|
Name |
Accession |
Description |
Interval |
E-value |
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
11-283 |
9.19e-88 |
|
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: 264.56 E-value: 9.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR----NRPHVVVATKV--------AG 78
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKdypvKRDKVVIATKVpdgdgpwpSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWGRILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTcTKKYEIVS 156
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTdyIDLYYLHWPDP-DTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALT-KGKIPIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 157 DQVVYNPL-HRAAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDPARRFDSVVNRAK-TAEGRRVAETIRKIAETRGV 234
Cdd:pfam00248 159 VQVEYNLLrRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKgTPLNLEALEALEEIAKEHGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499317429 235 SPAAVVLAWH--AAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKA 283
Cdd:pfam00248 239 SPAQVALRWAlsKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
7-281 |
1.48e-83 |
|
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: 253.69 E-value: 1.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGAW----RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR---NRPHVVVATKVAGS 79
Cdd:cd19093 1 EVSPLGLGTWQWGDRLWwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKelgDRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 80 NW----GRILKSAERSRRRIG--RVDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKY- 152
Cdd:cd19093 81 PWrltrRSVVKALKASLERLGldSIDLYQLHWPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 -EIVSDQVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGAVL-KENLGNDPARRFDSVVNRAKTAEGRRVAETIRKI 228
Cdd:cd19093 161 vPLASNQVEYSLLYRDPEQngLLPACDELGITLIAYSPLAQGLLTgKYSPENPPPGGRRRLFGRKNLEKVQPLLDALEEI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499317429 229 AETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19093 241 AEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
6-286 |
1.93e-74 |
|
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: 231.22 E-value: 1.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATKVAGSNWG- 82
Cdd:COG0667 11 LKVSRLGLGTMTFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRddVVIATKVGRRMGPg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 ---------RILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKAL-TCTK 150
Cdd:COG0667 91 pngrglsreHIRRAVEASLRRLGtdYIDLYQLHRPDPD-TPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALaIAEG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 151 KYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKG----AVLKENLGNDPARRFDSVVNRAKTAEGRRVAETI 225
Cdd:COG0667 170 LPPIVAVQNEYSLLDRSAEEeLLPAARELGVGVLAYSPLAGGlltgKYRRGATFPEGDRAATNFVQGYLTERNLALVDAL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 226 RKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASAP 286
Cdd:COG0667 250 RAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAA 312
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
7-283 |
4.10e-65 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 205.29 E-value: 4.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG 82
Cdd:COG0656 4 EIPALGLGTWQLPG-------EEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAAsgvpREELFVTTKVWNDNHG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R--ILKSAERSRRRIG--RVDLLQFHWPPPiyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKkYEIVSDQ 158
Cdd:COG0656 74 YddTLAAFEESLERLGldYLDLYLIHWPGP--GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG-VKPAVNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 159 VVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAA 238
Cdd:COG0656 151 VELHPYLQQRE-LLAFCREHGIVVEAYSPLGRGKLLDD--------------------------PVLAEIAEKHGKTPAQ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 239 VVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKA 283
Cdd:COG0656 204 VVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
5-281 |
2.98e-64 |
|
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: 204.68 E-value: 2.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 5 SLEVGKIGLGAWQAGGGAW-RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN-RPHVVVATKVaGSNWG 82
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWWgEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGrRDDVVIATKC-GLRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 ------------RILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTC 148
Cdd:cd19084 80 ggkgvtkdlspeSIRKEVEQSLRRLQtdYIDLYQIHWPDP-NTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 149 TkkyEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGaVL------KENLGNDPARRFDSVVNRAKTAEGRRV 221
Cdd:cd19084 159 G---PIVSLQPPYSMLEREIEEeLLPYCRENGIGVLPYGPLAQG-LLtgkykkEPTFPPDDRRSRFPFFRGENFEKNLEI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 222 AETIRKIAETRGVSPAAVVLAWHAAK--GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19084 235 VDKLKEIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
7-281 |
1.08e-63 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 202.07 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGAWRV--DFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATKVAGSNWG 82
Cdd:cd19072 3 EVPVLGLGTWGIGGGMSKDysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRedLFITTKVSPDHLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 --RILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVSDQ 158
Cdd:cd19072 83 ydDVIKAAKESLKRLGtdYIDLYLIHWPNP-SIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIVANQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 159 VVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGavlkeNLGNDPARRFdsvvnraktaegrrvaetIRKIAETRGVSPA 237
Cdd:cd19072 162 VEYNLFDREEESgLLPYCQKNGIAIIAYSPLEKG-----KLSNAKGSPL------------------LDEIAKKYGKTPA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 238 AVVLAWHAAK-GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19072 219 QIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
8-287 |
5.46e-58 |
|
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: 188.18 E-value: 5.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 8 VGKIGLGAWQAGGGAW--RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR-NRPHVVVATKVAGSN--WG 82
Cdd:cd19085 1 VSRLGLGCWQFGGGYWwgDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKgRRDDVVIATKVSPDNltPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 RILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKkyeIVSDQVV 160
Cdd:cd19085 81 DVRKSCERSLKRLGTdyIDLYQIHWPSS-DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR---IDSNQLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 161 YNPLHRAAER-LIEMGRARGFVVIAWSPLAKGavlkenL---GNDPARRFDSVVNRAKT---------AEGRRVAETIRK 227
Cdd:cd19085 157 YNLLWRAIEYeILPFCREHGIGVLAYSPLAQG------LltgKFSSAEDFPPGDARTRLfrhfepgaeEETFEALEKLKE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 228 IAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASAPF 287
Cdd:cd19085 231 IADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
7-281 |
1.19e-50 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 168.58 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGawRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN-RPHVVVATKVAGSNWGR-- 83
Cdd:cd19138 10 KVPALGQGTWYMGED--PAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGrRDKVFLVSKVLPSNASRqg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRRRIG--RVDLLQFHWPPPiyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVSDQVVY 161
Cdd:cd19138 88 TVRACERSLRRLGtdYLDLYLLHWRGG--VPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAANQVLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 162 NPLHRAAE-RLIEMGRARGFVVIAWSPLAKGAVLKENLGNDParrfdsvvnraktaegrrvaeTIRKIAETRGVSPAAVV 240
Cdd:cd19138 166 NLGSRGIEyDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENP---------------------TLKEIAARHGATPAQVA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499317429 241 LAWHAAKGS-FPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19138 225 LAWVLRDGNvIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
6-284 |
1.83e-46 |
|
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: 159.32 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGG------AWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH-VVVATKVA- 77
Cdd:cd19091 11 LKVSELALGTMTFGGGggffgaWGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDdVLIATKVRg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 ---------GSNWGRILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKAL 146
Cdd:cd19091 91 rmgegpndvGLSRHHIIRAVEASLKRLGTdyIDLYQLHGFDA-LTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 147 TCTKKY---EIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAK----GAVLKENLGNDPARRFDS-----VVNRA 213
Cdd:cd19091 170 GISERRglaRFVALQAYYSLLGRDLEHeLMPLALDQGVGLLVWSPLAGgllsGKYRRGQPAPEGSRLRRTgfdfpPVDRE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 214 KtaeGRRVAETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKAS 284
Cdd:cd19091 250 R---GYDVVDALREIAKETGATPAQVALAWllSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKVS 319
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-281 |
2.03e-46 |
|
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: 158.90 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 2 KIGS--LEVGKIGLGAWQAG---GGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR---NRPHVVVA 73
Cdd:cd19079 4 RLGNsgLKVSRLCLGCMSFGdpkWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKefaPRDEVVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 74 TKV-----AGSNWGR-----ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARL 141
Cdd:cd19079 84 TKVyfpmgDGPNGRGlsrkhIMAEVDASLKRLGtdYIDLYQIHRWDY-ETPIEETLEALHDVVKSGKVRYIGASSMYAWQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKALTCTKKYE---IVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAV---LKENLGNDPARRFDSVVNRAK 214
Cdd:cd19079 163 FAKALHLAEKNGwtkFVSMQNHYNLLYREEEReMIPLCEEEGIGVIPWSPLARGRLarpWGDTTERRRSTTDTAKLKYDY 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 215 TAE-GRRVAETIRKIAETRGVSPAAVVLAWHAAKGSF--PIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19079 243 FTEaDKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVtaPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-283 |
5.54e-46 |
|
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: 157.45 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAWR-----VDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN-RPHVVVATKVA--GSNWG 82
Cdd:cd19102 4 IGLGTWAIGGGGWGggwgpQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGlRDRPIVATKCGllWDEEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R---------ILKSAERSRRRIGR--VDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKaltCTKK 151
Cdd:cd19102 84 RirrslkpasIRAECEASLRRLGVdvIDLYQIHWPDPD-EPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR---CQAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 152 YEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKG----AVLKENLGNDPA---RRFDSVVNRAKTAEGRRVAE 223
Cdd:cd19102 160 HPIASLQPPYSLLRRGIEAeILPFCAEHGIGVIVYSPMQSGlltgKMTPERVASLPAddwRRRSPFFQEPNLARNLALVD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 224 TIRKIAETRGVSPAAVVLAW---HAAKGSfPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKA 283
Cdd:cd19102 240 ALRPIAERHGRTVAQLAIAWvlrRPEVTS-AIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
8-273 |
1.01e-44 |
|
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: 152.76 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 8 VGKIGLGAWQ-AGGGAW--RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH-VVVATKV-----AG 78
Cdd:cd19088 1 VSRLGYGAMRlTGPGIWgpPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDdVVIATKGglvrtGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWGR------ILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTk 150
Cdd:cd19088 81 GWWGPdgspeyLRQAVEASLRRLGldRIDLYQLHRIDPK-VPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 151 kyEIVSDQVVYNPLHRAAERLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvAETIRKIAE 230
Cdd:cd19088 159 --RIVSVQNRYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQP-------------------------GGLLAEVAA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 231 TRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANALQLS 273
Cdd:cd19088 212 RLGATPAQVALAWllARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
10-266 |
3.58e-43 |
|
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: 148.05 E-value: 3.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGgawRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRP---HVVVATKVAGSNWGR--- 83
Cdd:cd06660 2 RLGLGTMTFGG---DGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnrdDVVIATKGGHPPGGDpsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 -------ILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKY-- 152
Cdd:cd06660 79 srlspehIRRDLEESLRRLGtdYIDLYYLHRDDPS-TPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHgl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 -EIVSDQVVYNPLHRAA--ERLIEMGRARGFVVIAWSPLAKGavlkenlgndparrfdsvvnraktaegrrvaetirkia 229
Cdd:cd06660 158 pGFAAVQPQYSLLDRSPmeEELLDWAEENGLPLLAYSPLARG-------------------------------------- 199
|
250 260 270
....*....|....*....|....*....|....*....
gi 499317429 230 etrgvsPAAVVLAWHAAK--GSFPIPGVKTLKQAQEVLE 266
Cdd:cd06660 200 ------PAQLALAWLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
8-281 |
4.41e-43 |
|
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: 148.19 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 8 VGKIGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIR----NRPHVVVATKVAGSNW-- 81
Cdd:cd19073 1 IPALGLGTWQLRG-------DDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAesgvPREDLFITTKVWRDHLrp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 GRILKSAERSRRRIGR--VDLLQFHWPPPIYvPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKyEIVSDQV 159
Cdd:cd19073 71 EDLKKSVDRSLEKLGTdyVDLLLIHWPNPTV-PLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL-PIAVNQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 160 VYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLkenlgNDParrfdsvvnraktaegrrvaeTIRKIAETRGVSPAAV 239
Cdd:cd19073 149 EFHPFLYQAE-LLEYCRENDIVITAYSPLARGEVL-----RDP---------------------VIQEIAEKYDKTPAQV 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499317429 240 VLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19073 202 ALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
1-282 |
7.76e-43 |
|
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: 149.73 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 1 MKIGS--LEVGKIGLGAWQAGGGAW--RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN-RPHVVVATK 75
Cdd:cd19149 2 RKLGKsgIEASVIGLGTWAIGGGPWwgGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGrRDKVVLATK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 vAGSNWGR----------------------ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAE 131
Cdd:cd19149 82 -CGLRWDReggsfffvrdgvtvyknlspesIREEVEQSLKRLGtdYIDLYQTHWQDV-ETPIEETMEALEELKRQGKIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 132 IGVSNFDARLMEKALTCtkkYEIVSDQVVYNPLHRAAE-RLIEMGRARGFVVIAWSPLAKG-----AVLKENLGNDPARR 205
Cdd:cd19149 160 IGASNVSVEQIKEYVKA---GQLDIIQEKYSMLDRGIEkELLPYCKKNNIAFQAYSPLEQGlltgkITPDREFDAGDARS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 206 F---DSVVNRAKTAegrRVAETIRKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19149 237 GipwFSPENREKVL---ALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATM 313
|
..
