|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-269 |
4.48e-161 |
|
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: 448.24 E-value: 4.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 4 KMIQFSGDVSLPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYP 83
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCAT 163
Cdd:cd19138 81 SNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 164 NQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQAGRLRNGLLKNAVVNEIAHAHNISSAQVLLAWVISHQGVMAIPKA 243
Cdd:cd19138 161 NQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAIPKS 240
|
250 260
....*....|....*....|....*.
gi 447109083 244 ATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19138 241 GSPEHARENAAAADLELTEEDLAELD 266
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
12-271 |
7.66e-114 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 328.17 E-value: 7.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDAsqrktEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPWNAGG 88
Cdd:COG0656 3 VEIPALGLGTWQLPGEE-----AAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIaaSGVpREELFVTTKVWNDNHGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGnQCATNQVLY 168
Cdd:COG0656 75 DDTLAAFEESLERLGLDYLDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGV-KPAVNQVEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 169 HLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAgrlrnGLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAH 248
Cdd:COG0656 154 HPYLQ--QRELLAFCREHGIVVEAYSPLGRG-----KLLDDPVLAEIAEKHGKTPAQVVLRWHL-QRGVVVIPKSVTPER 225
|
250 260
....*....|....*....|...
gi 447109083 249 VQQNAAVLEVELSSAELTMLDKA 271
Cdd:COG0656 226 IRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-269 |
2.49e-109 |
|
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: 316.86 E-value: 2.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMGE----DASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYPWN 85
Cdd:cd19072 1 GEEVPVLGLGTWGIGGgmskDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFdREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLHRSGSF-AFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCATN 164
Cdd:cd19072 81 LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSiPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 165 QVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQaGRLRNGLLKnAVVNEIAHAHNISSAQVLLAWVISHQGVMAIPKAA 244
Cdd:cd19072 161 QVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEK-GKLSNAKGS-PLLDEIAKKYGKTPAQIALNWLISKPNVIAIPKAS 238
|
250 260
....*....|....*....|....*
gi 447109083 245 TIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19072 239 NIEHLEENAGALGWELSEEDLQRLD 263
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-274 |
3.74e-79 |
|
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: 242.01 E-value: 3.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQFSGdVSLPAIGQGTWYMGEDASQ--RKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFL 77
Cdd:COG0667 1 MEYRRLGRSG-LKVSRLGLGTMTFGGPWGGvdEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRpRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 78 VSKVY------PWNAGGQKA--INACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYAD 148
Cdd:COG0667 80 ATKVGrrmgpgPNGRGLSREhiRRAVEASLRRLGTDYIDLYQLHRpDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 149 MQE-LWQLPGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNG------------------- 205
Cdd:COG0667 160 LRRaLAIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGgllTGKYRRGatfpegdraatnfvqgylt 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447109083 206 ---LLKNAVVNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSSAELTMLDKAYPA 274
Cdd:COG0667 240 ernLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTsVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-271 |
9.84e-78 |
|
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: 237.87 E-value: 9.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGED----ASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYPWNAGGQ 89
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPDNLTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 90 KAINACEASLRRLNTDYLDLYLLH-RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpggNQCATNQVLY 168
Cdd:cd19085 81 DVRKSCERSLKRLGTDYIDLYQIHwPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDA---GRIDSNQLPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 169 HLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ--------------AGRLRNGLLK-----------NAV--VNEIAHAHNI 221
Cdd:cd19085 158 NLLWRAIEYEILPFCREHGIGVLAYSPLAQglltgkfssaedfpPGDARTRLFRhfepgaeeetfEALekLKEIADELGV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447109083 222 SSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19085 238 TMAQLALAWVLQQPGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
11-269 |
2.57e-76 |
|
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: 234.34 E-value: 2.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMGED---ASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYP-WNA 86
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLrWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAIN--------ACEASLRRLNTDYLDLYLLH-RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpg 157
Cdd:cd19084 81 GKGVTKDlspesirkEVEQSLRRLQTDYIDLYQIHwPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 158 gNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNG-------------------LLKN----AV 211
Cdd:cd19084 159 -GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQgllTGKYKKEptfppddrrsrfpffrgenFEKNleivDK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 212 VNEIAHAHNISSAQVLLAWVISHQGV-MAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19084 238 LKEIAEKYGKSLAQLAIAWTLAQPGVtSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
12-269 |
9.88e-71 |
|
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: 218.98 E-value: 9.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMG----EDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYPWNA 86
Cdd:cd19137 2 EKIPALGLGTWGIGgfltPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFpREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAINACEASLRRLNTDYLDLYLLH-RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpggnqCAT-- 163
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHwPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISK-----SQTpi 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 164 --NQVLYHLGSRGIEYD-LLPWCQQQQMPVMAYSPLAqagrlRNGLLKNAVVNEIAHAHNISSAQVLLAWVISHQGVMAI 240
Cdd:cd19137 157 vcNQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLR-----RGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVAI 231
|
250 260
....*....|....*....|....*....
gi 447109083 241 PKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19137 232 PKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-272 |
9.19e-68 |
|
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: 212.17 E-value: 9.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMG--EDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL---RDNVFLVSKV----YPWNAG 87
Cdd:pfam00248 1 IGLGTWQLGggWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpvkRDKVVIATKVpdgdGPWPSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 88 GQKA--INACEASLRRLNTDYLDLYLLHRS-GSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGnQCATN 164
Cdd:pfam00248 81 GSKEniRKSLEESLKRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKI-PIVAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 165 QVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQaGRLRNGLLKNA-----------------------VVNEIAHAHNI 221
Cdd:pfam00248 160 QVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGG-GLLTGKYTRDPdkgpgerrrllkkgtplnlealeALEEIAKEHGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447109083 222 SSAQVLLAWVISHQGV-MAIPKAATIAHVQQNAAVLEVELSSAELTMLDKAY 272
Cdd:pfam00248 239 SPAQVALRWALSKPGVtIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-269 |
1.40e-67 |
|
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: 210.42 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDASQRktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL---RDNVFLVSKVYPWNAGGQK 90
Cdd:cd19071 1 MPLIGLGTYKLKPEETAE-----AVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESgvpREELFITTKLWPTDHGYER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 91 AINACEASLRRLNTDYLDLYLLH-------RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQ----LPggn 159
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHwpvpgkeGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAaariKP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 160 qcATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLaqaGRLRNGLLKNAVVNEIAHAHNISSAQVLLAWVISHqGVMA 239
Cdd:cd19071 150 --AVNQIELHPYLQ--QKELVEFCKEHGIVVQAYSPL---GRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GVVV 221
|
250 260 270
....*....|....*....|....*....|
gi 447109083 240 IPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19071 222 IPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
15-254 |
1.17e-62 |
|
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: 197.36 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGEDASQRKTEvAALRAGIELGLTLIDTAEMYADGGAEKVVGEAL--TGLRDNVFLVSKVYPWNAGGQKA- 91
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAF-ALLDAALEAGGNFFDTADVYGDGRSERLLGRWLkgRGNRDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 -------INACEASLRRLNTDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL---PGGNQ 160
Cdd:cd06660 80 rlspehiRRDLEESLRRLGTDYIDLYYLHRDDpSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYakaHGLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 CATNQVLYHLGSRG-IEYDLLPWCQQQQMPVMAYSPLAQagrlrnGLlknavvneiahahnissAQVLLAWVISHQGVM- 238
Cdd:cd06660 160 FAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLAR------GP-----------------AQLALAWLLSQPFVTv 216
|
250
....*....|....*.
gi 447109083 239 AIPKAATIAHVQQNAA 254
Cdd:cd06660 217 PIVGARSPEQLEENLA 232
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-270 |
1.95e-61 |
|
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: 194.78 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 9 SGDVSLPAIGQGTWYM-GEDAsqrkteVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPW 84
Cdd:cd19140 3 VNGVRIPALGLGTYPLtGEEC------TRAVEHALELGYRHIDTAQMY---GNEAQVGEAIaaSGVpRDELFLTTKVWPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 NAGGQKAINACEASLRRLNTDYLDLYLLHRSGS-FAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpGGNQCAT 163
Cdd:cd19140 74 NYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKdVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVEL-SEAPLFT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 164 NQVLYH--LGSRgieyDLLPWCQQQQMPVMAYSPLAqagrlRNGLLKNAVVNEIAHAHNISSAQVLLAWVISHQGVMAIP 241
Cdd:cd19140 153 NQVEYHpyLDQR----KLLDAAREHGIALTAYSPLA-----RGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEGVAAIP 223
|
250 260
....*....|....*....|....*....
gi 447109083 242 KAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19140 224 KATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-269 |
3.35e-58 |
|
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: 186.32 E-value: 3.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYM-GEDASQrktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL---RDNVFLVSKVYPWNAGGQ 89
Cdd:cd19073 1 IPALGLGTWQLrGDDCAN------AVKEALELGYRHIDTAEIY---NNEAEVGEAIAESgvpREDLFITTKVWRDHLRPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 90 KAINACEASLRRLNTDYLDLYLLHRSGS-FAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpGGNQCATNQVLY 168
Cdd:cd19073 72 DLKKSVDRSLEKLGTDYVDLLLIHWPNPtVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDI-SPLPIAVNQVEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 169 HLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGRLRngllkNAVVNEIAHAHNISSAQVLLAWVIShQGVMAIPKAATIAH 248
Cdd:cd19073 151 HPFLY--QAELLEYCRENDIVITAYSPLARGEVLR-----DPVIQEIAEKYDKTPAQVALRWLVQ-KGIVVIPKASSEDH 222
|
250 260
....*....|....*....|.
gi 447109083 249 VQQNAAVLEVELSSAELTMLD 269
Cdd:cd19073 223 LKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
14-269 |
1.17e-56 |
|
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: 183.97 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTW------YMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEAL--TGLRDNVFLVSKV--YP 83
Cdd:cd19093 2 VSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLkeLGDRDEVVIATKFapLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAF--EETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL--PGGN 159
Cdd:cd19093 82 WRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSqiEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKAlkERGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 160 QCATNQVLYHLGSRGIEYD-LLPWCQQQQMPVMAYSPLAQaGRL-------------RNGLL--KN--------AVVNEI 215
Cdd:cd19093 162 PLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQ-GLLtgkyspenpppggRRRLFgrKNlekvqpllDALEEI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447109083 216 AHAHNISSAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19093 241 AEKYGKTPAQVALNWLIA-KGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-270 |
1.36e-56 |
|
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: 182.83 E-value: 1.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMG--EDASQrktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNVFLVSKVYPW 84
Cdd:cd19136 1 MPILGLGTFRLRgeEEVRQ------AVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyglsREDIFITSKLAPK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 NAGGQKAINACEASLRRLNTDYLDLYLLH-------RSGSFAFE----ETVAAMEKLIAQGKIRRWGVSNLDYADMQEL- 152
Cdd:cd19136 72 DQGYEKARAACLGSLERLGTDYLDLYLIHwpgvqglKPSDPRNAelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 153 --WQLPggnqCATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLaqaGRLRNGLLKNAVVNEIAHAHNISSAQVLLAW 230
Cdd:cd19136 152 kyCEVP----PAVNQVEFH--PHLVQKELLKFCKDHGIHLQAYSSL---GSGDLRLLEDPTVLAIAKKYGRTPAQVLLRW 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447109083 231 VISHqGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19136 223 ALQQ-GIGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
11-270 |
1.54e-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: 181.70 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMGEDASQRKTE----VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSK---VYP 83
Cdd:cd19149 8 GIEASVIGLGTWAIGGGPWWGGSDdnesIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLATKcglRWD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNAGG------QKAIN----------ACEASLRRLNTDYLDLYLLH-RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDY 146
Cdd:cd19149 88 REGGSfffvrdGVTVYknlspesireEVEQSLKRLGTDYIDLYQTHwQDVETPIEETMEALEELKRQGKIRAIGASNVSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 147 ADMQELWQlpgGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ--------------AGRLRNG------- 205
Cdd:cd19149 168 EQIKEYVK---AGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQglltgkitpdrefdAGDARSGipwfspe 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447109083 206 -LLKNAVVNE----IAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19149 245 nREKVLALLEkwkpLCEKYGCTLAQLVIAWTLAQPGITsALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
20-273 |
2.96e-55 |
|
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: 180.85 E-value: 2.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 20 GTWYMGEDASqRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVY----PW-NAGGQKA--- 91
Cdd:cd19087 19 GTMNFGGRTD-EETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLATKVFgpmgDDpNDRGLSRrhi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNL---DYADMQELWQLPGGNQCATNQVL 167
Cdd:cd19087 98 RRAVEASLRRLQTDYIDLYQMHHFDRDTpLEETLRALDDLVRQGKIRYIGVSNFaawQIAKAQGIAARRGLLRFVSEQPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 168 YHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNG-------LLKNAVVNE----------------IAHAHNI 221
Cdd:cd19087 178 YNLLKRQAELEILPAARAYGLGVIPYSPLAGgllTGKYGKGkrpesgrLVERARYQArygleeyrdiaerfeaLAAEAGL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447109083 222 SSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSAELTMLDKAYP 273
Cdd:cd19087 258 TPASLALAWVLSHPAVTSpIIGPRTLEQLEDSLAALEITLTPELLAEIDELFP 310
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-264 |
2.52e-54 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 178.04 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQfSGDVSLPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALT---GLRDNVFL 77
Cdd:COG4989 1 MKRIKLG-ASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKlspSLREKIEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 78 VSK---VYPWNAGGQKA----------INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSN 143
Cdd:COG4989 80 QTKcgiRLPSEARDNRVkhydtskehiIASVEGSLRRLGTDYLDLLLLHRPDPLMdPEEVAEAFDELKASGKVRHFGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 144 LDYADMqELWQLPGGNQCATNQV---LYHLGSrgIEYDLLPWCQQQQMPVMAYSPLAQaGRLRNGLLK-----NAVVNEI 215
Cdd:COG4989 160 FTPSQF-ELLQSALDQPLVTNQIelsLLHTDA--FDDGTLDYCQLNGITPMAWSPLAG-GRLFGGFDEqfprlRAALDEL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447109083 216 AHAHNISSAQVLLAWVISH-QGVMAIPKAATIAHVQQNAAVLEVELSSAE 264
Cdd:COG4989 236 AEKYGVSPEAIALAWLLRHpAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
12-255 |
1.36e-53 |
|
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: 174.20 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSlpAIGQGTWYMGEDASQRKTE---VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKV-YPWNAG 87
Cdd:cd19086 3 VS--EIGFGTWGLGGDWWGDVDDaeaIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFgNRFDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 88 GQKAIN--------ACEASLRRLNTDYLDLYLLHrSGSFAF---EETVAAMEKLIAQGKIRRWGVSnLDYADmqELWQLP 156
Cdd:cd19086 81 PERPQDfspeyireAVEASLKRLGTDYIDLYQLH-NPPDEVldnDELFEALEKLKQEGKIRAYGVS-VGDPE--EALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 157 GGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRLrngllknavvneiahahnissAQVLLAWVIS 233
Cdd:cd19086 157 RRGGIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASgllTGKL---------------------AQAALRFILS 215
|
250 260
....*....|....*....|...
