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Conserved domains on  [gi|18202476|sp|P97382|]
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RecName: Full=Voltage-gated potassium channel subunit beta-3; AltName: Full=K(+) channel subunit beta-3; AltName: Full=Kv-beta-3

Protein Classification

aldo-keto reductase family protein( domain architecture ID 305)

aldo-keto reductase family protein may be an NAD(P)(H) oxidoreductase that reduces aldehydes and ketones to primary and secondary alcohols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AKR_SF super family cl00470
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
 25-245 2.74e-171

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.


The actual alignment was detected with superfamily member cd19160:

Pssm-ID: 444925 [Multi-domain]  Cd Length: 325  Bit Score: 474.86  E-value: 2.74e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19160 105 GLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYH 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19160 185 LFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADR 264

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNKS 245
Cdd:cd19160 265 LGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
 
Name Accession Description Interval E-value
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
 25-245 2.74e-171

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: 474.86  E-value: 2.74e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19160 105 GLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYH 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19160 185 LFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADR 264

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNKS 245
Cdd:cd19160 265 LGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
Kv_beta TIGR01293
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ...
 25-241 6.54e-149

voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.


Pssm-ID: 213602 [Multi-domain]  Cd Length: 317  Bit Score: 417.80  E-value: 6.54e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:TIGR01293 101 GLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYH 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:TIGR01293 181 MFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAER 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476   185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALL 241
Cdd:TIGR01293 261 LGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
 12-241 4.95e-46

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: 155.72  E-value: 4.95e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  12 KVVFTFLSLPHPPG---------LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIM 82
Cdd:COG0667  82 KVGRRMGPGPNGRGlsrehirraVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLR 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  83 EAysMARQFNLIPPVCEQAENHFFQREkVEMQLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTCKATvkgyQWLK 160
Cdd:COG0667 162 RA--LAIAEGLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYrrGATFPEGDRAA----TNFV 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 161 EKVQSEEGKKQQARVMDLlptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:COG0667 235 QGYLTERNLALVDALRAI---AAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAA 309


                .
gi 18202476 241 L 241
Cdd:COG0667 310 L 310
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
 29-241 4.45e-35

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: 126.66  E-value: 4.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPVCEQAENHFFQR 108
Cdd:pfam00248  93 SLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLLRR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   109 EKVEMqLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTckatvkgyqwLKEKVQSEEGKKQQARVMDLLPTARQLG 186
Cdd:pfam00248 169 RQEEE-LLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPG----------ERRRLLKKGTPLNLEALEALEEIAKEHG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476   187 CTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDALL 241
Cdd:pfam00248 238 VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF--PLSDEEVARIDELL 290
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
 7-238 3.23e-34

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 125.87  E-value: 3.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    7 LIFSLKVVFTFLSLPHPPG---------LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWS 77
Cdd:PRK09912  92 LIISTKAGYDMWPGPYGSGgsrkyllasLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   78 AAEIMEAYSMARQFNlIPPVCEQAENHFFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKG-- 155
Cdd:PRK09912 172 PERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnk 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  156 YQWLKEKVQSeEGKKQQARVMDLLptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSqLTPQTVV 235
Cdd:PRK09912 251 VRGLTPKMLT-EANLNSLRLLNEM--AQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLT-FSTEELA 326


                 ...
gi 18202476  236 EID 238
Cdd:PRK09912 327 QID 329
 
Name Accession Description Interval E-value
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
 25-245 2.74e-171

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: 474.86  E-value: 2.74e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19160 105 GLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYH 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19160 185 LFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADR 264

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNKS 245
Cdd:cd19160 265 LGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
Kv_beta TIGR01293
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ...
 25-241 6.54e-149

voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.


Pssm-ID: 213602 [Multi-domain]  Cd Length: 317  Bit Score: 417.80  E-value: 6.54e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:TIGR01293 101 GLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYH 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:TIGR01293 181 MFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAER 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476   185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALL 241
Cdd:TIGR01293 261 LGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
 25-233 2.05e-146

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: 411.46  E-value: 2.05e-146
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19141 102 GLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYH 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19141 182 LFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADR 261

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQT 233
Cdd:cd19141 262 LGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
AKR_KCAB1B_AKR6A3-like cd19159
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ...
 25-244 4.11e-135

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: 383.24  E-value: 4.11e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19159 103 GLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYH 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19159 183 LFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAER 262

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNK 244
Cdd:cd19159 263 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNK 322
AKR_KCAB2B_AKR6A1-like cd19158
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ...
 25-246 2.89e-119

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: 343.22  E-value: 2.89e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19158 103 GLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYH 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19158 183 MFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAER 262

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNKSH 246
Cdd:cd19158 263 LGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY 324
AKR_AKR6C1_2 cd19143
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...
 25-239 9.07e-103

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: 301.05  E-value: 9.07e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19143 105 GTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYN 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQsEEGKKQQARVMDLLPTARQ 184
Cdd:cd19143 185 LFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKDRKE-ELGQEKIEKVRKLKPIAEE 263

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDA 239
Cdd:cd19143 264 LGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEA 318
AKR_AKR6B1 cd19142
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...
 26-244 5.32e-93

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: 276.27  E-value: 5.32e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHF 105
Cdd:cd19142 103 VRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHM 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYD---GRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTA 182
Cdd:cd19142 183 FCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEetrRLVTKLSFKSSKYKVGSDGNGIHEETRRASHKLRELSLIA 262

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202476 183 RQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNK 244
Cdd:cd19142 263 ERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNK 324
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
 25-223 1.39e-83