gi 499317429 281 DK 282
Cdd:cd19149 314 RS 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
6-282 |
1.82e-42 |
|
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: 148.49 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGgawRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELI-RNRPHVVVATKV-------- 76
Cdd:cd19087 11 LKVSRLCLGTMNFGG---RTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIaGRRDDIVLATKVfgpmgddp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 --AGSNWGRILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKY 152
Cdd:cd19087 88 ndRGLSRRHIRRAVEASLRRLQtdYIDLYQMHHFDR-DTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 E---IVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGaVLKENLGNDPARRFDSVVN------RAKTAEGRRVA 222
Cdd:cd19087 167 GllrFVSEQPMYNLLKRQAELeILPAARAYGLGVIPYSPLAGG-LLTGKYGKGKRPESGRLVEraryqaRYGLEEYRDIA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 223 ETIRKIAETRGVSPAAVVLAW---HAAKGSfPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19087 246 ERFEALAAEAGLTPASLALAWvlsHPAVTS-PIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-281 |
5.05e-42 |
|
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: 147.36 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAELKRAYeyaLDHGIKFIDTAEVYGS-------GKSEEFVAELIR---NRPHVVVATK 75
Cdd:cd19081 7 LSVSPLCLGTMVFGWTADEETSFALLDAF---VDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKsrgKRDRVVIATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 VAGSNWGR--------ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19081 84 VGFPMGPNgpglsrkhIRRAVEASLRRLQtdYIDLYQAHWDDP-ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LTCTKKY---EIVSDQVVYNPLHRAA--ERLIEMGRARGFVVIAWSPLAKGAVL-KENLGNDPA--RRFDSVVNRAKTAE 217
Cdd:cd19081 163 LELSRQHglpRYVSLQPEYNLVDRESfeGELLPLCREEGIGVIPYSPLAGGFLTgKYRSEADLPgsTRRGEAAKRYLNER 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 218 GRRVAETIRKIAETRGVSPAAVVLAWHAAKGSF--PIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19081 243 GLRILDALDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
6-191 |
8.54e-42 |
|
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: 144.54 E-value: 8.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWR-VDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR-NRPHVVVATKV--AGSNW 81
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWWGdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKgRRDKVVIATKFgnRFDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 GR---------ILKSAERSRRRIG--RVDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALtctK 150
Cdd:cd19086 81 PErpqdfspeyIREAVEASLKRLGtdYIDLYQLHNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAAL---R 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499317429 151 KYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKG 191
Cdd:cd19086 158 RGGIDVVQVIYNLLDQRPEEeLFPLAEEHGVGVIARVPLASG 199
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
10-281 |
1.89e-39 |
|
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: 138.77 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIR----NRPHVVVATKVAGSNWG--R 83
Cdd:cd19071 3 LIGLGTYKLKPE-------ETAEAVLAALEAGYRHIDTAAAYGN---EAEVGEAIResgvPREELFITTKLWPTDHGyeR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRRRIGR--VDLLQFHWP-----PPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKkYEIVS 156
Cdd:cd19071 73 VREALEESLKDLGLdyLDLYLIHWPvpgkeGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-IKPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 157 DQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAvlKENLGNdparrfdsvvnraktaegrrvaETIRKIAETRGVSP 236
Cdd:cd19071 152 NQIELHPYLQQKE-LVEFCKEHGIVVQAYSPLGRGR--RPLLDD----------------------PVLKEIAKKYGKTP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 237 AAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19071 207 AQVLLRWALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
1-282 |
4.78e-39 |
|
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: 138.16 E-value: 4.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 1 MKIGSLEVGKIGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKV 76
Cdd:cd19140 1 VTVNGVRIPALGLGTYPLTG-------EECTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAAsgvpRDELFLTTKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 AGSNW--GRILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKy 152
Cdd:cd19140 71 WPDNYspDDFLASVEESLRKLRtdYVDLLLLHWPNK-DVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 EIVSDQVVYNPLHRAAeRLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETR 232
Cdd:cd19140 149 PLFTNQVEYHPYLDQR-KLLDAAREHGIALTAYSPLARGEVLKD--------------------------PVLQEIGRKH 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499317429 233 GVSPAAVVLAWHAAK-GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19140 202 GKTPAQVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
6-281 |
1.25e-36 |
|
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: 133.11 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGG-AWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR-NRPHVVVATKV------- 76
Cdd:cd19080 8 LRVSPLALGTMTFGTEwGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAgNRDRIVLATKYtmnrrpg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 ---AGSNwGR--ILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCT 149
Cdd:cd19080 88 dpnAGGN-HRknLRRSVEASLRRLQtdYIDLLYVHAWDFT-TPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 KKY---EIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGaVL--KENLGNDPARRFDSVVNRAKTAEGRR--- 220
Cdd:cd19080 166 ELRgwsPFVALQIEYSLLERTPEReLLPMARALGLGVTPWSPLGGG-LLtgKYQRGEEGRAGEAKGVTVGFGKLTERnwa 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 221 VAETIRKIAETRGVSPAAVVLAWHAAK--GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19080 245 IVDVVAAVAEELGRSAAQVALAWVRQKpgVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
7-281 |
5.51e-36 |
|
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: 130.38 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGAWRvDFA---ELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN--RPHVVVATKVAGSNW 81
Cdd:cd19137 3 KIPALGLGTWGIGGFLTP-DYSrdeEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDfpREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 GR--ILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKyEIVSD 157
Cdd:cd19137 82 RYddLLRSLQNSLRRLDTdyIDLYLIHWPNP-NIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-PIVCN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 158 QVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVS 235
Cdd:cd19137 160 QVKYNLEDRDPERdgLLEYCQKNGITVVAYSPLRRGLEKTN--------------------------RTLEEIAKNYGKT 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499317429 236 PAAVVLAWHAAKGS-FPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19137 214 IAQIALAWLIQKPNvVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
37-282 |
1.05e-35 |
|
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: 129.01 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 37 ALDHGIKFIDTAEVYGSgksEEFVAELIR----NRPHVVVATKVAGSNW--GRILKSAERSRRRIG--RVDLLQFHWPPP 108
Cdd:cd19139 23 ALELGYRHIDTAQIYDN---EAAVGQAIAesgvPRDELFITTKIWIDNLskDKLLPSLEESLEKLRtdYVDLTLIHWPSP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 109 -IYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVSDQVVYNPLhRAAERLIEMGRARGFVVIAWSP 187
Cdd:cd19139 100 nDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY-LQNRKLVAHCKQHGIHVTSYMT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 188 LAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEA 267
Cdd:cd19139 179 LAYGKVLDD--------------------------PVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLA 232
|
250
....*....|....*
gi 499317429 268 NALQLSEAEVRAIDK 282
Cdd:cd19139 233 LDLTLDADDMAAIAA 247
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
2-283 |
2.45e-35 |
|
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: 129.85 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 2 KIG--SLEVGKIGLGAWQAGGGAW--RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR--NRPHVVVATK 75
Cdd:cd19083 3 KLGksDIDVNPIGLGTNAVGGHNLypNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKeyNRNEVVIATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 VAG---------SNWGRILKSA-ERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMe 143
Cdd:cd19083 83 GAHkfggdgsvlNNSPEFLRSAvEKSLKRLNTdyIDLYYIHFPDG-ETPKAEAVGALQELKDEGKIRAIGVSNFSLEQL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 144 KALTCTKKYEIVSDQvvYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAvlkenLGN--DPARRFDSVVNRAKTAE--G 218
Cdd:cd19083 161 KEANKDGYVDVLQGE--YNLLQREAEEdILPYCVENNISFIPYFPLASGL-----LAGkyTKDTKFPDNDLRNDKPLfkG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 219 RRVAETIRK------IAETRGVSPAAVVLAWHAAKGSFP--IPGVKTLKQAQEVLEANALQLSEAEVRAIDKA 283
Cdd:cd19083 234 ERFSENLDKvdklksIADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
6-276 |
5.62e-33 |
|
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: 123.05 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGgaWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH----VVVATK---VAG 78
Cdd:cd19092 4 LEVSRLVLGCMRLAD--WGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGlrekIEIQTKcgiRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWG------------RILKSAERSRRRIG--RVDLLQFHWPPPIYVPLcKVIRDLEKAAQLGLTAEIGVSNFDA---RL 141
Cdd:cd19092 82 DDPRpgrikhydtskeHILASVEGSLKRLGtdYLDLLLLHRPDPLMDPE-EVAEAFDELVKSGKVRYFGVSNFTPsqiEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKALtctkKYEIVSDQVVYNPLHRAAerlIEMG-----RARGFVVIAWSPLAKGAVLKENLGNDParrfdsvvnrakta 216
Cdd:cd19092 161 LQSYL----DQPLVTNQIELSLLHTEA---IDDGtldycQLLDITPMAWSPLGGGRLFGGFDERFQ-------------- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499317429 217 egrRVAETIRKIAETRGVSPAAVVLAW---HAAKgsfPIPGVKTLK--QAQEVLEANALQLSEAE 276
Cdd:cd19092 220 ---RLRAALEELAEEYGVTIEAIALAWllrHPAR---IQPILGTTNpeRIRSAVKALDIELTREE 278
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-280 |
6.66e-31 |
|
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: 117.70 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 2 KIGS--LEVGKIGLGAW---QAGGGAwrvDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR-NRPHVVVATK 75
Cdd:cd19076 4 KLGTqgLEVSALGLGCMgmsAFYGPA---DEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKdRRDEVVIATK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 -----VAGSNW----GR---ILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARL 141
Cdd:cd19076 81 fgivrDPGSGFrgvdGRpeyVRAACEASLKRLGTdvIDLYYQHRVDP-NVPIEETVGAMAELVEEGKVRYIGLSEASADT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKAltcTKKYEIVSDQVVYNPLHRAAERLIeMGRAR----GFVviAWSPLAKG-----AVLKENLGNDPARRFD---SV 209
Cdd:cd19076 160 IRRA---HAVHPITAVQSEYSLWTRDIEDEV-LPTCRelgiGFV--AYSPLGRGfltgaIKSPEDLPEDDFRRNNprfQG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 210 VNRAKTAEgrrVAETIRKIAETRGVSPAAVVLAWHAAKGS--FPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19076 234 ENFDKNLK---LVEKLEAIAAEKGCTPAQLALAWVLAQGDdiVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
6-282 |
1.17e-30 |
|
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: 117.02 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAW-RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN---RPHVVVATKVaGSNW 81
Cdd:cd19148 2 LPVSRIALGTWAIGGWMWgGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEygkRDRVVIATKV-GLEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 G------------RILKSAERSRRRIGR--VDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEkalT 147
Cdd:cd19148 81 DeggevvrnsspaRIRKEVEDSLRRLQTdyIDLYQVHWPDPL-VPIEETAEALKELLDEGKIRAIGVSNFSPEQME---T 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 148 CTKKYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAV---LKEN--LGNDPARRFDSVVNRAKTAEGRRV 221
Cdd:cd19148 157 FRKVAPLHTVQPPYNLFEREIEKdVLPYARKHNIVTLAYGALCRGLLsgkMTKDtkFEGDDLRRTDPKFQEPRFSQYLAA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 222 AETIRKIAETR-GVSPAAVVLAWHAAKGSFPIP--GVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19148 237 VEELDKLAQERyGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEIDA 300
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
11-235 |
2.53e-30 |
|
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: 115.02 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSgkSEEFVAELIRN--RPHVVVATKVaGSNWGR----- 83
Cdd:cd19095 3 LGLGTSGIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGlrRDDLFIATKV-GTHGEGgrdrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ------ILKSAERSRRR--IGRVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLmEKALTcTKKYEIV 155
Cdd:cd19095 80 dfspaaIRASIERSLRRlgTDYIDLLQLHGPSDD-ELTGEVLETLEDLKAAGKVRYIGVSGDGEEL-EAAIA-SGVFDVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 156 sdQVVYNPLHRAAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDPARRFDSVVNRAKTAEGRRVAET-IRKIAETRGV 234
Cdd:cd19095 157 --QLPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGGATWAQAaLRFVLSHPGV 234
|
.
gi 499317429 235 S 235
Cdd:cd19095 235 S 235
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
17-282 |
7.28e-30 |
|
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: 114.01 E-value: 7.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 17 QAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG--RILKSAER 90
Cdd:cd19131 12 QLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGN---EEGVGKAIRAsgvpREELFITTKLWNSDQGydSTLRAFDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 91 SRRRIGR--VDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQVVYNPLHRAA 168
Cdd:cd19131 89 SLRKLGLdyVDLYLIHWPVPAQDKYVETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVV-NQIELHPRFQQR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 169 ErLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAAVVLAWHAAKG 248
Cdd:cd19131 168 E-LRAFHAKHGIQTESWSPLGQGGLLSD--------------------------PVIGEIAEKHGKTPAQVVIRWHLQNG 220
|
250 260 270
....*....|....*....|....*....|....
gi 499317429 249 SFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19131 221 LVVIPKSVTPSRIAENFDVFDFELDADDMQAIAG 254
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
6-274 |
8.70e-30 |
|
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: 114.61 E-value: 8.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAE--LKRAYeyalDHGIKFIDTAEVYGSGKSEEFVAELIR--NRPHVVVATKV----- 76
Cdd:cd19074 2 LKVSELSLGTWLTFGGQVDDEDAKacVRKAY----DLGINFFDTADVYAAGQAEEVLGKALKgwPRESYVISTKVfwptg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 AGSN-WG----RILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCT 149
Cdd:cd19074 78 PGPNdRGlsrkHIFESIHASLKRLQldYVDIYYCHRYDPE-TPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 KKY---EIVSDQVVYNPLHRAAE-RLIEMGRARGFVVIAWSPLAKGaVL--KENLG-NDPARRFDSV------VNRAKTA 216
Cdd:cd19074 157 RQFgliPPVVEQPQYNMLWREIEeEVIPLCEKNGIGLVVWSPLAQG-LLtgKYRDGiPPPSRSRATDednrdkKRRLLTD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 217 EGRRVAETIRKIAETRGVSPAAVVLAWHAAK--GSFPIPGVKTLKQAQEVLEANALQLSE 274
Cdd:cd19074 236 ENLEKVKKLKPIADELGLTLAQLALAWCLRNpaVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-281 |
1.49e-29 |
|
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: 113.13 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWGR-- 83
Cdd:cd19132 9 AIGFGTYPLKG-------DEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRsgvpREELFVTTKLPGRHHGYee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRRRIG--RVDLLQFHWPPP---IYVPLCKVIRDLEKAaqlGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQ 158
Cdd:cd19132 79 ALRTIEESLYRLGldYVDLYLIHWPNPsrdLYVEAWQALIEAREE---GLVRSIGVSNFLPEHLDRLIDETGVTPAV-NQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 159 VVYNP-LHRAAERLIEmgRARGFVVIAWSPLAKGAVLKENlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPA 237
Cdd:cd19132 155 IELHPyFPQAEQRAYH--REHGIVTQSWSPLGRGSGLLDE-------------------------PVIKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499317429 238 AVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19132 208 QVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIA 251
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
35-283 |
2.73e-29 |
|
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: 112.71 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 35 EYALDHGIKFIDTAEVYGsgkSEEFVAELIRN----RPHVVVATKVAGSNwGRILKSAERSRRRIG--RVDLLQFHWPPP 108
Cdd:cd19120 32 KLALKAGFRHIDTAEMYG---NEKEVGEALKEsgvpREDLFITTKVSPGI-KDPREALRKSLAKLGvdYVDLYLIHSPFF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 109 IY---VPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTcTKKYEIVSDQVVYNP-LHRAAERLIEMGRARGFVVIA 184
Cdd:cd19120 108 AKeggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLD-TAKIKPAVNQIEFHPyLYPQQPALLEYCREHGIVVSA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 185 WSPLAKgavlkenLGNDPARRFDSVVNRaktaegrrvaetirkIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEV 264
Cdd:cd19120 187 YSPLSP-------LTRDAGGPLDPVLEK---------------IAEKYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEY 244
|
250
....*....|....*....