gi 447109083 234 HQGV-MAIPKAATIAHVQQNAAV 255
Cdd:cd19086 216 HPAVsTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-272 |
1.81e-52 |
|
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: 173.24 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 16 AIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYP-WNAGGQ----- 89
Cdd:cd19102 10 AIGGGGWGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLlWDEEGRirrsl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 90 --KAINA-CEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQelwqlpggnQC---- 161
Cdd:cd19102 90 kpASIRAeCEASLRRLGVDVIDLYQIHWpDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMK---------RCqaih 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 162 --ATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAqagrlrNGLLKNAVVNE------------------------- 214
Cdd:cd19102 161 piASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQ------SGLLTGKMTPErvaslpaddwrrrspffqepnlarn 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447109083 215 ---------IAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSSAELTMLDKAY 272
Cdd:cd19102 235 lalvdalrpIAERHGRTVAQLAIAWVLRRPEVTsAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-269 |
4.54e-52 |
|
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: 172.38 E-value: 4.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 10 GDVSLPAIGQGTWYMGEDASqRKTevaaLRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL--RDNVFLVSKVYP---- 83
Cdd:cd19079 18 GCMSFGDPKWRPWVLDEEES-RPI----IKRALDLGINFFDTANVYSGGASEEILGRALKEFapRDEVVIATKVYFpmgd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 -WNAGG--QKAI-NACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNL---DYADMQELWQL 155
Cdd:cd19079 93 gPNGRGlsRKHImAEVDASLKRLGTDYIDLYQIHRwDYETPIEETLEALHDVVKSGKVRYIGASSMyawQFAKALHLAEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 156 PGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQaGRL---------------RNGLLKNAV--------- 211
Cdd:cd19079 173 NGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLAR-GRLarpwgdtterrrsttDTAKLKYDYfteadkeiv 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447109083 212 --VNEIAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19079 252 drVEEVAKERGVSMAQVALAWLLSKPGVTApIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-264 |
1.18e-51 |
|
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: 170.81 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 9 SGDVSLPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEAL---TGLRDNVFLVSK---VY 82
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALalnPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 PWNAGGQKA----------INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNldYADMQ- 150
Cdd:cd19092 81 GDDPRPGRIkhydtskehiLASVEGSLKRLGTDYLDLLLLHRPDPLMdPEEVAEAFDELVKSGKVRYFGVSN--FTPSQi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 151 ELWQLPGGNQCATNQV---LYHLGSrgIEYDLLPWCQQQQMPVMAYSPLaQAGRLRNGLLK-----NAVVNEIAHAHNIS 222
Cdd:cd19092 159 ELLQSYLDQPLVTNQIelsLLHTEA--IDDGTLDYCQLLDITPMAWSPL-GGGRLFGGFDErfqrlRAALEELAEEYGVT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447109083 223 SAQVLLAWVISHqGVMAIPKAAT--IAHVQQNAAVLEVELSSAE 264
Cdd:cd19092 236 IEAIALAWLLRH-PARIQPILGTtnPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
12-265 |
8.01e-51 |
|
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: 168.93 E-value: 8.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDASQRKTE--VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSK-VYPWNAGG 88
Cdd:cd19076 10 LEVSALGLGCMGMSAFYGPADEEesIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIATKfGIVRDPGS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAIN---------ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL-Pg 157
Cdd:cd19076 90 GFRGVdgrpeyvraACEASLKRLGTDVIDLYYQHRvDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVhP- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 158 gnqCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLaqaGRlrnGLLKNAV-------------------------- 211
Cdd:cd19076 169 ---ITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPL---GR---GFLTGAIkspedlpeddfrrnnprfqgenfdkn 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447109083 212 ------VNEIAHAHNISSAQVLLAWVIsHQG--VMAIPKAATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19076 240 lklvekLEAIAAEKGCTPAQLALAWVL-AQGddIVPIPGTKRIKYLEENVGALDVVLTPEEL 300
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-269 |
1.67e-50 |
|
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: 167.12 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMGeDASQRKTeVAALRagiELGLTLIDTAEMYadgGAEKVVGEALT--GL-RDNVFLVSKVY 82
Cdd:cd19135 5 VRLSNGVEMPILGLGTSHSG-GYSHEAV-VYALK---ECGYRHIDTAKRY---GCEELLGKAIKesGVpREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 PWNAGGQKAINACEASLRRLNTDYLDLYLLH--------RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELwq 154
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHwpdcpssgKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 155 lpggNQCAT-----NQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQaGRlrngLLKNAVVNEIAHAHNISSAQVLLA 229
Cdd:cd19135 155 ----LEDCSvvphvNQVEFHPFQN--PVELIEYCRDNNIVFEGYCPLAK-GK----ALEEPTVTELAKKYQKTPAQILIR 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447109083 230 WVISHqGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19135 224 WSIQN-GVVTIPKSTKEERIKENCQVFDFSLSEEDMATLD 262
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
18-271 |
2.90e-49 |
|
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: 165.48 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 18 GQGTWYMGEDASQRKTEVAAL-RAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYPW-----NAGGQKA 91
Cdd:cd19091 24 GGGGGFFGAWGGVDQEEADRLvDIALDAGINFFDTADVYSEGESEEILGKALKGRRDDVLIATKVRGRmgegpNDVGLSR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 ---INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNL---DYADMQELWQLPGGNQCATN 164
Cdd:cd19091 104 hhiIRAVEASLKRLGTDYIDLYQLHGFDALTpLEETLRALDDLVRQGKVRYIGVSNFsawQIMKALGISERRGLARFVAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 165 QVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLA---------------QAGRLRNGLLKNAVVN------------EIAH 217
Cdd:cd19091 184 QAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAggllsgkyrrgqpapEGSRLRRTGFDFPPVDrergydvvdalrEIAK 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447109083 218 AHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19091 264 ETGATPAQVALAWLLSRPTVSsVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-262 |
5.05e-49 |
|
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: 164.30 E-value: 5.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTW--YMGEDASQRKTEVaaLRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYpWNAGGQKA-- 91
Cdd:cd19074 7 LSLGTWltFGGQVDDEDAKAC--VRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWpRESYVISTKVF-WPTGPGPNdr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 -------INACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL---PGGNQ 160
Cdd:cd19074 84 glsrkhiFESIHASLKRLQLDYVDIYYCHRyDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLarqFGLIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 CATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNG----------------LLKNAVVNE------- 214
Cdd:cd19074 164 PVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQgllTGKYRDGipppsrsratdednrdKKRRLLTDEnlekvkk 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447109083 215 ---IAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELSS 262
Cdd:cd19074 244 lkpIADELGLTLAQLALAWCLRNPAVSsAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
13-271 |
4.28e-48 |
|
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: 160.86 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGT---WYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPwna 86
Cdd:cd19120 3 KIPAIAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALkeSGVpREDLFITTKVSP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAINACEASLRRLNTDYLDLYLLH-----RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL----Pg 157
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHspffaKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTakikP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 158 gnqcATNQVLYH--LGSRGIeyDLLPWCQQQQMPVMAYSPLAQAGRLRNGLLKnAVVNEIAHAHNISSAQVLLAWVIShQ 235
Cdd:cd19120 156 ----AVNQIEFHpyLYPQQP--ALLEYCREHGIVVSAYSPLSPLTRDAGGPLD-PVLEKIAEKYGVTPAQVLLRWALQ-K 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 447109083 236 GVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19120 228 GIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
12-269 |
1.91e-47 |
|
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: 159.09 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMgEDASQrktEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEALT--GL-RDNVFLVSKVypWNA-- 86
Cdd:cd19157 8 VKMPWLGLGVFKV-EEGSE---VVNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKesGIpREELFITSKV--WNAdq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQ----LPggnqcA 162
Cdd:cd19157 79 GYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAdaeiVP-----M 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 163 TNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAgrlrnGLLKNAVVNEIAHAHNISSAQVLLAWVISHqGVMAIPK 242
Cdd:cd19157 154 VNQVEFH--PRLTQKELRDYCKKQGIQLEAWSPLMQG-----QLLDNPVLKEIAEKYNKSVAQVILRWDLQN-GVVTIPK 225
|
250 260
....*....|....*....|....*..
gi 447109083 243 AATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19157 226 SIKEHRIIENADVFDFELSQEDMDKID 252
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-270 |
3.02e-47 |
|
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: 158.29 E-value: 3.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDASqrkteVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPWNAGGQK 90
Cdd:cd19139 1 IPAFGLGTFRLKDDVV-----IDSVRTALELGYRHIDTAQIY---DNEAAVGQAIaeSGVpRDELFITTKIWIDNLSKDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 91 AINACEASLRRLNTDYLDLYLLH---RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCATNQVL 167
Cdd:cd19139 73 LLPSLEESLEKLRTDYVDLTLIHwpsPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 168 YH--LGSRGieydLLPWCQQQQMPVMAYSPLAQaGRlrngLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAAT 245
Cdd:cd19139 153 LSpyLQNRK----LVAHCKQHGIHVTSYMTLAY-GK----VLDDPVLAAIAERHGATPAQIALAWAM-ARGYAVIPSSTK 222
|
250 260
....*....|....*....|....*
gi 447109083 246 IAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19139 223 REHLRSNLLALDLTLDADDMAAIAA 247
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
11-269 |
9.56e-47 |
|
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: 158.53 E-value: 9.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMGEDASqRKTEVAALRAGIELGLTLIDTAEMYAD-------GGAEKVVGEAL--TGLRDNVFLVSKV 81
Cdd:cd19081 6 GLSVSPLCLGTMVFGWTAD-EETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLksRGKRDRVVIATKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 YPWNAGG-----QKAIN-ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDyadmqeLWQ 154
Cdd:cd19081 85 GFPMGPNgpglsRKHIRrAVEASLRRLQTDYIDLYQAHWdDPATPLEETLGALNDLIRQGKVRYIGASNYS------AWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 155 LPGGNQCATN---------QVLYHLGSRG-IEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNG--------------LL 207
Cdd:cd19081 159 LQEALELSRQhglpryvslQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGgflTGKYRSEadlpgstrrgeaakRY 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 208 KN-------AVVNEIAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19081 239 LNerglrilDALDEVAAEHGATPAQVALAWLLARPGVTApIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
18-261 |
1.10e-46 |
|
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: 156.99 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 18 GQGTWYMGEDasqRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKV-------YPWNAGGQK 90
Cdd:cd19088 13 GPGIWGPPAD---REEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGglvrtgpGWWGPDGSP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 91 A--INACEASLRRLNTDYLDLYLLHRSGSF-AFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPggnQCATNQVL 167
Cdd:cd19088 90 EylRQAVEASLRRLGLDRIDLYQLHRIDPKvPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIV---RIVSVQNR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 168 YHLGSRGIEyDLLPWCQQQQMPVMAYSPLAQAGRLRNGLLknavVNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATI 246
Cdd:cd19088 167 YNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQPGGL----LAEVAARLGATPAQVALAWLLARSPVMlPIPGTSSV 241
|
250
....*....|....*
gi 447109083 247 AHVQQNAAVLEVELS 261
Cdd:cd19088 242 EHLEENLAAAGLRLS 256
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
12-269 |
3.28e-45 |
|
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: 154.68 E-value: 3.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGT------WYMGEDASQrktevAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKvYPW- 84
Cdd:cd19080 10 VSPLALGTMTfgtewgWGADREEAR-----AMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATK-YTMn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 ------NAGGQKAIN---ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLD---YADMQE 151
Cdd:cd19080 84 rrpgdpNAGGNHRKNlrrSVEASLRRLQTDYIDLLYVHAwDFTTPVEEVMRALDDLVRAGKVLYVGISDTPawvVARANT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 152 LWQLPGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAqAGRL----------RNGLLKN------------ 209
Cdd:cd19080 164 LAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLG-GGLLtgkyqrgeegRAGEAKGvtvgfgkltern 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447109083 210 ----AVVNEIAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19080 243 waivDVVAAVAEELGRSAAQVALAWVRQKPGVVIpIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
12-270 |
9.56e-45 |
|
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: 151.96 E-value: 9.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDASqrkTEVAALRAgIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPWNAGG 88
Cdd:cd19133 7 VEMPILGFGVFQIPDPEE---CERAVLEA-IKAGYRLIDTAAAY---GNEEAVGRAIkkSGIpREELFITTKLWIQDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAINACEASLRRLNTDYLDLYLLHRsgSFA-FEETVAAMEKLIAQGKIRRWGVSNLdYADMQELWQLPGGNQCATNQVL 167
Cdd:cd19133 80 EKAKKAFERSLKRLGLDYLDLYLIHQ--PFGdVYGAWRAMEELYKEGKIRAIGVSNF-YPDRLVDLILHNEVKPAVNQIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 168 YHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAgrlRNGLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIA 247
Cdd:cd19133 157 THPFNQ--QIEAVEFLKKYGVQIEAWGPFAEG---RNNLFENPVLTEIAEKYGKSVAQVILRWLI-QRGIVVIPKSVRPE 230
|
250 260
....*....|....*....|...
