|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
57-360 |
1.02e-166 |
|
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: 467.48 E-value: 1.02e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWSWGDNSYWNdfqWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRERKERypg 136
Cdd:cd19093 1 EVSPLGLGTWQWGDRLWWG---YGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTG------RSERLLGRFLKELGDR--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 137 AEVSVATKFAALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWG--NEGYLDGLGDAVEQGLVKAVGVSNYSEKR 214
Cdd:cd19093 69 DEVVIATKFAPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYsqIEALMDGLADAVEEGLVRAVGVSNYSADQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 215 LRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFLT 294
Cdd:cd19093 149 LRRAHKALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 295 KLQPLLNRIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELR 360
Cdd:cd19093 229 KVQPLLDALEEIAEKYGKTPAQVALNWLIAKG-VVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
48-368 |
4.10e-88 |
|
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: 268.59 E-value: 4.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGVWSWGDNsywndfqWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGskfsLGAisSETLLGRFI 127
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGTMTFGGP-------WGGVDEAEAIAILDAALDAGINFFDTADVYG----PGR--SEELLGEAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERkeryPGAEVSVATKFA------ALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWP-GLWGNEGYLDGLGDAVEQG 200
Cdd:COG0667 70 KGR----PRDDVVIATKVGrrmgpgPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPdPDTPIEETLGALDELVREG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 201 LVKAVGVSNYSEKRLRDAYERLKKRGiPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKYTPENP- 279
Cdd:COG0667 146 KIRYIGVSNYSAEQLRRALAIAEGLP-PIVAVQNEYSLLDRSAEE-ELLPAARELGVGVLAYSPLAGGLLTGKYRRGATf 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 280 PSGPRGRIY--TREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSLTDNEV 356
Cdd:COG0667 224 PEGDRAATNfvQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTsVIPGARSPEQLEENLAAADLELSAEDL 303
|
330
....*....|..
gi 18390678 357 SELRSLASEIKP 368
Cdd:COG0667 304 AALDAALAAVPA 315
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
55-360 |
1.57e-72 |
|
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: 227.79 E-value: 1.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 55 DLKVTKLGIGVWSWGdNSYWNDFQWDD--RKLKAAkgafdtsLDNGIDFFDTAEVYGskfsLGaiSSETLLGRFIRERKE 132
Cdd:cd19084 1 DLKVSRIGLGTWAIG-GTWWGEVDDQEsiEAIKAA-------IDLGINFFDTAPVYG----FG--HSEEILGKALKGRRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 133 RypgaeVSVATKFAaLPWRFG--------RESVVTALKDSLSRLELSSVDLYQLHWP-GLWGNEGYLDGLGDAVEQGLVK 203
Cdd:cd19084 67 D-----VVIATKCG-LRWDGGkgvtkdlsPESIRKEVEQSLRRLQTDYIDLYQIHWPdPNTPIEETAEALEKLKKEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 204 AVGVSNYSEKRLRDAyerlkKRGIPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTPEN--PPS 281
Cdd:cd19084 141 YIGVSNFSVEQLEEA-----RKYGPIVSLQPPYSMLEREIEEE-LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfPPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 282 GPRGRI--YTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAIGWSLTDNEVSE 358
Cdd:cd19084 215 DRRSRFpfFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVtSAIVGAKNPEQLEENAGALDWELTEEELKE 294
|
..
gi 18390678 359 LR 360
Cdd:cd19084 295 ID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
61-363 |
2.94e-72 |
|
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: 227.19 E-value: 2.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 61 LGIGVWSWGdnsyWNDFQWDDRKLKAAkgaFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRERKERYPgaEVS 140
Cdd:pfam00248 1 IGLGTWQLG----GGWGPISKEEALEA---LRAALEAGINFIDTAEVYGDG------KSEELLGEALKDYPVKRD--KVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 141 VATKF----AALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWP-GLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKRL 215
Cdd:pfam00248 66 IATKVpdgdGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 216 RDAyerLKKRGIPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFLTK 295
Cdd:pfam00248 146 EKA---LTKGKIPIVAVQVEYNLLRRRQEE-ELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390678 296 LQPLLNRIKQIGENYSKTPTQIALNWLVAQ-GNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLA 363
Cdd:pfam00248 222 NLEALEALEEIAKEHGVSPAQVALRWALSKpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
58-366 |
4.17e-71 |
|
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: 224.00 E-value: 4.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 58 VTKLGIGVWSWGDNSYWNDfqwDDRKlkAAKGAFDTSLDNGIDFFDTAEVYGSkfslGaiSSETLLGRFIRERKErypga 137
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWGD---QDDE--ESIATIHAALDAGINFFDTAEAYGD----G--HSEEVLGKALKGRRD----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 138 EVSVATKFAalPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPglwgNEG-----YLDGLGDAVEQGLVKAVGVSNYSE 212
Cdd:cd19085 65 DVVIATKVS--PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP----SSDvpleeTMEALEKLKEEGKIRAIGVSNFGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 213 KRLRDAYERlkkrgIPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKYTP--ENPPSGPRGRIYT- 289
Cdd:cd19085 139 AQLEEALDA-----GRIDSNQLPYNLLWRAIEY-EILPFCREHGIGVLAYSPLAQGLLTGKFSSaeDFPPGDARTRLFRh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 290 --REFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASEI 366
Cdd:cd19085 213 fePGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
57-360 |
7.99e-67 |
|
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: 212.09 E-value: 7.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGvwSWGDNSYWNDFQWDDRK-LKAAKGAFDtsldNGIDFFDTAEVYGSKFSlgaissETLLGRFIRErkerYP 135
Cdd:cd19072 3 EVPVLGLG--TWGIGGGMSKDYSDDKKaIEALRYAIE----LGINLIDTAEMYGGGHA------EELVGKAIKG----FD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 GAEVSVATKFaaLPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGN-EGYLDGLGDAVEQGLVKAVGVSNYSEKR 214
Cdd:cd19072 67 REDLFITTKV--SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPiEETLRAMEELVEEGKIRYIGVSNFSLEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 215 LRDAYERLKKrgIPLASNQVNYSLIYRApEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENppsgprgriytreflt 294
Cdd:cd19072 145 LEEAQSYLKK--GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL---------------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 295 klqpllnrIKQIGENYSKTPTQIALNWLVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELR 360
Cdd:cd19072 206 --------LDEIAKKYGKTPAQIALNWLISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
49-359 |
1.81e-58 |
|
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: 192.41 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 49 VKLGGSDLKVTKLGIGVWSWGDNSYWndfQWDDRKlKAAKGAFDTSLDNGIDFFDTAEVYgskfSLGAisSETLLGRFIR 128
Cdd:cd19079 3 VRLGNSGLKVSRLCLGCMSFGDPKWR---PWVLDE-EESRPIIKRALDLGINFFDTANVY----SGGA--SEEILGRALK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 129 ERKERypgAEVSVATKFAAlPWR-------FGRESVVTALKDSLSRLELSSVDLYQLHWpglWGN----EGYLDGLGDAV 197
Cdd:cd19079 73 EFAPR---DEVVIATKVYF-PMGdgpngrgLSRKHIMAEVDASLKRLGTDYIDLYQIHR---WDYetpiEETLEALHDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 198 EQGLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRApEQTGVKAACDELGVTLIAYSPIAQGALTGKYTP 276
Cdd:cd19079 146 KSGKVRYIGASSMYAWQFAKALHLAEKNGwTKFVSMQNHYNLLYRE-EEREMIPLCEEEGIGVIPWSPLARGRLARPWGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 277 ENPpsgprgRIYTREFLTKLQ---------PLLNRIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGA 346
Cdd:cd19079 225 TTE------RRRSTTDTAKLKydyfteadkEIVDRVEEVAKERGVSMAQVALAWLLSKPGVtAPIVGATKLEHLEDAVAA 298
|
330
....*....|...
gi 18390678 347 IGWSLTDNEVSEL 359
Cdd:cd19079 299 LDIKLSEEEIKYL 311
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
55-363 |
2.04e-58 |
|
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: 191.78 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 55 DLKVTKLGIGVWSWGDNSYWND--F--QWDDRKLKAAkgaFDTSLDNGIDFFDTAEVYGskfsLGAisSETLLGRFIRer 130
Cdd:cd19103 1 DKKLPKIALGTWSWGSGGAGGDqvFgnHLDEDTLKAV---FDKAMAAGLNLWDTAAVYG----MGA--SEKILGEFLK-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 131 keRYPGAEVSVATKFAALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGlwGNEGYLDGLGDAVEQGLVKAVGVSNY 210
Cdd:cd19103 70 --RYPREDYIISTKFTPQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA--DVERWTPELIPLLKSGKVKHVGVSNH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 211 SEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENP-PSGP-RGRIY 288
Cdd:cd19103 146 NLAEIKRANEILAKAGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSgRAETY 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 289 TReFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLA 363
Cdd:cd19103 226 NP-LLPQLEELTAVMAEIGAKHGASIAQVAIAWAIAKG-TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLA 298
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
59-342 |
1.71e-55 |
|
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: 181.95 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 59 TKLGIGVWSWGDnsywndfqwdDRKLKAAKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRERKERypgAE 138
Cdd:cd06660 1 SRLGLGTMTFGG----------DGDEEEAFALLDAALEAGGNFFDTADVYG------DGRSERLLGRWLKGRGNR---DD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 139 VSVATKFAALPW------RFGRESVVTALKDSLSRLELSSVDLYQLHWPGL-WGNEGYLDGLGDAVEQGLVKAVGVSNYS 211
Cdd:cd06660 62 VVIATKGGHPPGgdpsrsRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPsTPVEETLEALNELVREGKIRYIGVSNWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 212 EKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGaltgkytpenppsgprgriytr 290
Cdd:cd06660 142 AERLAEALAYAKAHGlPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG---------------------- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18390678 291 efltklqpllnrikqigenysktPTQIALNWLVAQ-GNVIPIPGAKNAEQAKE 342
Cdd:cd06660 200 -----------------------PAQLALAWLLSQpFVTVPIVGARSPEQLEE 229
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
60-362 |
2.57e-55 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 182.18 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 60 KLGIGVWswgdnsywndfQWDDRKLKAA-KGAfdtsLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRE----RKEry 134
Cdd:COG0656 7 ALGLGTW-----------QLPGEEAAAAvRTA----LEAGYRHIDTAAMYGN---------EEGVGEAIAAsgvpREE-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 135 pgaeVSVATKFaaLPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKR 214
Cdd:COG0656 61 ----LFVTTKV--WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 215 LRDAYERLkkrGIPLASNQVNYSLIYRapeQTGVKAACDELGVTLIAYSPIAQGALtgkytPENPPsgprgriytreflt 294
Cdd:COG0656 135 LEELLAET---GVKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRGKL-----LDDPV-------------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390678 295 klqpllnrIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:COG0656 190 --------LAEIAEKHGKTPAQVVLRWHLQRG-VVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
48-361 |
3.26e-55 |
|
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: 184.01 E-value: 3.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGVWSWGDNSYWNDFqwDDRKlkaAKGAFDTSLDNGIDFFDTAEVYGskfsLGAisSETLLGRFI 127
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWWGGS--DDNE---SIRTIHAALDLGINLIDTAPAYG----FGH--SEEIVGKAI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERKErypgaEVSVATKFAaLPWR------------------FGRESVVTALKDSLSRLELSSVDLYQLHWPGlwgNE-- 187
Cdd:cd19149 70 KGRRD-----KVVLATKCG-LRWDreggsfffvrdgvtvyknLSPESIREEVEQSLKRLGTDYIDLYQTHWQD---VEtp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 188 -----GYLDGLgdaVEQGLVKAVGVSNYSEKRLrDAYERLKkrgiPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAY 262
Cdd:cd19149 141 ieetmEALEEL---KRQGKIRAIGASNVSVEQI-KEYVKAG----QLDIIQEKYSMLDRGIEKE-LLPYCKKNNIAFQAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 263 SPIAQGALTGKYTP--ENPPSGPRGRI--YTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQ-GNVIPIPGAKNA 337
Cdd:cd19149 212 SPLEQGLLTGKITPdrEFDAGDARSGIpwFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQpGITSALCGARKP 291
|
330 340
....*....|....*....|....
gi 18390678 338 EQAKEFAGAIGWSLTDNEVSELRS 361
Cdd:cd19149 292 EQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
58-363 |
6.28e-55 |
|
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: 182.87 E-value: 6.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 58 VTKLGIGVWSWG--DNSYWNDFQWDDRKLKAAKGAFDTsldnGIDFFDTAEVYGskfsLGaiSSETLLGRFIRERKERyp 135
Cdd:cd19102 1 LTTIGLGTWAIGggGWGGGWGPQDDRDSIAAIRAALDL----GINWIDTAAVYG----LG--HSEEVVGRALKGLRDR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gaeVSVATKFAALPWRFGR-------ESVVTALKDSLSRLELSSVDLYQLHWPGlwGNEGYLDG---LGDAVEQGLVKAV 205
Cdd:cd19102 69 ---PIVATKCGLLWDEEGRirrslkpASIRAECEASLRRLGVDVIDLYQIHWPD--PDEPIEEAwgaLAELKEEGKVRAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 206 GVSNYSEkrlrDAYERLKKRGiPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRG 285
Cdd:cd19102 144 GVSNFSV----DQMKRCQAIH-PIASLQPPYSLLRRGIEA-EILPFCAEHGIGVIVYSPMQSGLLTGKMTPERVASLPAD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 286 --RIYTREF----LTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSLTDNEVSE 358
Cdd:cd19102 218 dwRRRSPFFqepnLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTsAIVGARRPDQIDETVGAADLRLTPEELAE 297
|
....*
gi 18390678 359 LRSLA 363
Cdd:cd19102 298 IEALL 302
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
50-359 |
1.04e-54 |
|
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: 182.81 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSWGDNSYWNDfQWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYgskfSLGAisSETLLGRFIRE 129
Cdd:cd19091 5 TLGRSGLKVSELALGTMTFGGGGGFFG-AWGGVDQEEADRLVDIALDAGINFFDTADVY----SEGE--SEEILGKALKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERypgaeVSVATKFAalpWRFG---------RESVVTALKDSLSRLELSSVDLYQLH-WPGLWGNEGYLDGLGDAVEQ 199
Cdd:cd19091 78 RRDD-----VLIATKVR---GRMGegpndvglsRHHIIRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTPEN 278
Cdd:cd19091 150 GKVRYIGVSNFSAWQIMKALGISERRGlARFVALQAYYSLLGRDLEHE-LMPLALDQGVGLLVWSPLAGGLLSGKYRRGQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 279 P-PSGPRGRIYTREFL----TKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAIGWSLT 352
Cdd:cd19091 229 PaPEGSRLRRTGFDFPpvdrERGYDVVDALREIAKETGATPAQVALAWLLSRPTVsSVIIGARNEEQLEDNLGAAGLSLT 308
|
....*..
gi 18390678 353 DNEVSEL 359
Cdd:cd19091 309 PEEIARL 315
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
50-359 |
2.70e-52 |
|
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: 176.25 E-value: 2.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSWGDNSywndfqwdDRKlkAAKGAFDTSLDNGIDFFDTAEVYGS--KFSLGAiSSETLLGRFI 127
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTA--------DEE--TSFALLDAFVDAGGNFIDTADVYSAwvPGNAGG-ESETIIGRWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERKERypgAEVSVATKFAALPWRFG----RESVVTALKDSLSRLELSSVDLYQLHWpglWGN----EGYLDGLGDAVEQ 199
Cdd:cd19081 70 KSRGKR---DRVVIATKVGFPMGPNGpglsRKHIRRAVEASLRRLQTDYIDLYQAHW---DDPatplEETLGALNDLIRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIP-LASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPEN 278
Cdd:cd19081 144 GKVRYIGASNYSAWRLQEALELSRQHGLPrYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 279 PPSG--PRGRIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSLTDNE 355
Cdd:cd19081 224 DLPGstRRGEAAKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGVTaPIAGARTVEQLEDLLAAAGLRLTDEE 303
|
....