gi 499317429 265 LEANALQLSEAEVRAIDKA 283
Cdd:cd19120 245 LEAFDFELTEEEVEEIDKA 263
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-282 |
4.10e-28 |
|
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: 110.73 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 36 YALDHGIKFIDTAEVY-------GSGKSEEFVAELIRNRPH---VVVATKVAGS--------------NWGRILKSAERS 91
Cdd:cd19094 26 YAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKKKGNrdkVVLATKVAGPgegitwprgggtrlDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 92 RRRIGR--VDLLQFHWPP-----------------PIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDA-RLME-----KAL 146
Cdd:cd19094 106 LKRLGTdyIDLYQLHWPDrytplfgggyytepseeEDSVSFEEQLEALGELVKAGKIRHIGLSNETPwGVMKflelaEQL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 147 TCTKkyeIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAV----LKENLGNDPAR--RFDSVVNRAKTAEGR 219
Cdd:cd19094 186 GLPR---IVSIQNPYSLLNRNFEEgLAEACHRENVGLLAYSPLAGGVLtgkyLDGAARPEGGRlnLFPGYMARYRSPQAL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499317429 220 RVAETIRKIAETRGVSPAAVVLAWHAakgSFP-----IPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19094 263 EAVAEYVKLARKHGLSPAQLALAWVR---SRPfvtstIIGATTLEQLKENIDAFDVPLSDELLAEIDA 327
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-285 |
4.42e-28 |
|
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: 110.12 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGGAW--------RVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATK---- 75
Cdd:cd19103 6 KIALGTWSWGSGGAggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPRedYIISTKftpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 VAGSNWGRILKSAERSRRRIGRvDLLQFHWpppIYVPLcKVIRDLEKAAQL---GLTAEIGVSNFDarLMEkaltCTKKY 152
Cdd:cd19103 86 IAGQSADPVADMLEGSLARLGT-DYIDIYW---IHNPA-DVERWTPELIPLlksGKVKHVGVSNHN--LAE----IKRAN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 EIVSD--------QVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGAVLKENLGNDParrFDSVVNRAKTAEGR--- 219
Cdd:cd19103 155 EILAKagvslsavQNHYSLLYRSSEEagILDYCKENGITFFAYMVLEQGALSGKYDTKHP---LPEGSGRAETYNPLlpq 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499317429 220 --RVAETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASA 285
Cdd:cd19103 232 leELTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLAD 299
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
11-283 |
5.43e-28 |
|
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: 109.95 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAWRVDfaELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPHVVVATKVAGSNWGR-----IL 85
Cdd:cd19075 5 LGTMTFGSQGRFTTAE--AAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFKIDTKANPGVGGGlspenVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 86 KSAERSRRRIGR--VDLLQFHWPPPIyVPL---CKVIRDLEKAaqlGLTAEIGVSNFDARLMEKALT-CTKK-------Y 152
Cdd:cd19075 83 KQLETSLKRLKVdkVDVFYLHAPDRS-TPLeetLAAIDELYKE---GKFKEFGLSNYSAWEVAEIVEiCKENgwvlptvY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 eivsdQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAV---LKENLGNDPARRFDSVVNRAKTAEGR-------RV 221
Cdd:cd19075 159 -----QGMYNAITRQVETeLFPCLRKLGIRFYAYSPLAGGFLtgkYKYSEDKAGGGRFDPNNALGKLYRDRywkpsyfEA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 222 AETIRKIAETRGVSPAAVVLAW---HAA----KGSFPIPGVKTLKQAQEVLEA-NALQLSEAEVRAIDKA 283
Cdd:cd19075 234 LEKVEEAAEKEGISLAEAALRWlyhHSAldgeKGDGVILGASSLEQLEENLAAlEKGPLPEEVVKAIDEA 303
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
37-280 |
1.39e-27 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 108.19 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 37 ALDHGIKFIDTAEVYGSgksEEFVAELIR----NRPHVVVATKVAGSNW--GRILKSAERSRRRIG--RVDLLQFHWPPP 108
Cdd:PRK11172 25 ALELGYRAIDTAQIYDN---EAAVGQAIAesgvPRDELFITTKIWIDNLakDKLIPSLKESLQKLRtdYVDLTLIHWPSP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 109 -IYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVSDQVVYNPLHRAAeRLIEMGRARGFVVIAWSP 187
Cdd:PRK11172 102 nDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQNR-KVVAFAKEHGIHVTSYMT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 188 LAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEA 267
Cdd:PRK11172 181 LAYGKVLKD--------------------------PVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLA 234
|
250
....*....|...
gi 499317429 268 NALQLSEAEVRAI 280
Cdd:PRK11172 235 QDLQLDAEDMAAI 247
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
6-283 |
7.26e-27 |
|
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: 106.93 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAW---QAGGGAwrVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN-RPHVVVATK------ 75
Cdd:cd19078 2 LEVSAIGLGCMgmsHGYGPP--PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPfRDQVVIATKfgfkid 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 -------VAGSNWGRILKSAERSRRRIG--RVDLLQFHWPPPiYVPL---CKVIRDLEKAaqlGLTAEIGVSNFDARLME 143
Cdd:cd19078 80 ggkpgplGLDSRPEHIRKAVEGSLKRLQtdYIDLYYQHRVDP-NVPIeevAGTMKELIKE---GKIRHWGLSEAGVETIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 144 KALTCTKkyeIVSDQVVYNPLHRAAERLI-----EMGRarGFVviAWSPLAKG---AVLKENlgndpaRRFDSVVNRAK- 214
Cdd:cd19078 156 RAHAVCP---VTAVQSEYSMMWREPEKEVlptleELGI--GFV--PFSPLGKGfltGKIDEN------TKFDEGDDRASl 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499317429 215 ---TAEGRRVA----ETIRKIAETRGVSPAAVVLAWHAAKGSF--PIPGVKTLKQAQEVLEANALQLSEAEVRAIDKA 283
Cdd:cd19078 223 prfTPEALEANqalvDLLKEFAEEKGATPAQIALAWLLAKKPWivPIPGTTKLSRLEENIGAADIELTPEELREIEDA 300
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-281 |
2.02e-26 |
|
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: 104.83 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGGAwrvdfaELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIRN----RPHVVVATKVAGSNWG--R 83
Cdd:cd19126 11 WLGLGVFQTPDGD------ETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIREsgvpREELFVTTKLWNDDQRarR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRRRIG--RVDLLQFHWPPPiyvplCKVI---RDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQ 158
Cdd:cd19126 82 TEDAFQESLDRLGldYVDLYLIHWPGK-----DKFIdtwKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAV-NQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 159 VVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAA 238
Cdd:cd19126 156 VEFHPYLTQKE-LRGYCKSKGIVVEAWSPLGQGGLLSN--------------------------PVLAAIGEKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499317429 239 VVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19126 209 VVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
10-275 |
2.70e-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: 104.94 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYgsGKSEEFVAELIRN--RPHVVVATKV-------AGSN 80
Cdd:cd19090 2 ALGLGTAGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAElpREPLVLSTKVgrlpedtADYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 81 WGRILKSAERSRRRIGR--VDLLQFH---WPPPIYVPLCK-VIRDLEKAAQLGLTAEIGVSNFDARLMEKALTcTKKYEI 154
Cdd:cd19090 80 ADRVRRSVEESLERLGRdrIDLLMIHdpeRVPWVDILAPGgALEALLELKEEGLIKHIGLGGGPPDLLRRAIE-TGDFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 155 VSDQVVYNPLHR-AAERLIEMGRARGFVVIAWSPLAKGAvlkenLGNDPARRFDSVVNRAKTAEGRRvAETIRKIAETRG 233
Cdd:cd19090 159 VLTANRYTLLDQsAADELLPAAARHGVGVINASPLGMGL-----LAGRPPERVRYTYRWLSPELLDR-AKRLYELCDEHG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 234 VSPAAVVLAW---HAAKGSFpIPGVKTLKQAQEVLEANALQLSEA 275
Cdd:cd19090 233 VPLPALALRFllrDPRISTV-LVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
11-282 |
2.79e-25 |
|
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: 102.36 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAwrvdfaELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN--------RPHVVVATKVAGSNWG 82
Cdd:cd19116 14 IALGTWKLKDDE------GVRQAVKHAIEAGYRHIDTAYLYGN---EAEVGEAIREkiaegvvkREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R--ILKSAERSRRRIG--RVDLLQFHWPPPI-YVPLCKVI--------------RDLEKAAQLGLTAEIGVSNFDARLME 143
Cdd:cd19116 85 ReqVEPALRESLKRLGldYVDLYLIHWPVAFkENNDSESNgdgslsdidyletwRGMEDLVKLGLTRSIGVSNFNSEQIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 144 KALTCTKKYEIVsDQVVYNP-LHRaaERLIEMGRARGFVVIAWSPLakGAVLKENLGNDPARRFDsvvnraktaegrrva 222
Cdd:cd19116 165 RLLSNCNIKPAV-NQIEVHPtLTQ--EKLVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPRLDD--------------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 223 ETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19116 225 PTLVAIAKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNS 284
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
6-282 |
4.94e-25 |
|
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: 101.45 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYGsgkSEEFVAELIRN-------RPHVVVATKVAG 78
Cdd:cd19121 10 ASIPAVGLGTWQAKAG-------EVKAAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEaiaggvkREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWGRILKSAERSRRRIG--RVDLLQFHWPppiyVPL-------------------------CKVIRDLEKAAQLGLTAE 131
Cdd:cd19121 80 TYHRRVELCLDRSLKSLGldYVDLYLVHWP----VLLnpngnhdlfptlpdgsrdldwdwnhVDTWKQMEKVLKTGKTKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 132 IGVSNFDARLMEKALTCTKKYEIVsDQVVYNPlHRAAERLIEMGRARGFVVIAWSPL-AKGAVLKEnlgndparrfdsvv 210
Cdd:cd19121 156 IGVSNYSIPYLEELLKHATVVPAV-NQVENHP-YLPQQELVDFCKEKGILIEAYSPLgSTGSPLIS-------------- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 211 nraktaegrrvAETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEanALQLSEAEVRAIDK 282
Cdd:cd19121 220 -----------DEPVVEIAKKHNVGPGTVLISYQVARGAVVLPKSVTPDRIKSNLE--IIDLDDEDMNKLND 278
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-281 |
2.49e-24 |
|
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: 99.51 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 5 SLEVGKIGLGAWQAGGGAwrvdfaELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIRN----RPHVVVATKVAGSN 80
Cdd:cd19156 6 GVEMPRLGLGVWRVQDGA------EAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIREsgvpREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 81 WG--RILKSAERSRRRIG--RVDLLQFHWPppIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVs 156
Cdd:cd19156 77 QGyeSTLAAFEESLEKLGldYVDLYLIHWP--VKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPMV- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 157 DQVVYNPLHRAaERLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSP 236
Cdd:cd19156 154 NQIELHPLLTQ-EPLRKFCKEKNIAVEAWSPLGQGKLLSN--------------------------PVLKAIGKKYGKSA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 237 AAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19156 207 AQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQID 251
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
17-281 |
1.10e-23 |
|
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: 97.29 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 17 QAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG--RILKSAER 90
Cdd:cd19130 12 QLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGN---EEGVGAAIAAsgipRDELFVTTKLWNDRHDgdEPAAAFAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 91 SRRRIG--RVDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQVVYNPlhRAA 168
Cdd:cd19130 89 SLAKLGldQVDLYLVHWPTPAAGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAV-NQIELHP--AYQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 169 ERLI-EMGRARGFVVIAWSPLAKGAVLkenlgNDPArrfdsvvnraktaegrrvaetIRKIAETRGVSPAAVVLAWHAAK 247
Cdd:cd19130 166 QRTIrDWAQAHDVKIEAWSPLGQGKLL-----GDPP---------------------VGAIAAAHGKTPAQIVLRWHLQK 219
|
250 260 270
....*....|....*....|....*....|....