gi 447109083 248 HVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19133 231 RIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
6-270 |
3.00e-44 |
|
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: 151.67 E-value: 3.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMGEDasqrKTEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNVFLV 78
Cdd:cd19116 3 IKLNDGNEIPAIALGTWKLKDD----EGVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegvvkREDLFIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 79 SKVypWNAGGQKA--INACEASLRRLNTDYLDLYLLHRSGSFAFE-----------------ETVAAMEKLIAQGKIRRW 139
Cdd:cd19116 76 TKL--WNSYHEREqvEPALRESLKRLGLDYVDLYLIHWPVAFKENndsesngdgslsdidylETWRGMEDLVKLGLTRSI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 140 GVSNLDYADMQELWQL----PggnqcATNQVLYHLGSrgIEYDLLPWCQQQQMPVMAYSPLAQA----GRLRNGLLKNAV 211
Cdd:cd19116 154 GVSNFNSEQINRLLSNcnikP-----AVNQIEVHPTL--TQEKLVAYCQSNGIVVMAYSPFGRLvprgQTNPPPRLDDPT 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 212 VNEIAHAHNISSAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19116 227 LVAIAKKYGKTTAQIVLRYLID-RGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-269 |
6.26e-44 |
|
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: 149.90 E-value: 6.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMGEDasqrKTEVAALRAGIELGLTLIDTAEMYADggaEKVVGEAL--TGL-RDNVFLVSKVY 82
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDG----DETERAVQTALENGYRSIDTAAIYKN---EEGVGEAIreSGVpREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 PWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQ----LPgg 158
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAhadvVP-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 159 nqcATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAgrlrnGLLKNAVVNEIAHAHNISSAQVLLAWVISHqGVM 238
Cdd:cd19126 152 ---AVNQVEFH--PYLTQKELRGYCKSKGIVVEAWSPLGQG-----GLLSNPVLAAIGEKYGKSAAQVVLRWDIQH-GVV 220
|
250 260 270
....*....|....*....|....*....|.
gi 447109083 239 AIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19126 221 TIPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-265 |
2.24e-43 |
|
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: 148.29 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 5 MIQFSGDVSLPAIGQGTWYMGEDASqrkteVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKV 81
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEA-----ASAVREALEVGYRSIDTAAIY---GNEEGVGKAIraSGVpREELFITTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 ypWNA--GGQKAINACEASLRRLNTDYLDLYLLH----RSGSFAfeETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQl 155
Cdd:cd19131 73 --WNSdqGYDSTLRAFDESLRKLGLDYVDLYLIHwpvpAQDKYV--ETWKALIELKKEGRVKSIGVSNFTIEHLQRLID- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 156 PGGNQCATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQagrlrNGLLKNAVVNEIAHAHNISSAQVLLAWVIShQ 235
Cdd:cd19131 148 ETGVVPVVNQIELH--PRFQQRELRAFHAKHGIQTESWSPLGQ-----GGLLSDPVIGEIAEKHGKTPAQVVIRWHLQ-N 219
|
250 260 270
....*....|....*....|....*....|
gi 447109083 236 GVMAIPKAATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19131 220 GLVVIPKSVTPSRIAENFDVFDFELDADDM 249
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-207 |
1.53e-42 |
|
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: 147.45 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGED---ASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALT--GLRDNVFLVSKV-YPWNAGGQK 90
Cdd:cd19148 7 IALGTWAIGGWmwgGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKeyGKRDRVVIATKVgLEWDEGGEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 91 AINA--------CEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQlpgGNQC 161
Cdd:cd19148 87 VRNSsparirkeVEDSLRRLQTDYIDLYQVHWPDPLVpIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRK---VAPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447109083 162 ATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQagrlrnGLL 207
Cdd:cd19148 164 HTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCR------GLL 203
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
4-272 |
1.75e-42 |
|
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: 147.17 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 4 KMIQFSGDVSLPAIGQGTWYMGEDASQRktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEALT-----GL--RDNVF 76
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQ-----AVKQALEAGYRHIDCAAIY---GNEAEIGAALAevfkeGKvkREDLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 77 LVSKVypWNAGGQKA--INACEASLRRLNTDYLDLYLLH------------RSG----SFA---FEETVAAMEKLIAQGK 135
Cdd:cd19123 74 ITSKL--WNNSHAPEdvLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpESGedllSLSpipLEDTWRAMEELVDKGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 136 IRRWGVSNLDYADMQELW---QLPGgnqcATNQVLYH--LGSRgieyDLLPWCQQQQMPVMAYSPLAQAGRLRN------ 204
Cdd:cd19123 152 CRHIGVSNFSVKKLEDLLataRIKP----AVNQVELHpyLQQP----ELLAFCRDNGIHLTAYSPLGSGDRPAAmkaege 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447109083 205 -GLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAE---LTMLDKAY 272
Cdd:cd19123 224 pVLLEDPVINKIAEKHGASPAQVLIAWAI-QRGTVVIPKSVNPERIQQNLEAAEVELDASDmatIAALDRHH 294
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
13-269 |
3.34e-41 |
|
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: 142.79 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYM-GEDAsqrkteVAALRAGIELGLTLIDTAEMYADGGAekvVGEAL--TGL-RDNVFLVSKVYPWNAGG 88
Cdd:cd19132 6 QIPAIGFGTYPLkGDEG------VEAVVAALQAGYRLLDTAFNYENEGA---VGEAVrrSGVpREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAINACEASLRRLNTDYLDLYLLH----RSGSFAfeETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQ----LPggnq 160
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHwpnpSRDLYV--EAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDetgvTP---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 cATNQVLYHLGSRGIEydLLPWCQQQQMPVMAYSPLAQAgrlrNGLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAI 240
Cdd:cd19132 151 -AVNQIELHPYFPQAE--QRAYHREHGIVTQSWSPLGRG----SGLLDEPVIKAIAEKHGKTPAQVVLRWHV-QLGVVPI 222
|
250 260
....*....|....*....|....*....
gi 447109083 241 PKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19132 223 PKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
11-271 |
5.82e-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: 143.53 E-value: 5.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSlpAIGQGTwyMG-----EDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVYPWN 85
Cdd:cd19078 3 EVS--AIGLGC--MGmshgyGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAI-----------NACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNldyADMQELW 153
Cdd:cd19078 79 DGGKPGPlgldsrpehirKAVEGSLKRLQTDYIDLYYQHRvDPNVPIEEVAGTMKELIKEGKIRHWGLSE---AGVETIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 154 QLPGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRL-----------RNGLLKNA--------- 210
Cdd:cd19078 156 RAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKgflTGKIdentkfdegddRASLPRFTpealeanqa 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447109083 211 ---VVNEIAHAHNISSAQVLLAWVIsHQG--VMAIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19078 236 lvdLLKEFAEEKGATPAQIALAWLL-AKKpwIVPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-269 |
1.74e-40 |
|
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: 141.12 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMgEDASQrktEVAALRAGIELGLTLIDTAEMYADggaEKVVGEAL--TGL-RDNVFLVSKVy 82
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRV-QDGAE---AENAVKWAIEAGYRHIDTAAIYKN---EEGVGQGIreSGVpREEVFVTTKL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 pWNA--GGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQlpggnQ 160
Cdd:cd19156 73 -WNSdqGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLK-----S 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 CA----TNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAgrlrnGLLKNAVVNEIAHAHNISSAQVLLAWVISHqG 236
Cdd:cd19156 147 CKvapmVNQIELH--PLLTQEPLRKFCKEKNIAVEAWSPLGQG-----KLLSNPVLKAIGKKYGKSAAQVIIRWDIQH-G 218
|
250 260 270
....*....|....*....|....*....|...
gi 447109083 237 VMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19156 219 IITIPKSVHEERIQENFDVFDFELTAEEIRQID 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
6-270 |
1.40e-39 |
|
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: 139.85 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMGEDASqrkteVAALRAGIELGLTLIDTAEMYADggaEKVVGEAL-----TGL--RDNVFLV 78
Cdd:cd19154 4 ITLSNGVKMPLIGLGTWQSKGAEG-----ITAVRTALKAGYRLIDTAFLYQN---EEAIGEALaelleEGVvkREDLFIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 79 SKVYPWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSF--------------------AFEETVAAMEKLIAQGKIRR 138
Cdd:cd19154 76 TKLWTHEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFkddegesgtmengmsihdavDVEDVWRGMEKVYDEGLTKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 139 WGVSNLDYADMQELWQLpGGNQCATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGR----LRNG------LLK 208
Cdd:cd19154 156 IGVSNFNNDQIQRILDN-ARVKPHNNQVECHLYFP--QKELVEFCKKHNISVTSYATLGSPGRanftKSTGvspapnLLQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447109083 209 NAVVNEIAHAHNISSAQVLLAWVISHqGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19154 233 DPIVKAIAEKHGKTPAQVLLRYLLQR-GIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEE 293
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
11-272 |
3.96e-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: 138.71 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMG--------EDASQRKTEVAALRAGIelglTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKV 81
Cdd:cd19083 8 DIDVNPIGLGTNAVGghnlypnlDEEEGKDLVREALDNGV----NLLDTAFIYGLGRSEELVGEVLKEYnRNEVVIATKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 YPWNAGGQKAIN--------ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQEl 152
Cdd:cd19083 84 AHKFGGDGSVLNnspeflrsAVEKSLKRLNTDYIDLYYIHFpDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 153 wqLPGGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLA--------------------------QAGRLRNGL 206
Cdd:cd19083 163 --ANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLAsgllagkytkdtkfpdndlrndkplfKGERFSENL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 207 LKNAVVNEIAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSAELTMLDKAY 272
Cdd:cd19083 241 DKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
17-261 |
3.18e-38 |
|
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: 136.93 E-value: 3.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGEDASQRKTeVAALRAGIELGLTLIDTAEMYA-------DGGAEKVVGEAL--TGLRDNVFLVSKV------ 81
Cdd:cd19094 4 ICLGTMTWGEQNTEAEA-HEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLkkKGNRDKVVLATKVagpgeg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 YPWNAGGQKAIN------ACEASLRRLNTDYLDLYLLH-------------------RSGSFAFEETVAAMEKLIAQGKI 136
Cdd:cd19094 83 ITWPRGGGTRLDrenireAVEGSLKRLGTDYIDLYQLHwpdrytplfgggyytepseEEDSVSFEEQLEALGELVKAGKI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 137 RRWGVSN------LDYADMQELWQLPggnQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ------------ 198
Cdd:cd19094 163 RHIGLSNetpwgvMKFLELAEQLGLP---RIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGgvltgkyldgaa 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 199 -------------AGRLRNGLLKNAV--VNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLEVELS 261
Cdd:cd19094 240 rpeggrlnlfpgyMARYRSPQALEAVaeYVKLARKHGLSPAQLALAWVRSRPFVTsTIIGATTLEQLKENIDAFDVPLS 318
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
15-255 |
3.83e-37 |
|
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: 131.97 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGT---WYMGEDASQRKTEvAALRAGIELGLTLIDTAEMYadGGAEKVVGEALTGL-RDNVFLVSKV-YPWNAGGQ 89
Cdd:cd19095 1 SVLGLGTsgiGRVWGVPSEAEAA-RLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLrRDDLFIATKVgTHGEGGRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 90 -------KAINACEASLRRLNTDYLDLYLLHRSGSFAF-EETVAAMEKLIAQGKIRRWGVSNldyaDMQELWQLpggnqC 161
Cdd:cd19095 78 rkdfspaAIRASIERSLRRLGTDYIDLLQLHGPSDDELtGEVLETLEDLKAAGKVRYIGVSG----DGEELEAA-----I 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 162 ATN-----QVLYHLGSRGIEyDLLPWCQQQQMPVMAYSPLAQA------GRLRNGLLKNAVVNEIAHAHNISSAQVLLAW 230
Cdd:cd19095 149 ASGvfdvvQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGrlrrrvRRRPLYADYARRPEFAAEIGGATWAQAALRF 227
|
250 260
....*....|....*....|....*.