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: 251.36  E-value: 1.39e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19074  93 SIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYN 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEmQLPELYHKIGVGSVTWSPLACGLITSKY-DGRVPDTCKAtvKGYQWLKEKVQSEEGKKQQARVMDLLPTAR 183
Cdd:cd19074 173 MLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYrDGIPPPSRSR--ATDEDNRDKKRRLLTDENLEKVKKLKPIAD 249

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18202476 184 QLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSL 223
Cdd:cd19074 250 ELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
 12-241 4.95e-46

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: 155.72  E-value: 4.95e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  12 KVVFTFLSLPHPPG---------LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIM 82
Cdd:COG0667  82 KVGRRMGPGPNGRGlsrehirraVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLR 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  83 EAysMARQFNLIPPVCEQAENHFFQREkVEMQLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTCKATvkgyQWLK 160
Cdd:COG0667 162 RA--LAIAEGLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYrrGATFPEGDRAA----TNFV 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 161 EKVQSEEGKKQQARVMDLlptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:COG0667 235 QGYLTERNLALVDALRAI---AAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAA 309


                .
gi 18202476 241 L 241
Cdd:COG0667 310 L 310
AKR_AKR14A1_2 cd19089
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...
 25-224 7.82e-44

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: 150.10  E-value: 7.82e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNlIPPVCEQAENH 104
Cdd:cd19089 105 SLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYS 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQReKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATvKGYQWLKEKVQSEEgKKQQARVMDLLPTARQ 184
Cdd:cd19089 184 LLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRA-AESKFLTEEALTPE-KLEQLRKLNKIAAKRG 260

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18202476 185 LgcTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQ 224
Cdd:cd19089 261 Q--SLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALK 298
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
 28-240 6.55e-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: 145.02  E-value: 6.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  28 GSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHFFQ 107
Cdd:cd19087 103 ASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLK 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 REkVEMQLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTCKATVKGYQwlkEKVQSEEGKKQQARVMDLlptARQL 185
Cdd:cd19087 183 RQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYgkGKRPESGRLVERARYQ---ARYGLEEYRDIAERFEAL---AAEA 255

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 186 GCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:cd19087 256 GLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
AKR_AKR14A1 cd19150
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ...
 26-226 3.29e-39

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: 137.97  E-value: 3.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNlIPPVCEQAENHF 105
Cdd:cd19150 107 LDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNM 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYqwLKEKVQSEEgkkQQARVMDLLPTARQL 185
Cdd:cd19150 186 LNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS--LSPKMLTEA---NLNSIRALNEIAQKR 260

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18202476 186 GCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVL 226
Cdd:cd19150 261 GQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
AKR_AKR14A2 cd19151
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ...
 26-224 2.79e-38

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: 135.61  E-value: 2.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNlIPPVCEQAENHF 105
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSM 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREkVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATvKGYQWLKEKVQSEEgkkQQARVMDLLPTARQL 185
Cdd:cd19151 186 FNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQAR 260

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18202476 186 GCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQ 224
Cdd:cd19151 261 GQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
 26-238 1.26e-37

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: 133.88  E-value: 1.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHF 105
Cdd:cd19081 104 VEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNL 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDgRVPDTCKATVKGYQWlkEKVQSEEGkkqqARVMDLL-PTARQ 184
Cdd:cd19081 184 VDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYR-SEADLPGSTRRGEAA--KRYLNERG----LRILDALdEVAAE 256

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19081 257 HGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
 28-240 1.02e-36

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: 131.58  E-value: 1.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  28 GSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHFFQ 107
Cdd:cd19091 112 ASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLG 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 REkVEMQLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTCKATVKGYQWL---KEKVQseegkkqqaRVMD-LLPT 181
Cdd:cd19091 192 RD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLRRTGFDFPpvdRERGY---------DVVDaLREI 261

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18202476 182 ARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:cd19091 262 AKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLTPEEIARLDKV 318
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
 29-241 4.45e-35

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: 126.66  E-value: 4.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPVCEQAENHFFQR 108
Cdd:pfam00248  93 SLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLLRR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   109 EKVEMqLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTckatvkgyqwLKEKVQSEEGKKQQARVMDLLPTARQLG 186
Cdd:pfam00248 169 RQEEE-LLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPG----------ERRRLLKKGTPLNLEALEALEEIAKEHG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476   187 CTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDALL 241
Cdd:pfam00248 238 VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF--PLSDEEVARIDELL 290
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
 7-238 3.23e-34

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 125.87  E-value: 3.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476    7 LIFSLKVVFTFLSLPHPPG---------LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWS 77
Cdd:PRK09912  92 LIISTKAGYDMWPGPYGSGgsrkyllasLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   78 AAEIMEAYSMARQFNlIPPVCEQAENHFFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKG-- 155
Cdd:PRK09912 172 PERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnk 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  156 YQWLKEKVQSeEGKKQQARVMDLLptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSqLTPQTVV 235
Cdd:PRK09912 251 VRGLTPKMLT-EANLNSLRLLNEM--AQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLT-FSTEELA 326


                 ...
gi 18202476  236 EID 238
Cdd:PRK09912 327 QID 329
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
 25-240 5.94e-33

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: 121.54  E-value: 5.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQaeNH 104
Cdd:cd19079 107 EVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQ--NH 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 F---FQREKVEMqLPeLYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYqwLKEKVQSEEGKKQQARVMDLlpt 181
Cdd:cd19079 185 YnllYREEEREM-IP-LCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAK--LKYDYFTEADKEIVDRVEEV--- 257