gi 499317429 248 GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19130 220 GHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAID 253
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
11-282 |
1.10e-23 |
|
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: 97.26 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGggawrvDFAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG--RI 84
Cdd:cd19133 12 LGFGVFQIP------DPEECERAVLEAIKAGYRLIDTAAAYGN---EEAVGRAIKKsgipREELFITTKLWIQDAGyeKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 85 LKSAERSRRRIG--RVDLLQFHWPppiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDA-RLMEKALTCTKKYEIvsDQVVY 161
Cdd:cd19133 83 KKAFERSLKRLGldYLDLYLIHQP---FGDVYGAWRAMEELYKEGKIRAIGVSNFYPdRLVDLILHNEVKPAV--NQIET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 162 NPLHRAAErLIEMGRARGFVVIAWSPLAKGavlKENLGNDParrfdsvvnraktaegrrvaeTIRKIAETRGVSPAAVVL 241
Cdd:cd19133 158 HPFNQQIE-AVEFLKKYGVQIEAWGPFAEG---RNNLFENP---------------------VLTEIAEKYGKSVAQVIL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499317429 242 AWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19133 213 RWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
19-281 |
1.34e-23 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 97.46 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 19 GGGAWRVDFA-ELKRAYEYALDHGIKFIDTAEVYGsgkSEEFVAELIR----NRPHVVVATKVAGSNWG--RILKSAERS 91
Cdd:cd19157 14 GLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKesgiPREELFITSKVWNADQGydSTLKAFEAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 92 RRRIG--RVDLLQFHWP-PPIYVplcKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTctkKYEIVS--DQVVYNPLHR 166
Cdd:cd19157 91 LERLGldYLDLYLIHWPvKGKYK---ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA---DAEIVPmvNQVEFHPRLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 167 AAErLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETRGVSPAAVVLAWHAA 246
Cdd:cd19157 165 QKE-LRDYCKKQGIQLEAWSPLMQGQLLDN--------------------------PVLKEIAEKYNKSVAQVILRWDLQ 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 499317429 247 KGSFPIPgvKTLKqaQEVLEANA----LQLSEAEVRAID 281
Cdd:cd19157 218 NGVVTIP--KSIK--EHRIIENAdvfdFELSQEDMDKID 252
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
7-287 |
1.81e-23 |
|
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: 98.28 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGA--WQAGGGAWRVDfAELKRAYEYALDHGIKFIDTAEVYGSgkSEEFV----AELIRNRPHVVVATKV---- 76
Cdd:cd19144 12 SVPALGFGAmgLSAFYGPPKPD-EERFAVLDAAFELGCTFWDTADIYGD--SEELIgrwfKQNPGKREKIFLATKFgiek 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 ---AGSNWGR-----ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKAl 146
Cdd:cd19144 89 nveTGEYSVDgspeyVKKACETSLKRLGvdYIDLYYQHRVDG-KTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 147 tcTKKYEIVSDQVVYNPLHRAAER----LIEMGRARGFVVIAWSPLAKGAVL-----KENLGNDPARRFDSVVNRAKTAE 217
Cdd:cd19144 167 --HAVHPIAAVQIEYSPFSLDIERpeigVLDTCRELGVAIVAYSPLGRGFLTgairsPDDFEEGDFRRMAPRFQAENFPK 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 218 GRRVAETIRKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASAPF 287
Cdd:cd19144 245 NLELVDKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEA 316
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-281 |
2.66e-23 |
|
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: 96.71 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNW 81
Cdd:cd19127 7 VEMPALGLGVFQTPP-------EETADAVATALADGYRLIDTAAAYGN---EREVGEGIRRsgvdRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 G--RILKSAERSRRRIG--RVDLLQFHWP-PPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVs 156
Cdd:cd19127 77 GydKALRGFDASLRRLGldYVDLYLLHWPvPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVPAV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 157 DQVVYNPLHrAAERLIEMGRARGFVVIAWSPLakGAVLKENLGNDPARRfdSVVnraktaegrrVAETIRKIAETRGVSP 236
Cdd:cd19127 156 NQVELHPYF-SQKDLRAFHRRLGIVTQAWSPI--GGVMRYGASGPTGPG--DVL----------QDPTITGLAEKYGKTP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499317429 237 AAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19127 221 AQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAID 265
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-282 |
6.43e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 96.57 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH-VVVATKV------AG 78
Cdd:cd19104 10 LKVSELTFGGGGIGGLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAgPYITTKVrldpddLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWGRILKSAERSRRRIGR--VDLLQFH------------WPPPIYVPLCK--VIRDLEKAAQLGLTAEIGVSNFD-ARL 141
Cdd:cd19104 90 DIGGQIERSVEKSLKRLKRdsVDLLQLHnrigderdkpvgGTLSTTDVLGLggVADAFERLRSEGKIRFIGITGLGnPPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKALTcTKKYEIVsdQVVYNPLHRAA-------------ERLIEMGRARGFVVIAWSPLAKGAVlkenlgNDPARR--F 206
Cdd:cd19104 170 IRELLD-SGKFDAV--QVYYNLLNPSAaearprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAGAL------TTSLDRgrE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 207 DSVVNRAKTAEGRRVAETIRKIAETRGVSPAAVVLAWHAAKGSFP--IPGVKTLKQAQEVLEANAL-QLSEAEVRAIDK 282
Cdd:cd19104 241 APPTSDSDVAIDFRRAAAFRALAREWGETLAQLAHRFALSNPGVStvLVGVKNREELEEAVAAEAAgPLPAENLARLEA 319
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
5-290 |
1.54e-22 |
|
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: 95.57 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 5 SLEVGKIGLGAWQAGGgAWRVDFAELKRAYEYA-LDH----GIKFIDTAEVYGSGKSEEFVAELI---RNRPHVVVATKV 76
Cdd:cd19146 8 GVRVSPLCLGAMSFGE-AWKSMMGECDKETAFKlLDAfyeqGGNFIDTANNYQGEESERWVGEWMasrGNRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 A---------------GSNWGRILK-SAERSRR--RIGRVDLLQFHWPPpIYVPLCKVIRDLEKAAQLGLTAEIGVSNFD 138
Cdd:cd19146 87 TtgyrrggpikiksnyQGNHAKSLRlSVEASLKklQTSYIDILYVHWWD-YTTSIPELMQSLNHLVAAGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 139 ARLMEKALTCTK---KYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAVLKENlgnDPARRFDSVVN-RA 213
Cdd:cd19146 166 AWVVSKANAYARahgLTQFVVYQGHWSAAFRDFERdILPMCEAEGMALAPWGVLGQGQFRTEE---EFKRRGRSGRKgGP 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 214 KTAEGRRVAETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKAsAPFITG 290
Cdd:cd19146 243 QTEKERKVSEKLEKVAEEKGTAITSVALAYvmHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDA-YPFDVG 320
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-197 |
7.99e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 91.77 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGawqaGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYgsGKSEEFVAELIR-NRPHVVVATKVAGSNWGRI 84
Cdd:cd19100 9 LKVSRLGFG----GGPLGRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKgRRDKVFLATKTGARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 85 LKSAERSRRRIGR--VDLLQFHwpppiYVPLCK----------VIRDLEKAAQLGLTAEIGVSNFDARLMEKALtctKKY 152
Cdd:cd19100 83 KRDLERSLKRLGTdyIDLYQLH-----AVDTEEdldqvfgpggALEALLEAKEEGKIRFIGISGHSPEVLLRAL---ETG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499317429 153 EIVSDQVVYNPLHRA----AERLIEMGRARGFVVIAWSPLAKGAVLKEN 197
Cdd:cd19100 155 EFDVVLFPINPAGDHidsfREELLPLAREKGVGVIAMKVLAGGRLLSGD 203
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-281 |
1.25e-21 |
|
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: 92.18 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG 82
Cdd:cd19117 13 EIPAVGLGTWQSKPN-------EVAKAVEAALKAGYRHIDTAAIYGN---EEEVGQGIKDsgvpREEIFITTKLWCTWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 RILKSAERSRRRIG--RVDLLQFHWPPPI------YVPLC--------------KVIRDLEKAAQLGLTAEIGVSNFDAR 140
Cdd:cd19117 83 RVEEALDQSLKKLGldYVDLYLMHWPVPLdpdgndFLFKKddgtkdhepdwdfiKTWELMQKLPATGKVKAIGVSNFSIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 141 LMEKAL-TCTKKYEIVSDQVVYNPLHRAAErLIEMGRARGFVVIAWSPL--AKGAVLKENlgndparrfdsvvnraktae 217
Cdd:cd19117 163 NLEKLLaSPSAKIVPAVNQIELHPLLPQPK-LVDFCKSKGIHATAYSPLgsTNAPLLKEP-------------------- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 218 grrvaeTIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTlkqaQEVLEAN--ALQLSEAEVRAID 281
Cdd:cd19117 222 ------VIIKIAKKHGKTPAQVIISWGLQRGYSVLPKSVT----PSRIESNfkLFTLSDEEFKEID 277
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
4-281 |
1.69e-21 |
|
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: 92.30 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 4 GSLEVGKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSE-------EFVAELIRNRPHVVV---- 72
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlkllaRFFRKYPEYADKVVLsvkg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 73 ----ATKVAGSNWGRILKSAERSRRRIG---RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19077 81 gldpDTLRPDGSPEAVRKSIENILRALGgtkKIDIFEPARVDP-NVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LtctKKYEIVSDQVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKG---------AVLKENLGNDPARRFDSvVNRAK 214
Cdd:cd19077 160 H---AVHPIAAVEVEYSLFSREIEEngVLETCAELGIPIIAYSPLGRGlltgrikslADIPEGDFRRHLDRFNG-ENFEK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 215 TAEgrrVAETIRKIAETRGVSPAAVVLAWHAAKGS---FPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19077 236 NLK---LVDALQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
10-267 |
9.81e-21 |
|
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: 89.92 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGggaWRVDFAELKRAYEYALDHGIKFIDTAEVYGS----GKSEEFVAELIR---NRPHVVVATKVAGSNWG 82
Cdd:cd19082 2 RIVLGTADFG---TRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKsrgNRDKVVIATKGGHPDLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R----------ILKSAERSRRRIGR--VDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTK 150
Cdd:cd19082 79 DmsrsrlspedIRADLEESLERLGTdyIDLYFLHRDDP-SVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 151 K-----YEIVSDQ---VVYNPLHRAAERLIEMG-------RARGFVVIAWSPLAKG-----AVLKENLGNDPARRFDSVV 210
Cdd:cd19082 158 AhglpgFAASSPQwslARPNEPPWPGPTLVAMDeemrawhEENQLPVFAYSSQARGffskrAAGGAEDDSELRRVYYSEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 211 NRAKtaegrrvAETIRKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEA 267
Cdd:cd19082 238 NFER-------LERAKELAEEKGVSPTQIALAYVLNQPfpTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
6-191 |
9.83e-21 |
|
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: 89.92 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN--RPHVVVATKVA--GSNW 81
Cdd:cd19163 11 LKVSKLGFGASPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGipRDSYYLATKVGryGLDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 G--------RILKSAERSRRRIG--RVDLLQFHwpPPIYVPLCKVIRD-----LEKAAQLGLTAEIGVSNFDARLMEKAL 146
Cdd:cd19163 91 DkmfdfsaeRITKSVEESLKRLGldYIDIIQVH--DIEFAPSLDQILNetlpaLQKLKEEGKVRFIGITGYPLDVLKEVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499317429 147 TCTkKYEIvsDQVV----YNPLHRAAERLIEMGRARGFVVIAWSPLAKG 191
Cdd:cd19163 169 ERS-PVKI--DTVLsychYTLNDTSLLELLPFFKEKGVGVINASPLSMG 214
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
5-277 |
1.11e-20 |
|
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: 90.01 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 5 SLEVGKIGLGAWQAGGGAwrVDFAELKRAYEYALDHGIKFIDTAEVYGS--GKSEEFVAELIRN-----RPHVVVATKvA 77
Cdd:cd19089 8 GLHLPAISLGLWHNFGDY--TSPEEARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILKRdlrpyRDELVISTK-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 G--------SNWG---RILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEK 144
Cdd:cd19089 85 GygmwpgpyGDGGsrkYLLASLDQSLKRMGldYVDIFYHHRYDP-DTPLEETMTALADAVRSGKALYVGISNYPGAKARR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 145 AltctkkYEIVSD--------QVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKG----AVLKENLGNDPARRFDSVVN 211
Cdd:cd19089 164 A------IALLRElgvpliihQPRYSLLDRWAEDgLLEVLEEAGIGFIAFSPLAQGlltdKYLNGIPPDSRRAAESKFLT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 212 -RAKTAEGRRVAETIRKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEA-NALQLSEAEV 277
Cdd:cd19089 238 eEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPrvTSVLIGASSPSQLEDNVAAlKNLDFSEEEL 307
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-267 |
1.27e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 88.80 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGawqagGGAWRVDFAELkraYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATKV----AGS 79
Cdd:cd19105 11 LKVSRLGFG-----GGGLPRESPEL---LRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRdkVFLATKAsprlDKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 80 NWGRILKSAERSRRRIGR--VDLLQFH---WPPPIYVPLcKVIRDLEKAAQLGLTAEIGVS--NFDARLMEKALTCtKKY 152
Cdd:cd19105 83 DKAELLKSVEESLKRLQTdyIDIYQLHgvdTPEERLLNE-ELLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIES-GWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 EIVsdQVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGavlkenlgndPARRFDSVVNRAKTAEGRRVAetIRKIAE 230
Cdd:cd19105 161 DVI--MVAYNFLNQPAELeeALAAAAEKGIGVVAMKTLAGG----------YLQPALLSVLKAKGFSLPQAA--LKWVLS 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 499317429 231 TRGVspaavvlawHAAkgsfpIPGVKTLKQAQEVLEA 267
Cdd:cd19105 227 NPRV---------DTV-----VPGMRNFAELEENLAA 249
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-280 |
2.92e-20 |
|
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: 88.62 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYGSGK------SEEFVAELIRnRPHVVVATKVagsnWGR- 83
Cdd:cd19123 15 LGLGTWKSKPG-------EVGQAVKQALEAGYRHIDCAAIYGNEAeigaalAEVFKEGKVK-REDLWITSKL----WNNs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 -----ILKSAERSRR--RIGRVDLLQFHWP-----------------PPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDA 139
Cdd:cd19123 83 hapedVLPALEKTLAdlQLDYLDLYLMHWPvalkkgvgfpesgedllSLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 140 RLMEKALTcTKKYEIVSDQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGavlkenlgnDPARRFDsvvnraktAEGR 219
Cdd:cd19123 163 KKLEDLLA-TARIKPAVNQVELHPYLQQPE-LLAFCRDNGIHLTAYSPLGSG---------DRPAAMK--------AEGE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 220 RVA---ETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19123 224 PVLledPVINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATI 287
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-267 |
5.96e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 87.20 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 9 GKIGLGAWQAG---GGA---WRVDFAELKRAYEYALDHGIKFIDTAEVYGSgkSEEFVAELIRNRPHVVVATKVAGSNWG 82
Cdd:cd19097 1 SKLALGTAQFGldyGIAnksGKPSEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRLDKFKIITKLPPLKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R------ILKSAERSRRRIG--RVDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTcTKKYEI 154
Cdd:cd19097 79 KkedeaaIEASVEASLKRLKvdSLDGLLLHNPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFKIDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 155 VsdQVVYNPLHRaaeRLIEMG-----RARGFVVIAWSPLAKGAVLKENlgNDPARRFDSVvnraktaegRRVAETIRKIA 229
Cdd:cd19097 158 I--QLPFNILDQ---RFLKSGllaklKKKGIEIHARSVFLQGLLLMEP--DKLPAKFAPA---------KPLLKKLHELA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499317429 230 ETRGVSPAAVVLAWhaAKgSFP-----IPGVKTLKQAQEVLEA 267
Cdd:cd19097 222 KKLGLSPLELALGF--VL-SLPeidkiVVGVDSLEQLKEIIAA 261
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
11-282 |
6.69e-20 |
|
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: 87.30 E-value: 6.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgawrvdFAELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIR--------NRPHVVVATKVAGSNWG 82
Cdd:cd19136 4 LGLGTFRLRG------EEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpkyglSREDIFITSKLAPKDQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 --RILKSAERSRRRIGR--VDLLQFHWP--------PPIYVPLCKVI-RDLEKAAQLGLTAEIGVSNFDARLMEKALTCT 149
Cdd:cd19136 75 yeKARAACLGSLERLGTdyLDLYLIHWPgvqglkpsDPRNAELRRESwRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 KKYEIVsDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKGA-VLKENlgndparrfdsvvnraktaegrrvaETIRKI 228
Cdd:cd19136 155 EVPPAV-NQVEFHP-HLVQKELLKFCKDHGIHLQAYSSLGSGDlRLLED-------------------------PTVLAI 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 229 AETRGVSPAAVVLAWHAAKGSFPIPgvKTLKQAQ--EVLEANALQLSEAEVRAIDK 282
Cdd:cd19136 208 AKKYGRTPAQVLLRWALQQGIGVIP--KSTNPERiaENIKVFDFELSEEDMAELNA 261
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
19-281 |
1.36e-19 |
|
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: 86.45 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 19 GGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGsgkSEEFVAELIRN----RPHVVVATKVAGSNWG--RILKSAERSR 92
Cdd:cd19134 15 GLGVGELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAAsgipRGELFVTTKLATPDQGftASQAACRASL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 93 RRIG--RVDLLQFHWPPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQVVYNPLHRAAEr 170
Cdd:cd19134 92 ERLGldYVDLYLIHWPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPAV-NQIELHPLLNQAE- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 171 LIEMGRARGFVVIAWSPLAKGAVLKENlgndparrfdsvvnraktaegrrvaeTIRKIAETRGVSPAAVVLAWHAAKGSF 250
Cdd:cd19134 170 LRKVNAQHGIVTQAYSPLGVGRLLDNP--------------------------AVTAIAAAHGRTPAQVLLRWSLQLGNV 223
|
250 260 270
....*....|....*....|....*....|.