gi 447109083 231 VISHQGV-MAIPKAATIAHVQQNAAV 255
Cdd:cd19095 228 VLSHPGVsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
17-257 |
1.99e-36 |
|
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: 131.52 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDnvFLV-SKVYPWNAGGQKA---I 92
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERG--FKIdTKANPGVGGGLSPenvR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 93 NACEASLRRLNTDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpggnqCATN------- 164
Cdd:cd19075 83 KQLETSLKRLKVDKVDVFYLHAPDrSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEI-----CKENgwvlptv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 165 -QVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLA---------------QAGRLR--NGLLKN--------------AVV 212
Cdd:cd19075 158 yQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAggfltgkykysedkaGGGRFDpnNALGKLyrdrywkpsyfealEKV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447109083 213 NEIAHAHNISSAQVLLAWVISHQ--------GVmaIPKAATIAHVQQNAAVLE 257
Cdd:cd19075 238 EEAAEKEGISLAEAALRWLYHHSaldgekgdGV--ILGASSLEQLEENLAALE 288
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
13-270 |
3.14e-36 |
|
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: 130.34 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWymgedaSQRKTEV-AALRAGIELGLTLIDTAEMYadgGAEKVVG----EALTGL--RDNVFLVSKVypWN 85
Cdd:cd19121 11 SIPAVGLGTW------QAKAGEVkAAVAHALKIGYRHIDGALCY---QNEDEVGegikEAIAGGvkREDLFVTTKL--WS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLH-----------------RSGSFAFE------ETVAAMEKLIAQGKIRRWGVS 142
Cdd:cd19121 80 TYHRRVELCLDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptlPDGSRDLDwdwnhvDTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 143 NLDYADMQELwqLPGGNQC-ATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAGrlrNGLLKNAVVNEIAHAHNI 221
Cdd:cd19121 160 NYSIPYLEEL--LKHATVVpAVNQVENH--PYLPQQELVDFCKEKGILIEAYSPLGSTG---SPLISDEPVVEIAKKHNV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447109083 222 SSAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVleVELSSAELTMLDK 270
Cdd:cd19121 233 GPGTVLISYQVA-RGAVVLPKSVTPDRIKSNLEI--IDLDDEDMNKLND 278
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
11-271 |
3.50e-36 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 132.25 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMgedasQRKTEVAA---LRAGIELGLTLIDTAEMYadGGAEKVVGEALTGLRDNVFLVSKVYPWNAG 87
Cdd:COG1453 10 GLEVSVLGFGGMRL-----PRKDEEEAealIRRAIDNGINYIDTARGY--GDSEEFLGKALKGPRDKVILATKLPPWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 88 GQKAINACEASLRRLNTDYLDLYLLHRSGSFA-FEETV------AAMEKLIAQGKIRRWGVSN-LDYADMQELwqlpggn 159
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEdLEKVLkpggalEALEKAKAEGKIRHIGFSThGSLEVIKEA------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 160 qCATNQ---VLYHL---------GSRGIEYdllpwCQQQQMPVMAYSPLAqAGRLRNgllKNAVVNEIAHAhNISSAQVL 227
Cdd:COG1453 156 -IDTGDfdfVQLQYnyldqdnqaGEEALEA-----AAEKGIGVIIMKPLK-GGRLAN---PPEKLVELLCP-PLSPAEWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447109083 228 LAWVISHQGV-MAIPKAATIAHVQQNAAVLE--VELSSAELTMLDKA 271
Cdd:COG1453 225 LRFLLSHPEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERL 271
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-265 |
7.65e-36 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 128.99 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYMGEDASqrkteVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVYPWNAGGQ 89
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVV-----IDSVKTALELGYRAIDTAQIY---DNEAAVGQAIaeSGVpRDELFITTKIWIDNLAKD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 90 KAINACEASLRRLNTDYLDLYLLH---RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCATNQV 166
Cdd:PRK11172 74 KLIPSLKESLQKLRTDYVDLTLIHwpsPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 167 LYH--LGSRgieyDLLPWCQQQQMPVMAYSPLAqAGRlrngLLKNAVVNEIAHAHNISSAQVLLAWVIShQGVMAIPKAA 244
Cdd:PRK11172 154 ELSpyLQNR----KVVAFAKEHGIHVTSYMTLA-YGK----VLKDPVIARIAAKHNATPAQVILAWAMQ-LGYSVIPSST 223
|
250 260
....*....|....*....|.
gi 447109083 245 TIAHVQQNAAVLEVELSSAEL 265
Cdd:PRK11172 224 KRENLASNLLAQDLQLDAEDM 244
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-269 |
2.28e-35 |
|
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: 127.91 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWymgedASQRKTEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVY 82
Cdd:cd19127 1 ITLNNGVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAY---GNEREVGEGIrrSGVdRSDIFVTTKLW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 PWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEETVA---AMEKLIAQGKIRRWGVSNLDYADMQELWQ----L 155
Cdd:cd19127 73 ISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTIQaykALEKLLAEGRVRAIGVSNFTPEHLERLIDattvV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 156 PggnqcATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAGRLRNG-------LLKNAVVNEIAHAHNISSAQVLL 228
Cdd:cd19127 153 P-----AVNQVELH--PYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgptgpgdVLQDPTITGLAEKYGKTPAQIVL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 447109083 229 AWVISHqGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19127 226 RWHLQN-GVSAIPKSVHPERIAENIDIFDFALSAEDMAAID 265
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-269 |
9.53e-35 |
|
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: 126.84 E-value: 9.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 3 QKMIQFSGDVSLPAIGQGTWYMGEDASqRKTEVAALRAGielgLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVS 79
Cdd:cd19117 3 SKTFKLNTGAEIPAVGLGTWQSKPNEV-AKAVEAALKAG----YRHIDTAAIY---GNEEEVGQGIkdSGVpREEIFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 80 KVypWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGS----------------------FAFEETVAAMEKLIAQGKIR 137
Cdd:cd19117 75 KL--WCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPldpdgndflfkkddgtkdhepdWDFIKTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 138 RWGVSNLDYADMQELWQLPGGNQC-ATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGrlrNGLLKNAVVNEIA 216
Cdd:cd19117 153 AIGVSNFSIKNLEKLLASPSAKIVpAVNQIELHPLLP--QPKLVDFCKSKGIHATAYSPLGSTN---APLLKEPVIIKIA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447109083 217 HAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLevELSSAELTMLD 269
Cdd:cd19117 228 KKHGKTPAQVIISWGL-QRGYSVLPKSVTPSRIESNFKLF--TLSDEEFKEID 277
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-271 |
2.25e-34 |
|
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: 126.79 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQFSGDvSLPAIGQGTwyMGEDAS--QRKTEVAALR---AGIELGLTLIDTAEMYADggAEKVVG---EALTGLR 72
Cdd:cd19144 1 IPTRTLGRNGP-SVPALGFGA--MGLSAFygPPKPDEERFAvldAAFELGCTFWDTADIYGD--SEELIGrwfKQNPGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 73 DNVFLVSKV---------YPWNAGGQKAIN-ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGV 141
Cdd:cd19144 76 EKIFLATKFgieknvetgEYSVDGSPEYVKkACETSLKRLGVDYIDLYYQHRvDGKTPIEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 142 SNLDYADMQELWQLpggNQCATNQVLYHLGSRGIE---YDLLPWCQQQQMPVMAYSPLAQA---GRLRN----------- 204
Cdd:cd19144 156 SECSAETLRRAHAV---HPIAAVQIEYSPFSLDIErpeIGVLDTCRELGVAIVAYSPLGRGfltGAIRSpddfeegdfrr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 205 --------GLLKN-AVVNEI---AHAHNISSAQVLLAWVISH-QGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19144 233 maprfqaeNFPKNlELVDKIkaiAKKKNVTAGQLTLAWLLAQgDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREI 312
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
13-261 |
2.84e-34 |
|
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: 125.54 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWymgeDASQRKTEvAALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNVFLVSKVYPWN 85
Cdd:cd19125 10 KIPAVGLGTW----QADPGVVG-NAVKTAIKEGYRHIDCAAIY---GNEKEIGKALKKLfedgvvkREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLH-----RSGS----------FAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQ 150
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHwpvrlKKGAhmpepeevlpPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 151 ELWQL----PggnqcATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGR--LRNGLLKNAVVNEIAHAHNISSA 224
Cdd:cd19125 162 DLLAVarvpP-----AVNQVECHPGWQ--QDKLHEFCKSKGIHLSAYSPLGSPGTtwVKKNVLKDPIVTKVAEKLGKTPA 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 447109083 225 QVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELS 261
Cdd:cd19125 235 QVALRWGL-QRGTSVLPKSTNEERIKENIDVFDWSIP 270
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-256 |
3.14e-34 |
|
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: 124.23 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 34 EVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYPWNAGGQKA--INACEASLRRLNTDYLDLY 110
Cdd:cd19105 27 SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLrRDKVFLATKASPRLDKKDKAelLKSVEESLKRLQTDYIDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 111 LLH----RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYadMQELWQ--LPGGN----QCATNqvlYHLGSRGIEyDLL 180
Cdd:cd19105 107 QLHgvdtPEERLLNEELLEALEKLKKEGKVRFIGFSTHDN--MAEVLQaaIESGWfdviMVAYN---FLNQPAELE-EAL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 181 PWCQQQQMPVMAYSPLAQAGRLRNGLLKNAvvneiahAHNISSAQVLLAWVISHQGV-MAIPKAATIAHVQQNAAVL 256
Cdd:cd19105 181 AAAAEKGIGVVAMKTLAGGYLQPALLSVLK-------AKGFSLPQAALKWVLSNPRVdTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
14-269 |
9.27e-34 |
|
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: 124.80 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWymgedaSQRKTEV-AALRAGIELGLTLIDTAEMYadgGAEKVVGEALT-------GL-RDNVFLVSKVypW 84
Cdd:cd19106 7 MPLIGLGTW------KSKPGQVkAAVKYALDAGYRHIDCAAVY---GNEQEVGEALKekvgpgkAVpREDLFVTSKL--W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 NAG--GQKAINACEASLRRLNTDYLDLYLLHRSGSFA--------------------FEETVAAMEKLIAQGKIRRWGVS 142
Cdd:cd19106 76 NTKhhPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFErgdnpfpknpdgtirydsthYKETWKAMEKLVDKGLVKAIGLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 143 NLDYADMQELWQLpGGNQCATNQVLYH--LGsrgiEYDLLPWCQQQQMPVMAYSPLAQAGRL--RNG---LLKNAVVNEI 215
Cdd:cd19106 156 NFNSRQIDDILSV-ARIKPAVLQVECHpyLA----QNELIAHCKARGLVVTAYSPLGSPDRPwaKPDepvLLEEPKVKAL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447109083 216 AHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19106 231 AKKYNKSPAQILLRWQV-QRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLD 283
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-269 |
9.57e-34 |
|
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: 123.43 E-value: 9.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 6 IQFSGDVSLPAIGQGTWYMGEDASQRktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEAL--TGL-RDNVFLVSKVY 82
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAER-----SVSAALEAGYRLIDTAAAY---GNEAAVGRAIaaSGIpRGELFVTTKLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 PWNAGGQKAINACEASLRRLNTDYLDLYLLH----RSGSFAfeETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGG 158
Cdd:cd19134 75 TPDQGFTASQAACRASLERLGLDYVDLYLIHwpagREGKYV--DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 159 NQcATNQVLYHlgsrgieydllPWCQQQQMP---------VMAYSPLAqAGRlrngLLKNAVVNEIAHAHNISSAQVLLA 229
Cdd:cd19134 153 TP-AVNQIELH-----------PLLNQAELRkvnaqhgivTQAYSPLG-VGR----LLDNPAVTAIAAAHGRTPAQVLLR 215
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447109083 230 WVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19134 216 WSL-QLGNVVISRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
13-270 |
1.18e-33 |
|
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: 123.68 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYMGEDasqrktEV-AALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL--------RDNVFLVSKVyp 83
Cdd:cd19118 6 KIPAIGLGTWQAEPG------EVgAAVKIALKAGYRHLDLAKVY---QNQHEVGQALKELlkeepgvkREDLFITSKL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNAGGQ--KAINACEASLRRLNTDYLDLYLLHRSGSFAFE-------------------------ETVAAMEKLIAQGKI 136
Cdd:cd19118 75 WNNSHRpeYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdlnpltavptnggevdldlsvslvDTWKAMVELKKTGKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 137 RRWGVSNLDYADMQELWQlPGGNQCATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQ--AGRLRngLLKNAVVNE 214
Cdd:cd19118 155 KSIGVSNFSIDHLQAIIE-ETGVVPAVNQIEAH--PLLLQDELVDYCKSKNIHITAYSPLGNnlAGLPL--LVQHPEVKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447109083 215 IAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAvlEVELSSAELTMLDK 270
Cdd:cd19118 230 IAAKLGKTPAQVLIAWGI-QRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTA 282
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
12-269 |
2.11e-33 |
|
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: 122.33 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDASQRKTEVAalragIELGLTLIDTAEMYadgGAEKVVGEALTG---LRDNVFLVSKVYPWNAGG 88
Cdd:cd19130 8 NSIPQLGYGVFKVPPADTQRAVATA-----LEVGYRHIDTAAIY---GNEEGVGAAIAAsgiPRDELFVTTKLWNDRHDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAINACEASLRRLNTDYLDLYLLHRSGSFA--FEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQlPGGNQCATNQV 166
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWPTPAAgnYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVA-ATGVVPAVNQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 167 LYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAgrlrnGLLKNAVVNEIAHAHNISSAQVLLAWVISHqGVMAIPKAATI 246
Cdd:cd19130 159 ELH--PAYQQRTIRDWAQAHDVKIEAWSPLGQG-----KLLGDPPVGAIAAAHGKTPAQIVLRWHLQK-GHVVFPKSVRR 230
|
250 260
....*....|....*....|...