gi 18390678 356 VSEL 359
Cdd:cd19081 304 VARL 307
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
48-359 |
1.64e-50 |
|
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: 171.24 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGVWSWGDNsywndfqWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFI 127
Cdd:cd19076 2 TRKLGTQGLEVSALGLGCMGMSAF-------YGPADEEESIATLHRALELGVTFLDTADMYGPG------TNEELLGKAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERKErypgaEVSVATKFAALpWRFG---------RESVVTALKDSLSRLELSSVDLYQLH-------WPGLWGnegyld 191
Cdd:cd19076 69 KDRRD-----EVVIATKFGIV-RDPGsgfrgvdgrPEYVRAACEASLKRLGTDVIDLYYQHrvdpnvpIEETVG------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 192 GLGDAVEQGLVKAVGVSNYSEKRLRDAYerlkkRGIPLASNQVNYSLIYRAPEqTGVKAACDELGVTLIAYSPIAQGALT 271
Cdd:cd19076 137 AMAELVEEGKVRYIGLSEASADTIRRAH-----AVHPITAVQSEYSLWTRDIE-DEVLPTCRELGIGFVAYSPLGRGFLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 272 GKYT-PENPPSGPRGRIYTR---EFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQG-NVIPIPGAKNAEQAKEFAGA 346
Cdd:cd19076 211 GAIKsPEDLPEDDFRRNNPRfqgENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGdDIVPIPGTKRIKYLEENVGA 290
|
330
....*....|...
gi 18390678 347 IGWSLTDNEVSEL 359
Cdd:cd19076 291 LDVVLTPEELAEI 303
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
53-359 |
5.37e-50 |
|
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: 168.97 E-value: 5.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 53 GSDLKVTKLGIGVWSWGDnsywndfqwDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslGAisSETLLGRFIRERKE 132
Cdd:cd19138 6 PDGTKVPALGQGTWYMGE---------DPAKRAQEIEALRAGIDLGMTLIDTAEMYGD----GG--SEELVGEAIRGRRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 133 rypgaEVSVATKfaALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSE 212
Cdd:cd19138 71 -----KVFLVSK--VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 213 KRLRDAYERLKkrGIPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTPENPpsgprgriytref 292
Cdd:cd19138 144 DDMEELWAVPG--GGNCAANQVLYNLGSRGIEYD-LLPWCREHGVPVMAYSPLAQGGLLRRGLLENP------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 293 ltklqpllnRIKQIGENYSKTPTQIALNWLVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSEL 359
Cdd:cd19138 208 ---------TLKEIAARHGATPAQVALAWVLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
56-346 |
1.61e-48 |
|
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: 164.19 E-value: 1.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 56 LKVTKLGIGVWSWGdNSYWNDFqwDDRKlkaAKGAFDTSLDNGIDFFDTAEVYGSkfslGAisSETLLGRFIRERKERyp 135
Cdd:cd19086 1 LEVSEIGFGTWGLG-GDWWGDV--DDAE---AIRALRAALDLGINFFDTADVYGD----GH--SERLLGKALKGRRDK-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gaeVSVATKF-------AALPWRFGRESVVTALKDSLSRLELSSVDLYQLH-WPGLW-GNEGYLDGLGDAVEQGLVKAVG 206
Cdd:cd19086 67 ---VVIATKFgnrfdggPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVlDNDELFEALEKLKQEGKIRAYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 207 VSNyseKRLRDAYERLKKRGIplASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKytpenppsgprgr 286
Cdd:cd19086 144 VSV---GDPEEALAALRRGGI--DVVQVIYNLLDQRPEEE-LFPLAEEHGVGVIARVPLASGLLTGK------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390678 287 iytrefltklqpllnrikqigenysktPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGA 346
Cdd:cd19086 205 ---------------------------LAQAALRFILSHPAVsTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
57-355 |
2.78e-46 |
|
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: 158.89 E-value: 2.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWSWGDNSYwNDFQWDDRKLKAAKgafdTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRErkerYPG 136
Cdd:cd19137 3 KIPALGLGTWGIGGFLT-PDYSRDEEMVELLK----TAIELGYTHIDTAEMYG------GGHTEELVGKAIKD----FPR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 137 AEVSVATKfaALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPglwgN-----EGYLDGLGDAVEQGLVKAVGVSNYS 211
Cdd:cd19137 68 EDLFIVTK--VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP----NpniplEETLSAMAEGVRQGLIRYIGVSNFN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 212 EKRLRDAYERLKKrgiPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTpenppsgprgriytre 291
Cdd:cd19137 142 RRLLEEAISKSQT---PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRT---------------- 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390678 292 fltklqpllnrIKQIGENYSKTPTQIALNWLVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNE 355
Cdd:cd19137 203 -----------LEEIAKNYGKTIAQIALAWLIQKPNVVAIPKAGRVEHLKENLKATEIKLSEEE 255
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
56-354 |
5.25e-44 |
|
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: 153.90 E-value: 5.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 56 LKVTKLGIGVWSWgdnsywnDFQWDDrkLKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRerkeRYP 135
Cdd:cd19074 2 LKVSELSLGTWLT-------FGGQVD--DEDAKACVRKAYDLGINFFDTADVYAAG------QAEEVLGKALK----GWP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 GAEVSVATKfaaLPWRFG---------RESVVTALKDSLSRLELSSVDLYQLHWPG----LwgnEGYLDGLGDAVEQGLV 202
Cdd:cd19074 63 RESYVISTK---VFWPTGpgpndrglsRKHIFESIHASLKRLQLDYVDIYYCHRYDpetpL---EETVRAMDDLIRQGKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 203 KAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKYTPE-NPP 280
Cdd:cd19074 137 LYWGTSEWSAEQIAEAHDLARQFGlIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGiPPP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 281 SGPR----------GRIYTREFLTKLQpllnRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGW 349
Cdd:cd19074 216 SRSRatdednrdkkRRLLTDENLEKVK----KLKPIADELGLTLAQLALAWCLRNPAVSsAIIGASRPEQLEENVKASGV 291
|
....*
gi 18390678 350 SLTDN 354
Cdd:cd19074 292 KLSPE 296
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
51-362 |
3.85e-43 |
|
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: 151.96 E-value: 3.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVWSWGDNSywndfqwdDRKlkAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRER 130
Cdd:cd19087 6 LGRTGLKVSRLCLGTMNFGGRT--------DEE--TSFAIMDRALDAGINFFDTADVYGGG------RSEEIIGRWIAGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 131 KErypgaEVSVATKF----AALPWRFG--RESVVTALKDSLSRLELSSVDLYQLH-------WpglwgnEGYLDGLGDAV 197
Cdd:cd19087 70 RD-----DIVLATKVfgpmGDDPNDRGlsRRHIRRAVEASLRRLQTDYIDLYQMHhfdrdtpL------EETLRALDDLV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 198 EQGLVKAVGVSNYSEKRLRDAYERLKKRGI-PLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTP 276
Cdd:cd19087 139 RQGKIRYIGVSNFAAWQIAKAQGIAARRGLlRFVSEQPMYNLLKRQAELE-ILPAARAYGLGVIPYSPLAGGLLTGKYGK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 277 ENPPSGPRG----RIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSL 351
Cdd:cd19087 218 GKRPESGRLveraRYQARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTsPIIGPRTLEQLEDSLAALEITL 297
|
330
....*....|.
gi 18390678 352 TDNEVSELRSL 362
Cdd:cd19087 298 TPELLAEIDEL 308
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
47-371 |
4.33e-43 |
|
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: 152.60 E-value: 4.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 47 SKVKLGGSDLKVTKLGIGvwSWGDNSYWNDFQWDDRKLKAakgaFDTSLDNGIDFFDTAEVYGSkfslgaisSETLLGRF 126
Cdd:cd19144 2 PTRTLGRNGPSVPALGFG--AMGLSAFYGPPKPDEERFAV----LDAAFELGCTFWDTADIYGD--------SEELIGRW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 127 irerKERYPG--AEVSVATKF-------AALPWRFGR-ESVVTALKDSLSRLELSSVDLYQLH-WPGLWGNEGYLDGLGD 195
Cdd:cd19144 68 ----FKQNPGkrEKIFLATKFgieknveTGEYSVDGSpEYVKKACETSLKRLGVDYIDLYYQHrVDGKTPIEKTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 196 AVEQGLVKAVGVSNYSEKRLRDAYERLkkrgiPLASNQVNYSLIYRAPE--QTGVKAACDELGVTLIAYSPIAQGALTGK 273
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLRRAHAVH-----PIAAVQIEYSPFSLDIErpEIGVLDTCRELGVAIVAYSPLGRGFLTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 274 YT-PENPPSG------PRgriYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGN-VIPIPGAKNAEQAKEFAG 345
Cdd:cd19144 219 IRsPDDFEEGdfrrmaPR---FQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDdIIPIPGTTKLKRLEENLG 295
|
330 340
....*....|....*....|....*.
gi 18390678 346 AIGWSLTDNEVSELRSLASEIkPVVG 371
Cdd:cd19144 296 ALKVKLTEEEEKEIREIAEEA-EVVG 320
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
93-360 |
8.91e-43 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 150.85 E-value: 8.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 93 TSLDNGIDFFDTAEVYGSKFSLgaiSSETLLGRFIRERKERYPGAEVSV--ATKFAALPWRFGRESVVTALKDSLSRL-E 169
Cdd:cd19077 33 AALDAGSNLWNGGEFYGPPDPH---ANLKLLARFFRKYPEYADKVVLSVkgGLDPDTLRPDGSPEAVRKSIENILRALgG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 170 LSSVDLYQL-----HWPglwgNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYerlkkRGIPLASNQVNYSLIYRAPE 244
Cdd:cd19077 110 TKKIDIFEParvdpNVP----IEETIKALKELVKEGKIRGIGLSEVSAETIRRAH-----AVHPIAAVEVEYSLFSREIE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 245 QTGVKAACDELGVTLIAYSPIAQGALTGKY-TPENPPSGPRGRIYTR---EFLTKLQPLLNRIKQIGENYSKTPTQIALN 320
Cdd:cd19077 181 ENGVLETCAELGIPIIAYSPLGRGLLTGRIkSLADIPEGDFRRHLDRfngENFEKNLKLVDALQELAEKKGCTPAQLALA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18390678 321 WLVAQGN--VIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELR 360
Cdd:cd19077 261 WILAQSGpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
60-359 |
2.50e-42 |
|
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: 148.40 E-value: 2.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 60 KLGIGVWSWGDNsywndfqwddrklkAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKerYPGAEV 139
Cdd:cd19071 3 LIGLGTYKLKPE--------------ETAEAVLAALEAGYRHIDTAAAYGN---------EAEVGEAIRESG--VPREEL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 140 SVATKFAalPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEG----YLD---GLGDAVEQGLVKAVGVSNYSE 212
Cdd:cd19071 58 FITTKLW--PTDHGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGskeaRLEtwrALEELVDEGLVRSIGVSNFNV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 213 KRLrdayERLKK-RGIPLASNQVNYSLIYRAPEqtgVKAACDELGVTLIAYSPIAQGALTGKytpENPpsgprgriytre 291
Cdd:cd19071 136 EHL----EELLAaARIKPAVNQIELHPYLQQKE---LVEFCKEHGIVVQAYSPLGRGRRPLL---DDP------------ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390678 292 fltklqpllnRIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSEL 359
Cdd:cd19071 194 ----------VLKEIAKKYGKTPAQVLLRWALQRG-VVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
79-361 |
6.41e-42 |
|
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: 148.90 E-value: 6.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 79 WDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaisSETLLGRFIRERKERYPGA-EVSVATKFAALPWRFG--RE 155
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--------AEELIGEFRKRLRRERDAAdDVQIHTKWVPDPGELTmtRA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 156 SVVTALKDSLSRLELSSVDLYQLHWpglW--GNEGYLDG---LGDAVEQGLVKAVGVSNYSEKRLRDAYERlkkrGIPLA 230
Cdd:cd19101 89 YVEAAIDRSLKRLGVDRLDLVQFHW---WdySDPGYLDAakhLAELQEEGKIRHLGLTNFDTERLREILDA----GVPIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 231 SNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKY--TPE------NPPSGPRGRIYTREFL--TKLQPLL 300
Cdd:cd19101 162 SNQVQYSLLDRRPEN-GMAALCEDHGIKLLAYGTLAGGLLSEKYlgVPEptgpalETRSLQKYKLMIDEWGgwDLFQELL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390678 301 NRIKQIGENYSKTPTQIALNW-LVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRS 361
Cdd:cd19101 241 RTLKAIADKHGVSIANVAVRWvLDQPGVAGVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
93-359 |
2.32e-41 |
|
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: 147.38 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 93 TSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRERKErypgaEVSVATKFAalpWRFGRESVVT------------A 160
Cdd:cd19078 33 KAVELGITFFDTAEVYG------PYTNEELVGEALKPFRD-----QVVIATKFG---FKIDGGKPGPlgldsrpehirkA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 161 LKDSLSRLELSSVDLYQLHWPGLwgN---EGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLkkrgiPLASNQVNYS 237
Cdd:cd19078 99 VEGSLKRLQTDYIDLYYQHRVDP--NvpiEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC-----PVTAVQSEYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 238 LIYRAPEqTGVKAACDELGVTLIAYSPIAQGALTGKYTPEN--PPSGPRGRI--YTREFLTKLQPLLNRIKQIGENYSKT 313
Cdd:cd19078 172 MMWREPE-KEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfDEGDDRASLprFTPEALEANQALVDLLKEFAEEKGAT 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 18390678 314 PTQIALNWLVAQG-NVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSEL 359
Cdd:cd19078 251 PAQIALAWLLAKKpWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
51-359 |
3.14e-41 |
|
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: 146.98 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVWSWGDNSYWNdfqWDDrklKAAKGAFDTSLDNGIDFFDTAEVY--GSkfslgaisSETLLGRFIR 128
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWG---ADR---EEARAMFDAYVEAGGNFIDTANNYtnGT--------SERLLGEFIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 129 ERKERypgaeVSVATKFAALPWRF-------GRESVVTALKDSLSRLELSSVDLYQLH-WPGLWGNEGYLDGLGDAVEQG 200
Cdd:cd19080 69 GNRDR-----IVLATKYTMNRRPGdpnaggnHRKNLRRSVEASLRRLQTDYIDLLYVHaWDFTTPVEEVMRALDDLVRAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 201 LVKAVGVSNYSEKRLRDAYERLKKRGI-PLASNQVNYSLIYRAPEQTGVKAAcDELGVTLIAYSPIAQGALTGKYTPENP 279
Cdd:cd19080 144 KVLYVGISDTPAWVVARANTLAELRGWsPFVALQIEYSLLERTPERELLPMA-RALGLGVTPWSPLGGGLLTGKYQRGEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 280 PSGpRGRIYTREFLTKLQPLLNRI----KQIGENYSKTPTQIALNWLVAQ-GNVIPIPGAKNAEQAKEFAGAIGWSLTDN 354
Cdd:cd19080 223 GRA-GEAKGVTVGFGKLTERNWAIvdvvAAVAEELGRSAAQVALAWVRQKpGVVIPIIGARTLEQLKDNLGALDLTLSPE 301
|
....*
gi 18390678 355 EVSEL 359
Cdd:cd19080 302 QLARL 306
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
91-346 |
6.21e-41 |
|
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: 145.77 E-value: 6.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 91 FDTSLDNGIDFFDTAEVYGSKFSLGAisSETLLGRFIRERKERypgAEVSVATKFA------ALPWRFGRESVVTALKDS 164
Cdd:cd19082 23 LDAFVELGGNFIDTARVYGDWVERGA--SERVIGEWLKSRGNR---DKVVIATKGGhpdledMSRSRLSPEDIRADLEES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 165 LSRLELSSVDLYQLHW-----PGlwgnEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGI-PLASNQVNYSL 238
Cdd:cd19082 98 LERLGTDYIDLYFLHRddpsvPV----GEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLpGFAASSPQWSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 239 IYRAPE----QTGVKAACDEL------GVTLIAYSPIAQGALTGKYTPE-NPPSGPRGRIYTREFLTKLQpllnRIKQIG 307
Cdd:cd19082 174 ARPNEPpwpgPTLVAMDEEMRawheenQLPVFAYSSQARGFFSKRAAGGaEDDSELRRVYYSEENFERLE----RAKELA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18390678 308 ENYSKTPTQIALNWLVAQG-NVIPIPGAKNAEQAKEFAGA 346
Cdd:cd19082 250 EEKGVSPTQIALAYVLNQPfPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
55-358 |
8.03e-41 |
|
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: 145.91 E-value: 8.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 55 DLKVTKLGIGVWSWGDnsyWndfQWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGskFSLgaisSETLLGRFIRERKERy 134
Cdd:cd19148 1 DLPVSRIALGTWAIGG---W---MWGGTDEKEAIETIHKALDLGINLIDTAPVYG--FGL----SEEIVGKALKEYGKR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 135 pgAEVSVATKFAaLPWRFG--------RESVVTALKDSLSRLELSSVDLYQLHWPG-LWGNEGYLDGLGDAVEQGLVKAV 205
Cdd:cd19148 68 --DRVVIATKVG-LEWDEGgevvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDpLVPIEETAEALKELLDEGKIRAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 206 GVSNYSEKRLrdayERLKKrGIPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRg 285
Cdd:cd19148 145 GVSNFSPEQM----ETFRK-VAPLHTVQPPYNLFEREIEKD-VLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDD- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 286 riyTREFLTKLQP-----------LLNRIKQigENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAIGWSLTD 353
Cdd:cd19148 218 ---LRRTDPKFQEprfsqylaaveELDKLAQ--ERYGKSVIHLAVRWLLDQPGVsIALWGARKPEQLDAVDEVFGWSLND 292
|
....*
gi 18390678 354 NEVSE 358
Cdd:cd19148 293 EDMKE 297
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
48-362 |
1.49e-39 |
|
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: 142.56 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGV-WSWGDNSYWNDFQWDDRKL-KAAkgafdtsLDNGIDFFDTAEVYGSKfslgaiSSETLLGR 125
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTnAVGGHNLYPNLDEEEGKDLvREA-------LDNGVNLLDTAFIYGLG------RSEELVGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 126 FIRERKErypgAEVSVATKFAAlpwRFGRESVV---------TALKDSLSRLELSSVDLYQLHWPglwgnegylDG---L 193
Cdd:cd19083 68 VLKEYNR----NEVVIATKGAH---KFGGDGSVlnnspeflrSAVEKSLKRLNTDYIDLYYIHFP---------DGetpK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 194 GDAV-------EQGLVKAVGVSNYSEKRLRDAyerlKKRGIpLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIA 266
Cdd:cd19083 132 AEAVgalqelkDEGKIRAIGVSNFSLEQLKEA----NKDGY-VDVLQGEYNLLQREAEE-DILPYCVENNISFIPYFPLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 267 QGALTGKYTPEN--PPSGPRGRI--YTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAK 341
Cdd:cd19083 206 SGLLAGKYTKDTkfPDNDLRNDKplFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIdVVIPGAKRAEQVI 285
|
330 340
....*....|....*....|.