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18202476 182 ARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQtvvEIDAL 240
Cdd:cd19079 258 AKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLSEE---EIKYL 311
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
 26-218 7.41e-33

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: 119.16  E-value: 7.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHF 105
Cdd:cd06660  90 LEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSL 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPELYHKIGVGSVTWSPLACGLItskydgrvpdtckatvkgyqwlkekvqseegkkqqarvmdllptarql 185
Cdd:cd06660 170 LDRSPMEEELLDWAEENGLPLLAYSPLARGPA------------------------------------------------ 201

                       170       180       190
                ....*....|....*....|....*....|...
gi 18202476 186 gctvgQLAIAWCLRSEGVSSVLLGVSSAEQLME 218
Cdd:cd06660 202 -----QLALAWLLSQPFVTVPIVGARSPEQLEE 229
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
 26-238 1.01e-31

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: 118.01  E-value: 1.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAysmarqFNLIPPVCEQAENHF 105
Cdd:cd19084  97 VEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA------RKYGPIVSLQPPYSM 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPeLYHKIGVGSVTWSPLACGLITSKYDGR---VPDTCKATVKgyqwlkeKVQSEEGKKQQARVMDLLPTA 182
Cdd:cd19084 171 LEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFP-------FFRGENFEKNLEIVDKLKEIA 242

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18202476 183 RQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19084 243 EKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
 26-238 5.79e-30

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: 113.47  E-value: 5.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSR---WSAAEiMEAYSMARqfNLIPPVCEQAE 102
Cdd:cd19080 103 VEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDtpaWVVAR-ANTLAELR--GWSPFVALQIE 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 103 NHFFQREkVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRvpDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLlptA 182
Cdd:cd19080 180 YSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGFGKLTERNWAIVDVVAAV---A 253

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18202476 183 RQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19080 254 EELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
AKR_Tas-like cd19094
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...
 26-240 2.64e-29

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: 112.27  E-value: 2.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIV-----------FANRSDPNS-------PMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSM 87
Cdd:cd19094 102 VEGSLKRLGTDYIDLYqlhwpdrytplFGGGYYTEPseeedsvSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLEL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  88 ARQFNLIPPVCEQAENHFFQReKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEE 167
Cdd:cd19094 182 AEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAARPEGGRLNLFPGYMARYRSPQ 260

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202476 168 GKKQQARvmdLLPTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:cd19094 261 ALEAVAE---YVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDV--PLSDELLAEIDAV 328
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
 12-241 1.29e-24

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: 99.23  E-value: 1.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  12 KVVFTF-LSLPHPPGL-----------QGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAA 79
Cdd:cd19078  73 KFGFKIdGGKPGPLGLdsrpehirkavEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVE 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  80 EIMEAYSmarqfnlIPPVCE-QAENHFFQREKVEMQLPELyHKIGVGSVTWSPLACGLITSKYDGRV---PDTCKATVKG 155
Cdd:cd19078 153 TIRRAHA-------VCPVTAvQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPR 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 156 YqwlkekvqSEEGKKQQARVMDLLPT-ARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTV 234
Cdd:cd19078 225 F--------TPEALEANQALVDLLKEfAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEEL 294


                ....*..
gi 18202476 235 VEIDALL 241
Cdd:cd19078 295 REIEDAL 301
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 26-241 8.22e-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: 381328 [Multi-domain]  Cd Length: 302  Bit Score: 94.28  E-value: 8.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEA------------YSMARQ--F 91
Cdd:cd19102  98 CEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCqaihpiaslqppYSLLRRgiE 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  92 NLIPPVCEQaenhffqrekvemqlpelyHKIGVgsVTWSPLACGLITSKYDgrvPDTCKATVKGYQWLKEKVQSEEGKKQ 171
Cdd:cd19102 178 AEILPFCAE-------------------HGIGV--IVYSPMQSGLLTGKMT---PERVASLPADDWRRRSPFFQEPNLAR 233

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202476 172 QARVMDLL-PTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDALL 241
Cdd:cd19102 234 NLALVDALrPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
 26-240 1.78e-21

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: 90.94  E-value: 1.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAySMARQFNLIppvceQAENHF 105
Cdd:cd19083 105 VEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNL 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPELyHKIGVGSVTWSPLACGLITSKYDgrvPDTckaTVKGYQWLKEK--VQSEEGKKQQARVMDLLPTAR 183
Cdd:cd19083 179 LQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYT---KDT---KFPDNDLRNDKplFKGERFSENLDKVDKLKSIAD 251

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476 184 QLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:cd19083 252 EKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFIDAL 306
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
 26-239 3.06e-20

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: 87.26  E-value: 3.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSmarqfnLIPPVCEQAENHF 105
Cdd:cd19085  86 CERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD------AGRIDSNQLPYNL 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLPEL-YHKIGVgsVTWSPLACGLITSKY--DGRVPDTCKATvkgyqwlKEKVQSEEGKKQQA-RVMDLL-P 180
Cdd:cd19085 160 LWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFssAEDFPPGDART-------RLFRHFEPGAEEETfEALEKLkE 230

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18202476 181 TARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDA 239
Cdd:cd19085 231 IADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDE 287
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
 26-216 1.55e-19

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: 85.30  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQaeNHF 105
Cdd:cd19082  94 LEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASS--PQW 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQREKVEMQLP------------ELYHKIGVGSVTWSPLACGLITSKYDGRVPDtckatvkgyqwLKEKVQ---SEEGKK 170
Cdd:cd19082 172 SLARPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGAED-----------DSELRRvyySEENFE 240