gi 447109083 247 AHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19130 231 ERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
14-268 |
9.57e-33 |
|
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: 122.14 E-value: 9.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWymgedASQRKTEVAALRAGIELGLTLIDTAEMYADggaEKVVGEALTGL-------RDNVFLVSKVypWNA 86
Cdd:cd19107 4 MPILGLGTW-----KSPPGQVTEAVKVAIDAGYRHIDCAYVYQN---ENEVGEAIQEKikeqvvkREDLFIVSKL--WCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAI--NACEASLRRLNTDYLDLYLLHRSGSF--------------------AFEETVAAMEKLIAQGKIRRWGVSNL 144
Cdd:cd19107 74 FHEKGLvkGACQKTLSDLKLDYLDLYLIHWPTGFkpgkelfpldesgnvipsdtTFLDTWEAMEELVDEGLVKAIGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 145 DYADMQELWQLPG-GNQCATNQVLYHlgsrgiEY----DLLPWCQQQQMPVMAYSPLAQAGRL-----RNGLLKNAVVNE 214
Cdd:cd19107 154 NHLQIERILNKPGlKYKPAVNQIECH------PYltqeKLIQYCQSKGIVVTAYSPLGSPDRPwakpeDPSLLEDPKIKE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447109083 215 IAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTML 268
Cdd:cd19107 228 IAAKHNKTTAQVLIRFPI-QRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-269 |
1.10e-32 |
|
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: 121.86 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 3 QKMIQFSGDVSLPAIGQGTWymgeDASQRKTEvAALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNV 75
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTW----QSSPEEIE-TAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKWidsgkvkREEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 76 FLVSKVYPWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAFEE----------------------TVAAMEKLIAQ 133
Cdd:cd19155 73 FIVTKLPPGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEddsgkldptgehkqdyttdlldIWKAMEAQVDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 134 GKIRRWGVSNLDYADMQELWqlpggNQC----ATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGRLR------ 203
Cdd:cd19155 153 GLTRSIGLSNFNREQMARIL-----KNArikpANLQVELHVYLQ--QKDLVDFCSTHSITVTAYAPLGSPGAAHfspgtg 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447109083 204 ------NGLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19155 226 spsgssPDLLQDPVVKAIAERHGKSPAQVLLRWLM-QRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLS 296
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
12-269 |
1.38e-32 |
|
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: 121.07 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDasqrktEV-AALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNVFLVSKVYP 83
Cdd:cd19111 2 FPMPVIGLGTYQSPPE------EVrAAVDYALFVGYRHIDTALSY---QNEKAIGEALKWWlkngklkREEVFITTKLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSFAF--------------EETVAAMEKLIAQGKIRRWGVSNLDYADM 149
Cdd:cd19111 73 VYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNkkdkgerelassdvTSVWRAMEALVSEGKVKSIGLSNFNPRQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 150 QELWQLpGGNQCATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGRLRN-------GLLKNAVVNEIAHAHNIS 222
Cdd:cd19111 153 NKILAY-AKVKPSNLQLECHAYLQ--QRELRKFCNKKNIVVTAYAPLGSPGRANQslwpdqpDLLEDPTVLAIAKELDKT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447109083 223 SAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19111 230 PAQVLLRFVL-QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
14-265 |
1.46e-32 |
|
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: 120.84 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDASQRKTevAALRAgIELGLTLIDTAEMYadgGAEKVVGEAL-----TGL---RDNVFLVSKVYPWN 85
Cdd:cd19124 5 MPVIGMGTASDPPSPEDIKA--AVLEA-IEVGYRHFDTAAAY---GTEEALGEALaealrLGLvksRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLH-----RSGSFAF------------EETVAAMEKLIAQGKIRRWGVSNLDYAD 148
Cdd:cd19124 79 AHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslKPGKFSFpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNFSCKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 149 MQELWQL----PggnqcATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSPLAQAGR--LRNGLLKNAVVNEIAHAHNIS 222
Cdd:cd19124 159 LQELLSFatipP-----AVNQVEMNPAWQ--QKKLREFCKANGIHVTAYSPLGAPGTkwGSNAVMESDVLKEIAAAKGKT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 447109083 223 SAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19124 232 VAQVSLRWVYE-QGVSLVVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-257 |
2.02e-32 |
|
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: 120.74 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGEDASQRKTEvAALRAGIELGLTLIDTAEMYAD----GGAEKVVGEAL--TGLRDNVFLVSK--VYPWNAGG 88
Cdd:cd19082 3 IVLGTADFGTRIDEEEAF-ALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLksRGNRDKVVIATKggHPDLEDMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKAINA------CEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSN---------LDYADmQEL 152
Cdd:cd19082 82 RSRLSPediradLEESLERLGTDYIDLYFLHRdDPSVPVGEIVDTLNELVRAGKIRAFGASNwsteriaeaNAYAK-AHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 153 WQLPGGNQC----ATNQVLYHLGSRGIEYD--LLPWCQQQQMPVMAYSPLAQ---AGRLRNGLLKN-------------- 209
Cdd:cd19082 161 LPGFAASSPqwslARPNEPPWPGPTLVAMDeeMRAWHEENQLPVFAYSSQARgffSKRAAGGAEDDselrrvyyseenfe 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447109083 210 --AVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAA--TIAHVQQNAAVLE 257
Cdd:cd19082 241 rlERAKELAEEKGVSPTQIALAYVL-NQPFPTVPIIGprTPEQLRDSLAAAD 291
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-268 |
1.25e-31 |
|
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: 118.91 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWymgEDASQRKTEvaALRAGIELGLTLIDTAEMYADggaEKVVGEALTG-------LRDNVFLVSKVypWNA 86
Cdd:cd19110 4 IPAVGLGTW---KASPGEVTE--AVKVAIDAGYRHFDCAYLYHN---ESEVGAGIREkikegvvRREDLFIVSKL--WCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAI--NACEASLRRLNTDYLDLYLLH---------------RSGSF-----AFEETVAAMEKLIAQGKIRRWGVSNL 144
Cdd:cd19110 74 CHKKSLvkTACTRSLKALKLNYLDLYLIHwpmgfkpgepdlpldRSGMVipsdtDFLDTWEAMEDLVIEGLVKNIGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 145 DYADMQELWQLPGGN-QCATNQVLYH--LGSRgieyDLLPWCQQQQMPVMAYSPLAQAGRLRNgLLKNAVVNEIAHAHNI 221
Cdd:cd19110 154 NHEQLERLLNKPGLRvKPVTNQIECHpyLTQK----KLISFCQSRNVSVTAYRPLGGSCEGVD-LIDDPVIQRIAKKHGK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447109083 222 SSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTML 268
Cdd:cd19110 229 SPAQILIRFQI-QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-252 |
2.83e-31 |
|
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: 117.94 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 9 SGDVSLPAIGQGTwyMGEDASQRKTevaALRAGIELGLTLIDTAEMYADggaEKVVGEALTGL-------RDNVFLVSKV 81
Cdd:cd19129 1 NGSGAIPALGFGT--LIPDPSATRN---AVKAALEAGFRHFDCAERYRN---EAEVGEAMQEVfkagkirREDLFVTTKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 YPWNAGGQKAINACEASLRRLNTDYLDLYLLHRsgSFAFE-----------------------ETVAAMEKLIAQGKIRR 138
Cdd:cd19129 73 WNTNHRPERVKPAFEASLKRLQLDYLDLYLIHT--PFAFQpgdeqdprdangnviyddgvtllDTWRAMERLVDEGRCKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 139 WGVSNLDYADMQELWQLpGGNQCATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLAQAgrLRNGLLKNAVVNEIAHA 218
Cdd:cd19129 151 IGLSDVSLEKLREIFEA-ARIKPAVVQVESH--PYLPEWELLDFCKNHGIVLQAFAPLGHG--MEPKLLEDPVITAIARR 225
|
250 260 270
....*....|....*....|....*....|....
gi 447109083 219 HNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQN 252
Cdd:cd19129 226 VNKTPAQVLLAWAI-QRGTALLTTSKTPSRIREN 258
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-254 |
5.77e-31 |
|
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: 117.42 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 16 AIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-------RDNVFLVSK---VYPWN 85
Cdd:cd19099 5 SLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggikRDEVVIVTKagyIPGDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAIN------------------------------ACEASLRRLNTDYLDLYLLH--------RSGSF---AFEETV 124
Cdd:cd19099 85 DEPLRPLKyleeklgrglidvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHnpeeqlleLGEEEfydRLEEAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 125 AAMEKLIAQGKIRRWGVS-------------NLDYADMQELWQLPGGN--QCATNQVLYHLGSR----------GIEYDL 179
Cdd:cd19099 165 EALEEAVAEGKIRYYGIStwdgfrappalpgHLSLEKLVAAAEEVGGDnhHFKVIQLPLNLLEPealtekntvkGEALSL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 180 LPWCQQQQMPVMAYSPLAQAGRLRNGLLknavVNEIAHAHNISSAQVLLAWVISHQGVmaipKAA-----TIAHVQQNAA 254
Cdd:cd19099 245 LEAAKELGLGVIASRPLNQGQLLGELRL----ADLLALPGGATLAQRALQFARSTPGV----DSAlvgmrRPEHVDENLA 316
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-268 |
1.72e-30 |
|
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: 115.99 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 16 AIGQGTWYMGEDASQRKTE---VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYPWNAGGQKA 91
Cdd:cd19145 14 AQGLGCMGLSGDYGAPKPEeegIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGpREKVQLATKFGIHEIGGSGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 I---------NACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNldyADMQELWQLPGGNQC 161
Cdd:cd19145 94 EvrgdpayvrAACEASLKRLDVDYIDLYYQHRiDTTVPIEITMGELKKLVEEGKIKYIGLSE---ASADTIRRAHAVHPI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 162 ATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGR------LRNGLL-------------KNAV----VNEI 215
Cdd:cd19145 171 TAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRgffAGKakleelLENSDVrkshprfqgenleKNKVlyerVEAL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447109083 216 AHAHNISSAQVLLAWVIsHQG--VMAIPKAATIAHVQQNAAVLEVELSSAELTML 268
Cdd:cd19145 251 AKKKGCTPAQLALAWVL-HQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
14-265 |
3.22e-30 |
|
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: 115.43 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMY--ADGGAEKVVGEAL----TGLRDNVFLVSKV--YPW- 84
Cdd:cd19089 11 LPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILkrdlRPYRDELVISTKAgyGMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 ----NAGGQKAINA-CEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL--P 156
Cdd:cd19089 91 gpygDGGSRKYLLAsLDQSLKRMGLDYVDIFYHHRyDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALlrE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 157 GGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ--------------AGRLRNG------------LLKNA 210
Cdd:cd19089 171 LGVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQglltdkylngippdSRRAAESkflteealtpekLEQLR 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 211 VVNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLE-VELSSAEL 265
Cdd:cd19089 251 KLNKIAAKRGQSLAQLALSWVLRDPRVTsVLIGASSPSQLEDNVAALKnLDFSEEEL 307
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
12-270 |
4.19e-30 |
|
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: 114.90 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 12 VSLPAIGQGTWYMGEDASQRKTevaALRAGIELGLTLIDTAEMYadgGAEKVVGEAL-----TGL--RDNVFLVSKVYP- 83
Cdd:cd19119 10 ASIPALGLGTASPHEDRAEVKE---AVEAAIKEGYRHIDTAYAY---ETEDFVGEAIkraidDGSikREELFITTKVWPt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 -WNaggqKAINACEASLRRLNTDYLDLYLLH--------------------------RSGSFAFEETVAAMEKLIAQGKI 136
Cdd:cd19119 84 fYD----EVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgktrYAASGDHITTYKQLEKIYLDGRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 137 RRWGVSNLDYADMQELWQ----LPGGNQCATNQVLYHLgsrgieyDLLPWCQQQQMPVMAYSPLaqaGRLRNGLLKNAVV 212
Cdd:cd19119 160 KAIGVSNYSIVYLERLIKeckvVPAVNQVELHPHLPQM-------DLRDFCFKHGILVTAYSPL---GSHGAPNLKNPLV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447109083 213 NEIAHAHNISSAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVleVELSSAELTMLDK 270
Cdd:cd19119 230 KKIAEKYNVSTGDILISYHVR-QGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKLDD 284
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-271 |
6.59e-30 |
|
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: 114.35 E-value: 6.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 11 DVSLPAIGQGTWYMGEDASQRKT------EVAALRA----GIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVS 79
Cdd:cd19103 1 DKKLPKIALGTWSWGSGGAGGDQvfgnhlDEDTLKAvfdkAMAAGLNLWDTAAVYGMGASEKILGEFLKRYpREDYIIST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 80 KVYPWNAG--GQKAINACEASLRRLNTDYLDLYLLHRSgsfafEETVAAMEKLIA---QGKIRRWGVSNLDYADMQELWQ 154
Cdd:cd19103 81 KFTPQIAGqsADPVADMLEGSLARLGTDYIDIYWIHNP-----ADVERWTPELIPllkSGKVKHVGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 155 L--PGGNQCATNQVLYHLGSRGIEYD-LLPWCQQQQMPVMAYSPLAQ--------------AGRLR----NGLLK----- 208
Cdd:cd19103 156 IlaKAGVSLSAVQNHYSLLYRSSEEAgILDYCKENGITFFAYMVLEQgalsgkydtkhplpEGSGRaetyNPLLPqleel 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447109083 209 NAVVNEIAHAHNISSAQVLLAWVIShQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDKA 271
Cdd:cd19103 236 TAVMAEIGAKHGASIAQVAIAWAIA-KGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-257 |
7.15e-30 |
|
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: 113.97 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGEDASqRKTEVAALRAGIELGLTLIDTAEMYA-------DGGAEKVVGEALT--GLRDNVFLVSKV---- 81
Cdd:cd19752 1 SELCLGTMYFGTRTD-EETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKdrGNRDDVVIATKVgagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 -----YPWNAGGQKA---INACEASLRRLNTDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDyadmqeL 152
Cdd:cd19752 80 rdpdgGPESPEGLSAetiEQEIDKSLRRLGTDYIDLYYAHVDDrDTPLEETLEAFNELVKAGKVRAIGASNFA------A 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 153 WQLPGGNQCATNQVL-------------------YHLGSRGIEYDLLPWCQQQ-QMPVMAYSPLAQAGRLRNG------- 205
Cdd:cd19752 154 WRLERARQIARQQGWaefsaiqqrhsylrprpgaDFGVQRIVTDELLDYASSRpDLTLLAYSPLLSGAYTRPDrplpeqy 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 206 -----LLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIP--KAATIAHVQQNAAVLE 257
Cdd:cd19752 234 dgpdsDARLAVLEEVAGELGATPNQVVLAWLL-HRTPAIIPllGASTVEQLEENLAALD 291
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-254 |
7.43e-30 |
|
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: 112.58 E-value: 7.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEdASQRKTeVAALRAGIELGLTLIDTAEMYadGGAEKVVGEALTGLRDNVFLVSKVYPWNAGG-QKAI 92
Cdd:cd19100 11 VSRLGFGGGPLGR-LSQEEA-AAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKGRRDKVFLATKTGARDYEGaKRDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 93 nacEASLRRLNTDYLDLYLLHRSGS-FAFEETVA------AMEKLIAQGKIRRWGVSN---------LDYADMQELwqlp 156
Cdd:cd19100 87 ---ERSLKRLGTDYIDLYQLHAVDTeEDLDQVFGpggaleALLEAKEEGKIRFIGISGhspevllraLETGEFDVV---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 157 ggnQCATNQVLYHLGSRGIEydLLPWCQQQQMPVMAYSPLAqAGRLRNGllknavvneiahahNISSAQVLLAWVISHQG 236
Cdd:cd19100 160 ---LFPINPAGDHIDSFREE--LLPLAREKGVGVIAMKVLA-GGRLLSG--------------DPLDPEQALRYALSLPP 219
|
250
....*....|....*....