gi 18390678 342 EFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19083 286 DNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
91-353 |
1.94e-39 |
|
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: 142.70 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 91 FDTSLDNGIDFFDTAEVY---GSKFSLGAisSETLLGRFIRERKERypgAEVSVATKFA----ALPW------RFGRESV 157
Cdd:cd19094 24 LDYAFDEGVNFIDTAEMYpvpPSPETQGR--TEEIIGSWLKKKGNR---DKVVLATKVAgpgeGITWprgggtRLDRENI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 158 VTALKDSLSRLELSSVDLYQLHWP----GLWGNEGY---------------LDGLGDAVEQGLVKAVGVSNYSEKRLRDA 218
Cdd:cd19094 99 REAVEGSLKRLGTDYIDLYQLHWPdrytPLFGGGYYtepseeedsvsfeeqLEALGELVKAGKIRHIGLSNETPWGVMKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 219 YERLKKRGIP-LASNQVNYSLIYRAPEqTGVKAACDELGVTLIAYSPIAQGALTGKYT-PENPPSGPRGRIYTREFLTKL 296
Cdd:cd19094 179 LELAEQLGLPrIVSIQNPYSLLNRNFE-EGLAEACHRENVGLLAYSPLAGGVLTGKYLdGAARPEGGRLNLFPGYMARYR 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 297 QPL----LNRIKQIGENYSKTPTQIALNW-----LVAQgNVIpipGAKNAEQAKEFAGAIGWSLTD 353
Cdd:cd19094 258 SPQaleaVAEYVKLARKHGLSPAQLALAWvrsrpFVTS-TII---GATTLEQLKENIDAFDVPLSD 319
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
79-360 |
3.40e-39 |
|
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: 139.71 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 79 WDDRKlKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRErkERYPGAEVSVATKFaalpWR--FGRES 156
Cdd:cd19073 9 WQLRG-DDCANAVKEALELGYRHIDTAEIYNN---------EAEVGEAIAE--SGVPREDLFITTKV----WRdhLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 157 VVTALKDSLSRLELSSVDLYQLHWPglwgNEGY-----LDGLGDAVEQGLVKAVGVSNYSEKRLRDAyerLKKRGIPLAS 231
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIHWP----NPTVpleetLGALKELKEAGKVKSIGVSNFTIELLEEA---LDISPLPIAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 232 NQVNYSLIYRapeQTGVKAACDELGVTLIAYSPIAQGALtgkytPENPPsgprgriytrefltklqpllnrIKQIGENYS 311
Cdd:cd19073 146 NQVEFHPFLY---QAELLEYCRENDIVITAYSPLARGEV-----LRDPV----------------------IQEIAEKYD 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 18390678 312 KTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELR 360
Cdd:cd19073 196 KTPAQVALRWLVQKG-IVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
85-362 |
3.21e-38 |
|
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: 137.39 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 85 KAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKerYPGAEVSVATKfaALPWRFGRESVVTALKDS 164
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYGN---------EAQVGEAIAASG--VPRDELFLTTK--VWPDNYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 165 LSRLELSSVDLYQLHWPGLWG-NEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLkkrGIPLASNQVNYSLIYRap 243
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPNKDVpLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELS---EAPLFTNQVEYHPYLD-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 244 eQTGVKAACDELGVTLIAYSPIAQGALTGkytpenppsgprgriytrefltklQPLLNRIkqiGENYSKTPTQIALNWLV 323
Cdd:cd19140 163 -QRKLLDAAREHGIALTAYSPLARGEVLK------------------------DPVLQEI---GRKHGKTPAQVALRWLL 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 18390678 324 AQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19140 215 QQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
48-359 |
3.80e-35 |
|
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: 130.63 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGVWswGDNSYWNDFQWDDRKLKAAKGAFDTsldnGIDFFDTAEVYGSKfslgaiSSETLLGRFI 127
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCM--GLSGDYGAPKPEEEGIALIHHAFNS----GVTFLDTSDIYGPN------TNEVLLGKAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERkeryPGAEVSVATKFA-ALPWRFGRES------VVTALKDSLSRLELSSVDLYQLHW-----PglwgNEGYLDGLGD 195
Cdd:cd19145 70 KDG----PREKVQLATKFGiHEIGGSGVEVrgdpayVRAACEASLKRLDVDYIDLYYQHRidttvP----IEITMGELKK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 196 AVEQGLVKAVGVSNYSEKRLRDAYERLkkrgiPLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYT 275
Cdd:cd19145 142 LVEEGKIKYIGLSEASADTIRRAHAVH-----PITAVQLEWSLWTRDIEEE-IIPTCRELGIGIVPYSPLGRGFFAGKAK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 276 PENPPSG-------PRgriYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGN-VIPIPGAKNAEQAKEFAGAI 347
Cdd:cd19145 216 LEELLENsdvrkshPR---FQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEdVVPIPGTTKIKNLNQNIGAL 292
|
330
....*....|..
gi 18390678 348 GWSLTDNEVSEL 359
Cdd:cd19145 293 SVKLTKEDLKEI 304
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
50-347 |
2.14e-34 |
|
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: 128.91 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSwgDNSYWNDFQwddrklkAAKGAFDTSLDNGIDFFDTAEVYGSkfSLGaiSSETLLGRFIRE 129
Cdd:cd19089 3 RCGRSGLHLPAISLGLWH--NFGDYTSPE-------EARELLRTAFDLGITHFDLANNYGP--PPG--SAEENFGRILKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYPgAEVSVATKFAALPW-----RFG-RESVVTALKDSLSRLELSSVDLYQLHWPG----LwgnEGYLDGLGDAVEQ 199
Cdd:cd19089 70 DLRPYR-DELVISTKAGYGMWpgpygDGGsRKYLLASLDQSLKRMGLDYVDIFYHHRYDpdtpL---EETMTALADAVRS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEqTGVKAACDELGVTLIAYSPIAQGALTGKYTPENP 279
Cdd:cd19089 146 GKALYVGISNYPGAKARRAIALLRELGVPLIIHQPRYSLLDRWAE-DGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIP 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390678 280 PS----GPRGRIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVIP-IPGAKNAEQAKEFAGAI 347
Cdd:cd19089 225 PDsrraAESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSvLIGASSPSQLEDNVAAL 297
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
58-352 |
1.15e-33 |
|
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: 125.41 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 58 VTKLGIGVWSWGdnsyWNDFQWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKFSlgaissETLLGRFIRERKERypga 137
Cdd:cd19088 1 VSRLGYGAMRLT----GPGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVN------ERLIAEALHPYPDD---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 138 eVSVATKFAAL-----PW-RFGR-ESVVTALKDSLSRLELSSVDLYQLHWPGLWGN-EGYLDGLGDAVEQGLVKAVGVSN 209
Cdd:cd19088 67 -VVIATKGGLVrtgpgWWgPDGSpEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPfEEQLGALAELQDEGLIRHIGLSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 210 YSEKRLRDAyerlkkRGI-PLASNQVNYSLIYRAPEqtGVKAACDELGVTLIAYSPIAQGALTgkytpenPPSGPrgriy 288
Cdd:cd19088 146 VTVAQIEEA------RAIvRIVSVQNRYNLANRDDE--GVLDYCEAAGIAFIPWFPLGGGDLA-------QPGGL----- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 289 trefltklqpllnrIKQIGENYSKTPTQIALNWLVAQGNVI-PIPGAKNAEQAKEFAGAIGWSLT 352
Cdd:cd19088 206 --------------LAEVAARLGATPAQVALAWLLARSPVMlPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
52-348 |
4.27e-33 |
|
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: 125.26 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 52 GGSDLKVTKLGIGVW-SWGDnsywndfqwdDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKFSlgaiSSETLLGRFIRER 130
Cdd:cd19150 6 GKSGLKLPALSLGLWhNFGD----------DTPLETQRAILRTAFDLGITHFDLANNYGPPPG----SAEENFGRILRED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 131 KERYPGaEVSVATK--FAALPWRFG----RESVVTALKDSLSRLELSSVDLYQLH-----WPglwgNEGYLDGLGDAVEQ 199
Cdd:cd19150 72 FAGYRD-ELIISTKagYDMWPGPYGewgsRKYLLASLDQSLKRMGLDYVDIFYSHrfdpdTP----LEETMGALDHAVRS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKY---TP 276
Cdd:cd19150 147 GKALYVGISSYSPERTREAAAILRELGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYlngIP 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 277 ENPPSGpRGRIYTREFLTklQPLLNRIK---QIGENYSKTPTQIALNWLVAQGNVIP-IPGAKNAEQAKEFAGAIG 348
Cdd:cd19150 227 EGSRAS-KERSLSPKMLT--EANLNSIRalnEIAQKRGQSLAQMALAWVLRDGRVTSaLIGASRPEQLEENVGALD 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
53-352 |
5.33e-32 |
|
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: 121.89 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 53 GSDLKVTKLGIGVWSWGDNsywndfqWDDRKlkAAKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRERke 132
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADW-------GESAE--ELLSLIEAALELGITTFDHADIYG------GGKCEELFGEALALN-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 133 ryPGA--EVSVATK------FAALPWRFGR-----ESVVTALKDSLSRLELSSVDLYQLHWPglwgnegylDGLGDAVE- 198
Cdd:cd19092 64 --PGLreKIEIQTKcgirlgDDPRPGRIKHydtskEHILASVEGSLKRLGTDYLDLLLLHRP---------DPLMDPEEv 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 199 ---------QGLVKAVGVSNYSEKRLrdayERLKKR-GIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQG 268
Cdd:cd19092 133 aeafdelvkSGKVRYFGVSNFTPSQI----ELLQSYlDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 269 ALTGkytpenppsgprgriytrEFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQ-GNVIPIPGAKNAEQAKEFAGAI 347
Cdd:cd19092 209 RLFG------------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHpARIQPILGTTNPERIRSAVKAL 270
|
....*
gi 18390678 348 GWSLT 352
Cdd:cd19092 271 DIELT 275
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
86-347 |
5.07e-31 |
|
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: 119.58 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 86 AAKGAFDTSLDNGIDFFDTAEVYGSkfslGAisSETLLGRFirerkeRYPGAEVSVATKfaALPWRFG---RESVVTALK 162
Cdd:cd19075 21 AAAELLDAFLERGHTEIDTARVYPD----GT--SEELLGEL------GLGERGFKIDTK--ANPGVGGglsPENVRKQLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 163 DSLSRLELSSVDLYQLHWPG----LwgnEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIPLAS-NQVNYS 237
Cdd:cd19075 87 TSLKRLKVDKVDVFYLHAPDrstpL---EETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTvYQGMYN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 238 LIYRAPEqTGVKAACDELGVTLIAYSPIAQGALTGKYTPENP--------PSGPRGRIYTREFLTK-LQPLLNRIKQIGE 308
Cdd:cd19075 164 AITRQVE-TELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDkagggrfdPNNALGKLYRDRYWKPsYFEALEKVEEAAE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18390678 309 NYSKTPTQIALNWLV-------AQGNVIpIPGAKNAEQAKEFAGAI 347
Cdd:cd19075 243 KEGISLAEAALRWLYhhsaldgEKGDGV-ILGASSLEQLEENLAAL 287
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
79-362 |
5.18e-31 |
|
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: 119.31 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 79 WDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKERypG----AEVSVATKFaalpW--RF 152
Cdd:cd19116 19 WKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGN---------EAEVGEAIREKIAE--GvvkrEDLFITTKL----WnsYH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 153 GRESVVTALKDSLSRLELSSVDLYQLHWP--------------GLWGNEGYLD---GLGDAVEQGLVKAVGVSNYSEKRL 215
Cdd:cd19116 84 EREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesngdGSLSDIDYLEtwrGMEDLVKLGLTRSIGVSNFNSEQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 216 RDAYERLKkrgIPLASNQVNYSLIYrapEQTGVKAACDELGVTLIAYSPIaqgaltGKYTPENPPSGPRgRIYTrefltk 295
Cdd:cd19116 164 NRLLSNCN---IKPAVNQIEVHPTL---TQEKLVAYCQSNGIVVMAYSPF------GRLVPRGQTNPPP-RLDD------ 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 296 lqpllNRIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19116 225 -----PTLVAIAKKYGKTTAQIVLRYLI-DRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSF 285
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
95-365 |
1.98e-30 |
|
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: 117.33 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 95 LDNGIDFFDTAEVYGSKFSLGAISSETLLgrfirERKERYpgaevsVATKfaalpWRFGRESVVTALKDSLSRLELSSVD 174
Cdd:cd19120 35 LKAGFRHIDTAEMYGNEKEVGEALKESGV-----PREDLF------ITTK-----VSPGIKDPREALRKSLAKLGVDYVD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 175 LYQLHWPGLWGNEGY-LDG----LGDAVEQGLVKAVGVSNYsekRLRDAYERLKKRGIPLASNQVNYSlIYRAPEQTGVK 249
Cdd:cd19120 99 LYLIHSPFFAKEGGPtLAEawaeLEALKDAGLVRSIGVSNF---RIEDLEELLDTAKIKPAVNQIEFH-PYLYPQQPALL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 250 AACDELGVTLIAYSPIAqgALTGKytpenpPSGPrgriytrefltkLQPLLNRikqIGENYSKTPTQIALNWLVAQGnVI 329
Cdd:cd19120 175 EYCREHGIVVSAYSPLS--PLTRD------AGGP------------LDPVLEK---IAEKYGVTPAQVLLRWALQKG-IV 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 18390678 330 PIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASE 365
Cdd:cd19120 231 VVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQ 266
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
52-347 |
2.47e-28 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 113.55 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 52 GGSDLKVTKLGIGVW-SWGDNsywndfqwddRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgAISSETLLGRFIRER 130
Cdd:PRK09912 19 GKSGLRLPALSLGLWhNFGHV----------NALESQRAILRKAFDLGITHFDLANNYGPP----PGSAEENFGRLLRED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 131 KERYPGaEVSVATK--FAALPWRFG----RESVVTALKDSLSRLELSSVDLYQLH-----WPglwgNEGYLDGLGDAVEQ 199
Cdd:PRK09912 85 FAAYRD-ELIISTKagYDMWPGPYGsggsRKYLLASLDQSLKRMGLEYVDIFYSHrvdenTP----MEETASALAHAVQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKY---TP 276
Cdd:PRK09912 160 GKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngIP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390678 277 ENP---PSGPRGRIYTREFLTKLQplLNRIK---QIGENYSKTPTQIALNWLVAQGNVIPI-PGAKNAEQAKEFAGAI 347
Cdd:PRK09912 240 QDSrmhREGNKVRGLTPKMLTEAN--LNSLRllnEMAQQRGQSMAQMALSWLLKDERVTSVlIGASRAEQLEENVQAL 315
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
83-363 |
4.34e-28 |
|
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: 110.44 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 83 KLKAAKG--AFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKerYPGAEVSVATKfaaLPWRF-GRESVVT 159
Cdd:cd19132 16 PLKGDEGveAVVAALQAGYRLLDTAFNYEN---------EGAVGEAVRRSG--VPREELFVTTK---LPGRHhGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 160 ALKDSLSRLELSSVDLYQLHWPgLWGNEGYLD---GLGDAVEQGLVKAVGVSNYSEKRLrdayERL-KKRGIPLASNQVN 235
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWP-NPSRDLYVEawqALIEAREEGLVRSIGVSNFLPEHL----DRLiDETGVTPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 236 yslIYRAPEQTGVKAACDELGVTLIAYSPIAQGAltgkytpenppsgprgriytrEFLTklQPLlnrIKQIGENYSKTPT 315
Cdd:cd19132 157 ---LHPYFPQAEQRAYHREHGIVTQSWSPLGRGS---------------------GLLD--EPV---IKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 18390678 316 QIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLA 363
Cdd:cd19132 208 QVVLRWHVQLG-VVPIPKSANPERQRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
82-362 |
4.51e-28 |
|
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: 110.80 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 82 RKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKERY--PGAEVSVATKFAalPWRFGRESVVT 159
Cdd:cd19136 12 RGEEEVRQAVDAALKAGYRLIDTASVYRN---------EADIGKALRDLLPKYglSREDIFITSKLA--PKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 160 ALKDSLSRLELSSVDLYQLHWPGLWG-------NEGYLDG----LGDAVEQGLVKAVGVSNYSEKRLRdayERLKKRGIP 228
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQGlkpsdprNAELRREswraLEDLYKEGKLRAIGVSNYTVRHLE---ELLKYCEVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 229 LASNQVNYSLIYrapEQTGVKAACDELGVTLIAYSPIAQGALTgkyTPENPPsgprgriytrefltklqpllnrIKQIGE 308
Cdd:cd19136 158 PAVNQVEFHPHL---VQKELLKFCKDHGIHLQAYSSLGSGDLR---LLEDPT----------------------VLAIAK 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18390678 309 NYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19136 210 KYGRTPAQVLLRWALQQG-IGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
52-347 |
1.26e-27 |
|
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: 110.57 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 52 GGSDLKVTKLGIGVW-SWGD-NSYWNDfqwddRKLkaAKGAFDTsldnGIDFFDTAEVYGSKfslgAISSETLLGRFIRE 129
Cdd:cd19151 6 GRSGLKLPAISLGLWhNFGDvDRYENS-----RAM--LRRAFDL----GITHFDLANNYGPP----PGSAEENFGRILKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYPGaEVSVATKFAALPWR-----FG-RESVVTALKDSLSRLELSSVDLYQLHWPG----LwgnEGYLDGLGDAVEQ 199
Cdd:cd19151 71 DLKPYRD-ELIISTKAGYTMWPgpygdWGsKKYLIASLDQSLKRMGLDYVDIFYHHRPDpetpL---EETMGALDQIVRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEQtGVKAACDELGVTLIAYSPIAQGALTGKY---TP 276
Cdd:cd19151 147 GKALYVGISNYPPEEAREAAAILKDLGTPCLIHQPKYSMFNRWVEE-GLLDVLEEEGIGCIAFSPLAQGLLTDRYlngIP 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 277 ENPPSGPRGRIYTREFLTklQPLLNRIKQ---IGENYSKTPTQIALNWLVAQGNVIP-IPGAKNAEQAKEFAGAI 347
Cdd:cd19151 226 EDSRAAKGSSFLKPEQIT--EEKLAKVRRlneIAQARGQKLAQMALAWVLRNKRVTSvLIGASKPSQIEDAVGAL 298
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
60-362 |
2.98e-27 |
|
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: 108.29 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 60 KLGIGVWSWGDnsywndfqwDDRKLKAAKgafdTSLDNGIDFFDTAEVYgskfslgaiSSETLLGRFIRERKerYPGAEV 139
Cdd:cd19126 11 WLGLGVFQTPD---------GDETERAVQ----TALENGYRSIDTAAIY---------KNEEGVGEAIRESG--VPREEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 140 SVATKFaalpWR--FGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRd 217
Cdd:cd19126 67 FVTTKL----WNddQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 218 ayERLKKRGIPLASNQVNYSLIYRAPEqtgVKAACDELGVTLIAYSPIAQGALTgkytpENPpsgprgriytrefltklq 297
Cdd:cd19126 142 --ELLAHADVVPAVNQVEFHPYLTQKE---LRGYCKSKGIVVEAWSPLGQGGLL-----SNP------------------ 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 298 pllnRIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19126 194 ----VLAAIGEKYGKSAAQVVLRWDI-QHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
59-351 |
4.43e-27 |
|
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: 108.41 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 59 TKLGIGVWSWGDNsywndfqWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaisSETLLGRFIRErkerYPGAE 138
Cdd:cd19090 1 SALGLGTAGLGGV-------FGGVDDDEAVATIRAALDLGINYIDTAPAYGD--------SEERLGLALAE----LPREP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 139 VSVATKFAALP---WRFGRESVVTALKDSLSRLELSSVDLYQLH---WPGLW---GNEGYLDGLGDAVEQGLVKAVGVSN 209
Cdd:cd19090 62 LVLSTKVGRLPedtADYSADRVRRSVEESLERLGRDRIDLLMIHdpeRVPWVdilAPGGALEALLELKEEGLIKHIGLGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 210 YSEKRLRDAyerlkkrgipLASNQV-------NYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYtPENPPSG 282
Cdd:cd19090 142 GPPDLLRRA----------IETGDFdvvltanRYTLLDQSAADE-LLPAAARHGVGVINASPLGMGLLAGRP-PERVRYT 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 283 PRGRiyTREFLTKLQpllnRIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAIGWSL 351
Cdd:cd19090 210 YRWL--SPELLDRAK----RLYELCDEHGVPLPALALRFLLRDPRIsTVLVGASSPEELEQNVAAAEGPL 273
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
61-362 |
1.55e-26 |
|
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: 106.64 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 61 LGIGVWSWGDNSywndfqwDDRKLKAAKgafdtslDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKerYPGAEVS 140
Cdd:cd19135 16 LGLGTSHSGGYS-------HEAVVYALK-------ECGYRHIDTAKRYGC---------EELLGKAIKESG--VPREDLF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 141 VATKFaaLPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPG--LWGN------EGYLDGLGDAVEQGLVKAVGVSNYSE 212
Cdd:cd19135 71 LTTKL--WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDcpSSGKnvketrAETWRALEELYDEGLCRAIGVSNFLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 213 KRLRDAYERLkkrGIPLASNQVNYSlIYRAPEQtgVKAACDELGVTLIAYSPIAQGaltgkytpenppsgprgriytref 292
Cdd:cd19135 149 EHLEQLLEDC---SVVPHVNQVEFH-PFQNPVE--LIEYCRDNNIVFEGYCPLAKG------------------------ 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390678 293 ltklqPLLN--RIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19135 199 -----KALEepTVTELAKKYQKTPAQILIRWSI-QNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
60-362 |
1.63e-26 |
|
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: 106.30 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 60 KLGIGVWswgdnsywndfQWDDRKlkaAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRerKERYPGAEV 139
Cdd:cd19131 12 QLGLGVW-----------QVSNDE---AASAVREALEVGYRSIDTAAIYGN---------EEGVGKAIR--ASGVPREEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 140 SVATKFaalpWR--FGRESVVTALKDSLSRLELSSVDLYQLHWPgLWGNEGYLD---GLGDAVEQGLVKAVGVSNYSEKR 214
Cdd:cd19131 67 FITTKL----WNsdQGYDSTLRAFDESLRKLGLDYVDLYLIHWP-VPAQDKYVEtwkALIELKKEGRVKSIGVSNFTIEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 215 LrdayERLKKR-GIPLASNQVNYSLIYrapEQTGVKAACDELGVTLIAYSPIAQGALTgkytpENPpsgprgriytrefl 293
Cdd:cd19131 142 L----QRLIDEtGVVPVVNQIELHPRF---QQRELRAFHAKHGIQTESWSPLGQGGLL-----SDP-------------- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390678 294 tklqpllnRIKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19131 196 --------VIGEIAEKHGKTPAQVVIRWHLQNGLVV-IPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
85-342 |
3.37e-26 |
|
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: 105.69 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 85 KAAKGAFDTSLDNGIDFFDTAEVYGskfslgaiSSETLLGRFIRERKerypgaEVSVATKFAALPWRFG--RESVVTALK 162
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYG--------DSEKVLGKFLKRLD------KFKIITKLPPLKEDKKedEAAIEASVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 163 DSLSRLELSSVDLYQLHWPGLW--GNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIplasnQVNYSLIY 240
Cdd:cd19097 92 ASLKRLKVDSLDGLLLHNPDDLlkHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDII-----QLPFNILD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 241 RAPEQTGVKAACDELGVTLIAYSPIAQGALTGKytPENPPsgprgriytrEFLTKLQPLLNRIKQIGENYSKTPTQIALN 320
Cdd:cd19097 167 QRFLKSGLLAKLKKKGIEIHARSVFLQGLLLME--PDKLP----------AKFAPAKPLLKKLHELAKKLGLSPLELALG 234
|
250 260
....*....|....*....|....*.
gi 18390678 321 WLVAQGN----VIpipGAKNAEQAKE 342
Cdd:cd19097 235 FVLSLPEidkiVV---GVDSLEQLKE 257
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
59-346 |
6.05e-26 |
|
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: 104.62 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 59 TKLGIGVWSWGDNsywndfqWDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGskfslgaiSSETLLGRFIRERkERypgAE 138
Cdd:cd19095 1 SVLGLGTSGIGRV-------WGVPSEAEAARLLNTALDLGINLIDTAPAYG--------RSEERLGRALAGL-RR---DD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 139 VSVATKfAALPWR-------FGRESVVTALKDSLSRLELSSVDLYQLHWPGLW-GNEGYLDGLGDAVEQGLVKAVGVSNY 210
Cdd:cd19095 62 LFIATK-VGTHGEggrdrkdFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDeLTGEVLETLEDLKAAGKVRYIGVSGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 211 SEkRLRDAyerlkkrgipLASN-----QVNYSLIYRAPEQTGVKAAcdELGVTLIAYSPIAQGALTGKYTPENPPSGPRg 285
Cdd:cd19095 141 GE-ELEAA----------IASGvfdvvQLPYNVLDREEEELLPLAA--EAGLGVIVNRPLANGRLRRRVRRRPLYADYA- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390678 286 riytrefltKLQPLLNRIKqigenySKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGA 346
Cdd:cd19095 207 ---------RRPEFAAEIG------GATWAQAALRFVLSHPGVsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
83-362 |
1.16e-25 |
|
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: 105.19 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 83 KLKAAKG--AFDTSLDNGIDFFDTAEVYGSKFSLG-AISSETLLGRFIRErkerypgaEVSVATKFAalPWRFGRESVVT 159
Cdd:cd19154 21 QSKGAEGitAVRTALKAGYRLIDTAFLYQNEEAIGeALAELLEEGVVKRE--------DLFITTKLW--THEHAPEDVEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 160 ALKDSLSRLELSSVDLYQLHWP----------GLWGNEGYLD----------GLGDAVEQGLVKAVGVSNYSEKRLRDAY 219
Cdd:cd19154 91 ALRESLKKLQLEYVDLYLIHAPaafkddegesGTMENGMSIHdavdvedvwrGMEKVYDEGLTKAIGVSNFNNDQIQRIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 220 ERLKkrgIPLASNQVNYSLIYRAPEqtgVKAACDELGVTLIAYSPIAqgaltgkyTPE-NPPSGPRGRIYTRefltklQP 298
Cdd:cd19154 171 DNAR---VKPHNNQVECHLYFPQKE---LVEFCKKHNISVTSYATLG--------SPGrANFTKSTGVSPAP------NL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 299 LLNRI-KQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19154 231 LQDPIvKAIAEKHGKTPAQVLLRYLLQRG-IAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEI 294
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
50-347 |
2.50e-25 |
|
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: 104.60 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVW-SWGDNSywndfqwddrKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslGAisSETLLGRFIR 128
Cdd:cd19143 5 RLGRSGLKVSALSFGSWvTFGNQV----------DVDEAKECMKAAYDAGVNFFDNAEVYAN----GQ--SEEIMGQAIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 129 ERkeRYPGAEVSVATKFAalpWRFG----------RESVVTALKDSLSRLELSSVDLYQLHWPglwgnegylD------- 191
Cdd:cd19143 69 EL--GWPRSDYVVSTKIF---WGGGgpppndrglsRKHIVEGTKASLKRLQLDYVDLVFCHRP---------Dpatpiee 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 192 ---GLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQ 267
Cdd:cd19143 135 tvrAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLAS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 268 GALTGKYTpENPPSGPRGRIYTREFLTKLQPLLN--------RIKQIGENYSKTPTQIALNWLVAQGNV-IPIPGAKNAE 338
Cdd:cd19143 215 GLLTGKYN-NGIPEGSRLALPGYEWLKDRKEELGqekiekvrKLKPIAEELGCSLAQLAIAWCLKNPNVsTVITGATKVE 293
|
....*....