gi 499317429 251 PIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19134 224 VISRSSNPERIASNLDVFDFELTADHMDALD 254
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-281 |
1.85e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 86.49 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 7 EVGKIGLGAWQAGGGAWRV-DFAELKRAYEYALDHGIKFIDTAEVYGSgkSEEFVAELIR-------NRPHVVVATK-VA 77
Cdd:cd19101 1 TISRVINGMWQLSGGHGGIrDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKrlrrerdAADDVQIHTKwVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 GSNWGRILKSA-----ERSRRRIG--RVDLLQFHW---PPPIYVplcKVIRDLEKAAQLGLTAEIGVSNFDARLMEKAlt 147
Cdd:cd19101 79 DPGELTMTRAYveaaiDRSLKRLGvdRLDLVQFHWwdySDPGYL---DAAKHLAELQEEGKIRHLGLTNFDTERLREI-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 148 CTKKYEIVSDQVVYNPL-HRAAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDPARRFDSvVNRAKTAEGRRVAE--- 223
Cdd:cd19101 154 LDAGVPIVSNQVQYSLLdRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTGPAL-ETRSLQKYKLMIDEwgg 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 224 ---------TIRKIAETRGVSPAAVVLAW---HAAKGSfPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19101 233 wdlfqellrTLKAIADKHGVSIANVAVRWvldQPGVAG-VIVGARNSEHIDDNVRAFSFRLDDEDRAAID 301
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-281 |
5.78e-19 |
|
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: 84.86 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYGSGKS-EEFVAELIRN----RPHVVVATKV--AGSNWGR 83
Cdd:cd19111 7 IGLGTYQSPP-------EEVRAAVDYALFVGYRHIDTALSYQNEKAiGEALKWWLKNgklkREEVFITTKLppVYLEFKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRR--RIGRVDLLQFHWP------------PPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTcT 149
Cdd:cd19111 80 TEKSLEKSLEnlKLPYVDLYLIHHPcgfvnkkdkgerELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILA-Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 KKYEIVSDQVVYNPLHRAAErLIEMGRARGFVVIAWSPL-AKGAVLKENLGNDPARRFDSVVNraktaegrrvaetirKI 228
Cdd:cd19111 159 AKVKPSNLQLECHAYLQQRE-LRKFCNKKNIVVTAYAPLgSPGRANQSLWPDQPDLLEDPTVL---------------AI 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499317429 229 AETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19111 223 AKELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
6-283 |
7.08e-19 |
|
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: 85.34 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAE--LKRAYeyalDHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKV--- 76
Cdd:cd19143 11 LKVSALSFGSWVTFGNQVDVDEAKecMKAAY----DAGVNFFDNAEVYANGQSEEIMGQAIKElgwpRSDYVVSTKIfwg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 --------AGSNWGRILKSAERSRRRIG--RVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKAL 146
Cdd:cd19143 87 gggpppndRGLSRKHIVEGTKASLKRLQldYVDLVFCHRPDPA-TPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 147 TCTKKYEI---VSDQVVYNPLHRaaERlIEMGRAR-----GFVVIAWSPLAKGaVL--KENLGNDPARRFD----SVVNR 212
Cdd:cd19143 166 EIADRLGLippVMEQPQYNLFHR--ER-VEVEYAPlyekyGLGTTTWSPLASG-LLtgKYNNGIPEGSRLAlpgyEWLKD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 213 AKTAEGRRVAETIRK---IAETRGVSPAAVVLAWhAAKG---SFPIPGVKTLKQAQEVLEANAL--QLSEAEVRAIDKA 283
Cdd:cd19143 242 RKEELGQEKIEKVRKlkpIAEELGCSLAQLAIAW-CLKNpnvSTVITGATKVEQLEENLKALEVlpKLTPEVMEKIEAI 319
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-267 |
2.89e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 83.15 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgawRVDFAELKRAYEYALDHGIKFIDTAEVYGS-------GKSEEFVAELIR---NRPHVVVATKVA--- 77
Cdd:cd19752 3 LCLGTMYFGT---RTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKdrgNRDDVVIATKVGagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 -----------GSNWGRILKSAERSRRRIG--RVDLLQFHWPPPIYvPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEK 144
Cdd:cd19752 80 rdpdggpespeGLSAETIEQEIDKSLRRLGtdYIDLYYAHVDDRDT-PLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 145 ALTCTKK-----YEIVSDQVVY---NPL-----HRAA-ERLIEMGRARG-FVVIAWSPLAKGAVlkenlgNDPARRFDSv 209
Cdd:cd19752 159 ARQIARQqgwaeFSAIQQRHSYlrpRPGadfgvQRIVtDELLDYASSRPdLTLLAYSPLLSGAY------TRPDRPLPE- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 210 vnRAKTAEGRRVAETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEA 267
Cdd:cd19752 232 --QYDGPDSDARLAVLEEVAGELGATPNQVVLAWllHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
10-235 |
4.68e-18 |
|
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: 81.84 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQA-GGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATKvagSNWGRILK 86
Cdd:cd19096 2 VLGFGTMRLpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPRekFYLATK---LPPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 87 SA------ERSRRRIG--RVDLLQFHWP-----PPIYVPLcKVIRDLEKAAQLGLTAEIGVSNFD-ARLMEKALTCtkkY 152
Cdd:cd19096 79 AEdfrrilEESLKRLGvdYIDFYLLHGLnspewLEKARKG-GLLEFLEKAKKEGLIRHIGFSFHDsPELLKEILDS---Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 EIVSDQVVYNPL---HRAAERLIEMGRARGFVVIAWSPLAKGavlkeNLGNDParrfdSVVNRAKTAEGRRVAE-TIRKI 228
Cdd:cd19096 155 DFDFVQLQYNYLdqeNQAGRPGIEYAAKKGMGVIIMEPLKGG-----GLANNP-----PEALAILCGAPLSPAEwALRFL 224
|
....*..
gi 499317429 229 AETRGVS 235
Cdd:cd19096 225 LSHPEVT 231
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-286 |
7.42e-18 |
|
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: 82.07 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIRN--------RPHVVVATKVAGS--N 80
Cdd:cd19154 15 IGLGTWQSKG-------AEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAElleegvvkREDLFITTKLWTHehA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 81 WGRILKSAERS--RRRIGRVDLLQFHWP------------------PPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDAR 140
Cdd:cd19154 85 PEDVEEALRESlkKLQLEYVDLYLIHAPaafkddegesgtmengmsIHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 141 LMEKALT-CTKKyeIVSDQV---VYNPLHraaeRLIEMGRARGFVVIAWSPLAKgavlkenlgndPARRFDSVVNRAKTA 216
Cdd:cd19154 165 QIQRILDnARVK--PHNNQVechLYFPQK----ELVEFCKKHNISVTSYATLGS-----------PGRANFTKSTGVSPA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 217 EGRRVAETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASAP 286
Cdd:cd19154 228 PNLLQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKS 297
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
11-282 |
9.36e-18 |
|
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: 81.77 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAgggawRVDFAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIRN--------RPHVVVATKVAGSNWG 82
Cdd:cd19119 15 LGLGTASP-----HEDRAEVKEAVEAAIKEGYRHIDTAYAYET---EDFVGEAIKRaiddgsikREELFITTKVWPTFYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 RILKSAERSRRRIG--RVDLLQFHWPPPIYV---PLCKVI---------------------RDLEKAAQLGLTAEIGVSN 136
Cdd:cd19119 87 EVERSLDESLKALGldYVDLLLVHWPVCFEKdsdDSGKPFtpvnddgktryaasgdhittyKQLEKIYLDGRAKAIGVSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 137 FDARLMEKALtctKKYEIVS--DQVVYNPlHRAAERLIEMGRARGFVVIAWSPL-AKGAVLKENlgndparrfdsvvnra 213
Cdd:cd19119 167 YSIVYLERLI---KECKVVPavNQVELHP-HLPQMDLRDFCFKHGILVTAYSPLgSHGAPNLKN---------------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 214 ktaegrrvaETIRKIAETRGVSPAAVVLAWHAAKGSFPIPgvKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19119 227 ---------PLVKKIAEKYNVSTGDILISYHVRQGVIVLP--KSLKPVRIVSNGKIVSLTKEDLQKLDD 284
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
17-282 |
2.05e-17 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 80.50 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 17 QAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIR----NRPHVVVATKVAGSNWGRILKSAERS- 91
Cdd:PRK11565 17 QLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKeasvAREELFITTKLWNDDHKRPREALEESl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 92 -RRRIGRVDLLQFHWPPPI---YVPLCKVIRDLEKAaqlGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQVVYNPLHRA 167
Cdd:PRK11565 94 kKLQLDYVDLYLMHWPVPAidhYVEAWKGMIELQKE---GLIKSIGVCNFQIHHLQRLIDETGVTPVI-NQIELHPLMQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 168 AErLIEMGRARGFVVIAWSPLAKGAvlkENLgndparrFDsvvnraktaegrrvAETIRKIAETRGVSPAAVVLAWHAAK 247
Cdd:PRK11565 170 RQ-LHAWNATHKIQTESWSPLAQGG---KGV-------FD--------------QKVIRDLADKYGKTPAQIVIRWHLDS 224
|
250 260 270
....*....|....*....|....*....|....*
gi 499317429 248 GSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:PRK11565 225 GLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAK 259
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
6-283 |
2.74e-17 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 81.40 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWqaggGAWRVDFAELKRAYEYALDHGIKFIDTAEVYgsGKSEEFVAELIRN-RPHVVVATKVAGSNWGR- 83
Cdd:COG1453 11 LEVSVLGFGGM----RLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGpRDKVILATKLPPWVRDPe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 -ILKSAERSRRRIG--RVDLLQFH-------WPppiyvplcKVIRD------LEKAAQLGLTAEIGVSNFDAR-LMEKAL 146
Cdd:COG1453 85 dMRKDLEESLKRLQtdYIDLYLIHglnteedLE--------KVLKPggaleaLEKAKAEGKIRHIGFSTHGSLeVIKEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 147 TcTKKYEIVsdQVVYNPL---HRAAERLIEMGRARGFVVIAWSPLAKGavlkeNLGNDParrfdsvvnraktaegrrvaE 223
Cdd:COG1453 157 D-TGDFDFV--QLQYNYLdqdNQAGEEALEAAAEKGIGVIIMKPLKGG-----RLANPP--------------------E 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499317429 224 TIRKIAETrGVSPAavVLAWHAAkGSFP-----IPGVKTLKQAQEVLEA--NALQLSEAEVRAIDKA 283
Cdd:COG1453 209 KLVELLCP-PLSPA--EWALRFL-LSHPevttvLSGMSTPEQLDENLKTadNLEPLTEEELAILERL 271
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
11-281 |
3.34e-17 |
|
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: 79.68 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGAwrvdfaelKRAYEYALDH-GIKFIDTAEVYGSgksEEFVAELIRN----RPHVVVATKVAGSNWG--R 83
Cdd:cd19135 16 LGLGTSHSGGYS--------HEAVVYALKEcGYRHIDTAKRYGC---EELLGKAIKEsgvpREDLFLTTKLWPSDYGyeS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 84 ILKSAERSRRRIG--RVDLLQFHWP-PPIYVPLCKVIRD-----LEKAAQLGLTAEIGVSNFDARLMEKAL-TCTkkyeI 154
Cdd:cd19135 85 TKQAFEASLKRLGvdYLDLYLLHWPdCPSSGKNVKETRAetwraLEELYDEGLCRAIGVSNFLIEHLEQLLeDCS----V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 155 VS--DQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLKEnlgndparrfdsvvnraktaegrrvaETIRKIAETR 232
Cdd:cd19135 161 VPhvNQVEFHPFQNPVE-LIEYCRDNNIVFEGYCPLAKGKALEE--------------------------PTVTELAKKY 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499317429 233 GVSPAAVVLAWHAAKGSFPIPgvKTLKqaQEVLEANA----LQLSEAEVRAID 281
Cdd:cd19135 214 QKTPAQILIRWSIQNGVVTIP--KSTK--EERIKENCqvfdFSLSEEDMATLD 262
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-281 |
8.09e-17 |
|
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: 79.35 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVY------GSGKSEEFVAELIRNRPHVVVATKVagsnW--- 81
Cdd:cd19106 10 IGLGTWKSKPG-------QVKAAVKYALDAGYRHIDCAAVYgneqevGEALKEKVGPGKAVPREDLFVTSKL----Wntk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 -------GRILKSAerSRRRIGRVDLLQFHWPPPI------------------YVPLCKVIRDLEKAAQLGLTAEIGVSN 136
Cdd:cd19106 79 hhpedvePALRKTL--KDLQLDYLDLYLIHWPYAFergdnpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 137 FDARLMEKALTCTKKYEIVSdQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKgavlkenlgndPARRFdsvvnrAKTA 216