gi 447109083 237 V-MAIPKAATIAHVQQNAA 254
Cdd:cd19100 220 VdVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-272 |
4.00e-29 |
|
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: 112.74 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 16 AIGqGTWYMGEDASQRktevAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKVY--PWNAG--GQKA 91
Cdd:cd19104 21 GIG-GLMGRTTREEQI----AAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITTKVRldPDDLGdiGGQI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 INACEASLRRLNTDYLDLYLLH----------------RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDyaDMQELWQL 155
Cdd:cd19104 96 ERSVEKSLKRLKRDSVDLLQLHnrigderdkpvggtlsTTDVLGLGGVADAFERLRSEGKIRFIGITGLG--NPPAIREL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 156 PGGNQCATNQVLYHL-----------GSRGIEYD-LLPWCQQQQMPVMAYSPLAqAGRL----RNGLL------------ 207
Cdd:cd19104 174 LDSGKFDAVQVYYNLlnpsaaearprGWSAQDYGgIIDAAAEHGVGVMGIRVLA-AGALttslDRGREapptsdsdvaid 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 208 --KNAVVNEIAHAHNISSAQVLLAWVISHQGV-MAIPKAATIAHVQQN-AAVLEVELSSAELTMLDKAY 272
Cdd:cd19104 253 frRAAAFRALAREWGETLAQLAHRFALSNPGVsTVLVGVKNREELEEAvAAEAAGPLPAENLARLEALW 321
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
13-272 |
6.00e-29 |
|
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: 111.81 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYMGEDasqrKTEVAALRAgIELGLTLIDTAemyADGGAEKVVGEAL-----TGL--RDNVFLVSKVypWN 85
Cdd:cd19112 10 KMPVIGLGVWRMEPG----EIKELILNA-IKIGYRHFDCA---ADYKNEKEVGEALaeafkTGLvkREDLFITTKL--WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLH-----------RSGSFAFEETVA-------------AMEKLIAQGKIRRWGV 141
Cdd:cd19112 80 SDHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgTTGSALGEDGVLdidvtislettwhAMEKLVSAGLVRSIGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 142 SNLDYADMQELWQL----PGGNQCATNQVLYhlgsrgiEYDLLPWCQQQQMPVMAYSPL--AQAGRLRNGL---LKNAVV 212
Cdd:cd19112 160 SNYDIFLTRDCLAYskikPAVNQIETHPYFQ-------RDSLVKFCQKHGISVTAHTPLggAAANAEWFGSvspLDDPVL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447109083 213 NEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTM---LDKAY 272
Cdd:cd19112 233 KDLAKKYGKSAAQIVLRWGI-QRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLiksLDRKY 294
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
38-257 |
2.31e-28 |
|
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: 109.19 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 38 LRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKVYPWN----AGGQKAInacEASLRRLNTDYLDLYLL 112
Cdd:cd19096 27 IRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGpREKFYLATKLPPWSvksaEDFRRIL---EESLKRLGVDYIDFYLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 113 HRSGSFAFEET------VAAMEKLIAQGKIRRWGVSNLDYADmqELWQLPGGNQCATNQVLYHL-------GSRGIEYdl 179
Cdd:cd19096 104 HGLNSPEWLEKarkgglLEFLEKAKKEGLIRHIGFSFHDSPE--LLKEILDSYDFDFVQLQYNYldqenqaGRPGIEY-- 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 180 lpwCQQQQMPVMAYSPLAQAGRLRNgllkNAVVNEIAHAHNISSAQVLLAWVISHQGV-MAIPKAATIAHVQQNAAVLE 257
Cdd:cd19096 180 ---AAKKGMGVIIMEPLKGGGLANN----PPEALAILCGAPLSPAEWALRFLLSHPEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-270 |
4.09e-28 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQFSGDVSLPAIGQGTWymgeDASQRKTEVAALRAgIELGLTLIDTAEMYADggaEKVVGEAL--TGL-RDNVFL 77
Cdd:PRK11565 2 ANPTVIKLQDGNVMPQLGLGVW----QASNEEVITAIHKA-LEVGYRSIDTAAIYKN---EEGVGKALkeASVaREELFI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 78 VSKVypWNAGGQKAINACEASLRRLNTDYLDLYLLHRSGSfAFEETVAAMEKLIA---QGKIRRWGVSNLDYADMQELWQ 154
Cdd:PRK11565 74 TTKL--WNDDHKRPREALEESLKKLQLDYVDLYLMHWPVP-AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIHHLQRLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 155 lPGGNQCATNQVLYH--LGSRgieyDLLPWCQQQQMPVMAYSPLAQAGRlrnGLLKNAVVNEIAHAHNISSAQVLLAWVI 232
Cdd:PRK11565 151 -ETGVTPVINQIELHplMQQR----QLHAWNATHKIQTESWSPLAQGGK---GVFDQKVIRDLADKYGKTPAQIVIRWHL 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 447109083 233 ShQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:PRK11565 223 D-SGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAK 259
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-270 |
4.48e-27 |
|
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: 106.45 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGEDASQRktevaALRAGIELGLTLIDTAEMYadgGAEKVVGEALTGL-------RDNVFLVSKVYPWNAG 87
Cdd:cd19128 2 PRLGFGTYKITESESKE-----AVKNAIKAGYRHIDCAYYY---GNEAFIGIAFSEIfkdggvkREDLFITSKLWPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 88 GQKAINACEASLRRLNTDYLDLYLLH--------------------RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYA 147
Cdd:cd19128 74 PENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiqSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 148 DMQELWqlpggNQCA----TNQV---LYHLGSRGIEYdllpwCQQQQMPVMAYSPLaqAGRLRNGllKNAVVN-----EI 215
Cdd:cd19128 154 LLTDLL-----NYCKikpfMNQIechPYFQNDKLIKF-----CIENNIHVTAYRPL--GGSYGDG--NLTFLNdselkAL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 216 AHAHNISSAQVLLAWVISH--QGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19128 220 ATKYNTTPPQVIIAWHLQKwpKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINT 276
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
14-270 |
1.24e-26 |
|
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: 105.61 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDasqrkTEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEALT-----GL--RDNVFLVSKVypWNA 86
Cdd:cd19113 11 MPSVGFGCWKLDNA-----TAADQIYQAIKAGYRLFDGAEDY---GNEKEVGEGVNraideGLvkREELFLTSKL--WNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 -----GGQKAINAceaSLRRLNTDYLDLYLLHRSGSFAF---EE-----------------------TVAAMEKLIAQGK 135
Cdd:cd19113 81 fhdpkNVETALNK---TLSDLKLDYVDLFLIHFPIAFKFvpiEEkyppgfycgdgdnfvyedvpildTWKALEKLVDAGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 136 IRRWGVSNLDYADMQELwqLPGGN-QCATNQVLYH---LGSRGIEYdllpwCQQQQMPVMAYS---PLA----QAGRLRN 204
Cdd:cd19113 158 IKSIGVSNFPGALILDL--LRGATiKPAVLQIEHHpylQQPKLIEY-----AQKAGITITAYSsfgPQSfvelNQGRALN 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447109083 205 G--LLKNAVVNEIAHAHNISSAQVLLAWViSHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19113 231 TptLFEHDTIKSIAAKHNKTPAQVLLRWA-TQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAK 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
15-263 |
1.86e-26 |
|
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: 104.56 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGEDASQRKTE--VAALRAGIELGLTLIDTAEMYadGGAEKVVGEALTGL-RDNVFLVSKV-----YPWNA 86
Cdd:cd19090 1 SALGLGTAGLGGVFGGVDDDeaVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELpREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 87 GGQKAINACEASLRRLNTDYLDLYLLHR------SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELwqlpggnq 160
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDpervpwVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRA-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 CATNQ---VL----YHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGR-------LRNGLLKNAV-----VNEIAHA 218
Cdd:cd19090 151 IETGDfdvVLtanrYTLLDQSAADELLPAAARHGVGVINASPLGMgllAGRppervryTYRWLSPELLdrakrLYELCDE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447109083 219 HNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSA 263
Cdd:cd19090 231 HGVPLPALALRFLLRDPRISTvLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-269 |
4.74e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 101.52 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYMGEDASQRKTEVAALRA---GIELGLTLIDTAEMYadGGAEKVVGEALTGLRDNVFLVSKV-------- 81
Cdd:cd19101 1 TISRVINGMWQLSGGHGGIRDEDAAVRAmaaYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRERDAADDVqihtkwvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 --YPWNAGGQKAINACEASLRRLNTDYLDLYLLH--RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELwqLPG 157
Cdd:cd19101 79 dpGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHwwDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI--LDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 158 GNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLA------------QAGRLRN---GLLKN------------- 209
Cdd:cd19101 157 GVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAggllsekylgvpEPTGPALetrSLQKYklmidewggwdlf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447109083 210 ----AVVNEIAHAHNISSAQVLLAWVISHQGVMAIPKAATIA-HVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19101 237 qellRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSeHIDDNVRAFSFRLDDEDRAAID 301
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-275 |
2.98e-24 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 99.93 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQFSG-DVSLpaIGQGTWYMGEDASQRKTEvAALRAGIELGLTLIDTAEMYA-------DGGAEKVVGEAL--TG 70
Cdd:PRK10625 1 MQYHRIPHSSlEVST--LGLGTMTFGEQNSEADAH-AQLDYAVAQGINLIDVAEMYPvpprpetQGLTETYIGNWLakRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 71 LRDNVFLVSKVY-----------PWNAGGQKAIN-ACEASLRRLNTDYLDLYLLHRS-------GSFAFE---------- 121
Cdd:PRK10625 78 SREKLIIASKVSgpsrnndkgirPNQALDRKNIReALHDSLKRLQTDYLDLYQVHWPqrptncfGKLGYSwtdsapavsl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 122 -ETVAAMEKLIAQGKIRRWGVSN------LDYADMQELWQLPggnQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYS 194
Cdd:PRK10625 158 lETLDALAEQQRAGKIRYIGVSNetafgvMRYLHLAEKHDLP---RIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 195 PL------------AQAGRLRNGLL-----------KNAVVN--EIAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAH 248
Cdd:PRK10625 235 CLafgtltgkylngAKPAGARNTLFsrftrysgeqtQKAVAAyvDIAKRHGLDPAQMALAFVRRQPFVAStLLGATTMEQ 314
|
330 340 350
....*....|....*....|....*....|..
gi 447109083 249 VQQNAAVLEVELSSAELTMLDKA-----YPAP 275
Cdd:PRK10625 315 LKTNIESLHLTLSEEVLAEIEAVhqvytYPAP 346
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
9-266 |
2.98e-24 |
|
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: 99.40 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 9 SGdVSLPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYAD--GGAE----KVVGEALTGLRDNVFLVSKV- 81
Cdd:cd19151 8 SG-LKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPppGSAEenfgRILKEDLKPYRDELIISTKAg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 -YPWNA-----GGQK-AINACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQE-- 151
Cdd:cd19151 87 yTMWPGpygdwGSKKyLIASLDQSLKRMGLDYVDIFYHHRpDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 152 --LWQLpgGNQCATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQaGRLRNGLL---------------------- 207
Cdd:cd19151 167 aiLKDL--GTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQ-GLLTDRYLngipedsraakgssflkpeqit 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447109083 208 -----KNAVVNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLE-VELSSAELT 266
Cdd:cd19151 244 eeklaKVRRLNEIAQARGQKLAQMALAWVLRNKRVTsVLIGASKPSQIEDAVGALDnREFSEEELA 309
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
20-258 |
3.39e-24 |
|
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: 99.21 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 20 GTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL---RDNVFLVSKVYpWNAGGQKA----- 91
Cdd:cd19143 19 GSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwpRSDYVVSTKIF-WGGGGPPPndrgl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 -----INACEASLRRLNTDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL--------Pg 157
Cdd:cd19143 98 srkhiVEGTKASLKRLQLDYVDLVFCHRPDpATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIadrlglipP- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 158 gnqcATNQVLYHLGSRG-IEYDLLPWCQQQQMPVMAYSPLAQ---AGRLRNGLL-----------------------KNA 210
Cdd:cd19143 177 ----VMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASgllTGKYNNGIPegsrlalpgyewlkdrkeelgqeKIE 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447109083 211 VVNE---IAHAHNISSAQVLLAWVISHQGV-MAIPKAATIAHVQQNAAVLEV 258
Cdd:cd19143 253 KVRKlkpIAEELGCSLAQLAIAWCLKNPNVsTVITGATKVEQLEENLKALEV 304
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
13-269 |
7.35e-24 |
|
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: 98.33 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTwYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYadgGAEKVVGEAL-------TGLRDNVFLVSKVypWN 85
Cdd:cd19109 3 SIPIIGLGT-YSEPKTTPKGACAEAVKVAIDTGYRHIDGAYIY---QNEHEVGQAIrekiaegKVKREDIFYCGKL--WN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAI--NACEASLRRLNTDYLDLYLLH---------------RSGSFAFEE-----TVAAMEKLIAQGKIRRWGVSN 143
Cdd:cd19109 77 TCHPPELvrPTLERTLKVLQLDYVDLYIIEmpmafkpgdeiyprdENGKWLYHKtnlcaTWEALEACKDAGLVKSIGVSN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 144 LDYADMQELWQLPG-GNQCATNQVLYHlgSRGIEYDLLPWCQQQQMPVMAYSPLaqaGRLRNG---------LLKNAVVN 213
Cdd:cd19109 157 FNRRQLELILNKPGlKHKPVSNQVECH--PYFTQPKLLEFCQQHDIVIVAYSPL---GTCRDPiwvnvssppLLEDPLLN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447109083 214 EIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19109 232 SIGKKYNKTAAQVVLRFNI-QRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIE 286
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
35-265 |
3.77e-23 |
|
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: 96.08 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 35 VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKV--Y------PWNAGGQKAINACEASLRRLNTD 105
Cdd:cd19163 36 IRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIpRDSYYLATKVgrYgldpdkMFDFSAERITKSVEESLKRLGLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 106 YLDLYLLH-----RSGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGnqcATNQVL----YHLGSRGIE 176
Cdd:cd19163 116 YIDIIQVHdiefaPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERSPV---KIDTVLsychYTLNDTSLL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 177 yDLLPWCQQQQMPVMAYSPLAQaGRLRNGL----------LKNAVVNEIAH--AHNISSAQVLLAWVISHQGVMA-IPKA 243
Cdd:cd19163 193 -ELLPFFKEKGVGVINASPLSM-GLLTERGppdwhpaspeIKEACAKAAAYckSRGVDISKLALQFALSNPDIATtLVGT 270
|
250 260
....*....|....*....|..