gi 18390678 339 QAKEFAGAI 347
Cdd:cd19143 294 QLEENLKAL 302
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
87-362 |
1.88e-24 |
|
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: 100.73 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 87 AKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRerKERYPGAEVSVATKFaalpW--RFGRESVVTALKDS 164
Cdd:cd19133 25 CERAVLEAIKAGYRLIDTAAAYGN---------EEAVGRAIK--KSGIPREELFITTKL----WiqDAGYEKAKKAFERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 165 LSRLELSSVDLYQLHWPglWGN-EGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKkrgIPLASNQVNYSLIYrap 243
Cdd:cd19133 90 LKRLGLDYLDLYLIHQP--FGDvYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE---VKPAVNQIETHPFN--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 244 EQTGVKAACDELGVTLIAYSPIAQGaltgkytpenppsgpRGRIYTREFLTKlqpllnrikqIGENYSKTPTQIALNWLV 323
Cdd:cd19133 162 QQIEAVEFLKKYGVQIEAWGPFAEG---------------RNNLFENPVLTE----------IAEKYGKSVAQVILRWLI 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 18390678 324 aQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19133 217 -QRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
57-369 |
2.07e-24 |
|
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: 101.27 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWSWGDNSywndfqwddrklkaAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIReRKERYpg 136
Cdd:cd19125 10 KIPAVGLGTWQADPGV--------------VGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVK-REDLF-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 137 aevsVATKFaalpWR--FGRESVVTALKDSLSRLELSSVDLYQLHWP-------GLWGNEGYLD----GLGDAVEQ---- 199
Cdd:cd19125 73 ----ITSKL----WCtdHAPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgaHMPEPEEVLPpdipSTWKAMEKlvds 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAyerLKKRGIPLASNQVNYSLIYRapeQTGVKAACDELGVTLIAYSPIaqgaltgkytpenp 279
Cdd:cd19125 145 GKVRAIGVSNFSVKKLEDL---LAVARVPPAVNQVECHPGWQ---QDKLHEFCKSKGIHLSAYSPL-------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 280 psGPRGRIYTREFLTKLqPLlnrIKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSEL 359
Cdd:cd19125 205 --GSPGTTWVKKNVLKD-PI---VTKVAEKLGKTPAQVALRWGLQRGTSV-LPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
330
....*....|
gi 18390678 360 rslaSEIKPV 369
Cdd:cd19125 278 ----SSIEQQ 283
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
57-362 |
2.67e-24 |
|
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: 101.45 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWswgdnsywndfQWDDRKLKAAkgaFDTSLDNGIDFFDTAEVYGSKFSLGAISSETL-LGRFIRErkeryp 135
Cdd:cd19155 11 KMPVVGLGTW-----------QSSPEEIETA---VDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIdSGKVKRE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gaEVSVATKFAALPWRfgRESVVTALKDSLSRLELSSVDLYQLHWP-GLWGNE---GYLD------------------GL 193
Cdd:cd19155 71 --ELFIVTKLPPGGNR--REKVEKFLLKSLEKLQLDYVDLYLIHFPvGSLSKEddsGKLDptgehkqdyttdlldiwkAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 194 GDAVEQGLVKAVGVSNYSEKRLRdayERLKKRGIPLASNQVNYSLIYrapEQTGVKAACDELGVTLIAYSPIAQGALTGK 273
Cdd:cd19155 147 EAQVDQGLTRSIGLSNFNREQMA---RILKNARIKPANLQVELHVYL---QQKDLVDFCSTHSITVTAYAPLGSPGAAHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 274 YTPENPPSGPRGRIYTrefltklQPLLnriKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTD 353
Cdd:cd19155 221 SPGTGSPSGSSPDLLQ-------DPVV---KAIAERHGKSPAQVLLRWLMQRG-VVVIPKSTNAARIKENFQVFDFELTE 289
|
....*....
gi 18390678 354 NEVSELRSL 362
Cdd:cd19155 290 ADMAKLSSL 298
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
54-362 |
8.42e-24 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 100.70 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 54 SDLKVTKLGIGVWSWGDNSYWNDfqwddrklkaAKGAFDTSLDNGIDFFDTAEVYG---SKFSLGAisSETLLGRFIRER 130
Cdd:PRK10625 9 SSLEVSTLGLGTMTFGEQNSEAD----------AHAQLDYAVAQGINLIDVAEMYPvppRPETQGL--TETYIGNWLAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 131 KERypgAEVSVATKFAAlPWR-----------FGRESVVTALKDSLSRLELSSVDLYQLHWP----GLWGNEGY------ 189
Cdd:PRK10625 77 GSR---EKLIIASKVSG-PSRnndkgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptNCFGKLGYswtdsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 190 --------LDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIP-LASNQVNYSLIYRAPEqTGVKAACDELGVTLI 260
Cdd:PRK10625 153 pavslletLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPrIVTIQNPYSLLNRSFE-VGLAEVSQYEGVELL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 261 AYSPIAQGALTGKYTPENPPSGPRGRI---YTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGNVIP-IPGAKN 336
Cdd:PRK10625 232 AYSCLAFGTLTGKYLNGAKPAGARNTLfsrFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVAStLLGATT 311
|
330 340
....*....|....*....|....*.
gi 18390678 337 AEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:PRK10625 312 MEQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
57-362 |
1.12e-23 |
|
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: 98.62 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWSWGDNSywndfqwddrklkAAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRfirerkerypg 136
Cdd:cd19157 9 KMPWLGLGVFKVEEGS-------------EVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPR----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 137 AEVSVATKFaalpWR--FGRESVVTALKDSLSRLELSSVDLYQLHWPGLWGNEGYLDGLGDAVEQGLVKAVGVSNYSEKR 214
Cdd:cd19157 65 EELFITSKV----WNadQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 215 LRDAyerLKKRGIPLASNQVNYSliyraPE--QTGVKAACDELGVTLIAYSPIAQGALTgkytpENPpsgprgriytref 292
Cdd:cd19157 141 LEDL---LADAEIVPMVNQVEFH-----PRltQKELRDYCKKQGIQLEAWSPLMQGQLL-----DNP------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 293 ltklqpllnRIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19157 195 ---------VLKEIAEKYNKSVAQVILRWDLQNG-VVTIPKSIKEHRIIENADVFDFELSQEDMDKIDAL 254
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
102-362 |
1.15e-23 |
|
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: 98.88 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 102 FDTAEVYGSKFSLGAISSETLLGRFIRERkerypgAEVSVATKFAALPWRFGResVVTALKDSLSRLELSSVDLYQLHWP 181
Cdd:cd19124 37 FDTAAAYGTEEALGEALAEALRLGLVKSR------DELFVTSKLWCSDAHPDL--VLPALKKSLRNLQLEYVDLYLIHWP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 182 -----------------------GLWgnegylDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKkrgIPLASNQVNYSL 238
Cdd:cd19124 109 vslkpgkfsfpieeedflpfdikGVW------EAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT---IPPAVNQVEMNP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 239 IYRapeQTGVKAACDELGVTLIAYSPIaqGALTGKYTP----ENPPsgprgriytrefltklqpllnrIKQIGENYSKTP 314
Cdd:cd19124 180 AWQ---QKKLREFCKANGIHVTAYSPL--GAPGTKWGSnavmESDV----------------------LKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 18390678 315 TQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19124 233 AQVSLRWVYEQGVSL-VVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-273 |
1.27e-23 |
|
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: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 48 KVKLGGSDLKVTKLGIGVWSWGDNSYwndfqwddrklKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaisSETLLGRFI 127
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQ-----------EEAAAIIRRALDLGINYFDTAPSYGD--------SEEKIGKAL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RERKErypgaEVSVATKFAAlpwrFGRESVVTALKDSLSRLELSSVDLYQLH-------WPGLWGNEGYLDGLGDAVEQG 200
Cdd:cd19100 62 KGRRD-----KVFLATKTGA----RDYEGAKRDLERSLKRLGTDYIDLYQLHavdteedLDQVFGPGGALEALLEAKEEG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 201 LVKAVGVSNYSEKRLRDAYERLkkrgiPLASNQ--VNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGK 273
Cdd:cd19100 133 KIRFIGISGHSPEVLLRALETG-----EFDVVLfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSG 202
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
93-362 |
4.90e-23 |
|
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: 96.65 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 93 TSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRErkERYPGAEVSVATKFaalpW--RFGRESVVTALKDSLSRLEL 170
Cdd:cd19139 22 TALELGYRHIDTAQIYDN---------EAAVGQAIAE--SGVPRDELFITTKI----WidNLSKDKLLPSLEESLEKLRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 171 SSVDLYQLHWPGLWGN---EGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIplASNQVNYS--LIYRApeq 245
Cdd:cd19139 87 DYVDLTLIHWPSPNDEvpvEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAI--ATNQIELSpyLQNRK--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 246 tgVKAACDELGVTLIAYSPIAQGALTGKYTpenppsgprgriytrefltklqpllnrIKQIGENYSKTPTQIALNWLVAQ 325
Cdd:cd19139 162 --LVAHCKQHGIHVTSYMTLAYGKVLDDPV---------------------------LAAIAERHGATPAQIALAWAMAR 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 18390678 326 GNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19139 213 GYAV-IPSSTKREHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
92-348 |
9.21e-23 |
|
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: 96.63 E-value: 9.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 92 DTSLDNGIDFFDTAEVYGSkFSLGAI--SSETLLGRFIRERKERypgAEVSVATKFAALPWRF----------GRESVVT 159
Cdd:cd19752 24 DRYVAAGGNFLDTANNYAF-WTEGGVggESERLIGRWLKDRGNR---DDVVIATKVGAGPRDPdggpespeglSAETIEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 160 ALKDSLSRLELSSVDLYQLH-----WPglwgNEGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIPLASN-Q 233
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAHvddrdTP----LEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAiQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 234 VNYSLIYRAP--EQTGVKAACDEL--------GVTLIAYSPIAQGAltgkYT-PENPPSGPRGRIYTREFLTKLqpllnr 302
Cdd:cd19752 176 QRHSYLRPRPgaDFGVQRIVTDELldyassrpDLTLLAYSPLLSGA----YTrPDRPLPEQYDGPDSDARLAVL------ 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 18390678 303 iKQIGENYSKTPTQIALNWLVAQ-GNVIPIPGAKNAEQAKEFAGAIG 348
Cdd:cd19752 246 -EEVAGELGATPNQVVLAWLLHRtPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
61-362 |
1.16e-22 |
|
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: 96.08 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 61 LGIGVWSWGDNSywndfqwddrklkaAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRerKERYPGAEVS 140
Cdd:cd19134 14 IGLGVGELSDDE--------------AERSVSAALEAGYRLIDTAAAYGN---------EAAVGRAIA--ASGIPRGELF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 141 VATKFAALPwrFGRESVVTALKDSLSRLELSSVDLYQLHWPGlwGNEG-YLD---GLGDAVEQGLVKAVGVSNYSEKRLR 216
Cdd:cd19134 69 VTTKLATPD--QGFTASQAACRASLERLGLDYVDLYLIHWPA--GREGkYVDswgGLMKLREEGLARSIGVSNFTAEHLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 217 DAyerLKKRGIPLASNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTgkytpENPpsgprgriytrefltkl 296
Cdd:cd19134 145 NL---IDLTFFTPAVNQIE---LHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLL-----DNP----------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 297 qpllnRIKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19134 197 -----AVTAIAAAHGRTPAQVLLRWSLQLGNVV-ISRSSNPERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
57-362 |
2.69e-22 |
|
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: 94.89 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWSWGD-NSYWNDFQWddrklkaakgafdtSLDNGIDFFDTAEVYgskfslgaiSSETLLGRFIRERKerYP 135
Cdd:cd19156 8 EMPRLGLGVWRVQDgAEAENAVKW--------------AIEAGYRHIDTAAIY---------KNEEGVGQGIRESG--VP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 GAEVSVATKFaalpWRF--GRESVVTALKDSLSRLELSSVDLYQLHWPglwGNEGYLD---GLGDAVEQGLVKAVGVSNY 210
Cdd:cd19156 63 REEVFVTTKL----WNSdqGYESTLAAFEESLEKLGLDYVDLYLIHWP---VKGKFKDtwkAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 211 SEKRLRDAYERLKKRgiPLAsNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTgkytpENPpsgprgriytr 290
Cdd:cd19156 136 HEHHLEELLKSCKVA--PMV-NQIE---LHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLL-----SNP----------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390678 291 efltklqpllnRIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19156 194 -----------VLKAIGKKYGKSAAQVIIRWDI-QHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGL 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-347 |
4.51e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 93.80 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSWGDNSywndfqwdDRKLKAAkgafdtsLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRe 129
Cdd:cd19105 5 TLGKTGLKVSRLGFGGGGLPRES--------PELLRRA-------LDLGINYFDTAEGYGNG------NSEEIIGEALK- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 rkeRYPGAEVSVATKFAALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPG----LWGNEGYLDGLGDAVEQGLVKAV 205
Cdd:cd19105 63 ---GLRRDKVFLATKASPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDtpeeRLLNEELLEALEKLKKEGKVRFI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 206 GVS--NYSEKRLRDAyerLKKRGIPLAsnQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAqgaltgkytpenppSGP 283
Cdd:cd19105 140 GFSthDNMAEVLQAA---IESGWFDVI--MVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLA--------------GGY 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 284 RGRIYTREFLTKlqpllnrikqigenySKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAI 347
Cdd:cd19105 201 LQPALLSVLKAK---------------GFSLPQAALKWVLSNPRVdTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
89-362 |
7.17e-22 |
|
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: 93.63 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 89 GAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKerYPGAEVSVATKFaalpW--RFGRESVVTALKDSLS 166
Cdd:cd19127 26 DAVATALADGYRLIDTAAAYGN---------EREVGEGIRRSG--VDRSDIFVTTKL----WisDYGYDKALRGFDASLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 167 RLELSSVDLYQLHWP--GLWGN--EGYLDgLGDAVEQGLVKAVGVSNYSEKRLrdayERLKKR-GIPLASNQVNYSLIYr 241
Cdd:cd19127 91 RLGLDYVDLYLLHWPvpNDFDRtiQAYKA-LEKLLAEGRVRAIGVSNFTPEHL----ERLIDAtTVVPAVNQVELHPYF- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 242 apEQTGVKAACDELGVTLIAYSPIAqGALTgkYTPENPPSgpRGRIYTREFLTKLqpllnrikqiGENYSKTPTQIALNW 321
Cdd:cd19127 165 --SQKDLRAFHRRLGIVTQAWSPIG-GVMR--YGASGPTG--PGDVLQDPTITGL----------AEKYGKTPAQIVLRW 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 18390678 322 LVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19127 228 HLQNG-VSAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
51-347 |
1.51e-21 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 93.95 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVW-SWGDnsywndfQWDDrklKAAKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRE 129
Cdd:cd19159 6 LGKSGLRVSCLGLGTWvTFGG-------QISD---EVAERLMTIAYESGVNLFDTAEVYA------AGKAEVILGSIIKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYpgAEVSVATKF-----AALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGlwGN---EGYLDGLGDAVEQGL 201
Cdd:cd19159 70 KGWRR--SSLVITTKLywggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPD--SNtpmEEIVRAMTHVINQGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 202 VKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYtpENP- 279
Cdd:cd19159 146 AMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGv 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390678 280 PSGPRGRIYTREFLT---------KLQPLLNRIKQIGENYSKTPTQIALNW-LVAQGNVIPIPGAKNAEQAKEFAGAI 347
Cdd:cd19159 224 PESSRASLKCYQWLKerivseegrKQQNKLKDLSPIAERLGCTLPQLAVAWcLRNEGVSSVLLGSSTPEQLIENLGAI 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
50-367 |
1.93e-21 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 94.12 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSwgdnsywndFQWDDrkLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaisSETLLGRFIRE 129
Cdd:COG1453 5 RLGKTGLEVSVLGFGGMR---------LPRKD--EEEAEALIRRAIDNGINYIDTARGYGD--------SEEFLGKALKG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERypgaeVSVATKFAalPWRFGRESVVTALKDSLSRLELSSVDLYQLH---WPGLWGNE----GYLDGLGDAVEQGLV 202
Cdd:COG1453 66 PRDK-----VILATKLP--PWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglnTEEDLEKVlkpgGALEALEKAKAEGKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 203 KAVGVSNYsekrlrDAYERLKKrgIpLASN-------QVNYSLIYRAPEQTGVKaACDELGVTLIAYSPIAQGALTgkyt 275
Cdd:COG1453 139 RHIGFSTH------GSLEVIKE--A-IDTGdfdfvqlQYNYLDQDNQAGEEALE-AAAEKGIGVIIMKPLKGGRLA---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 276 peNPPSgprgriytrefltKLQPLLNRikqigenySKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAI--GWSLT 352
Cdd:COG1453 205 --NPPE-------------KLVELLCP--------PLSPAEWALRFLLSHPEVtTVLSGMSTPEQLDENLKTAdnLEPLT 261
|
330
....*....|....*
gi 18390678 353 DNEVSELRSLASEIK 367
Cdd:COG1453 262 EEELAILERLAEELG 276
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
51-347 |
2.86e-20 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 90.20 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVW-SWGDnsywndfQWDDrklKAAKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRE 129
Cdd:cd19141 5 LGKSGLRVSCLGLGTWvTFGS-------QISD---EVAEELVTLAYENGINLFDTAEVYA------AGKAEIVLGKILKK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYpgAEVSVATKF-----AALPWRFGRESVVTALKDSLSRLELSSVDLyqlhwpgLWGN--------EGYLDGLGDA 196
Cdd:cd19141 69 KGWRR--SSYVITTKIfwggkAETERGLSRKHIIEGLKASLERLQLEYVDI-------VFANrpdpntpmEEIVRAFTHV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 197 VEQGLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYT 275
Cdd:cd19141 140 INQGMAMYWGTSRWSAMEIMEAYSVARQFNlIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 276 ---PENPPSGPRGRIYTREFLT-----KLQPLLNRIKQIGENYSKTPTQIALNW-LVAQGNVIPIPGAKNAEQAKEFAGA 346
Cdd:cd19141 220 dgvPEYSRASLKGYQWLKEKILseegrRQQAKLKELQIIADRLGCTLPQLAIAWcLKNEGVSSVLLGASSTEQLYENLQA 299
|
.