Cdd:cd19106 157 FNSRQIDDILSVARIKPAVL-QVECHP-YLAQNELIAHCKARGLVVTAYSPLGS-----------PDRPW------AKPD 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 217 EGRRVAE-TIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19106 218 EPVLLEEpKVKALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLD 283
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
5-280 |
1.59e-16 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 78.74 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 5 SLEVGKIGLGAWQAGGGAWRVD-FAELkrayEYALDHGIKFIDTAEVY-------GSGKSEEFVAELIR---NRPHVVVA 73
Cdd:PRK10625 10 SLEVSTLGLGTMTFGEQNSEADaHAQL----DYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAkrgSREKLIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 74 TKVAGSNWG--------------RILKSAERSRRRIGR--VDLLQFHWP-----------------PPIyVPLCKVIRDL 120
Cdd:PRK10625 86 SKVSGPSRNndkgirpnqaldrkNIREALHDSLKRLQTdyLDLYQVHWPqrptncfgklgyswtdsAPA-VSLLETLDAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 121 EKAAQLGLTAEIGVSNFDARLMEKALTCTKKYE---IVSDQVVYNPLHRAAE-RLIEMGRARGFVVIAWSPLAKGAVLKE 196
Cdd:PRK10625 165 AEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDlprIVTIQNPYSLLNRSFEvGLAEVSQYEGVELLAYSCLAFGTLTGK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 197 NL-GNDPARRFDSVVNRAKTAEGRR----VAETIrKIAETRGVSPAAVVLAWhAAKGSF---PIPGVKTLKQAQEVLEAN 268
Cdd:PRK10625 245 YLnGAKPAGARNTLFSRFTRYSGEQtqkaVAAYV-DIAKRHGLDPAQMALAF-VRRQPFvasTLLGATTMEQLKTNIESL 322
|
330
....*....|....*
gi 499317429 269 ALQLSE---AEVRAI 280
Cdd:PRK10625 323 HLTLSEevlAEIEAV 337
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
29-282 |
1.95e-16 |
|
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: 77.69 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 29 ELKRAYEYALDHGIKFIDTAEVYGS------GKSEEFVAELIRNRPHVVVATK--VAGSNWGRILKSAERSRRRIG--RV 98
Cdd:cd19124 21 DIKAAVLEAIEVGYRHFDTAAAYGTeealgeALAEALRLGLVKSRDELFVTSKlwCSDAHPDLVLPALKKSLRNLQleYV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 99 DLLQFHWP---------PPI----YVPL--CKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKYEIVsDQVVYNP 163
Cdd:cd19124 101 DLYLIHWPvslkpgkfsFPIeeedFLPFdiKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFATIPPAV-NQVEMNP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 164 LHRaAERLIEMGRARGFVVIAWSPL-AKGAVLKEN--LGNDparrfdsvvnraktaegrrvaeTIRKIAETRGVSPAAVV 240
Cdd:cd19124 180 AWQ-QKKLREFCKANGIHVTAYSPLgAPGTKWGSNavMESD----------------------VLKEIAAAKGKTVAQVS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499317429 241 LAWHAAKGSFPIpgVKTLKQAQ--EVLEANALQLSEAEVRAIDK 282
Cdd:cd19124 237 LRWVYEQGVSLV--VKSFNKERmkQNLDIFDWELTEEDLEKISE 278
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
1-280 |
2.87e-16 |
|
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: 77.86 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 1 MKIGS--LEVGKIGLG--AWQAGGGAWRVDfAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN--RPHVVVAT 74
Cdd:cd19145 3 VKLGSqgLEVSAQGLGcmGLSGDYGAPKPE-EEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDgpREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 75 KVA---GSNWGRILK--------SAERSRRRIGrVDLLQFHWPPPI--YVPLCKVIRDLEKAAQLGLTAEIGVSNFDARL 141
Cdd:cd19145 82 KFGiheIGGSGVEVRgdpayvraACEASLKRLD-VDYIDLYYQHRIdtTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKALTCtkkYEIVSDQVVYNPLHR-AAERLIEMGRARGFVVIAWSPLAKG-----AVLKENLGNDPAR----RFdsvvn 211
Cdd:cd19145 161 IRRAHAV---HPITAVQLEWSLWTRdIEEEIIPTCRELGIGIVPYSPLGRGffagkAKLEELLENSDVRkshpRF----- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 212 RAKTAEGRRVA-ETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19145 233 QGENLEKNKVLyERVEALAKKKGCTPAQLALAWvlHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
17-282 |
4.44e-15 |
|
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: 74.10 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 17 QAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGsgkSEEFV----AELIRN----RPHVVVATKVAGSNWgRILKSA 88
Cdd:cd19128 3 RLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIgiafSEIFKDggvkREDLFITSKLWPTMH-QPENVK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 89 ER-----SRRRIGRVDLLQFHWP----------PPIY--------VPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19128 79 EQllitlQDLQLEYLDLFLIHWPlafdmdtdgdPRDDnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LT-CTKKyeIVSDQVVYNPLHRaAERLIEMGRARGFVVIAWSPLAKGAvlkenlgNDPARRFDSVvnraktaegrrvaET 224
Cdd:cd19128 159 LNyCKIK--PFMNQIECHPYFQ-NDKLIKFCIENNIHVTAYRPLGGSY-------GDGNLTFLND-------------SE 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499317429 225 IRKIAETRGVSPAAVVLAWHAAK--GSFP-IPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19128 216 LKALATKYNTTPPQVIIAWHLQKwpKNYSvIPKSANKSRCQQNFDINDLALTKEDMDAINT 276
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
19-280 |
1.07e-14 |
|
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: 73.29 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 19 GGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGK------SEEFVAELIRnRPHVVVATKVAGSNWGRILKSAERSR 92
Cdd:cd19112 15 GLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKevgealAEAFKTGLVK-REDLFITTKLWNSDHGHVIEACKDSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 93 RR--IGRVDLLQFHWPPP----------------------IYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTC 148
Cdd:cd19112 94 KKlqLDYLDLYLVHFPVAtkhtgvgttgsalgedgvldidVTISLETTWHAMEKLVSAGLVRSIGISNYDIFLTRDCLAY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 149 TKKYEIVSdQVVYNPLHRaAERLIEMGRARGFVVIAWSPLAKGAVLKENLG-----NDPArrfdsvvnraktaegrrvae 223
Cdd:cd19112 174 SKIKPAVN-QIETHPYFQ-RDSLVKFCQKHGISVTAHTPLGGAAANAEWFGsvsplDDPV-------------------- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499317429 224 tIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19112 232 -LKDLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLI 287
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
11-243 |
1.13e-14 |
|
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: 73.21 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrVDFAELKRAYEY-ALDHGIKFIDTAEVYG--SGKSEEFVAELIRN-----RPHVVVATKvAG---- 78
Cdd:cd19151 15 ISLGLWHNFGD---VDRYENSRAMLRrAFDLGITHFDLANNYGppPGSAEENFGRILKEdlkpyRDELIISTK-AGytmw 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 ----SNWGR---ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCT 149
Cdd:cd19151 91 pgpyGDWGSkkyLIASLDQSLKRMGldYVDIFYHHRPDP-ETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 K--KYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKGAVLKENLGNDPArrfDSVVNRAK--------TAEG 218
Cdd:cd19151 170 KdlGTPCLIHQPKYSMFNRWVEEgLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPE---DSRAAKGSsflkpeqiTEEK 246
|
250 260
....*....|....*....|....*
gi 499317429 219 RRVAETIRKIAETRGVSPAAVVLAW 243
Cdd:cd19151 247 LAKVRRLNEIAQARGQKLAQMALAW 271
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
6-281 |
1.39e-14 |
|
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: 73.10 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAE--LKRAYEyaldHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKVAgs 79
Cdd:cd19160 13 LRVSCLGLGTWVTFGSQISDETAEdlLTVAYE----HGVNLFDTAEVYAAGKAERTLGNILKSkgwrRSSYVVTTKIY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 80 nWGRILKSaER--SRRRI-----GRVDLLQFHWPPPIYV-------PLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19160 87 -WGGQAET-ERglSRKHIieglrGSLDRLQLEYVDIVFAnrsdpnsPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LTCTKKYEI---VSDQVVYNPLHR--AAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDP------ARRFDSVVNRAK 214
Cdd:cd19160 165 YSVARQFNLippVCEQAEYHLFQRekVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPdtcraaVKGYQWLKEKVQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 215 TAEGRRVAETIRK---IAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANAL--QLSEAEVRAID 281
Cdd:cd19160 245 SEEGKKQQAKVKElhpIADRLGCTVAQLAIAWclRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTPQTVMEID 318
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
19-282 |
2.58e-14 |
|
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: 72.09 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 19 GGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSgksEEFVAELIR--------NRPHVVVATKVAGS-----NWGRIL 85
Cdd:cd19113 15 GFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGN---EKEVGEGVNraideglvKREELFLTSKLWNNfhdpkNVETAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 86 KSAeRSRRRIGRVDLLQFHWP------------PP----------IY--VPLCKVIRDLEKAAQLGLTAEIGVSNFDARL 141
Cdd:cd19113 92 NKT-LSDLKLDYVDLFLIHFPiafkfvpieekyPPgfycgdgdnfVYedVPILDTWKALEKLVDAGKIKSIGVSNFPGAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 142 MEKAL-TCTKKyeIVSDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKGAVLKENLGndparrfdsvvnRAKTAEGRR 220
Cdd:cd19113 171 ILDLLrGATIK--PAVLQIEHHP-YLQQPKLIEYAQKAGITITAYSSFGPQSFVELNQG------------RALNTPTLF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 221 VAETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19113 236 EHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAK 297
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
6-282 |
9.11e-14 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 70.79 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGgawRVDFAELKRA-YEYALDHGIKFIDTAEVYG--SGKSEEFVAELIRN-----RPHVVVATKVA 77
Cdd:PRK09912 23 LRLPALSLGLWHNFG---HVNALESQRAiLRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdfaayRDELIISTKAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 --------GSNWGR--ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:PRK09912 100 ydmwpgpyGSGGSRkyLLASLDQSLKRMGleYVDIFYSHRVDE-NTPMEETASALAHAVQSGKALYVGISSYSPERTQKM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LTCTKKYEI--VSDQVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGAVLKENLGNDP--------ARRFDSVVNRA 213
Cdd:PRK09912 179 VELLREWKIplLIHQPSYNLLNRWVDKsgLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPqdsrmhreGNKVRGLTPKM 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 214 KTAEGRRVAETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEA-NALQLSEAEVRAIDK 282
Cdd:PRK09912 259 LTEANLNSLRLLNEMAQQRGQSMAQMALSWllKDERVTSVLIGASRAEQLEENVQAlNNLTFSTEELAQIDQ 330
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-239 |
1.04e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 70.42 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQagGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIR--------NRPHVVVATKV- 76
Cdd:cd19099 1 LTLSSLGLGTYR--GDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekggiKRDEVVIVTKAg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 --------------------AGSNWGR--------------ILKSAERSRRRIG--RVDLLQFHWPP---------PIYV 111
Cdd:cd19099 79 yipgdgdeplrplkyleeklGRGLIDVadsaglrhcispayLEDQIERSLKRLGldTIDLYLLHNPEeqllelgeeEFYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 112 PLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA----LTCTKKYEIVSD-----------QVVYNPLHRAA-------- 168
Cdd:cd19099 159 RLEEAFEALEEAVAEGKIRYYGISTWDGFRAPPAlpghLSLEKLVAAAEEvggdnhhfkviQLPLNLLEPEAltekntvk 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 169 ---ERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDPA--RRFDSVVNRAktaegrrvaetIRKIAETRGVSPAAV 239
Cdd:cd19099 239 geaLSLLEAAKELGLGVIASRPLNQGQLLGELRLADLLalPGGATLAQRA-----------LQFARSTPGVDSALV 303
