|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
7-296 |
0e+00 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 522.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 7 DSTKILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQ 86
Cdd:cd19117 1 PSSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHEPEVALDQSLKRLGLDYVDLYLMHWPARLDPAYIKNEDilsvptKKDGSRAVDITNWNFIKTWELMQELPKTGKTKAV 166
Cdd:cd19117 81 HRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLF------KKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 167 GVSNFSINNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQP 246
Cdd:cd19117 155 GVSNFSIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAPLLKEPVIIKIAKKHGKTP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6324694 247 GHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNISKEKG 296
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEFKEIDELHKEYG 284
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
10-291 |
3.98e-136 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 386.89 E-value: 3.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 10 KILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDS---GVPREEIFVTTKLWCTQ 86
Cdd:cd19121 2 TSFKLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLWSTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHEPEVALDQSLKRLGLDYVDLYLMHWPARLDPAyiKNEDILsvPTKKDGSRAVDITnWNFIKTWELMQELPKTGKTKAV 166
Cdd:cd19121 82 HRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPN--GNHDLF--PTLPDGSRDLDWD-WNHVDTWKQMEKVLKTGKTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 167 GVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQP 246
Cdd:cd19121 157 GVSNYSIPYLEELLKHA--TVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSPLISDEPVVEIAKKHNVGP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6324694 247 GHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNI 291
Cdd:cd19121 235 GTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
20-289 |
2.09e-127 |
|
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: 363.73 E-value: 2.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEV--ALDQS 97
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVreALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 98 LKRLGLDYVDLYLMHWParldpayiknedilsVPTKKDGSRavditnWNFIKTWELMQELPKTGKTKAVGVSNFSINNLK 177
Cdd:cd19071 81 LKDLGLDYLDLYLIHWP---------------VPGKEGGSK------EARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 178 DLLASQGNKltPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQPGHVVISWHVQR 257
Cdd:cd19071 140 ELLAAARIK--PAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR 217
|
250 260 270
....*....|....*....|....*....|....
gi 6324694 258 GYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19071 218 GVVVIPKSSNPERIKENLDVfdFELSEEDMAAID 251
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
17-304 |
4.25e-126 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 360.52 E-value: 4.25e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWcTQHHEPE---VA 93
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVW-NDNHGYDdtlAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 94 LDQSLKRLGLDYVDLYLMHWPARldpayiknedilsvptkkdgsravditnWNFIKTWELMQELPKTGKTKAVGVSNFSI 173
Cdd:COG0656 81 FEESLERLGLDYLDLYLIHWPGP----------------------------GPYVETWRALEELYEEGLIRAIGVSNFDP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 174 NNLKDLLASQGNKltPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDapLLKEPVILEIAKKNNVQPGHVVISW 253
Cdd:COG0656 133 EHLEELLAETGVK--PAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK--LLDDPVLAEIAEKHGKTPAQVVLRW 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 6324694 254 HVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNIskEKGEKRVVHPN 304
Cdd:COG0656 209 HLQRGVVVIPKSVTPERIRENLDAfdFELSDEDMAAIDAL--DRGERLGPDPD 259
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
12-295 |
8.08e-115 |
|
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: 333.16 E-value: 8.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSG----VPREEIFVTTKLWCTqH 87
Cdd:cd19125 3 FKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCT-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPE---VALDQSLKRLGLDYVDLYLMHWPARLdpayiknedilsvptkKDGsrAVDITNWNFIK-----TWELMQELPK 159
Cdd:cd19125 82 HAPEdvpPALEKTLKDLQLDYLDLYLIHWPVRL----------------KKG--AHMPEPEEVLPpdipsTWKAMEKLVD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 160 TGKTKAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP-----LLKEPV 234
Cdd:cd19125 144 SGKVRAIGVSNFSVKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTwvkknVLKDPI 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324694 235 ILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIF--TLSTEDFEAINNISKEK 295
Cdd:cd19125 222 VTKVAEKLGKTPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFdwSIPEEDFAKFSSIEQQR 284
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
14-291 |
1.36e-112 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 327.45 E-value: 1.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDS-----GVPREEIFVTTKLWCTqHH 88
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNN-SH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPE---VALDQSLKRLGLDYVDLYLMHWPARLDPAyiKNEDILSVPTKKDGSRAVDiTNWNFIKTWELMQELPKTGKTKA 165
Cdd:cd19118 80 RPEyvePALDDTLKELGLDYLDLYLIHWPVAFKPT--GDLNPLTAVPTNGGEVDLD-LSVSLVDTWKAMVELKKTGKVKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 166 VGVSNFSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGST---DAPLLKEPVILEIAKKN 242
Cdd:cd19118 157 IGVSNFSIDHLQAIIEETG--VVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNlagLPLLVQHPEVKAIAAKL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6324694 243 NVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNI 291
Cdd:cd19118 235 GKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDEFNAVTAL 283
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
10-293 |