gi 18390678 347 I 347
Cdd:cd19141 300 I 300
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-362 |
2.96e-20 |
|
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: 90.40 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIG------VWSWGDnsywndfqwDDRKLKAAKGAfdtsLDNGIDFFDTAEVYGskfslgAISSETLL 123
Cdd:cd19104 4 RFGRTGLKVSELTFGgggiggLMGRTT---------REEQIAAVRRA----LDLGINFFDTAPSYG------DGKSEENL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 124 GRFIRERkerypGAEVSVATKFaalpwRFGRES-------VVTALKDSLSRLELSSVDLYQLH--------WPGLW---- 184
Cdd:cd19104 65 GRALKGL-----PAGPYITTKV-----RLDPDDlgdiggqIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVGGtlst 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 185 ----GNEGYLDGLGDAVEQGLVKAVGVSNYSEKrlrDAYERLKKRGiPLASNQVNYSLI-----------YRAPEQTGVK 249
Cdd:cd19104 135 tdvlGLGGVADAFERLRSEGKIRFIGITGLGNP---PAIRELLDSG-KFDAVQVYYNLLnpsaaearprgWSAQDYGGII 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 250 AACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFlTKLQPLLNRIKQIGEnyskTPTQIALNWLVAQGNVI 329
Cdd:cd19104 211 DAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTSDSDVAIDF-RRAAAFRALAREWGE----TLAQLAHRFALSNPGVS 285
|
330 340 350
....*....|....*....|....*....|....*
gi 18390678 330 P-IPGAKNAEQAKEFAGAIGW-SLTDNEVSELRSL 362
Cdd:cd19104 286 TvLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
51-362 |
3.91e-20 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 90.04 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVW-SWGDnsywndfQWDDrklKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRE 129
Cdd:cd19160 8 LGKSGLRVSCLGLGTWvTFGS-------QISD---ETAEDLLTVAYEHGVNLFDTAEVYAAG------KAERTLGNILKS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYpgAEVSVATKF-----AALPWRFGRESVVTALKDSLSRLELSSVDLyqlhwpgLWGN--------EGYLDGLGDA 196
Cdd:cd19160 72 KGWRR--SSYVVTTKIywggqAETERGLSRKHIIEGLRGSLDRLQLEYVDI-------VFANrsdpnspmEEIVRAMTYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 197 VEQGLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYT 275
Cdd:cd19160 143 INQGMAMYWGTSRWSAMEIMEAYSVARQFNlIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 276 ---PENPPSGPRGRIYTREFL-----TKLQPLLNRIKQIGENYSKTPTQIALNW-LVAQGNVIPIPGAKNAEQAKEFAGA 346
Cdd:cd19160 223 grvPDTCRAAVKGYQWLKEKVqseegKKQQAKVKELHPIADRLGCTVAQLAIAWcLRSEGVSSVLLGVSSAEQLIENLGS 302
|
330
....*....|....*...
gi 18390678 347 IG--WSLTDNEVSELRSL 362
Cdd:cd19160 303 IQvlSQLTPQTVMEIDAL 320
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
51-347 |
4.21e-20 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 89.76 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVW-SWGDnsywndfQWDDrklKAAKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRE 129
Cdd:cd19158 6 LGKSGLRVSCLGLGTWvTFGG-------QITD---EMAEHLMTLAYDNGINLFDTAEVYA------AGKAEVVLGNIIKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKERYpgAEVSVATKF-----AALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGL-WGNEGYLDGLGDAVEQGLVK 203
Cdd:cd19158 70 KGWRR--SSLVITTKIfwggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPnTPMEETVRAMTHVINQGMAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 204 AVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSG 282
Cdd:cd19158 148 YWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYS 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390678 283 pRGRIYTREFLT---------KLQPLLNRIKQIGENYSKTPTQIALNW-LVAQGNVIPIPGAKNAEQAKEFAGAI 347
Cdd:cd19158 228 -RASLKGYQWLKdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVSSVLLGASNAEQLMENIGAI 301
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
90-362 |
5.17e-20 |
|
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: 89.09 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 90 AFDTSLDNGIDFFDTAEVYGSKFSLGAISSETL-LGRFIRErkerypgaEVSVATKfaALPWRFGRESVVTALKDSLSRL 168
Cdd:cd19111 22 AVDYALFVGYRHIDTALSYQNEKAIGEALKWWLkNGKLKRE--------EVFITTK--LPPVYLEFKDTEKSLEKSLENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 169 ELSSVDLYQLHWPglWGNEGYLDG----------------LGDAVEQGLVKAVGVSNYSEKRLRDAyerLKKRGIPLASN 232
Cdd:cd19111 92 KLPYVDLYLIHHP--CGFVNKKDKgerelassdvtsvwraMEALVSEGKVKSIGLSNFNPRQINKI---LAYAKVKPSNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 233 QVNYSLIYrapEQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSgprgriytrefLTKLQPLLnrikQIGENYSK 312
Cdd:cd19111 167 QLECHAYL---QQRELRKFCNKKNIVVTAYAPLGSPGRANQSLWPDQPD-----------LLEDPTVL----AIAKELDK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18390678 313 TPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19111 229 TPAQVLLRFVLQRG-TGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTL 277
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
88-362 |
5.26e-20 |
|
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: 89.37 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 88 KGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIRERKErypgaeVSVATKFaalpW--RFGRESVVTALKDSL 165
Cdd:cd19106 23 KAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPRED------LFVTSKL----WntKHHPEDVEPALRKTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 166 SRLELSSVDLYQLHWPG-----------------LWGNEGYLD---GLGDAVEQGLVKAVGVSNYSEKRLRDAyerLKKR 225
Cdd:cd19106 93 KDLQLDYLDLYLIHWPYafergdnpfpknpdgtiRYDSTHYKEtwkAMEKLVDKGLVKAIGLSNFNSRQIDDI---LSVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 226 GIPLASNQVNySLIYRApeQTGVKAACDELGVTLIAYSPIAqgaltgkyTPENPPSGPRgriytrefltklQPLL---NR 302
Cdd:cd19106 170 RIKPAVLQVE-CHPYLA--QNELIAHCKARGLVVTAYSPLG--------SPDRPWAKPD------------EPVLleePK 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 303 IKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19106 227 VKALAKKYNKSPAQILLRWQVQRG-VVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDAL 285
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
61-362 |
1.44e-19 |
|
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: 87.85 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 61 LGIGVWswgdnsywndfqwddrklKAAKG----AFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLL-GRFIRErkeryp 135
Cdd:cd19123 15 LGLGTW------------------KSKPGevgqAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKeGKVKRE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gaEVSVATKF---AALPwrfgrESVVTALKDSLSRLELSSVDLYQLHWP-----GLWGNEGYLDGLGD------------ 195
Cdd:cd19123 71 --DLWITSKLwnnSHAP-----EDVLPALEKTLADLQLDYLDLYLMHWPvalkkGVGFPESGEDLLSLspipledtwram 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 196 --AVEQGLVKAVGVSNYSEKRLRDAyerLKKRGIPLASNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIAqgaltgk 273
Cdd:cd19123 144 eeLVDKGLCRHIGVSNFSVKKLEDL---LATARIKPAVNQVE---LHPYLQQPELLAFCRDNGIHLTAYSPLG------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 274 ytpenppSGPRGRIYTREFLTKL--QPLlnrIKQIGENYSKTPTQIALNWLVAQgNVIPIPGAKNAEQAKEFAGAIGWSL 351
Cdd:cd19123 211 -------SGDRPAAMKAEGEPVLleDPV---INKIAEKHGASPAQVLIAWAIQR-GTVVIPKSVNPERIQQNLEAAEVEL 279
|
330
....*....|.
gi 18390678 352 TDNEVSELRSL 362
Cdd:cd19123 280 DASDMATIAAL 290
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
90-362 |
3.11e-19 |
|
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: 86.12 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 90 AFDTSLDNGIDFFDTAEVYGSKFSLG-AISSETLlgrfirerkeryPGAEVSVATKFaalpW--RFGRESVVTALKDSLS 166
Cdd:cd19130 28 AVATALEVGYRHIDTAAIYGNEEGVGaAIAASGI------------PRDELFVTTKL----WndRHDGDEPAAAFAESLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 167 RLELSSVDLYQLHWPgLWGNEGYL---DGLGDAVEQGLVKAVGVSNYSEKRLrdayERL-KKRGIPLASNQVNyslIYRA 242
Cdd:cd19130 92 KLGLDQVDLYLVHWP-TPAAGNYVhtwEAMIELRAAGRTRSIGVSNFLPPHL----ERIvAATGVVPAVNQIE---LHPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 243 PEQTGVKAACDELGVTLIAYSPIAQGALTGkytpenppsgprgriytrefltklQPLLNRIKQIgenYSKTPTQIALNWL 322
Cdd:cd19130 164 YQQRTIRDWAQAHDVKIEAWSPLGQGKLLG------------------------DPPVGAIAAA---HGKTPAQIVLRWH 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18390678 323 VAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19130 217 LQKGHVV-FPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
93-330 |
5.83e-18 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 82.76 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 93 TSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRE----RKERYpgaevsVATKFaalpW--RFGRESVVTALKDSLS 166
Cdd:PRK11172 24 TALELGYRAIDTAQIYDN---------EAAVGQAIAEsgvpRDELF------ITTKI----WidNLAKDKLIPSLKESLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 167 RLELSSVDLYQLHWPGLwGNE----GYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIplASNQVNYS--LIY 240
Cdd:PRK11172 85 KLRTDYVDLTLIHWPSP-NDEvsveEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENI--ATNQIELSpyLQN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 241 RApeqtgVKAACDELGVTLIAYSPIAQGALTGkytpenppsgprgriytrefltklQPLlnrIKQIGENYSKTPTQIALN 320
Cdd:PRK11172 162 RK-----VVAFAKEHGIHVTSYMTLAYGKVLK------------------------DPV---IARIAAKHNATPAQVILA 209
|
250
....*....|.
gi 18390678 321 WLVAQG-NVIP 330
Cdd:PRK11172 210 WAMQLGySVIP 220
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
60-362 |
1.17e-17 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 82.04 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 60 KLGIGVWSWGDNSywndfqwddrklkaAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRfirerkerypgAEV 139
Cdd:PRK11565 17 QLGLGVWQASNEE--------------VITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAR-----------EEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 140 SVATKFaalpWRFGRESVVTALKDSLSRLELSSVDLYQLHWPgLWGNEGYLD---GLGDAVEQGLVKAVGVSNYSEKRLr 216
Cdd:PRK11565 72 FITTKL----WNDDHKRPREALEESLKKLQLDYVDLYLMHWP-VPAIDHYVEawkGMIELQKEGLIKSIGVCNFQIHHL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 217 dayERLK-KRGIPLASNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIAQGaltGKYTPENPPsgprgriytrefltk 295
Cdd:PRK11565 146 ---QRLIdETGVTPVINQIE---LHPLMQQRQLHAWNATHKIQTESWSPLAQG---GKGVFDQKV--------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 296 lqpllnrIKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:PRK11565 202 -------IRDLADKYGKTPAQIVIRWHLDSGLVV-IPKSVTPSRIAENFDVFDFRLDKDELGEIAKL 260
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
102-362 |
1.27e-17 |
|
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: 82.53 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 102 FDTAEVYGSKFSLGAISSETL-LGRFIRErkerypgaEVSVATKFaalpWRFGRESVVTALKDSLSRLELSSVDLYQLHW 180
Cdd:cd19112 41 FDCAADYKNEKEVGEALAEAFkTGLVKRE--------DLFITTKL----WNSDHGHVIEACKDSLKKLQLDYLDLYLVHF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 181 PGLW------------GNEGYLD------------GLGDAVEQGLVKAVGVSNYSEKRLRD--AYERLKKrgiplASNQV 234
Cdd:cd19112 109 PVATkhtgvgttgsalGEDGVLDidvtislettwhAMEKLVSAGLVRSIGISNYDIFLTRDclAYSKIKP-----AVNQI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 235 NYSLIYRapEQTGVKAaCDELGVTLIAYSPIAQGALT----GKYTPENPPSgprgriytrefltklqpllnrIKQIGENY 310
Cdd:cd19112 184 ETHPYFQ--RDSLVKF-CQKHGISVTAHTPLGGAAANaewfGSVSPLDDPV---------------------LKDLAKKY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 18390678 311 SKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSL 362
Cdd:cd19112 240 GKSAAQIVLRWGI-QRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
79-342 |
3.55e-17 |
|
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: 80.30 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 79 WDDRK-LKAAKGAFDTSLDNGIDFFDTAEVYGSKFSlgaissETLLGRFIRERkeryPGAEVSVATKFAalPWRF-GRES 156
Cdd:cd19096 14 DDDSIdEEKAIEMIRYAIDAGINYFDTAYGYGGGKS------EEILGEALKEG----PREKFYLATKLP--PWSVkSAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 157 VVTALKDSLSRLELSSVDLYQLHWPGLWGNE------GYLDGLGDAVEQGLVKAVGVS---NYSE-KRLRDAYerlkkrg 226
Cdd:cd19096 82 FRRILEESLKRLGVDYIDFYLLHGLNSPEWLekarkgGLLEFLEKAKKEGLIRHIGFSfhdSPELlKEILDSY------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 227 iPLASNQVNYSLIYRAPEQT--GVKAACdELGVTLIAYSPIAQGALtgkytPENPPsgprgriytrEFLTKLqpllnrik 304
Cdd:cd19096 155 -DFDFVQLQYNYLDQENQAGrpGIEYAA-KKGMGVIIMEPLKGGGL-----ANNPP----------EALAIL-------- 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 18390678 305 qigENYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKE 342
Cdd:cd19096 210 ---CGAPLSPAEWALRFLLSHPEVtTVLSGMSTPEQLDE 245
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
50-284 |
1.39e-16 |
|
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: 79.13 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSWGdNSYWNdfqWDDRKlkaAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRE 129
Cdd:cd19163 5 KLGKTGLKVSKLGFGASPLG-GVFGP---VDEEE---AIRTVHEALDSGINYIDTAPWYGQG------RSETVLGKALKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 -RKERYpgaevSVATK---FAALP---WRFGRESVVTALKDSLSRLELSSVDLYQLHWP------GLWGNEGyLDGLGDA 196
Cdd:cd19163 72 iPRDSY-----YLATKvgrYGLDPdkmFDFSAERITKSVEESLKRLGLDYIDIIQVHDIefapslDQILNET-LPALQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 197 VEQGLVKAVGVSNYSEKRLRDAYERlkkrgiplASNQVNYSLIY--------RAPEQTgvkAACDELGVTLIAYSPIAQG 268
Cdd:cd19163 146 KEEGKVRFIGITGYPLDVLKEVLER--------SPVKIDTVLSYchytlndtSLLELL---PFFKEKGVGVINASPLSMG 214
|
250
....*....|....*.