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
6-243 |
1.17e-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: 70.46 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAElkRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKVAgsnW 81
Cdd:cd19159 11 LRVSCLGLGTWVTFGGQISDEVAE--RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwrRSSLVITTKLY---W 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 GRILKSaER--SRRRI-----GRVDLLQFHW-------PPPIYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALT 147
Cdd:cd19159 86 GGKAET-ERglSRKHIieglkGSLQRLQLEYvdvvfanRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 148 CTKKYEI---VSDQVVYNPLHR--AAERLIEMGRARGFVVIAWSPLAKGAVLK--ENLGNDPARR----FDSVVNRAKTA 216
Cdd:cd19159 165 VARQFNMippVCEQAEYHLFQRekVEVQLPELYHKIGVGAMTWSPLACGIISGkyGNGVPESSRAslkcYQWLKERIVSE 244
|
250 260 270
....*....|....*....|....*....|
gi 499317429 217 EGRRVAETIRK---IAETRGVSPAAVVLAW 243
Cdd:cd19159 245 EGRKQQNKLKDlspIAERLGCTLPQLAVAW 274
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
11-249 |
1.69e-13 |
|
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: 69.70 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRP--HVVVATKV--------AGSN 80
Cdd:cd19162 3 LGLGAASLGN-LARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPraEYVVSTKVgrllepgaAGRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 81 WGR----------ILKSAERSRRRIG--RVDLLQFHWPPP-IYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALT 147
Cdd:cd19162 82 AGAdrrfdfsadgIRRSIEASLERLGldRLDLVFLHDPDRhLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLRAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 148 ctkkyEIVSDQVV----YNPL-HRAAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDparRFDSvvnRAKTAEGRRVA 222
Cdd:cd19162 162 -----RADVDVVMvagrYTLLdRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGD---RYDY---RPATPEVLARA 230
|
250 260 270
....*....|....*....|....*....|
gi 499317429 223 ETIRKIAETRGVSPAAVVLAW---HAAKGS 249
Cdd:cd19162 231 RRLAAVCRRYGVPLPAAALQFplrHPAVAS 260
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
6-277 |
1.89e-13 |
|
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: 69.41 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGawrVDFAELKRAY-EYALDHGIKFIDTAEVYG--SGKSEEFVAELIRN-----RPHVVVATKvA 77
Cdd:cd19150 10 LKLPALSLGLWHNFGD---DTPLETQRAIlRTAFDLGITHFDLANNYGppPGSAEENFGRILREdfagyRDELIISTK-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 78 GSN--------WGR---ILKSAERSRRRIG--RVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEK 144
Cdd:cd19150 86 GYDmwpgpygeWGSrkyLLASLDQSLKRMGldYVDIFYSHRFDP-DTPLEETMGALDHAVRSGKALYVGISSYSPERTRE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 145 ALTCTKKYEI--VSDQVVYNPLHRAAER--LIEMGRARGFVVIAWSPLAKGAVLKENLGNDPArrfDSVVNRAK------ 214
Cdd:cd19150 165 AAAILRELGTplLIHQPSYNMLNRWVEEsgLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPE---GSRASKERslspkm 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499317429 215 -TAEGRRVAETIRKIAETRGVSPAAVVLAWHAAKG--SFPIPGVKTLKQAQEVLEA-NALQLSEAEV 277
Cdd:cd19150 242 lTEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGAlDNLTFSADEL 308
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
11-282 |
2.26e-13 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 68.98 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVY------GSGKSEEFVAELIRNRPHVVVATKVagsnWG-- 82
Cdd:cd19118 10 IGLGTWQAEPG-------EVGAAVKIALKAGYRHLDLAKVYqnqhevGQALKELLKEEPGVKREDLFITSKL----WNns 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 ----RILKSAERSRRRIG--RVDLLQFHWP----------PPIYVPLCKVIRDLEKAAQL-------------GLTAEIG 133
Cdd:cd19118 79 hrpeYVEPALDDTLKELGldYLDLYLIHWPvafkptgdlnPLTAVPTNGGEVDLDLSVSLvdtwkamvelkktGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 134 VSNFDARlMEKALTCTKKYEIVSDQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLKENLGNDParrfdsvvnra 213
Cdd:cd19118 159 VSNFSID-HLQAIIEETGVVPAVNQIEAHPLLLQDE-LVDYCKSKNIHITAYSPLGNNLAGLPLLVQHP----------- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499317429 214 ktaegrrvaeTIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEanALQLSEAEVRAIDK 282
Cdd:cd19118 226 ----------EVKAIAAKLGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTA 282
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
9-263 |
4.04e-13 |
|
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: 68.40 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 9 GKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRPH--VVVATKV---------- 76
Cdd:cd19152 1 PKLGFGTAPLGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGRedYVISTKVgrllvplqev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 ----AGSNWGR-------------ILKSAERSRRRIG--RVDLLQFHWP-PPIYVPLCKVIRD---------LEKAAQLG 127
Cdd:cd19152 81 eptfEPGFWNPlpfdavfdysydgILRSIEDSLQRLGlsRIDLLSIHDPdEDLAGAESDEHFAqaikgafraLEELREEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 128 LTAEIGVSNFDARLMEKALtctkkYEIVSDQVV----YNPL-HRAAERLIEMGRARGFVVIAWSPLAKGAvlkenLGNDP 202
Cdd:cd19152 161 VIKAIGLGVNDWEVILRIL-----EEADLDWVMlagrYTLLdHSAARELLPECEKRGVKVVNAGPFNSGF-----LAGGD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 203 arRFDSVVNRAKTAEGRRVAETIRKIAETRGVSPAAVVLAW---HAAKGSFpIPGVKTLKQAQE 263
Cdd:cd19152 231 --NFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFalaPPAVASV-APGASSPERVEE 291
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
6-243 |
1.11e-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: 67.42 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAElkRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKV----- 76
Cdd:cd19158 11 LRVSCLGLGTWVTFGGQITDEMAE--HLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwrRSSLVITTKIfwggk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 ----AGSNWGRILKSAERS--RRRIGRVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTK 150
Cdd:cd19158 89 aeteRGLSRKHIIEGLKASleRLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 151 KYEI---VSDQVVYNPLHR--AAERLIEMGRARGFVVIAWSPLAKGAVL-KENLGNDPARR-----FDSVVNRAKTAEGR 219
Cdd:cd19158 168 QFNLippICEQAEYHMFQRekVEVQLPELFHKIGVGAMTWSPLACGIVSgKYDSGIPPYSRaslkgYQWLKDKILSEEGR 247
|
250 260
....*....|....*....|....*..
gi 499317429 220 RVAETIRK---IAETRGVSPAAVVLAW 243
Cdd:cd19158 248 RQQAKLKElqaIAERLGCTLPQLAIAW 274
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
20-281 |
2.53e-12 |
|
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: 66.39 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 20 GGAWRVDFAELKRAYEYAL-----DHGIKFIDTAEVYGSGKSEEFVAELI---RNRPHVVVATKVAGSN----------- 80
Cdd:cd19147 21 GDAWSGFMGSMDKEQAFELldafyEAGGNFIDTANNYQDEQSETWIGEWMksrKNRDQIVIATKFTTDYkayevgkgkav 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 81 --WGRILKSAERSRR------RIGRVDLLQFH-WPPPIYVPlcKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTK- 150
Cdd:cd19147 101 nyCGNHKRSLHVSVRdslrklQTDWIDILYVHwWDYTTSIE--EVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 151 --KYEIVSDQVVYNPLHRAAER-LIEMGRARGFVVIAWSPLAKG-----AVLKENLGNDPARRfDSVVNRAKTAEGRRVA 222
Cdd:cd19147 179 hgKTPFSVYQGRWNVLNRDFERdIIPMARHFGMALAPWDVLGGGkfqskKAVEERKKNGEGLR-SFVGGTEQTPEEVKIS 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499317429 223 ETIRKIAETRGV-SPAAVVLAWHAAKGS--FPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19147 258 EALEKVAEEHGTeSVTAIALAYVRSKAPnvFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
6-243 |
2.06e-11 |
|
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: 63.62 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAE--LKRAYEyaldHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKVAgs 79
Cdd:cd19141 10 LRVSCLGLGTWVTFGSQISDEVAEelVTLAYE----NGINLFDTAEVYAAGKAEIVLGKILKKkgwrRSSYVITTKIF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 80 nWG------------RILKSAERS--RRRIGRVDLLQFHWPPPiYVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19141 84 -WGgkaeterglsrkHIIEGLKASleRLQLEYVDIVFANRPDP-NTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LTCTKKYEI---VSDQVVYNPLHR--AAERLIEMGRARGFVVIAWSPLAKGAVLKENLGNDPA------RRFDSVVNRAK 214
Cdd:cd19141 162 YSVARQFNLippIVEQAEYHLFQRekVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEysraslKGYQWLKEKIL 241
|
250 260 270
....*....|....*....|....*....|..
gi 499317429 215 TAEGRRVAETIRK---IAETRGVSPAAVVLAW 243
Cdd:cd19141 242 SEEGRRQQAKLKElqiIADRLGCTLPQLAIAW 273
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
19-287 |
3.61e-11 |
|
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: 62.96 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 19 GGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGS----GKS-EEFVAELIRNRPHVVVATKVAGSNWGR--ILKSAERS 91
Cdd:cd19114 8 GFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNeaevGRGiRKAIQEGLVKREDLFIVTKLWNNFHGKdhVREAFDRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 92 RRRIG--RVDLLQFHWPPPI-YV-----------------------PLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKA 145
Cdd:cd19114 88 LKDYGldYIDLYLIHFPIPAaYVdpaenypflwkdkelkkfpleqsPMQECWREMEKLVDAGLVRNIGIANFNVQLILDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 146 LTCTKKYEIVSdQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKGAvlkenlgndparrFDSVVNRAKTAEGRRVAETI 225
Cdd:cd19114 168 LTYAKIKPAVL-QIEHHP-YLQQKRLIDWAKKQGIQITAYSSFGNAV-------------YTKVTKHLKHFTNLLEHPVV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 226 RKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID--KASAPF 287
Cdd:cd19114 233 KKLADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYelEANARF 296
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
11-280 |
4.24e-11 |
|
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: 62.67 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVY------GSGKSEEFVAELIRnRPHVVVATKVagsnW--- 81
Cdd:cd19110 7 VGLGTWKASPG-------EVTEAVKVAIDAGYRHFDCAYLYhnesevGAGIREKIKEGVVR-REDLFIVSKL----Wctc 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 --GRILKSA-ERSRR--RIGRVDLLQFHWP-----PPIYVPL---CKVI----------RDLEKAAQLGLTAEIGVSNFD 138
Cdd:cd19110 75 hkKSLVKTAcTRSLKalKLNYLDLYLIHWPmgfkpGEPDLPLdrsGMVIpsdtdfldtwEAMEDLVIEGLVKNIGVSNFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 139 ARLMEKALTCTK-KYEIVSDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAkGAVLKENLGNDParrfdsvvnraktae 217
Cdd:cd19110 155 HEQLERLLNKPGlRVKPVTNQIECHP-YLTQKKLISFCQSRNVSVTAYRPLG-GSCEGVDLIDDP--------------- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 218 grrvaeTIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19110 218 ------VIQRIAKKHGKSPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-253 |
1.23e-10 |
|
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: 61.21 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYGSGKS-----EEFVAELIRNRPHVVVATKVagsnW---- 81
Cdd:cd19125 14 VGLGTWQADPG-------VVGNAVKTAIKEGYRHIDCAAIYGNEKEigkalKKLFEDGVVKREDLFITSKL----Wctdh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 82 --GRILKSAERSRRR--IGRVDLLQFHWP-----------PPIYVP--LCKVIRDLEKAAQLGLTAEIGVSNFDARLMEK 144
Cdd:cd19125 83 apEDVPPALEKTLKDlqLDYLDLYLIHWPvrlkkgahmpePEEVLPpdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 145 ALTCTKKYEIVsDQVVYNPLHRaAERLIEMGRARGFVVIAWSPLAKG--AVLKENLGNDParrfdsvvnraktaegrrva 222
Cdd:cd19125 163 LLAVARVPPAV-NQVECHPGWQ-QDKLHEFCKSKGIHLSAYSPLGSPgtTWVKKNVLKDP-------------------- 220
|
250 260 270
....*....|....*....|....*....|.