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 18202476 171 QQARVMDLlptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQL 216
Cdd:cd19082 241 RLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQL 283
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
 26-238 4.04e-19

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: 84.20  E-value: 4.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPN-SPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNlIPPVCEQAENH 104
Cdd:cd19093  93 LKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYS 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKY--DGRVPDTCKATVKGYQWlkEKVQSeegkkqqarVMDLL-PT 181
Cdd:cd19093 172 LLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYspENPPPGGRRRLFGRKNL--EKVQP---------LLDALeEI 240

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476 182 ARQLGCTVGQLAIAWCLrSEGVsSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19093 241 AEKYGKTPAQVALNWLI-AKGV-VPIPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
AKR_AKR13A_13D cd19076
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...
 28-237 1.46e-18

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: 82.65  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  28 GSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSmarqfnlIPPVCE-QAENHFF 106
Cdd:cd19076 107 ASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHA-------VHPITAvQSEYSLW 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 107 QREKVEMQLP---ELyhkiGVGSVTWSPLACGLITSKYdgRVPDTCKATvkGYQWLKEKVQSEEGKKQQARVMDLLPTAR 183
Cdd:cd19076 180 TRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAI--KSPEDLPED--DFRRNNPRFQGENFDKNLKLVEKLEAIAA 251

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 184 QLGCTVGQLAIAWCL-RSEGVSSVlLGVSSAEQLMEHLGSLQVlsQLTPQTVVEI 237
Cdd:cd19076 252 EKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 25-223 1.57e-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: 82.38  E-value: 1.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENH 104
Cdd:cd19752 100 EIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHS 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 105 FFQR-----EKVEMQL-PEL-----YHKiGVGSVTWSPLACGLITSkydgrvPDtckatvkgyqwlKEKVQSEEGKKQQA 173
Cdd:cd19752 180 YLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPLLSGAYTR------PD------------RPLPEQYDGPDSDA 240

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18202476 174 RVMDLLPTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSL 223
Cdd:cd19752 241 RLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
AKR_AKR13A1 cd19144
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...
 29-237 3.71e-18

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: 81.72  E-value: 3.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSmarqfnlIPPVCE-QAENHFF- 106
Cdd:cd19144 111 SLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-------VHPIAAvQIEYSPFs 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 107 -QREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYdgRVPDTCKAtvKGYQWLKEKVQSEEGKKQQARVMDLLPTARQL 185
Cdd:cd19144 184 lDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI--RSPDDFEE--GDFRRMAPRFQAENFPKNLELVDKIKAIAKKK 259

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18202476 186 GCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEI 237
Cdd:cd19144 260 NVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEEEKEI 309
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
 28-224 1.00e-17

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: 79.97  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  28 GSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQfnlIPPVCEQAENHFFQ 107
Cdd:cd19072  92 ESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFD 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 REkVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVpdtckatvkgyqwLKEkvqseegkkqqarvmdllpTARQLGC 187
Cdd:cd19072 169 RE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL-------------LDE-------------------IAKKYGK 215

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18202476 188 TVGQLAIAWCLRSEGVsSVLLGVSSAEQLMEHLGSLQ 224
Cdd:cd19072 216 TPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
 29-239 1.27e-17

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381375 [Multi-domain]  Cd Length: 315  Bit Score: 80.39  E-value: 1.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEA------------YSMARQF--NLI 94
Cdd:cd19149 118 SLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYvkagqldiiqekYSMLDRGieKEL 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  95 PPVCEQaenhffqrekvemqlpelyHKIGVgsVTWSPLACGLITSKYD-GR--VPDTCKATVKGYQwlKEKVqseegkkq 171
Cdd:cd19149 198 LPYCKK-------------------NNIAF--QAYSPLEQGLLTGKITpDRefDAGDARSGIPWFS--PENR-------- 246

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202476 172 qARVMDLL----PTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDA 239
Cdd:cd19149 247 -EKVLALLekwkPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI--RLSAEDIATMRS 315
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
 24-238 8.57e-15

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: 71.83  E-value: 8.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  24 PGLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQfnliPPVCEQAEN 103
Cdd:cd19137  88 RSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT----PIVCNQVKY 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 104 HFFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSkydgrvpdtckatvkgyqwlKEKVQSeegkkqqarvmdllpTAR 183
Cdd:cd19137 164 NLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKT--------------------NRTLEE---------------IAK 208

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 184 QLGCTVGQLAIAWCLRSEGVSSVLLGvSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19137 209 NYGKTIAQIALAWLIQKPNVVAIPKA-GRVEHLKENLKATEI--KLSEEEMKLLD 260
AKR_AKR8A1-2 cd19077
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ...
 29-238 1.45e-14

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: 71.50  E-value: 1.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRL-QLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMArqfnliPPVCEQAENHFFQ 107
Cdd:cd19077 103 ILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFS 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 REKVEMQLPELYHKIGVGSVTWSPLACGLITskydGRVP---DTCKATVKGYQwlkEKVQSEEGKKQQARVMDLLPTARQ 184
Cdd:cd19077 177 REIEENGVLETCAELGIPIIAYSPLGRGLLT----GRIKslaDIPEGDFRRHL---DRFNGENFEKNLKLVDALQELAEK 249

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 185 LGCTVGQLAIAWCLRSEGVSSV-LLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19077 250 KGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
 27-237 3.84e-14