gi 18390678 269 ALTGKYTPENPPSGPR 284
Cdd:cd19163 215 LLTERGPPDWHPASPE 230
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
59-362 |
1.96e-16 |
|
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: 78.72 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 59 TKLGIGVWSWGDnsywndfqwddrklKAAKGAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRE--RKERYPG 136
Cdd:cd19128 2 PRLGFGTYKITE--------------SESKEAVKNAIKAGYRHIDCAYYYGN---------EAFIGIAFSEifKDGGVKR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 137 AEVSVATKFaaLPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLW----------GNEGYLDG---LGDA------- 196
Cdd:cd19128 59 EDLFITSKL--WPTMHQPENVKEQLLITLQDLQLEYLDLFLIHWPLAFdmdtdgdprdDNQIQSLSkkpLEDTwrameqc 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 197 VEQGLVKAVGVSNYSEKRLRD--AYERLKkrgiPLaSNQVNYSLIYraPEQTGVKaACDELGVTLIAYSPIAQGALTGKY 274
Cdd:cd19128 137 VDEKLTKNIGVSNYSTKLLTDllNYCKIK----PF-MNQIECHPYF--QNDKLIK-FCIENNIHVTAYRPLGGSYGDGNL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 275 TPENPPSgprgriytrefltklqpllnrIKQIGENYSKTPTQIALNWLVAQ--GNVIPIPGAKNAEQAKEFAGAIGWSLT 352
Cdd:cd19128 209 TFLNDSE---------------------LKALATKYNTTPPQVIIAWHLQKwpKNYSVIPKSANKSRCQQNFDINDLALT 267
|
330
....*....|
gi 18390678 353 DNEVSELRSL 362
Cdd:cd19128 268 KEDMDAINTL 277
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
86-270 |
2.57e-16 |
|
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: 78.55 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 86 AAKGAFDTSLDNGIDFFDTAEVYGskfsLGAisSETLLGRFIRerkeRYPGAEVSVATKFAALP--------------WR 151
Cdd:cd19162 20 EAAATLDAAWDAGIRYFDTAPLYG----LGL--SERRLGAALA----RHPRAEYVVSTKVGRLLepgaagrpagadrrFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 152 FGRESVVTALKDSLSRLELSSVDLYQLHWPGlwgnEGYLDGLGDAVE-------QGLVKAVGVSNYSEKRLRDAYERLKK 224
Cdd:cd19162 90 FSADGIRRSIEASLERLGLDRLDLVFLHDPD----RHLLQALTDAFPaleelraEGVVGAIGVGVTDWAALLRAARRADV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18390678 225 RGIPLASnqvNYSLIYRAPeQTGVKAACDELGVTLIAYSPIAQGAL 270
Cdd:cd19162 166 DVVMVAG---RYTLLDRRA-ATELLPLCAAKGVAVVAAGVFNSGIL 207
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
57-374 |
4.24e-16 |
|
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: 78.08 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 57 KVTKLGIGVWswgdnsywndfqwddrklKAAKG----AFDTSLDNGIDFFDTAEVYGSKFSLGA-ISSETLLGRFIRErk 131
Cdd:cd19110 3 DIPAVGLGTW------------------KASPGevteAVKVAIDAGYRHFDCAYLYHNESEVGAgIREKIKEGVVRRE-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 132 erypgaEVSVATKFaalpW-RFGRESVV-TALKDSLSRLELSSVDLYQLHWPG-----------------LWGNEGYLD- 191
Cdd:cd19110 63 ------DLFIVSKL----WcTCHKKSLVkTACTRSLKALKLNYLDLYLIHWPMgfkpgepdlpldrsgmvIPSDTDFLDt 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 192 --GLGDAVEQGLVKAVGVSNYSEKRLRDAYERLKKRGIPLaSNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIAqGA 269
Cdd:cd19110 133 weAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVKPV-TNQIE---CHPYLTQKKLISFCQSRNVSVTAYRPLG-GS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 270 LTGKYTPENPPsgprgriytrefltklqpllnrIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGW 349
Cdd:cd19110 208 CEGVDLIDDPV----------------------IQRIAKKHGKSPAQILIRFQI-QRNVIVIPKSVTPSRIKENIQVFDF 264
|
330 340
....*....|....*....|....*
gi 18390678 350 SLTDNEVSELRSLASEIKpVVGFPV 374
Cdd:cd19110 265 ELTEHDMDNLLSLDRNLR-LATFPI 288
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
54-367 |
1.47e-14 |
|
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: 73.30 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 54 SDLKVTKLGIGVWSWGDNsywndfqwddrklKAAKgAFDTSLDNGIDFFDTAEVYGSkfslgaissETLLGRFIRERKer 133
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN-------------EVAK-AVEAALKAGYRHIDTAAIYGN---------EEEVGQGIKDSG-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 134 YPGAEVSVATKFaalpWRFGRESVVTALKDSLSRLELSSVDLYQLHWP-----GLWGNEGYLDGLGDAVEQ--------- 199
Cdd:cd19117 65 VPREEIFITTKL----WCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPvpldpDGNDFLFKKDDGTKDHEPdwdfiktwe 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 --------GLVKAVGVSNYSEKRLRDAYERLKKRGIPlASNQVNyslIYRAPEQTGVKAACDELGVTLIAYSPIaqGALT 271
Cdd:cd19117 141 lmqklpatGKVKAIGVSNFSIKNLEKLLASPSAKIVP-AVNQIE---LHPLLPQPKLVDFCKSKGIHATAYSPL--GSTN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 272 GkytpenppsgprgriytrefltklqPLLNR--IKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKefAGAIGW 349
Cdd:cd19117 215 A-------------------------PLLKEpvIIKIAKKHGKTPAQVIISWGLQRGYSV-LPKSVTPSRIE--SNFKLF 266
|
330
....*....|....*...
gi 18390678 350 SLTDNEVSELRSLASEIK 367
Cdd:cd19117 267 TLSDEEFKEIDELHKEYG 284
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
87-362 |
2.16e-14 |
|
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: 72.56 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 87 AKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIRErkerypgaEVSVATKFaalpWRFGRESVVTALKDSLS 166
Cdd:cd19121 27 VKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGVKRE--------DLFVTTKL----WSTYHRRVELCLDRSLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 167 RLELSSVDLYQLHWPGLWGNEG-------YLDG----------------LGDAVEQGLVKAVGVSNYSEKRLrdayERLK 223
Cdd:cd19121 95 SLGLDYVDLYLVHWPVLLNPNGnhdlfptLPDGsrdldwdwnhvdtwkqMEKVLKTGKTKAIGVSNYSIPYL----EELL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 224 KRG--IPlASNQV-NYSLIyraPEQTGVKaACDELGVTLIAYSPIAQgalTGKYTPENPPsgprgriytrefltklqpll 300
Cdd:cd19121 171 KHAtvVP-AVNQVeNHPYL---PQQELVD-FCKEKGILIEAYSPLGS---TGSPLISDEP-------------------- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390678 301 nrIKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIgwSLTDNEVSELRSL 362
Cdd:cd19121 223 --VVEIAKKHNVGPGTVLISYQVARGAVV-LPKSVTPDRIKSNLEII--DLDDEDMNKLNDI 279
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
51-339 |
1.96e-13 |
|
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: 70.57 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 51 LGGSDLKVTKLGIGVW---SWGDNSywndfqwddrklKAAKGAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFI 127
Cdd:cd19142 6 LGKSGLRVSNVGLGTWstfSTAISE------------EQAEEIVTLAYENGINYFDTSDAFTSG------QAETELGRIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 128 RerKERYPGAEVSVATKfaaLPWRFG-------RESVVTALKDSLSRLELSSVDLYQLH-WPGLWGNEGYLDGLGDAVEQ 199
Cdd:cd19142 68 K--KKGWKRSSYIVSTK---IYWSYGseerglsRKHIIESVRASLRRLQLDYIDIVIIHkADPMCPMEEVVRAMSYLIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLA-SNQVNYSLIYRAPEQTGVKAACDELGVTLIAYSPIAQGALTG------ 272
Cdd:cd19142 143 GLIMYWGTSRWSPVEIMEAFSIARQFNCPTPiCEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGiseetr 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 273 --------KYTPENPPSGPRGRI-YTREFLTKLQpllnRIKQIGENYSKTPTQIALNWLVAQGNVIPI-PGAKNAEQ 339
Cdd:cd19142 223 rlvtklsfKSSKYKVGSDGNGIHeETRRASHKLR----ELSLIAERLGCDLTQLLIAWSLKNENVQCVlIGASSLEQ 295
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
90-330 |
2.09e-13 |
|
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: 69.75 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 90 AFDTSLDNGIDFFDTAEVYGSKFSLGAISSETLLGRFIRERKERYpgaevsVATKFaalpW--RFGRESVVTALKDSLSR 167
Cdd:cd19118 25 AVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLF------ITSKL----WnnSHRPEYVEPALDDTLKE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 168 LELSSVDLYQLHWP-------------GLWGNEGYLDgLGDAV-------------EQGLVKAVGVSNYSEKRLRDAyer 221
Cdd:cd19118 95 LGLDYLDLYLIHWPvafkptgdlnpltAVPTNGGEVD-LDLSVslvdtwkamvelkKTGKVKSIGVSNFSIDHLQAI--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 222 LKKRGIPLASNQVNYS--LIyrapeQTGVKAACDELGVTLIAYSPIAQGALTGKYTPENPpsgprgriytrefltklqpl 299
Cdd:cd19118 171 IEETGVVPAVNQIEAHplLL-----QDELVDYCKSKNIHITAYSPLGNNLAGLPLLVQHP-------------------- 225
|
250 260 270
....*....|....*....|....*....|..
gi 18390678 300 lnRIKQIGENYSKTPTQIALNWLVAQG-NVIP 330
Cdd:cd19118 226 --EVKAIAAKLGKTPAQVLIAWGIQRGhSVIP 255
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
87-361 |
2.40e-13 |
|
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: 70.14 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 87 AKGAFDTSLDNGIDFFDTAEVYGSKFSLG-AISSETLLGRFIRErkerypgaEVSVATKFaaLPWRFGRESVVTALKDSL 165
Cdd:cd19107 19 VTEAVKVAIDAGYRHIDCAYVYQNENEVGeAIQEKIKEQVVKRE--------DLFIVSKL--WCTFHEKGLVKGACQKTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 166 SRLELSSVDLYQLHWPG-----------------LWGNEGYLD---GLGDAVEQGLVKAVGVSNYSekrlRDAYER-LKK 224
Cdd:cd19107 89 SDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvIPSDTTFLDtweAMEELVDEGLVKAIGVSNFN----HLQIERiLNK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 225 RGIPL--ASNQVNYSliyraPEQTGVK--AACDELGVTLIAYSPIAqgaltgkyTPENPPSGPRgriytrefltklQPLL 300
Cdd:cd19107 165 PGLKYkpAVNQIECH-----PYLTQEKliQYCQSKGIVVTAYSPLG--------SPDRPWAKPE------------DPSL 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390678 301 ---NRIKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRS 361
Cdd:cd19107 220 ledPKIKEIAAKHNKTTAQVLIRFPI-QRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILS 282
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
56-286 |
3.31e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 69.65 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 56 LKVTKLGIGvwswgdnSYWNDFqwDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSkfslGAisSETLLGRFIRERKERYP 135
Cdd:cd19099 1 LTLSSLGLG-------TYRGDS--DDETDEEYREALKAALDSGINVIDTAINYRG----GR--SERLIGKALRELIEKGG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 GA--EVSVATK-----------FAALPW--------RFGRESVVT------------ALKDSLSRLELSSVDLYQLHWP- 181
Cdd:cd19099 66 IKrdEVVIVTKagyipgdgdepLRPLKYleeklgrgLIDVADSAGlrhcispayledQIERSLKRLGLDTIDLYLLHNPe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 182 ---GLWGNEGYLDGLGDA-------VEQGLVKAVGVSNYSEKRLRDAYE-----RLKKRGIPLASN--------QVNYSL 238
Cdd:cd19099 146 eqlLELGEEEFYDRLEEAfealeeaVAEGKIRYYGISTWDGFRAPPALPghlslEKLVAAAEEVGGdnhhfkviQLPLNL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 239 IYRAP--EQTGVK-------AACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGR 286
Cdd:cd19099 226 LEPEAltEKNTVKgealsllEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGA 282
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
56-377 |
1.45e-12 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 67.83 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 56 LKVTKLGIGVWSWGDNsyWNDFQWDDRKLKAAKgAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRERKERyp 135
Cdd:cd19146 9 VRVSPLCLGAMSFGEA--WKSMMGECDKETAFK-LLDAFYEQGGNFIDTANNYQGE------ESERWVGEWMASRGNR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gAEVSVATKFAALPWRFGRE------------SVVTALKDSLSRLELSSVDLYQLHWpglW----GNEGYLDGLGDAVEQ 199
Cdd:cd19146 78 -DEMVLATKYTTGYRRGGPIkiksnyqgnhakSLRLSVEASLKKLQTSYIDILYVHW---WdyttSIPELMQSLNHLVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGI-PLASNQVNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTgkyTPEN 278
Cdd:cd19146 154 GKVLYLGVSDTPAWVVSKANAYARAHGLtQFVVYQGHWSAAFRDFERD-ILPMCEAEGMALAPWGVLGQGQFR---TEEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 279 PPSGPRGRIYTREFLTKLQPLLNRIKQIGENYSKTPTQIALNWLVAQGN-VIPIPGAKNAEQAKEFAGAIGWSLTDNEVS 357
Cdd:cd19146 230 FKRRGRSGRKGGPQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPyVFPIVGGRKVEHLKGNIEALGISLSDEEIQ 309
|
330 340
....*....|....*....|.
gi 18390678 358 ELRSlaseIKPV-VGFPVEYL 377
Cdd:cd19146 310 EIED----AYPFdVGFPMNFL 326
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
86-369 |
1.42e-11 |
|
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: 64.82 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 86 AAKGAFDTSLDNGIDFFDTAEVYgskfslgaiSSETLLGRFIRERKerypgAEVSVATK---FAALPWRFGR--ESVVTA 160
Cdd:cd19109 22 ACAEAVKVAIDTGYRHIDGAYIY---------QNEHEVGQAIREKI-----AEGKVKREdifYCGKLWNTCHppELVRPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 161 LKDSLSRLELSSVDLYQLHWPGLW--GNEGY---------------------LDGLGDAveqGLVKAVGVSNYSEKRLRD 217
Cdd:cd19109 88 LERTLKVLQLDYVDLYIIEMPMAFkpGDEIYprdengkwlyhktnlcatweaLEACKDA---GLVKSIGVSNFNRRQLEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 218 AyerLKKRGIPL--ASNQVNYSLIYrapEQTGVKAACDELGVTLIAYSPIAqgaltgkyTPENPpsgprgrIYTReflTK 295
Cdd:cd19109 165 I---LNKPGLKHkpVSNQVECHPYF---TQPKLLEFCQQHDIVIVAYSPLG--------TCRDP-------IWVN---VS 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 296 LQPLLNR--IKQIGENYSKTPTQIALNWLVaQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASEIKPV 369
Cdd:cd19109 221 SPPLLEDplLNSIGKKYNKTAAQVVLRFNI-QRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
56-359 |
7.95e-11 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 62.53 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 56 LKVTKLGIGVWSWGDNsyWNDFQWDDRKLKAAKgAFDTSLDNGIDFFDTAEVYGSKfslgaiSSETLLGRFIRERKERyp 135
Cdd:cd19147 8 IRVSPLILGAMSIGDA--WSGFMGSMDKEQAFE-LLDAFYEAGGNFIDTANNYQDE------QSETWIGEWMKSRKNR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 136 gAEVSVATKF-------------AALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWpglW----GNEGYLDGLGDAVE 198
Cdd:cd19147 77 -DQIVIATKFttdykayevgkgkAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHW---WdyttSIEEVMDSLHILVQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 199 QGLVKAVGVSNYSEKRLRDAYERLKKRG-IPLASNQVNYSLIYRAPEQTGVKAAcDELGVTLIAYSPIAQGALTGKYTPE 277
Cdd:cd19147 153 QGKVLYLGVSDTPAWVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMA-RHFGMALAPWDVLGGGKFQSKKAVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 278 NPPSGPRGriyTREFLTKLQPLLNRIK------QIGENY-SKTPTQIALNWLVAQG-NVIPIPGAKNAEQAKEFAGAIGW 349
Cdd:cd19147 232 ERKKNGEG---LRSFVGGTEQTPEEVKisealeKVAEEHgTESVTAIALAYVRSKApNVFPLVGGRKIEHLKDNIEALSI 308
|
330
....*....|
gi 18390678 350 SLTDNEVSEL 359
Cdd:cd19147 309 KLTPEEIEYL 318
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
61-365 |
1.17e-10 |
|
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: 61.74 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 61 LGIGVWSwgdnsywndfqwDDRKLKAAKGAFDTSLDNGIDFFDTAEVYGSKFSLG-AISSETLLGRFIRErkerypgaEV 139
Cdd:cd19119 15 LGLGTAS------------PHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGeAIKRAIDDGSIKRE--------EL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 140 SVATKFaalpWRFGRESVVTALKDSLSRLELSSVDLYQLHWP----------GLWGNEGYLDGL------GDAVE----- 198
Cdd:cd19119 75 FITTKV----WPTFYDEVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsGKPFTPVNDDGKtryaasGDHITtykql 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 199 -----QGLVKAVGVSNYSEKRLrdayERLKK--RGIPlASNQVnySLIYRAPEQTGVKaACDELGVTLIAYSPIAQGalt 271
Cdd:cd19119 151 ekiylDGRAKAIGVSNYSIVYL----ERLIKecKVVP-AVNQV--ELHPHLPQMDLRD-FCFKHGILVTAYSPLGSH--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 272 GKYTPENPPsgprgriytrefltklqpllnrIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKEFAGAIGwsL 351
Cdd:cd19119 220 GAPNLKNPL----------------------VKKIAEKYNVSTGDILISYHVRQG-VIVLPKSLKPVRIVSNGKIVS--L 274
|
330
....*....|....