gi 499317429 223 eTIRKIAETRGVSPAAVVLAWHAAKGSFPIP 253
Cdd:cd19125 221 -IVTKVAEKLGKTPAQVALRWGLQRGTSVLP 250
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
6-243 |
1.24e-10 |
|
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: 61.33 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAE--LKRAYEyaldHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKV--- 76
Cdd:cd19142 11 LRVSNVGLGTWSTFSTAISEEQAEeiVTLAYE----NGINYFDTSDAFTSGQAETELGRILKKkgwkRSSYIVSTKIyws 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 77 -----AGSNWGRILKSAERSRRRI--GRVDLLQFHWPPPIyVPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCT 149
Cdd:cd19142 87 ygseeRGLSRKHIIESVRASLRRLqlDYIDIVIIHKADPM-CPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 150 KKYEIVS---DQVVYNPLHRAAERL--IEMGRARGFVVIAWSPLAkgavlkenLGNDPARRFDS---VVNRAKTA----- 216
Cdd:cd19142 166 RQFNCPTpicEQSEYHMFCREKMELymPELYNKVGVGLITWSPLS--------LGLDPGISEETrrlVTKLSFKSskykv 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 499317429 217 ---------EGRRVAETIR---KIAETRGVSPAAVVLAW 243
Cdd:cd19142 238 gsdgngiheETRRASHKLRelsLIAERLGCDLTQLLIAW 276
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
10-103 |
1.43e-10 |
|
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: 61.19 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 10 KIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRNRP--HVVVATKVagsnwGRILKS 87
Cdd:cd19161 2 ELGLGTAGLGNLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPrdEFVLSTKV-----GRLLKP 76
|
90
....*....|....*...
gi 499317429 88 AERSRRR--IGRVDLLQF 103
Cdd:cd19161 77 AREGSVPdpNGFVDPLPF 94
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
17-282 |
1.46e-10 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 60.90 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 17 QAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGK-SEEFVAELIR--------------------NRPHVVVATK 75
Cdd:cd19115 15 LVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVeAGQGVARAIKegivkredlfivsklwntfhDGERVEPICR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 76 VAGSNWGrilksaersrrrIGRVDLLQFHWP------------PPIY-----------VPLCKVIRDLEKAAQLGLTAEI 132
Cdd:cd19115 95 KQLADWG------------IDYFDLFLIHFPialkyvdpavryPPGWfydgkkvefsnAPIQETWTAMEKLVDKGLARSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 133 GVSNFDARLMEKALTcTKKYEIVSDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKGAVLKENlgndparrfdsvVNR 212
Cdd:cd19115 163 GVSNFSAQLLMDLLR-YARIRPATLQIEHHP-YLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELD------------LPG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 213 AKTAEGRRVAETIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDK 282
Cdd:cd19115 229 AKDTPPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISA 298
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
11-281 |
2.36e-10 |
|
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: 60.62 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGgawrvdfAELKRAYEYALDHGIKFIDTAEVYG--------------SG--KSEEF--VAEL--IRNRPHV 70
Cdd:cd19155 15 VGLGTWQSSP-------EEIETAVDTALEAGYRHIDTAYVYRneaaignvlkkwidSGkvKREELfiVTKLppGGNRREK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 71 VVATkvagsnwgrILKSAERsrRRIGRVDLLQFHWPPPIYVP--------------------LCKVIRDLEKAAQLGLTA 130
Cdd:cd19155 88 VEKF---------LLKSLEK--LQLDYVDLYLIHFPVGSLSKeddsgkldptgehkqdyttdLLDIWKAMEAQVDQGLTR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 131 EIGVSNFDARLMEKALTcTKKYEIVSDQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGAVLKEN--LGNDPARRFDS 208
Cdd:cd19155 157 SIGLSNFNREQMARILK-NARIKPANLQVELHVYLQQKD-LVDFCSTHSITVTAYAPLGSPGAAHFSpgTGSPSGSSPDL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499317429 209 VVNRAktaegrrvaetIRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAID 281
Cdd:cd19155 235 LQDPV-----------VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLS 296
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
26-270 |
1.26e-09 |
|
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: 58.24 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 26 DFAELKRAYEYALDHGIKFIDTAEVY------GSGKSEEFVAELIRnRPHVVVATKVAGSNW--GRILKSAERSRRRIG- 96
Cdd:cd19129 17 DPSATRNAVKAALEAGFRHFDCAERYrneaevGEAMQEVFKAGKIR-REDLFVTTKLWNTNHrpERVKPAFEASLKRLQl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 97 -RVDLLQFHWP---PP-------------IY---VPLCKVIRDLEKAAQLGLTAEIGVSNFD-ARLMEKALTCTKKYEIV 155
Cdd:cd19129 96 dYLDLYLIHTPfafQPgdeqdprdangnvIYddgVTLLDTWRAMERLVDEGRCKAIGLSDVSlEKLREIFEAARIKPAVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 156 sdQVVYNPLHRAAErLIEMGRARGFVVIAWSPLAKGavLKENLGNDParrfdsVVnrakTAEGRRVAETirkiaetrgvs 235
Cdd:cd19129 176 --QVESHPYLPEWE-LLDFCKNHGIVLQAFAPLGHG--MEPKLLEDP------VI----TAIARRVNKT----------- 229
|
250 260 270
....*....|....*....|....*....|....*
gi 499317429 236 PAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANAL 270
Cdd:cd19129 230 PAQVLLAWAIQRGTALLTTSKTPSRIRENFDISTL 264
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
3-286 |
1.79e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 57.67 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 3 IGSLEVGKIGLGAWQ-AGGGAW------RVDFAELKRAYEYALDHgikfIDTAEVYGSGKSEEfvaeLIRNRPH-----V 70
Cdd:PRK10376 12 LGGRSVNRLGYGAMQlAGPGVFgppkdrDAAIAVLREAVALGVNH----IDTSDFYGPHVTNQ----LIREALHpypddL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 71 VVATKVAGS-----NWGRILKSAERSR------RRIGrVDLLQ---------FHWPPP--IYVPLcKVIRDLEkaaQLGL 128
Cdd:PRK10376 84 TIVTKVGARrgedgSWLPAFSPAELRRavhdnlRNLG-LDVLDvvnlrlmgdGHGPAEgsIEEPL-TVLAELQ---RQGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 129 TAEIGVSNFDARLMEKALTCTkkyEIVSDQVVYNPLHRAAERLIEMGRARGFVVIAWSPLAkgavlkenlGNDPARrfds 208
Cdd:PRK10376 159 VRHIGLSNVTPTQVAEARKIA---EIVCVQNHYNLAHRADDALIDALARDGIAYVPFFPLG---------GFTPLQ---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 209 vvnraktaegrrvAETIRKIAETRGVSPAAVVLAW--HAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAIDKASAP 286
Cdd:PRK10376 223 -------------SSTLSDVAASLGATPMQVALAWllQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-280 |
5.70e-09 |
|
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: 56.27 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 11 IGLGAWQAGGGawrvdfaELKRAYEYALDHGIKFIDTAEVYgsgKSEEFVAELIRN--------RPHVVVATKVAGSNWG 82
Cdd:cd19107 7 LGLGTWKSPPG-------QVTEAVKVAIDAGYRHIDCAYVY---QNENEVGEAIQEkikeqvvkREDLFIVSKLWCTFHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 83 R-ILKSAER---SRRRIGRVDLLQFHWPP-----PIYVPL---CKVIRD----------LEKAAQLGLTAEIGVSNFDAR 140
Cdd:cd19107 77 KgLVKGACQktlSDLKLDYLDLYLIHWPTgfkpgKELFPLdesGNVIPSdttfldtweaMEELVDEGLVKAIGVSNFNHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 141 LMEKALTctK---KYEIVSDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAKgavlkenlgndPARRFdsvvnrAKTAE 217
Cdd:cd19107 157 QIERILN--KpglKYKPAVNQIECHP-YLTQEKLIQYCQSKGIVVTAYSPLGS-----------PDRPW------AKPED 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499317429 218 GRRVAET-IRKIAETRGVSPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANALQLSEAEVRAI 280
Cdd:cd19107 217 PSLLEDPkIKEIAAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
113-281 |
9.22e-08 |
|
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: 52.49 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 113 LCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALTCTK-KYEIVSDQVVYNPlHRAAERLIEMGRARGFVVIAWSPLAK- 190
Cdd:cd19109 133 LCATWEALEACKDAGLVKSIGVSNFNRRQLELILNKPGlKHKPVSNQVECHP-YFTQPKLLEFCQQHDIVIVAYSPLGTc 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 191 GAVLKENLGNDPARRfDSVVNraktAEGRRVAETirkiaetrgvsPAAVVLAWHAAKGSFPIPGVKTLKQAQEVLEANAL 270
Cdd:cd19109 212 RDPIWVNVSSPPLLE-DPLLN----SIGKKYNKT-----------AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDF 275
|
170
....*....|.
gi 499317429 271 QLSEAEVRAID 281
Cdd:cd19109 276 SLTEEEMKDIE 286
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
37-188 |
1.63e-07 |
|
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: 51.85 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 37 ALDHGIKFIDTAEVYGSgksEEFVAELIRN--------RPHVVVATKVagsnWG------RILKSAERSRRRIG--RVDL 100
Cdd:cd19108 36 AIDAGFRHIDSAYLYQN---EEEVGQAIRSkiadgtvkREDIFYTSKL----WCtfhrpeLVRPALEKSLKKLQldYVDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 101 LQFHWP----------------PPIY--VPLCKVIRDLEKAAQLGLTAEIGVSNFDARLMEKALtcTK---KYEIVSDQV 159
Cdd:cd19108 109 YLIHFPvalkpgeelfpkdengKLIFdtVDLCATWEAMEKCKDAGLAKSIGVSNFNRRQLEMIL--NKpglKYKPVCNQV 186
|
170 180 190
....*....|....*....|....*....|
gi 499317429 160 VYNP-LHRAaeRLIEMGRARGFVVIAWSPL 188
Cdd:cd19108 187 ECHPyLNQS--KLLDFCKSKDIVLVAYSAL 214
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
29-284 |
2.49e-07 |
|
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: 51.08 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 29 ELKRAYEYALDHGIKFIDTAEVY-GSGKSEEFVAELIRNRPHV-----VVATKVagsnWGR------ILKSAERSRRRIG 96
Cdd:cd19122 25 ETYAAVTKALDVGYRHLDCAWFYlNEDEVGDAVRDFLKENPSVkredlFICTKV----WNHlhepedVKWSIDNSLKNLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 97 --RVDLLQFHWP----------PPI-----YVPLCKVI-------RDLEKAAQLGLTAEIGVSNFDARLMEKALTCTKKY 152
Cdd:cd19122 101 ldYIDLFLVHWPiaaekndqrsPKLgpdgkYVILKDLTenpeptwRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAKVK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 153 EIVsDQVVYNPLhRAAERLIEMGRARGFVVIAWSPLAKGavlkenlgndparrfdsvvNRAKTAeGRRVAE--TIRKIAE 230
Cdd:cd19122 181 PHV-NQIEIHPF-LPNEELVDYCFSNDILPEAYSPLGSQ-------------------NQVPST-GERVSEnpTLNEVAE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499317429 231 TRGVSPAAVVLAWHAAKGSFPIPGVKTLKQaqevLEAN--ALQLSEAEVRAIDKAS 284
Cdd:cd19122 239 KGGYSLAQVLIAWGLRRGYVVLPKSSTPSR----IESNfkSIELSDEDFEAINQVA 290
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-280 |
5.51e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 50.42 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 37 ALDHGIKFIDTAEVYGsgKSEEFVAELIRNRPHVVVATKVaGSNWG----------------------RILKSAERSRRR 94
Cdd:cd19098 44 AWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIAPDAVFV-GSKWGytytadwqvdaavhevkdhslaRLLKQWEETRSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 95 IGR-VDLLQFHWPPPIYVPL--CKVIRDLEKAAQLGLTAEIGVSNFD-ARLMEKALTCTKKYEIVSD--QVVYNPLHRAA 168
Cdd:cd19098 121 LGKhLDLYQIHSATLESGVLedADVLAALAELKAEGVKIGLSLSGPQqAETLRRALEIEIDGARLFDsvQATWNLLEQSA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 169 ERLIEMGRARGFVVIAWSPLAKGAVLKENlgndparrfDSVVNRAKTAEgrrvaetIRKIAETRGVSPAAVVLAWHAAKG 248
Cdd:cd19098 201 GEALEEAHEAGMGVIVKEALANGRLTDRN---------PSPELAPLMAV-------LKAVADRLGVTPDALALAAVLAQP 264
|
250 260 270
....*....|....*....|....*....|....
gi 499317429 249 SFPI--PGVKTLKQAQEVLEANALQLSeAEVRAI 280
Cdd:cd19098 265 FVDVvlSGAATPEQLRSNLRALDVSLD-LELLAA 297
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
6-191 |
8.07e-05 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 43.68 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGG---GAWRVDFAElkRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATKVAG 78
Cdd:cd19153 10 GNVSPVGLGTAALGGvygDGLEQDEAV--AIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAAlqvpRSSYTVATKVGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 79 SNWGRILKSAERSRRRIGR---------VDLLQFH------WPPPIYvplcKVIRDLEKAAQLGLTAEIGVSNFDARLME 143
Cdd:cd19153 88 YRDSEFDYSAERVRASVATslerlhttyLDVVYLHdiefvdYDTLVD----EALPALRTLKDEGVIKRIGIAGYPLDTLT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499317429 144 KAltcTKKYEIVSDQVVYNPLH------RAAERLIEMGRARGFVVIAWSPLAKG 191
Cdd:cd19153 164 RA---TRRCSPGSLDAVLSYCHltlqdaRLESDAPGLVRGAGPHVINASPLSMG 214
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
6-104 |
3.29e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 38.61 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499317429 6 LEVGKIGLGAWQAGGGAWRVDFAELKRAYEYALDHGIKFIDTAEVYGSGKSEEFVAELIRN----RPHVVVATK----VA 77
Cdd:PLN02587 9 LKVSSVGFGASPLGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKAlgipREKYVVSTKcgryGE 88
|
90 100 110
....*....|....*....|....*....|.
gi 499317429 78 GSNW--GRILKSAERSRRRIG--RVDLLQFH 104
Cdd:PLN02587 89 GFDFsaERVTKSVDESLARLQldYVDILHCH 119
|
|
| |