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: 70.54  E-value: 3.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  27 QGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMArqfnliPPVCEQAENHFF 106
Cdd:cd19145 107 EASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVH------PITAVQLEWSLW 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 107 QREkVEMQLPELYHKIGVGSVTWSPLACGLITSK---YDGRVPDTCKATVKGYQwlKEKVqsEEGKKQQARVMDLlptAR 183
Cdd:cd19145 181 TRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKaklEELLENSDVRKSHPRFQ--GENL--EKNKVLYERVEAL---AK 252

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 184 QLGCTVGQLAIAWCL-RSEGVSSVlLGVSSAEQLMEHLGSLQVlsQLTPQTVVEI 237
Cdd:cd19145 253 KKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
 26-240 4.79e-14

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: 70.28  E-value: 4.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHF 105
Cdd:cd19075  85 LETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNA 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 106 FQReKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDtckatVKGYQWlkeKVQSEEGKKQQAR---------VM 176
Cdd:cd19075 165 ITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDK-----AGGGRF---DPNNALGKLYRDRywkpsyfeaLE 235

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202476 177 DLLPTARQLGCTVGQLAIAWC-----LRSEGVSSVLLGVSSAEQLMEHLGSLQVlSQLTPQTVVEIDAL 240
Cdd:cd19075 236 KVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEK-GPLPEEVVKAIDEA 303
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
 27-220 1.96e-13

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: 67.63  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  27 QGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIppVCEQAENHFF 106
Cdd:cd19088  97 EASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----I--VSVQNRYNLA 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 107 QREKVEMQlpELYHKIGVGSVTWSPLACGlitskyDGRVPDTCKATVkgyqwlkekvqseegkkqqarvmdllptARQLG 186
Cdd:cd19088 171 NRDDEGVL--DYCEAAGIAFIPWFPLGGG------DLAQPGGLLAEV----------------------------AARLG 214

                       170       180       190
                ....*....|....*....|....*....|....
gi 18202476 187 CTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHL 220
Cdd:cd19088 215 ATPAQVALAWLLARSPVMLPIPGTSSVEHLEENL 248
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
 29-240 2.69e-12

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: 64.59  E-value: 2.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPVCEQAENHFF-- 106
Cdd:cd19140  87 SLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHPYld 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 107 QRekvemQLPELYHKIGVGSVTWSPLAcglitskyDGRVPDtckatvkgYQWLKEkvqseegkkqqarvmdllpTARQLG 186
Cdd:cd19140 163 QR-----KLLDAAREHGIALTAYSPLA--------RGEVLK--------DPVLQE-------------------IGRKHG 202

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18202476 187 CTVGQLAIAWCLRSEGVsSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:cd19140 203 KTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
AKR_YeaE cd19138
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...
 20-238 8.91e-12

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: 63.42  E-value: 8.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  20 LPHPPGLQG-------SLDRLQLEYVDIVFAN-RSdpNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQF 91
Cdd:cd19138  79 LPSNASRQGtvracerSLRRLGTDYLDLYLLHwRG--GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGG 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  92 NLippVCEQAENHFFQReKVEMQLPELYHKIGVGSVTWSPLAcglitskydgrvpdtckatvkgyqwlkekvQSEEGKKQ 171
Cdd:cd19138 157 NC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLA------------------------------QGGLLRRG 202

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476 172 QARVMDLLPTARQLGCTVGQLAIAWCLRSEGVSSVlLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19138 203 LLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
 26-239 7.82e-11

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: 60.90  E-value: 7.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQ----A 101
Cdd:cd19146 114 VEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQghwsA 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 102 ENHFFQREKVEMQLPElyhkiGVGSVTWSPLACGLITSKYDGRVPDTckatvkgyQWLKEKVQSEEGKKQQARvmdLLPT 181
Cdd:cd19146 194 AFRDFERDILPMCEAE-----GMALAPWGVLGQGQFRTEEEFKRRGR--------SGRKGGPQTEKERKVSEK---LEKV 257

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18202476 182 ARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDA 239
Cdd:cd19146 258 AEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEIQEIED 313
tas PRK10625
putative aldo-keto reductase; Provisional
 26-240 9.45e-11

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 61.02  E-value: 9.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   26 LQGSLDRLQLEYVDI-----------VFA------NRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMA 88
Cdd:PRK10625 114 LHDSLKRLQTDYLDLyqvhwpqrptnCFGklgyswTDSAPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476   89 RQFNLIPPVCEQAENHFFQREkVEMQLPELYHKIGVGSVTWSPLACGLITSKY-DGRVPDTCKATvkgyqwLKEKVQSEE 167
Cdd:PRK10625 194 EKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYlNGAKPAGARNT------LFSRFTRYS 266

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202476  168 GKKQQARVMDLLPTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:PRK10625 267 GEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
 29-216 2.26e-10

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: 59.49  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVF---ANRSDPNSPM--EEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMAR-----QFNLIPPVC 98
Cdd:cd19090  90 SLERLGRDRIDLLMihdPERVPWVDILapGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGDfdvvlTANRYTLLD 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  99 EQAENHFFqrekvemqlpELYHKIGVGSVTWSPLACGLITSKYDGRVPDTckatvkgYQWLkekvqseeGKKQQARVMDL 178
Cdd:cd19090 170 QSAADELL----------PAAARHGVGVINASPLGMGLLAGRPPERVRYT-------YRWL--------SPELLDRAKRL 224

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18202476 179 LPTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQL 216
Cdd:cd19090 225 YELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEEL 262
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
 26-240 3.55e-10