gi 18390678 352 TDNEVSELRSLASE 365
Cdd:cd19119 275 TKEDLQKLDDIGEK 288
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
86-342 |
1.49e-10 |
|
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: 61.32 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 86 AAKGAFDTSLDNGIDFFDTAEVYGSKFSLGAISSETL-LGRFIRErkerypgaEVSVATKFaalpWRFGR--ESVVTALK 162
Cdd:cd19129 20 ATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFkAGKIRRE--------DLFVTTKL----WNTNHrpERVKPAFE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 163 DSLSRLELSSVDLYQLHWPGLW------------GNEGYLDG---------LGDAVEQGLVKAVGVSNYSEKRLRDAYER 221
Cdd:cd19129 88 ASLKRLQLDYLDLYLIHTPFAFqpgdeqdprdanGNVIYDDGvtlldtwraMERLVDEGRCKAIGLSDVSLEKLREIFEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 222 LKkrgIPLASNQVNySLIYRapEQTGVKAACDELGVTLIAYSPIAQGAltgkyTPeNPPSGPrgriytrefltklqplln 301
Cdd:cd19129 168 AR---IKPAVVQVE-SHPYL--PEWELLDFCKNHGIVLQAFAPLGHGM-----EP-KLLEDP------------------ 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 18390678 302 RIKQIGENYSKTPTQIALNWLVAQGnVIPIPGAKNAEQAKE 342
Cdd:cd19129 218 VITAIARRVNKTPAQVLLAWAIQRG-TALLTTSKTPSRIRE 257
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
98-365 |
2.27e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 60.75 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 98 GIDFFDTAEVYGSKFSlgaissetllGRFIRERKERYPGAEVSVaTKFAA--------LPwRFGRESVVTALKDSLSRLE 169
Cdd:PRK10376 53 GVNHIDTSDFYGPHVT----------NQLIREALHPYPDDLTIV-TKVGArrgedgswLP-AFSPAELRRAVHDNLRNLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 170 LSSVDLYQLHwpgLWGN---------EGYLDGLGDAVEQGLVKAVGVSNYSEKRLRDAyerlkkRGI-PLASNQVNYSLI 239
Cdd:PRK10376 121 LDVLDVVNLR---LMGDghgpaegsiEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEA------RKIaEIVCVQNHYNLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 240 YRAPEqtgvkAACDELGVTLIAYSPIAQgalTGKYTPenppsgprgriytrefltkLQP-LLNRIkqiGENYSKTPTQIA 318
Cdd:PRK10376 192 HRADD-----ALIDALARDGIAYVPFFP---LGGFTP-------------------LQSsTLSDV---AASLGATPMQVA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 18390678 319 LNWLVAQG-NVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASE 365
Cdd:PRK10376 242 LAWLLQRSpNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
154-362 |
5.13e-10 |
|
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: 60.13 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 154 RESVVTALKDSLSRLELSSVDLYQLHWP-GL------------WGNEGYLDGLGDA------------VEQGLVKAVGVS 208
Cdd:cd19115 86 GERVEPICRKQLADWGIDYFDLFLIHFPiALkyvdpavryppgWFYDGKKVEFSNApiqetwtameklVDKGLARSIGVS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 209 NYSEKRLRDA--YERLKKrgiplASNQVNYSLIYRAPEQtgVKAACDElGVTLIAYSPIaqgaltgkytpenppsGPRGR 286
Cdd:cd19115 166 NFSAQLLMDLlrYARIRP-----ATLQIEHHPYLTQPRL--VKYAQKE-GIAVTAYSSF----------------GPQSF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 287 IytrEF----LTKLQPLLNR--IKQIGENYSKTPTQIALNWlVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELR 360
Cdd:cd19115 222 L---ELdlpgAKDTPPLFEHdvIKSIAEKHGKTPAQVLLRW-ATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAIS 297
|
..
gi 18390678 361 SL 362
Cdd:cd19115 298 AL 299
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
50-319 |
1.93e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 58.25 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 50 KLGGSDLKVTKLGIGVWSWGdnSYWNDFQWDDrklkaAKGAFDTSLDNGIDFFDTAEVYGSKFSlgaissETLLGRFIRE 129
Cdd:PLN02587 3 ELGSTGLKVSSVGFGASPLG--SVFGPVSEED-----AIASVREAFRLGINFFDTSPYYGGTLS------EKVLGKALKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 130 RKerYPGAEVSVATKFA--ALPWRFGRESVVTALKDSLSRLELSSVDLYQLHWPGLwgneGYLD--------GLGDAVEQ 199
Cdd:PLN02587 70 LG--IPREKYVVSTKCGryGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEF----GSLDqivnetipALQKLKES 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 200 GLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQVNYSLIYRAPEqtGVKAACDELGVTLIAYSPIAQGALTGKYTPENP 279
Cdd:PLN02587 144 GKVRFIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSLNDSSLE--DLLPYLKSKGVGVISASPLAMGLLTENGPPEWH 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18390678 280 PSGPrgriytrEFLTKLQPLLNRIKQIGENYSKTPTQIAL 319
Cdd:PLN02587 222 PAPP-------ELKSACAAAATHCKEKGKNISKLALQYSL 254
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
87-342 |
6.41e-09 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 56.46 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 87 AKGAFDTSLDNGIDFFDTAEVYGSKFS---LGA-----------ISseTLLGRFIRERKERYPGAEVSVA--TKFAALpW 150
Cdd:cd19152 22 AKATLVAAWDLGIRYFDTAPWYGAGLSeerLGAalrelgredyvIS--TKVGRLLVPLQEVEPTFEPGFWnpLPFDAV-F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 151 RFGRESVVTALKDSLSRLELSSVDLYQLHWP-----GLWGNEGYLDGLGDAV-------EQGLVKAVGVSNYSEKRLRDA 218
Cdd:cd19152 99 DYSYDGILRSIEDSLQRLGLSRIDLLSIHDPdedlaGAESDEHFAQAIKGAFraleelrEEGVIKAIGLGVNDWEVILRI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 219 YERLKKRGIPLASnqvNYSLIYRAPEQTgVKAACDELGVTLIAYSPIAQGALTGKYTPENPPSGPRGriytREFLTKLQp 298
Cdd:cd19152 179 LEEADLDWVMLAG---RYTLLDHSAARE-LLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPAP----PELIARRD- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 18390678 299 llnRIKQIGENYSKTPTQIALNWLVAQGNVIP-IPGAKNAEQAKE 342
Cdd:cd19152 250 ---RIEALCEQHGVSLAAAALQFALAPPAVASvAPGASSPERVEE 291
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
84-329 |
4.59e-08 |
|
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: 54.16 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 84 LKAAKGAfdtsLDNGIDFFDTAEVYGSKFSLG-AISSETLLGRFIRErkerypgaEVSVATKfaaLPWRFGR-ESVVTAL 161
Cdd:cd19108 30 LEATKLA----IDAGFRHIDSAYLYQNEEEVGqAIRSKIADGTVKRE--------DIFYTSK---LWCTFHRpELVRPAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 162 KDSLSRLELSSVDLYQLHWP-GLWGNEGYL--DGLG-------------DAVEQ----GLVKAVGVSNYSEKRLrdayER 221
Cdd:cd19108 95 EKSLKKLQLDYVDLYLIHFPvALKPGEELFpkDENGklifdtvdlcatwEAMEKckdaGLAKSIGVSNFNRRQL----EM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 222 -LKKRGI---PLAsNQVNYSLIYrapEQTGVKAACDELGVTLIAYSpiaqgAL-TGKYTPENPPSGPrgriytreFLTKl 296
Cdd:cd19108 171 iLNKPGLkykPVC-NQVECHPYL---NQSKLLDFCKSKDIVLVAYS-----ALgSQRDKEWVDQNSP--------VLLE- 232
|
250 260 270
....*....|....*....|....*....|...
gi 18390678 297 QPLLNrikQIGENYSKTPTQIALNWLVAQGNVI 329
Cdd:cd19108 233 DPVLC---ALAKKHKRTPALIALRYQLQRGVVV 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
155-367 |
7.11e-08 |
|
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: 53.60 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 155 ESVVTALKDSLSRLELSSVDLYQLHWP--------------GLWGNEG----YLD--------GLGDAVEQGLVKAVGVS 208
Cdd:cd19113 85 KNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppGFYCGDGdnfvYEDvpildtwkALEKLVDAGKIKSIGVS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 209 NYSEKRLRDAyerLKKRGIPLASNQVNYSLIYRAPEqtgVKAACDELGVTLIAYSPIaqgaltgkytpenppsGPRGRIY 288
Cdd:cd19113 165 NFPGALILDL---LRGATIKPAVLQIEHHPYLQQPK---LIEYAQKAGITITAYSSF----------------GPQSFVE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 289 TREFLTKLQPLL---NRIKQIGENYSKTPTQIALNWlVAQGNVIPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASE 365
Cdd:cd19113 223 LNQGRALNTPTLfehDTIKSIAAKHNKTPAQVLLRW-ATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
..
gi 18390678 366 IK 367
Cdd:cd19113 302 LR 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
87-297 |
7.86e-08 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 53.31 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 87 AKGAFDTSLDNGIDFFDTAEVYGskfslgAISSETLLGRFIRerKERYPGAEVSVATK---FAALPWRFGRESVVTALKD 163
Cdd:cd19153 35 AVAIVAEAFAAGINHFDTSPYYG------AESSEAVLGKALA--ALQVPRSSYTVATKvgrYRDSEFDYSAERVRASVAT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 164 SLSRLELSSVDLYQLHwpglwgNEGYLDGLGDAVE----------QGLVKAVGVSNYSEKRLRDAYERLKKRGIPLASNQ 233
Cdd:cd19153 107 SLERLHTTYLDVVYLH------DIEFVDYDTLVDEalpalrtlkdEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAVLSY 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390678 234 VNYS-----LIYRAPEQtgVKAAcdelGVTLIAYSPIAQGALTGKYTPENPPSGPRGRIYTREFLTKLQ 297
Cdd:cd19153 181 CHLTlqdarLESDAPGL--VRGA----GPHVINASPLSMGLLTSQGPPPWHPASGELRHYAAAADAVCA 243
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
95-358 |
6.27e-07 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 50.35 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 95 LDNGIDFFDTAEVYGskfslgaiSSETLLGRFIRERKERYPGAEVSVATKFAAL-PWRF--GRESVVTALKDSLSRLELS 171
Cdd:cd19164 44 LELGIRAFDTSPYYG--------PSEIILGRALKALRDEFPRDTYFIITKVGRYgPDDFdySPEWIRASVERSLRRLHTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 172 SVDLYQLHWPGLWGNEGYLDGLGDAVE---QGLVKAVGVSNYSEKRLRDAYERLKKR-GIPLAS-------NQVNYSLiy 240
Cdd:cd19164 116 YLDLVYLHDVEFVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVLLRLAELARTTaGRPLDAvlsychyTLQNTTL-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 241 raPEQTGVKAACDELGVTLIAySPIAQGALTGKYTPENPPSGPRGRIYTREFLTKLQPLLNRIKQIGENYsktptqiALN 320
Cdd:cd19164 194 --LAYIPKFLAAAGVKVVLNA-SPLSMGLLRSQGPPEWHPASPELRAAAAKAAEYCQAKGTDLADVALRY-------ALR 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 18390678 321 WLVAQG-NVIpipGAKNAEQAKEfAGAIGWSLTDNEVSE 358
Cdd:cd19164 264 EWGGEGpTVV---GCSNVDELEE-AVEAYWSVLAGASEE 298
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
98-367 |
2.55e-06 |
|
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: 48.71 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 98 GIDFFDTAEVYGSKFSLG-AISSETLLGRFIRErkerypgaEVSVATKFaalpWR--FGRESVVTALKDSLSRLELSSVD 174
Cdd:cd19114 30 GYRLIDGALLYGNEAEVGrGIRKAIQEGLVKRE--------DLFIVTKL----WNnfHGKDHVREAFDRQLKDYGLDYID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 175 LYQLHWP-------------GLWgNEGYLDG--------------LGDAVEQGLVKAVGVSNYSEKRLRD--AYERLKKR 225
Cdd:cd19114 98 LYLIHFPipaayvdpaenypFLW-KDKELKKfpleqspmqecwreMEKLVDAGLVRNIGIANFNVQLILDllTYAKIKPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 226 GIPLASN---QVNySLIYRAPEQtgvkaacdelGVTLIAYSPIAQGALTgKYTPENppsgprgriytreflTKLQPLLNR 302
Cdd:cd19114 177 VLQIEHHpylQQK-RLIDWAKKQ----------GIQITAYSSFGNAVYT-KVTKHL---------------KHFTNLLEH 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390678 303 --IKQIGENYSKTPTQIALNWLVAQGNVIpIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLASEIK 367
Cdd:cd19114 230 pvVKKLADKHKRDTGQVLLRWAVQRNITV-IPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
85-206 |
2.17e-05 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 45.78 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 85 KAAKGAFDTSLDNGIDFFDTAEVYGskFSLgaisSETLLGRFIRErkerYPGAEVSVATK-------------------F 145
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYG--HGL----AEHRLGDFLRE----KPRDEFVLSTKvgrllkparegsvpdpngfV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390678 146 AALPWR----FGRESVVTALKDSLSRLELSSVDLYQLH-----WPG------LWGN--EGYLDGLGDAVEQGLVKAVG 206
Cdd:cd19161 90 DPLPFEivydYSYDGIMRSFEDSLQRLGLNRIDILYVHdigvyTHGdrkerhHFAQlmSGGFKALEELKKAGVIKAFG 167
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
92-363 |
1.37e-04 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 43.49 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 92 DTSLDNGIDFFDTAEVYGskfslgaiSSETLLGRFIRERKERyPGAeVSVATKFA---ALPWRFgrESVVTALKD-SLSR 167
Cdd:cd19098 42 DAAWAAGVRYFDAARSYG--------RAEEFLGSWLRSRNIA-PDA-VFVGSKWGytyTADWQV--DAAVHEVKDhSLAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 168 LEL----------SSVDLYQLHW----PGLWGNEGYLDGLGDAVEQGLvkAVGVSNYSEKR---LRDAYERLKKRGIPLA 230
Cdd:cd19098 110 LLKqweetrsllgKHLDLYQIHSatleSGVLEDADVLAALAELKAEGV--KIGLSLSGPQQaetLRRALEIEIDGARLFD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390678 231 SNQVNYSLIyrapEQTGVKA--ACDELGVTLIAYSPIAQGALTgkytpenppsgprGRIYTREFLTKLQPLlnriKQIGE 308
Cdd:cd19098 188 SVQATWNLL----EQSAGEAleEAHEAGMGVIVKEALANGRLT-------------DRNPSPELAPLMAVL----KAVAD 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 18390678 309 NYSKTPTQIALNWLVAQGNV-IPIPGAKNAEQAKEFAGAIGWSLTDNEVSELRSLA 363
Cdd:cd19098 247 RLGVTPDALALAAVLAQPFVdVVLSGAATPEQLRSNLRALDVSLDLELLAALADLA 302
|
|
| |