1.56e-106 |
|
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: 312.42 E-value: 1.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 10 KILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAI----KDSGVPREEIFVTTKLWCT 85
Cdd:cd19123 2 KTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALaevfKEGKVKREDLWITSKLWNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 86 QHHEPEV--ALDQSLKRLGLDYVDLYLMHWPARLDPayiknedilSVPTKKDGSRAVDITNWNFIKTWELMQELPKTGKT 163
Cdd:cd19123 82 SHAPEDVlpALEKTLADLQLDYLDLYLMHWPVALKK---------GVGFPESGEDLLSLSPIPLEDTWRAMEELVDKGLC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 164 KAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP----------LLKEP 233
Cdd:cd19123 153 RHIGVSNFSVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPaamkaegepvLLEDP 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324694 234 VILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTN--RKIFTLSTEDFEAINNISK 293
Cdd:cd19123 231 VINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNleAAEVELDASDMATIAALDR 292
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
12-288 |
2.86e-102 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 300.06 E-value: 2.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLW--CTQHHE 89
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWnsDQGYDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEVALDQSLKRLGLDYVDLYLMHWPArldPAYIKnedilsvptkkdgsravditnwnFIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19131 82 TLRAFDESLRKLGLDYVDLYLIHWPV---PAQDK-----------------------YVETWKALIELKKEGRVKSIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 170 NFSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNVQPGHV 249
Cdd:cd19131 136 NFTIEHLQRLIDETG--VVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ--GGLLSDPVIGEIAEKHGKTPAQV 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6324694 250 VISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19131 212 VIRWHLQNGLVVIPKSVTPSRIAENFDVfdFELDADDMQAI 252
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
20-291 |
1.03e-101 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 298.78 E-value: 1.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQSK-ENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDS----GVPREEIFVTTKLWCTQHHEPEV-- 92
Cdd:cd19136 1 MPILGLGTFRLRgEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKAra 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 ALDQSLKRLGLDYVDLYLMHWP--ARLDPAYIKNEDIlsvptkkdgsRAVditnwnfikTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvQGLKPSDPRNAEL----------RRE---------SWRALEDLYKEGKLRAIGVSN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQPGHVV 250
Cdd:cd19136 142 YTVRHLEELLKY--CEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLRLLEDPTVLAIAKKYGRTPAQVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 6324694 251 ISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19136 220 LRWALQQGIGVIPKSTNPERIAENIKVfdFELSEEDMAELNAL 262
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
14-294 |
1.08e-101 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 300.46 E-value: 1.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK-----DSGVPREEIFVTTKLWCTQHH 88
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKekvgpGKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPEV--ALDQSLKRLGLDYVDLYLMHWP---ARLDPAYIKNEdilsvptkkDGSRAVDITnwNFIKTWELMQELPKTGKT 163
Cdd:cd19106 81 PEDVepALRKTLKDLQLDYLDLYLIHWPyafERGDNPFPKNP---------DGTIRYDST--HYKETWKAMEKLVDKGLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 164 KAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP--------LLKEPVI 235
Cdd:cd19106 150 KAIGLSNFNSRQIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPwakpdepvLLEEPKV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324694 236 LEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISKE 294
Cdd:cd19106 228 KALAKKYNKSPAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVfdFTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-299 |
5.54e-100 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 295.56 E-value: 5.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 9 TKILSLNTGAQIPQIGLGTWQSKENDAY--KAVLTALKDGYRHIDTAAIYRNEDQVGQAIK----DSGVPREEIFVTTKL 82
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEDRAEvkEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKraidDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 WCTQHHEPEVALDQSLKRLGLDYVDLYLMHWPArldPAYIKNEDILSV--PTKKDGSRAVDITNwNFIKTWELMQELPKT 160
Cdd:cd19119 81 WPTFYDEVERSLDESLKALGLDYVDLLLVHWPV---CFEKDSDDSGKPftPVNDDGKTRYAASG-DHITTYKQLEKIYLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 161 GKTKAVGVSNFSINNLKDLLasQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAK 240
Cdd:cd19119 157 GRAKAIGVSNYSIVYLERLI--KECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNLKNPLVKKIAE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 241 KNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNISKEKGEKR 299
Cdd:cd19119 235 KYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQKLDDIGEKYPVRF 293
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
14-288 |
1.10e-99 |
|
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: 293.33 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQ-SKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEV 92
Cdd:cd19133 3 LNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 --ALDQSLKRLGLDYVDLYLMHWPARldpayiknedilsvptkkdgsravditnwNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19133 83 kkAFERSLKRLGLDYLDLYLIHQPFG-----------------------------DVYGAWRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQPGHVV 250
Cdd:cd19133 134 FYPDRLVDLILH--NEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGRNNLFENPVLTEIAEKYGKSVAQVI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6324694 251 ISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19133 212 LRWLIQRGIVVIPKSVRPERIAENFDIfdFELSDEDMEAI 251