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 58.53  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVD---IVFanrsdPNS-PMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPVCEQA 101
Cdd:COG0656  81 FEESLERLGLDYLDlylIHW-----PGPgPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQV 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 102 ENH-FFQREKVemqLPelYHK-IGVGSVTWSPLAcglitskydgrvpdtckatvkgyqwlkekvqseegkkqQARVMDlL 179
Cdd:COG0656 152 ELHpYLQQREL---LA--FCReHGIVVEAYSPLG--------------------------------------RGKLLD-D 187

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202476 180 PT----ARQLGCTVGQLAIAWCLRsEGVsSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEIDAL 240
Cdd:COG0656 188 PVlaeiAEKHGKTPAQVVLRWHLQ-RGV-VVIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
 26-216 8.45e-09

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: 54.41  E-value: 8.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFA-NRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMAR------QFNLIppvc 98
Cdd:cd19086  96 VEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRGGidvvqvIYNLL---- 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  99 EQ-AENHFFqrekvemqlpELYHKIGVGSVTWSPLACGLITSKydgrvpdtckatvkgyqwlkekvqseegkkqqarvmd 177
Cdd:cd19086 172 DQrPEEELF----------PLAEEHGVGVIARVPLASGLLTGK------------------------------------- 204

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18202476 178 llptarqlgctVGQLAIAWCLRSEGVSSVLLGVSSAEQL 216
Cdd:cd19086 205 -----------LAQAALRFILSHPAVSTVIPGARSPEQV 232
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 25-240 2.23e-08

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: 53.81  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIVF------ANRSDPNSPM---------EEIVRAMTYVINQGLALYWGTSRWSAAEIME------ 83
Cdd:cd19104  98 SVEKSLKRLKRDSVDLLQlhnrigDERDKPVGGTlsttdvlglGGVADAFERLRSEGKIRFIGITGLGNPPAIRelldsg 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  84 AYSMARQF-NLI--PPVCEQAENHFFQREKvemQLPELYHKIGVGSVTWSPLACGLITSKYD-GRVPDtckatvkgyqwL 159
Cdd:cd19104 178 KFDAVQVYyNLLnpSAAEARPRGWSAQDYG---GIIDAAAEHGVGVMGIRVLAAGALTTSLDrGREAP-----------P 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 160 KEKVQSEEGKKQQARVMDLlptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEhlgSLQVLSQ--LTPQTVVEI 237
Cdd:cd19104 244 TSDSDVAIDFRRAAAFRAL---AREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEE---AVAAEAAgpLPAENLARL 317


                ...
gi 18202476 238 DAL 240
Cdd:cd19104 318 EAL 320
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
 29-216 3.57e-08

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: 53.08  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEiMEAY-SMARQFNLIPPVceqaenHFFQ 107
Cdd:cd19148 102 SLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQ-METFrKVAPLHTVQPPY------NLFE 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 REKVEMQLPelY-HKIGVGSVTWSPLACGLITSKYDgrvPDTckatvkgyQWLKEKVQSEEGKKQQAR-------VMDLL 179
Cdd:cd19148 175 REIEKDVLP--YaRKHNIVTLAYGALCRGLLSGKMT---KDT--------KFEGDDLRRTDPKFQEPRfsqylaaVEELD 241

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 18202476 180 PTARQ-LGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQL 216
Cdd:cd19148 242 KLAQErYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
 28-199 4.41e-08

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: 52.56  E-value: 4.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  28 GSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEImeaySMARQFNLIPPVCEQAEnhffq 107
Cdd:cd19092 105 GSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQI----ELLQSYLDQPLVTNQIE----- 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 108 rekvemqlpelyhkigvgsvtWSPLACGLItskYDGRVpDTCKAtvKGYQWLK---------EKVQSEegkkQQARVMDL 178
Cdd:cd19092 176 ---------------------LSLLHTEAI---DDGTL-DYCQL--LDITPMAwsplgggrlFGGFDE----RFQRLRAA 224

                       170       180
                ....*....|....*....|..
gi 18202476 179 L-PTARQLGCTVGQLAIAWCLR 199
Cdd:cd19092 225 LeELAEEYGVTIEAIALAWLLR 246
AKR_AKR1G1_CeAKR cd19154
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...
 23-189 2.49e-07

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: 50.49  E-value: 2.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  23 PPGLQGSLDRLQLEYVDI-------VFANRSDPNSPM------------EEIVRAMTYVINQGLALYWGTSRWSAAEIME 83
Cdd:cd19154  89 EEALRESLKKLQLEYVDLylihapaAFKDDEGESGTMengmsihdavdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQR 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  84 AYSMARqfnlIPPVCEQAENHFFQREKvemQLPELYHKIGVGSVTWSPLacGLItskydGRV-PDTCKATVKGYQWLKEK 162
Cdd:cd19154 169 ILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL--GSP-----GRAnFTKSTGVSPAPNLLQDP 234

                       170       180       190
                ....*....|....*....|....*....|
gi 18202476 163 VQSEEGKKQQ---ARVmdLLPTARQLGCTV 189
Cdd:cd19154 235 IVKAIAEKHGktpAQV--LLRYLLQRGIAV 262
AKR_AKR3G1 cd19123
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ...
 24-238 9.69e-07

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: 48.56  E-value: 9.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  24 PGLQGSLDRLQLEYVDI------------VFANRS------DPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAY 85
Cdd:cd19123  90 PALEKTLADLQLDYLDLylmhwpvalkkgVGFPESgedllsLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLL 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  86 SMARqfnlIPPVCEQAENHFFqrekveMQLPELY----HKiGVGSVTWSPLacglitskydGRvPDTCKATvkgyqwlke 161
Cdd:cd19123 170 ATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPL----------GS-GDRPAAM--------- 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 162 KVQSEEgkkqqaRVMD---LLPTARQLGCTVGQLAIAWCLRSEgvSSVLLGVSSAEQLMEHLGSLQV-LSQLTPQTVVEI 237
Cdd:cd19123 219 KAEGEP------VLLEdpvINKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERIQQNLEAAEVeLDASDMATIAAL 290