gi 447109083 244 ATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19163 271 ASPENLRKNLEAAEEPLDAHLL 292
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
17-265 |
8.89e-23 |
|
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: 95.00 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQG----TWymGEDASQRKTEVAALRAGIELGLTLIDTAEMYADGGAE---KVVGEALTG---LRDNVFLVSK---VYP 83
Cdd:cd19077 8 IGLGlmglTW--RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlKLLARFFRKypeYADKVVLSVKgglDPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 84 WNA--GGQKAI-NACEASLRRLN-TDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLpgg 158
Cdd:cd19077 86 TLRpdGSPEAVrKSIENILRALGgTKKIDIFEPARVDpNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAV--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 159 NQCATNQVLYHLGSRGIEY-DLLPWCQQQQMPVMAYSPLAQ---AGRLRNG-------------------LLKN----AV 211
Cdd:cd19077 163 HPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRgllTGRIKSLadipegdfrrhldrfngenFEKNlklvDA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447109083 212 VNEIAHAHNISSAQVLLAWVI--SHQGVMAIPKAATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19077 243 LQELAEKKGCTPAQLALAWILaqSGPKIIPIPGSTTLERVEENLKAANVELTDEEL 298
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-269 |
5.36e-21 |
|
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: 90.31 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 10 GDvSLPAIGQGTWYMGEDasqrKTEVAALRAgIELGLTLIDTAEMYAD-----GGAEKVVGEALTGlRDNVFLVSKVypW 84
Cdd:cd19114 1 GD-KMPLVGFGTAKIKAN----ETEEVIYNA-IKVGYRLIDGALLYGNeaevgRGIRKAIQEGLVK-REDLFIVTKL--W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 85 NA--GGQKAINACEASLRRLNTDYLDLYLLH---------------------RSGSFAFE-----ETVAAMEKLIAQGKI 136
Cdd:cd19114 72 NNfhGKDHVREAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypflwkdkELKKFPLEqspmqECWREMEKLVDAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 137 RRWGVSN---------LDYADMQElwqlpggnqcATNQVLYHLGSRgiEYDLLPWCQQQQMPVMAYSP--------LAQA 199
Cdd:cd19114 152 RNIGIANfnvqlildlLTYAKIKP----------AVLQIEHHPYLQ--QKRLIDWAKKQGIQITAYSSfgnavytkVTKH 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 200 GRLRNGLLKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19114 220 LKHFTNLLEHPVVKKLADKHKRDTGQVLLRWAV-QRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALY 288
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
13-265 |
6.10e-21 |
|
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: 90.17 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTWYMGEDasqrkTEVAALRAGIELGLTLIDTAemyADGGAEKVVGEALT-----GL--RDNVFLVSKVypWN 85
Cdd:cd19115 12 DMPLVGFGLWKVNND-----TCADQVYNAIKAGYRLFDGA---CDYGNEVEAGQGVAraikeGIvkREDLFIVSKL--WN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 A--GGQKAINACEASLRRLNTDYLDLYLLH-------------------------RSGSFAFEETVAAMEKLIAQGKIRR 138
Cdd:cd19115 82 TfhDGERVEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgwfydgkkvEFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 139 WGVSN---------LDYADMQElwqlpggnqcATNQVLYHlgsrgiEY----DLLPWCQQQQMPVMAYSPLAQAGRLRNG 205
Cdd:cd19115 162 IGVSNfsaqllmdlLRYARIRP----------ATLQIEHH------PYltqpRLVKYAQKEGIAVTAYSSFGPQSFLELD 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 206 ---------LLKNAVVNEIAHAHNISSAQVLLAWViSHQGVMAIPKAATIAHVQQNAAVLEVELSSAEL 265
Cdd:cd19115 226 lpgakdtppLFEHDVIKSIAEKHGKTPAQVLLRWA-TQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEI 293
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-270 |
9.03e-21 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 89.60 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 8 FSGDVSLPAIGQGTWymGEDASQRKTEVAALRAgIELGLTLIDTAEMYADggaEKVVGEALTGL--------RDNVFLVS 79
Cdd:cd19122 3 LNNGVKIPAVGFGTF--ANEGAKGETYAAVTKA-LDVGYRHLDCAWFYLN---EDEVGDAVRDFlkenpsvkREDLFICT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 80 KVypWNA--GGQKAINACEASLRRLNTDYLDLYLLH----------------RSGSFAF--------EETVAAMEKLIAQ 133
Cdd:cd19122 77 KV--WNHlhEPEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspklgPDGKYVIlkdltenpEPTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 134 GKIRRWGVSNLDYADMQELWQL----PGGNQCATNQVLYHlgsrgieYDLLPWCQQQQMPVMAYSPLA---QAGRLRNGL 206
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFakvkPHVNQIEIHPFLPN-------EELVDYCFSNDILPEAYSPLGsqnQVPSTGERV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447109083 207 LKNAVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVleVELSSAELTMLDK 270
Cdd:cd19122 228 SENPTLNEVAEKGGYSLAQVLIAWGL-RRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQ 288
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
18-277 |
1.26e-20 |
|
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: 89.79 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 18 GQGTWYMGEdaSQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGE--ALTGLRDNVFLVSK---VYPWNAGGQKAI 92
Cdd:cd19146 23 EAWKSMMGE--CDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDEMVLATKyttGYRRGGPIKIKS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 93 N-----------ACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNL---------DYADMQE 151
Cdd:cd19146 101 NyqgnhakslrlSVEASLKKLQTSYIDILYVHWwDYTTSIPELMQSLNHLVAAGKVLYLGVSDTpawvvskanAYARAHG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 152 LWQLpggnqcATNQVLYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQA------------GRLRNGLLKN-------AVV 212
Cdd:cd19146 181 LTQF------VVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGqfrteeefkrrgRSGRKGGPQTekerkvsEKL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 213 NEIAHAHNISSAQVLLAWVIsHQG--VMAIPKAATIAHVQQNAAVLEVELSSAELTMLDKAYPAPKG 277
Cdd:cd19146 255 EKVAEEKGTAITSVALAYVM-HKApyVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYPFDVG 320
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-270 |
5.79e-20 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 88.12 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 1 MQQKMIQFSGdVSLPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYAD--GGAEKVVG----EALTGLRDN 74
Cdd:PRK09912 13 MQYRYCGKSG-LRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGrllrEDFAAYRDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 75 VFLVSKV-Y-----PWNAGGQKA--INACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLD 145
Cdd:PRK09912 92 LIISTKAgYdmwpgPYGSGGSRKylLASLDQSLKRMGLEYVDIFYSHRvDENTPMEETASALAHAVQSGKALYVGISSYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 146 YADMQEL------WQLPggnqCATNQVLYHLGSRGIE-YDLLPWCQQQQMPVMAYSPLAQA---GRLRNGLLKNA----- 210
Cdd:PRK09912 172 PERTQKMvellreWKIP----LLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGlltGKYLNGIPQDSrmhre 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 211 ---------------------VVNEIAHAHNISSAQVLLAWVISHQGVMAIPKAATIA-HVQQNAAVLE-VELSSAELTM 267
Cdd:PRK09912 248 gnkvrgltpkmlteanlnslrLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAeQLEENVQALNnLTFSTEELAQ 327
|
...
gi 447109083 268 LDK 270
Cdd:PRK09912 328 IDQ 330
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
14-265 |
1.03e-19 |
|
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: 86.74 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTWYMGEDASQRKTEVAALRAGIELGLTLIDTAEMYAD--GGAEKVVGEAL----TGLRDNVFLVSKV-Y---- 82
Cdd:cd19150 12 LPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPppGSAEENFGRILredfAGYRDELIISTKAgYdmwp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 -PWNAGGQKA--INACEASLRRLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQE----LWQ 154
Cdd:cd19150 92 gPYGEWGSRKylLASLDQSLKRMGLDYVDIFYSHRfDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREaaaiLRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 155 LpgGNQCATNQVLYHLGSRGIE-YDLLPWCQQQQMPVMAYSPLAQA---GRLRNGLLKNA-------------------- 210
Cdd:cd19150 172 L--GTPLLIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGlltDKYLNGIPEGSraskerslspkmlteanlns 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447109083 211 --VVNEIAHAHNISSAQVLLAWVISHQGVM-AIPKAATIAHVQQNAAVLE-VELSSAEL 265
Cdd:cd19150 250 irALNEIAQKRGQSLAQMALAWVLRDGRVTsALIGASRPEQLEENVGALDnLTFSADEL 308
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
13-269 |
3.27e-19 |
|
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: 85.36 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 13 SLPAIGQGTwYMGEDASQRKTEVAALRAgIELGLTLIDTAEMYadgGAEKVVGEAL-------TGLRDNVFLVSKVYPWN 85
Cdd:cd19108 10 FIPVLGFGT-YAPEEVPKSKALEATKLA-IDAGFRHIDSAYLY---QNEEEVGQAIrskiadgTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 86 AGGQKAINACEASLRRLNTDYLDLYLLH---------------RSGSFAFE-----ETVAAMEKLIAQGKIRRWGVSNLD 145
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHfpvalkpgeelfpkdENGKLIFDtvdlcATWEAMEKCKDAGLAKSIGVSNFN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 146 YADMQELWQLPGGNQ---CatNQVLYHLgsrgieY----DLLPWCQQQQMPVMAYSPLaqaGRLRNG---------LLKN 209
Cdd:cd19108 165 RRQLEMILNKPGLKYkpvC--NQVECHP------YlnqsKLLDFCKSKDIVLVAYSAL---GSQRDKewvdqnspvLLED 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 210 AVVNEIAHAHNISSAQVLLAWVIsHQGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19108 234 PVLCALAKKHKRTPALIALRYQL-QRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALD 292
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-142 |
2.49e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 82.19 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 38 LRAGIELGLTLIDTAEMYadGGAEKVVGEALTGLrDNVFLVSKVYPWNAGGQKA----INACEASLRRLNTDYLDLYLLH 113
Cdd:cd19097 32 LEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL-DKFKIITKLPPLKEDKKEDeaaiEASVEASLKRLKVDSLDGLLLH 108
|
90 100 110
....*....|....*....|....*....|.
