpnTNEVLLGKALKDgpreKVQLATKFGIHEIGGSGVEVRGD-PAYVRAACEASLKRLDVDYIDL 120
|
....
gi 1709623 114 YLIH 117
Cdd:cd19145 121 YYQH 124
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
41-285 |
2.25e-04 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 42.44 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 41 AIDVGFRHIDCSHLY-----QNEEEIGQAIVskiEDGTVKREDIFYTSK----LWSTSH-----RPELVrPSLENSLRKL 106
Cdd:cd19150 39 AFDLGITHFDLANNYgpppgSAEENFGRILR---EDFAGYRDELIISTKagydMWPGPYgewgsRKYLL-ASLDQSLKRM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 107 NLDYVDLYLIH-FpvslkpgDELLPQDEhgnlildtvdlcdTWEAMEKCKDAGLAKSIGVSNFN---RRQLEKILNK--- 179
Cdd:cd19150 115 GLDYVDIFYSHrF-------DPDTPLEE-------------TMGALDHAVRSGKALYVGISSYSperTREAAAILRElgt 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 180 PGLKHRPVCNQVecHLYLNQSKLLAYCKMNDIVLVAYGALG----TQRYKYCINED---------TPVLLDDPILC---- 242
Cdd:cd19150 175 PLLIHQPSYNML--NRWVEESGLLDTLQELGVGCIAFTPLAqgllTDKYLNGIPEGsraskerslSPKMLTEANLNsira 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1709623 243 --TMAKKYKRTPALIALRYQLERGIVT--LVKSFNEERIRENLQVFD 285
Cdd:cd19150 253 lnEIAQKRGQSLAQMALAWVLRDGRVTsaLIGASRPEQLEENVGALD 299
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
13-117 |
5.84e-04 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 40.91 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 13 GHSIPVLGFGTYATEEN-LRKKSMES-TKIAIDVGFRHIDCSHLYQN---EEEIGqAIVSKiedGTVKREDIFYTSKL-W 86
Cdd:cd19142 10 GLRVSNVGLGTWSTFSTaISEEQAEEiVTLAYENGINYFDTSDAFTSgqaETELG-RILKK---KGWKRSSYIVSTKIyW 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1709623 87 STshRPE---LVRP----SLENSLRKLNLDYVDLYLIH 117
Cdd:cd19142 86 SY--GSEergLSRKhiieSVRASLRRLQLDYIDIVIIH 121
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
11-300 |
1.63e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 39.76 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 11 NDGHSIPVLGFGT--------YATEENlrkkSMESTKIAIDVGFRHIDCSHLYQN---EEEIGQAIvskiEDGTVKREDI 79
Cdd:PLN02587 6 STGLKVSSVGFGAsplgsvfgPVSEED----AIASVREAFRLGINFFDTSPYYGGtlsEKVLGKAL----KALGIPREKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 80 FYTSKLWSTSH----RPELVRPSLENSLRKLNLDYVDLYLIHfpvslkpgdellpQDEHGNliLDTVdLCDTWEAMEKCK 155
Cdd:PLN02587 78 VVSTKCGRYGEgfdfSAERVTKSVDESLARLQLDYVDILHCH-------------DIEFGS--LDQI-VNETIPALQKLK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 156 DAGLAKSIGVSNFNRRQLEKILNK--PGlkhrpvcnQVE-----CHLYLNQS---KLLAYCKMNDIVLV-----AYGALG 220
Cdd:PLN02587 142 ESGKVRFIGITGLPLAIFTYVLDRvpPG--------TVDvilsyCHYSLNDSsleDLLPYLKSKGVGVIsasplAMGLLT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709623 221 TQRYKycinEDTPVLLDDPILCTMA----KKYKRTPALIALRYQL-ERGIVT-LVKSFNEERIRENLQ-VFDFQLASDDM 293
Cdd:PLN02587 214 ENGPP----EWHPAPPELKSACAAAathcKEKGKNISKLALQYSLsNKDISTtLVGMNSVQQVEENVAaATELETSGIDE 289
|
....*..
gi 1709623 294 EILDNLD 300
Cdd:PLN02587 290 ELLSEVE 296
|
|
| |