                .
gi 18202476 238 D 238
Cdd:cd19123 291 D 291
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
 24-238 2.39e-06

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: 47.27  E-value: 2.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  24 PGLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPVCEQAEN 103
Cdd:cd19073  75 KSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEF 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 104 HFF--QREkvemqLPELYHKIGVGSVTWSPLAcglitskyDGRVPDTckatvkgyqwlkEKVQSEEGKKqqarvmdllpt 181
Cdd:cd19073 151 HPFlyQAE-----LLEYCRENDIVITAYSPLA--------RGEVLRD------------PVIQEIAEKY----------- 194

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202476 182 arqlGCTVGQLAIAWcLRSEGVsSVLLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19073 195 ----DKTPAQVALRW-LVQKGI-VVIPKASSEDHLKENLAIFDW--ELTSEDVAKID 243
AKR_AKR1G1_1I cd19111
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...
 25-111 3.17e-06

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: 47.11  E-value: 3.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  25 GLQGSLDRLQLEYVDIV-------FANRSDPN------SPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqf 91
Cdd:cd19111  83 SLEKSLENLKLPYVDLYlihhpcgFVNKKDKGerelasSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK-- 160

                        90       100
                ....*....|....*....|..
gi 18202476  92 nlIPPVCEQAENH--FFQREKV 111
Cdd:cd19111 161 --VKPSNLQLECHayLQQRELR 180
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
 24-238 3.99e-06

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: 46.71  E-value: 3.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  24 PGLQGSLDRLQLEYVDIV-----FANRSDPN-SPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqfnlIPPV 97
Cdd:cd19071  75 EALEESLKDLGLDYLDLYlihwpVPGKEGGSkEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPA 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  98 CEQAENH-FFQREKVEMQLPElyHKIGVgsVTWSPLACGlitskydgrvpdtckatvkGYQWLKEKVqseegkkqqarvm 176
Cdd:cd19071 151 VNQIELHpYLQQKELVEFCKE--HGIVV--QAYSPLGRG-------------------RRPLLDDPV------------- 194

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202476 177 dLLPTARQLGCTVGQLAIAWCLRSeGVsSVLLGVSSAEQLMEhlgSLQVLS-QLTPQTVVEID 238
Cdd:cd19071 195 -LKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKE---NLDVFDfELSEEDMAAID 251
AKR_AKR4C1-15 cd19125
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ...
 23-220 4.69e-05

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: 43.49  E-value: 4.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  23 PPGLQGSLDRLQLEYVDI--------------VFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMA 88
Cdd:cd19125  88 PPALEKTLKDLQLDYLDLylihwpvrlkkgahMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVA 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  89 RqfnlIPPVCEQAENHFFQREKvemQLPELYHKIGVGSVTWSPLACGlitskydgrvpdtckatvkGYQWLKEKVQSEEg 168
Cdd:cd19125 168 R----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPLGSP-------------------GTTWVKKNVLKDP- 220

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 18202476 169 kkqqarvmDLLPTARQLGCTVGQLAIAWCLRSEgvSSVLLGVSSAEQLMEHL 220
Cdd:cd19125 221 --------IVTKVAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEERIKENI 262
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 26-224 1.48e-04

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381323 [Multi-domain]  Cd Length: 267  Bit Score: 42.13  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANR-SDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSmARQFNLIppvceQAE-N 103
Cdd:cd19097  90 VEASLKRLKVDSLDGLLLHNpDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFKIDII-----QLPfN 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 104 HFFQREKVEMQLPELyHKIGVGSVTWSPLACGLITSKYDgRVPDtckatvkgyqwlkekvQSEEGKKQQARVMDLlptAR 183
Cdd:cd19097 164 ILDQRFLKSGLLAKL-KKKGIEIHARSVFLQGLLLMEPD-KLPA----------------KFAPAKPLLKKLHEL---AK 222

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18202476 184 QLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQ 224
Cdd:cd19097 223 KLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
 17-246 2.24e-04

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: 41.45  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  17 FLSLPHPPG-LQGSLDRLQLEYVD--IVFANRSDPNSP--MEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARqf 91
Cdd:cd19120  75 SPGIKDPREaLRKSLAKLGVDYVDlyLIHSPFFAKEGGptLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK-- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  92 nlIPPVCEQAENHFFqrekVEMQLPEL--YHKigvgsvtwsplACGLITSKYDGRVPdtckatvkgyqwlkeKVQSEEGK 169
Cdd:cd19120 153 --IKPAVNQIEFHPY----LYPQQPALleYCR-----------EHGIVVSAYSPLSP---------------LTRDAGGP 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202476 170 KQQArvmdLLPTARQLGCTVGQLAIAWCLrSEGVssVLLGVSSAEQLMEhlGSLQVLS-QLTPQTVVEIDALLGNKSH 246
Cdd:cd19120 201 LDPV----LEKIAEKYGVTPAQVLLRWAL-QKGI--VVVTTSSKEERMK--EYLEAFDfELTEEEVEEIDKAGKQKHF 269
AKR_galDH-like cd19153
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...
 26-229 2.47e-04