gi 447109083 114 RSGSFAF--EETVAAMEKLIAQGKIRRWGVS 142
Cdd:cd19097 109 NPDDLLKhgGKLVEALLELKKEGLIRKIGVS 139
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
14-270 |
4.26e-17 |
|
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: 79.82 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 14 LPAIGQGTW--YMGEDASQRKTEVaaLRAGIELGLTLIDTAEMYADGGAEKVVGEALT--GLRDNVFLVS-KVYpWNAGG 88
Cdd:cd19142 13 VSNVGLGTWstFSTAISEEQAEEI--VTLAYENGINYFDTSDAFTSGQAETELGRILKkkGWKRSSYIVStKIY-WSYGS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 89 QKA-------INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQ 160
Cdd:cd19142 90 EERglsrkhiIESVRASLRRLQLDYIDIVIIHKADPMCpMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 CAT---NQVLYHLGSR-GIEYDLLPWCQQQQMPVMAYSPLA--------------------QAGRLRNGLLKNAVVNEIA 216
Cdd:cd19142 170 CPTpicEQSEYHMFCReKMELYMPELYNKVGVGLITWSPLSlgldpgiseetrrlvtklsfKSSKYKVGSDGNGIHEETR 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 217 HAHNI-------------SSAQVLLAWVISHQGVMAIPKAATIAH---VQQNAAVLEVELSSAELTMLDK 270
Cdd:cd19142 250 RASHKlrelsliaerlgcDLTQLLIAWSLKNENVQCVLIGASSLEqlySQLNSLQLLPKLNSAVMEELER 319
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
35-142 |
1.30e-15 |
|
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: 75.01 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 35 VAALRAGIELGLTLIDTAEMYADggAEKVVGEALTGLRDN-----VFLVSKVypwnagGQKAIN-----------ACEAS 98
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP--SEIILGRALKALRDEfprdtYFIITKV------GRYGPDdfdyspewiraSVERS 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447109083 99 LRRLNTDYLDLYLLHRSGSFAFEETVAAME---KLIAQGKIRRWGVS 142
Cdd:cd19164 109 LRRLHTDYLDLVYLHDVEFVADEEVLEALKelfKLKDEGKIRNVGIS 155
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
17-240 |
1.98e-15 |
|
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: 75.02 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGedASQRKTEVAA--LRAGIELGLTLIDTAEMYADGGAEKVVGEAL--TGLRDNVFLV-SKVYpWnaGGQKA 91
Cdd:cd19160 18 LGLGTWVTF--GSQISDETAEdlLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVVtTKIY-W--GGQAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 ----------INACEASLRRLNTDYLDLYLLHRS-GSFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQ 160
Cdd:cd19160 93 terglsrkhiIEGLRGSLDRLQLEYVDIVFANRSdPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 161 C---ATNQVLYHLGSR-GIEYDLLPWCQQQQMPVMAYSPLA-------QAGRLRNG---------LLKNAVVNE------ 214
Cdd:cd19160 173 LippVCEQAEYHLFQReKVEMQLPELYHKIGVGSVTWSPLAcglitgkYDGRVPDTcraavkgyqWLKEKVQSEegkkqq 252
|
250 260 270
....*....|....*....|....*....|....
gi 447109083 215 --------IAHAHNISSAQVLLAWVISHQGVMAI 240
Cdd:cd19160 253 akvkelhpIADRLGCTVAQLAIAWCLRSEGVSSV 286
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
38-269 |
2.01e-14 |
|
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: 72.16 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 38 LRAGIELGLTLIDTAEMYADGGAEKVVGE--ALTGLRDNVFLVSKV----YPWNAGGQKAINAC-----------EASLR 100
Cdd:cd19147 40 LDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIATKFttdyKAYEVGKGKAVNYCgnhkrslhvsvRDSLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 101 RLNTDYLDLYLLHR-SGSFAFEETVAAMEKLIAQGKIRRWGVSNldyadmQELWQLPGGNQCATN---------QVLYHL 170
Cdd:cd19147 120 KLQTDWIDILYVHWwDYTTSIEEVMDSLHILVQQGKVLYLGVSD------TPAWVVSAANYYATAhgktpfsvyQGRWNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 171 GSRGIEYDLLPWCQQQQMPVMAY---------SPLAQAGRLRNG----------------LLKNAVVNEIAHAHNISS-A 224
Cdd:cd19147 194 LNRDFERDIIPMARHFGMALAPWdvlgggkfqSKKAVEERKKNGeglrsfvggteqtpeeVKISEALEKVAEEHGTESvT 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447109083 225 QVLLAWVISH-QGVMAIPKAATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:cd19147 274 AIALAYVRSKaPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-237 |
4.08e-14 |
|
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: 70.94 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 16 AIGQGTWYMGedASQRKTEVAA--LRAGIELGLTLIDTAEMYADGGAEKVVGEAL--TGLRDNVFLVS-KVYpWnaGGQK 90
Cdd:cd19141 14 CLGLGTWVTF--GSQISDEVAEelVTLAYENGINLFDTAEVYAAGKAEIVLGKILkkKGWRRSSYVITtKIF-W--GGKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 91 A----------INACEASLRRLNTDYLDLYLLHRSGSFA-FEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQL---- 155
Cdd:cd19141 89 EterglsrkhiIEGLKASLERLQLEYVDIVFANRPDPNTpMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVarqf 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 156 ----PggnqcATNQVLYHLGSR-GIEYDLLPWCQQQQMPVMAYSPLA---QAGRLRNGL-------------LKNAVVNE 214
Cdd:cd19141 169 nlipP-----IVEQAEYHLFQReKVEMQLPELFHKIGVGAMTWSPLAcgiLSGKYDDGVpeysraslkgyqwLKEKILSE 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 447109083 215 --------------IAHAHNISSAQVLLAWVISHQGV 237
Cdd:cd19141 244 egrrqqaklkelqiIADRLGCTLPQLAIAWCLKNEGV 280
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-256 |
6.87e-14 |
|
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: 70.08 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGEDASQRKTEV-AALRAGIELGLTLIDTAEMYADGGAEKVVGEALTG-LRDNVFLVSKV----------Y 82
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAaATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARhPRAEYVVSTKVgrllepgaagR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 83 P------WN--AGGQKAinACEASLRRLNTDYLDLYLLHRSGS---FAFEETVAAMEKLIAQGKIRRWGVSNldyADMQE 151
Cdd:cd19162 81 PagadrrFDfsADGIRR--SIEASLERLGLDRLDLVFLHDPDRhllQALTDAFPALEELRAEGVVGAIGVGV---TDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 152 LWQLpgGNQCATNQVL----YHLGSRGIEYDLLPWCQQQQMPVMAYSPLaQAGRLRNGLLKNAVVN-------------- 213
Cdd:cd19162 156 LLRA--ARRADVDVVMvagrYTLLDRRAATELLPLCAAKGVAVVAAGVF-NSGILATDDPAGDRYDyrpatpevlararr 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447109083 214 --EIAHAHNISSAQVLLAWVISHQGVMAI-PKAATIAHVQQNAAVL 256
Cdd:cd19162 233 laAVCRRYGVPLPAAALQFPLRHPAVASVvVGAASPAELRDNLALL 278
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
17-240 |
1.05e-13 |
|
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: 70.07 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTWYMGedASQRKTEVAA--LRAGIELGLTLIDTAEMYADGGAEKVVGEALTG---LRDNVFLVSKVYpWNAGGQKA 91
Cdd:cd19159 16 LGLGTWVTF--GGQISDEVAErlMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLY-WGGKAETE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 --------INACEASLRRLNTDYLDLYLLHRSGS-FAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQC- 161
Cdd:cd19159 93 rglsrkhiIEGLKGSLQRLQLEYVDVVFANRPDSnTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 162 --ATNQVLYHLGSR-GIEYDLLPWCQQQQMPVMAYSPLA---QAGRLRNGL-------------LKNAVVNE-------- 214
Cdd:cd19159 173 ppVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLAcgiISGKYGNGVpessraslkcyqwLKERIVSEegrkqqnk 252
|
250 260 270
....*....|....*....|....*....|..
gi 447109083 215 ------IAHAHNISSAQVLLAWVISHQGVMAI 240
Cdd:cd19159 253 lkdlspIAERLGCTLPQLAVAWCLRNEGVSSV 284
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-257 |
2.70e-13 |
|
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: 68.51 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMGE--DASQRKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKV----YPWNAG 87
Cdd:cd19161 1 SELGLGTAGLGNlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKpRDEFVLSTKVgrllKPAREG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 88 GQKAIN---------------------ACEASLRRLNTDYLDLYLLHRSGSFAFEETVA-------------AMEKLIAQ 133
Cdd:cd19161 81 SVPDPNgfvdplpfeivydysydgimrSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsggfkALEELKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 134 GKIRRWG---------VSNLDYADMqelwqlpggnQCATNQVLYHLGSRGIEYDLLPWCQQQQMpvmaysPLAQAGRLRN 204
Cdd:cd19161 161 GVIKAFGlgvnevqicLEALDEADL----------DCFLLAGRYSLLDQSAEEEFLPRCEQRGT------SLVIGGVFNS 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447109083 205 GLLKNAVVNEIAHAHNISSAQVLlawvishQGVMAIPKAATIAHVQQNAAVLE 257
Cdd:cd19161 225 GILATGTKSGAKFNYGDAPAEII-------SRVMEIEKICDAYNVPLAAAALQ 270
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|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
31-279 |
1.58e-12 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 66.34 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 31 RKTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL---RDNVFLVSKVYPWNAG----GQKAINACEASLRRLN 103
Cdd:PLN02587 30 EEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgipREKYVVSTKCGRYGEGfdfsAERVTKSVDESLARLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 104 TDYLDLYLLH--RSGSF--AFEETVAAMEKLIAQGKIRRWGVSNLDYADMQE-LWQLPGGnqcATNQVL----YHLGSRG 174
Cdd:PLN02587 110 LDYVDILHCHdiEFGSLdqIVNETIPALQKLKESGKVRFIGITGLPLAIFTYvLDRVPPG---TVDVILsychYSLNDSS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 175 IEyDLLPWCQQQQMPVMAYSPLAQAGRLRNGL---------LKNAVVNEIAH----AHNISsaQVLLAWVISHQGVMAI- 240
Cdd:PLN02587 187 LE-DLLPYLKSKGVGVISASPLAMGLLTENGPpewhpappeLKSACAAAATHckekGKNIS--KLALQYSLSNKDISTTl 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 447109083 241 PKAATIAHVQQN-AAVLEVELSSAELTMLD--KAYPAP-KGKT 279
Cdd:PLN02587 264 VGMNSVQQVEENvAAATELETSGIDEELLSevEAILAPvKNKT 306
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|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
17-269 |
3.73e-12 |
|
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: 65.49 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 17 IGQGTW--YMGEDASQRKTEVAALraGIELGLTLIDTAEMYADGGAEKVVGEAL--TGLRDNVFLVSKVYPWNAGGQKA- 91
Cdd:cd19158 16 LGLGTWvtFGGQITDEMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFWGGKAETEr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 92 -------INACEASLRRLNTDYLDLYLLHRSG-SFAFEETVAAMEKLIAQGKIRRWGVSNLDYADMQELWQLPGGNQCA- 162
Cdd:cd19158 94 glsrkhiIEGLKASLERLQLEYVDVVFANRPDpNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 163 --TNQVLYHLGSR-GIEYDLLPWCQQQQMPVMAYSPLA---QAGRLRNGL-------------LKNAVVNE--------- 214
Cdd:cd19158 174 piCEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLAcgiVSGKYDSGIppysraslkgyqwLKDKILSEegrrqqakl 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447109083 215 -----IAHAHNISSAQVLLAWVISHQGVMAIPKAATIA-HVQQNAAVLEV--ELSSAELTMLD 269
Cdd:cd19158 254 kelqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAeQLMENIGAIQVlpKLSSSIVHEID 316
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-263 |
3.81e-12 |
|
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: 65.32 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 15 PAIGQGTWYMG---EDASQRKTEvAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL-RDNVFLVSKV--------- 81
Cdd:cd19152 1 PKLGFGTAPLGnlyEAVSDEEAK-ATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELgREDYVISTKVgrllvplqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 82 ----------------YPWNAGGQkAINAC-EASLRRLNTDYLDLYLLH-------RSGSFAFEETVA-----AMEKLIA 132
Cdd:cd19152 80 veptfepgfwnplpfdAVFDYSYD-GILRSiEDSLQRLGLSRIDLLSIHdpdedlaGAESDEHFAQAIkgafrALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 133 QGKIRRWGV-SN-----LDYADMQEL-WQLPGGNqcatnqvlYHLGSRGIEYDLLPWCQQQQMPVMAYSPLAQ---AGRL 202
Cdd:cd19152 159 EGVIKAIGLgVNdweviLRILEEADLdWVMLAGR--------YTLLDHSAARELLPECEKRGVKVVNAGPFNSgflAGGD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447109083 203 RNGLLKNAVVNE-----------IAHAHNISSAQVLLAWVISHQGVMA-IPKAATIAHVQQNAAVLEVELSSA 263
Cdd:cd19152 231 NFDYYEYGPAPPeliarrdrieaLCEQHGVSLAAAALQFALAPPAVASvAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
3-144 |
6.35e-12 |
|
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: 64.48 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 3 QKMIQFSGDVS---LPAIGQGTWYMGEDASQrkTEVAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGL---RDNVF 76
Cdd:cd19153 3 ETLEIALGNVSpvgLGTAALGGVYGDGLEQD--EAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqvpRSSYT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447109083 77 LVSKVYPWNAGG-----QKAINACEASLRRLNTDYLDLYLLH--RSGSFA--FEETVAAMEKLIAQGKIRRWGVSNL 144
Cdd:cd19153 81 VATKVGRYRDSEfdysaERVRASVATSLERLHTTYLDVVYLHdiEFVDYDtlVDEALPALRTLKDEGVIKRIGIAGY 157
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
35-269 |
8.91e-12 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 64.22 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 35 VAALRAGIELGLTLIDTAEMYADGGAEKVVGEALTGLRDNVFLVSKV-------YPWNAGGQKA--INACEASLRRLNTD 105
Cdd:PRK10376 43 IAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTKVgarrgedGSWLPAFSPAelRRAVHDNLRNLGLD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 106 YLDLYLLHRSGSF------AFEETVAAMEKLIAQGKIRRWGVSNLDYAdmqelwQLPGGNQ-----CATNQV-LYH---- 169
Cdd:PRK10376 123 VLDVVNLRLMGDGhgpaegSIEEPLTVLAELQRQGLVRHIGLSNVTPT------QVAEARKiaeivCVQNHYnLAHradd 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447109083 170 -----LGSRGIEYdlLPWcqqqqMPVMAYSPLaQAGRLrngllknavvNEIAHAHNISSAQVLLAWVISHQ-GVMAIPKA 243
Cdd:PRK10376 197 alidaLARDGIAY--VPF-----FPLGGFTPL-QSSTL----------SDVAASLGATPMQVALAWLLQRSpNILLIPGT 258
|
250 260
....*....|....*....|....*.
gi 447109083 244 ATIAHVQQNAAVLEVELSSAELTMLD 269
Cdd:PRK10376 259 SSVAHLRENLAAAELVLSEEVLAELD 284
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