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: 41.37  E-value: 2.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANR---SDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAysmARQFNLIPPVCEQAE 102
Cdd:cd19153 104 VATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRA---TRRCSPGSLDAVLSY 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 103 NHF-FQREKVEMQLPELYHKIGVGSVTWSPLACGLITSK-------YDGRVPDTCKATVKgyqWLKEKvqseegkkqqar 174
Cdd:cd19153 181 CHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQgpppwhpASGELRHYAAAADA---VCASV------------ 245

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18202476 175 vmdllptarqlGCTVGQLAIAWCLRSE-GVSSVLLGVSSAEQLMEHLGSLQVLSQL 229
Cdd:cd19153 246 -----------EASLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASL 290
AKR_AKR4A_4B cd19124
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ...
 24-132 3.12e-04

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: 41.10  E-value: 3.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  24 PGLQGSLDRLQLEYVD---IVFANRSDPNS-----------P--MEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSM 87
Cdd:cd19124  86 PALKKSLRNLQLEYVDlylIHWPVSLKPGKfsfpieeedflPfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSF 165

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18202476  88 ARqfnlIPPVCEQAENH-FFQREKvemqLPELYHKIGVGSVTWSPL 132
Cdd:cd19124 166 AT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPL 203
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
 26-238 3.45e-04

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: 40.96  E-value: 3.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAE--- 102
Cdd:cd19147 114 VRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRwnv 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 103 -NHFFQREKVEMQlpelyHKIGVGSVTWSPLACGLITSKydgrvpDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPT 181
Cdd:cd19147 194 lNRDFERDIIPMA-----RHFGMALAPWDVLGGGKFQSK------KAVEERKKNGEGLRSFVGGTEQTPEEVKISEALEK 262

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 182 -ARQLGC-TVGQLAIAWcLRSEGVSSV-LLGVSSAEQLMEHLGSLQVlsQLTPQTVVEID 238
Cdd:cd19147 263 vAEEHGTeSVTAIALAY-VRSKAPNVFpLVGGRKIEHLKDNIEALSI--KLTPEEIEYLE 319
AKR_AKR3E1 cd19122
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ...
 26-199 7.43e-04

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: 39.91  E-value: 7.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVDI------VFANRSDPNSPM-----------------EEIVRAMTYVINQGLALYWGTSRWSAAEIM 82
Cdd:cd19122  92 IDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYESGKAKAIGVSNWTIPGLK 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  83 EAYSMARqfnlIPPVCEQAENHFFQREKvemQLPELYHKIGVGSVTWSPLACglitskyDGRVPDTckatvkgyqwlKEK 162
Cdd:cd19122 172 KLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------QNQVPST-----------GER 226

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18202476 163 VQSEEGKKQqarvmdllpTARQLGCTVGQLAIAWCLR 199
Cdd:cd19122 227 VSENPTLNE---------VAEKGGYSLAQVLIAWGLR 254
AKR_GlAR-like cd19128
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ...
 26-240 8.87e-04

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: 39.81  E-value: 8.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  26 LQGSLDRLQLEYVD-------IVF------------ANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYS 86
Cdd:cd19128  81 LLITLQDLQLEYLDlflihwpLAFdmdtdgdprddnQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  87 MARqfnlIPPVCEQAENH-FFQREKvemqLPELYHKIGVGSVTWSPL--ACGlitskYDGRVPDTCKAtvkgyqwlkekv 163
Cdd:cd19128 161 YCK----IKPFMNQIECHpYFQNDK----LIKFCIENNIHVTAYRPLggSYG-----DGNLTFLNDSE------------ 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202476 164 qseegkkqqarvmdLLPTARQLGCTVGQLAIAWCL-RSEGVSSVLLGVSSAEQLMEHLGSLQVlsQLTPQtvvEIDAL 240
Cdd:cd19128 216 --------------LKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNFDINDL--ALTKE---DMDAI 274
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
 21-135 1.70e-03

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: 38.71  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  21 PHPPGLQGSLDRLQLEYVDIV-----FANRSDPNSPMEEIVRAmtyvinqGLALYWGTSRWSAAEIMEAYSmarqFNLIP 95
Cdd:cd19133  81 KAKKAFERSLKRLGLDYLDLYlihqpFGDVYGAWRAMEELYKE-------GKIRAIGVSNFYPDRLVDLIL----HNEVK 149

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18202476  96 PVCEQAENH-FFQREkvemQLPELYHKIGVGSVTWSPLACG 135
Cdd:cd19133 150 PAVNQIETHpFNQQI----EAVEFLKKYGVQIEAWGPFAEG 186
AKR_unchar cd19098
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 171-225 2.38e-03

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: 38.48  E-value: 2.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18202476 171 QQARVMDLLPT-ARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQV 225
Cdd:cd19098 233 ELAPLMAVLKAvADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
AKR_AKR15A cd19152
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...
 29-225 2.41e-03

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: 38.36  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  29 SLDRLQLEYVDIVFANRSDPNSP-----------MEEIVRAMTYVINQGLALYW--GTSRWSAAE----------IMeay 85
Cdd:cd19152 112 SLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIglGVNDWEVILrileeadldwVM--- 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476  86 sMARQFNLIppvcEQAENHFFqrekvemqLPELyHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATvkgyQWLKEKVQs 165
Cdd:cd19152 189 -LAGRYTLL----DHSAAREL--------LPEC-EKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPAP----PELIARRD- 249

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202476 166 eegkkqqaRVMDLlptARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQV 225
Cdd:cd19152 250 --------RIEAL---CEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
 183-231 6.67e-03

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: 36.77  E-value: 6.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18202476 183 RQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHlgsLQVLSQLTP 231
Cdd:cd19096 210 CGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDEN---IAAADEFEP 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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