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
12-291 |
1.44e-98 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 290.49 E-value: 1.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKEND-AYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCT--QHH 88
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDeTERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDdqRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPEVALDQSLKRLGLDYVDLYLMHWPArldpayiknedilsvptkKDGsravditnwnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19126 81 RTEDAFQESLDRLGLDYVDLYLIHWPG------------------KDK----------FIDTWKALEKLYASGKVKAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 169 SNFSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDapLLKEPVILEIAKKNNVQPGH 248
Cdd:cd19126 133 SNFQEHHLEELLAH--ADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG--LLSNPVLAAIGEKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6324694 249 VVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19126 209 VVLRWDIQHGVVTIPKSVHASRIKENADIfdFELSEDDMTAIDAL 253
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
14-291 |
6.04e-98 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 290.34 E-value: 6.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKEND-AYKAVLTALKDGYRHIDTAAIYRNEDQVGQA----IKDSGVPREEIFVTTKLWCTqHH 88
Cdd:cd19116 5 LNDGNEIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNS-YH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPE---VALDQSLKRLGLDYVDLYLMHWPArldpAYIKNEDILSvptkKDGSRAVDItnwNFIKTWELMQELPKTGKTKA 165
Cdd:cd19116 84 EREqvePALRESLKRLGLDYVDLYLIHWPV----AFKENNDSES----NGDGSLSDI---DYLETWRGMEDLVKLGLTRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 166 VGVSNFSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDA-------PLLKEPVILEI 238
Cdd:cd19116 153 IGVSNFNSEQINRLLSN--CNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppPRLDDPTLVAI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 239 AKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19116 231 AKKYGKTTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIfdFQLTPEEVAALNSF 285
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
12-295 |
4.91e-95 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 281.97 E-value: 4.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKE-NDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEP 90
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEgSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 91 EV--ALDQSLKRLGLDYVDLYLMHWParldpayiknedilsVPTKkdgsravditnwnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19157 82 STlkAFEASLERLGLDYLDLYLIHWP---------------VKGK-------------YKETWKALEKLYKDGRVRAIGV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 169 SNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLgsTDAPLLKEPVILEIAKKNNVQPGH 248
Cdd:cd19157 134 SNFQVHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPL--MQGQLLDNPVLKEIAEKYNKSVAQ 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6324694 249 VVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISKEK 295
Cdd:cd19157 210 VILRWDLQNGVVTIPKSIKEHRIIENADVfdFELSQEDMDKIDALNENL 258
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
14-292 |
9.99e-95 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 280.70 E-value: 9.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEV- 92
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 -ALDQSLKRLGLDYVDLYLMHWPA-RLDpayiknedilsvptkkdgsravditnwNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19132 81 rTIEESLYRLGLDYVDLYLIHWPNpSRD---------------------------LYVEAWQALIEAREEGLVRSIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStDAPLLKEPVILEIAKKNNVQPGHVV 250
Cdd:cd19132 134 FLPEHLDRLIDETG--VTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGR-GSGLLDEPVIKAIAEKHGKTPAQVV 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324694 251 ISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNIS 292
Cdd:cd19132 211 LRWHVQLGVVPIPKSANPERQRENLAIfdFELSDEDMAAIAALD 254
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
20-289 |
1.81e-91 |
|
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: 272.22 E-value: 1.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWcTQHHEPEV---ALDQ 96
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVW-RDHLRPEDlkkSVDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 97 SLKRLGLDYVDLYLMHWParldpayiknedilsvptkkdgSRAVDITNwnfikTWELMQELPKTGKTKAVGVSNFSINNL 176
Cdd:cd19073 80 SLEKLGTDYVDLLLIHWP----------------------NPTVPLEE-----TLGALKELKEAGKVKSIGVSNFTIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 177 KDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDapLLKEPVILEIAKKNNVQPGHVVISWHVQ 256
Cdd:cd19073 133 EEALDISP--LPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGE--VLRDPVIQEIAEKYDKTPAQVALRWLVQ 208
|
250 260 270
....*....|....*....|....*....|....*
gi 6324694 257 RGYVVLPKSVNPDRIKTNRKIF--TLSTEDFEAIN 289
Cdd:cd19073 209 KGIVVIPKASSEDHLKENLAIFdwELTSEDVAKID 243
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
12-291 |
1.98e-91 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 272.74 E-value: 1.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQH--HE 89
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYgyDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEVALDQSLKRLGLDYVDLYLMHWParldpayiknedilsVPTKKDgsravditnwNFIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19127 81 ALRGFDASLRRLGLDYVDLYLLHWP---------------VPNDFD----------RTIQAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 170 NFSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLG---------STDAP-LLKEPVILEIA 239
Cdd:cd19127 136 NFTPEHLERLIDATT--VVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgPTGPGdVLQDPTITGLA 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6324694 240 KKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19127 214 EKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIfdFALSAEDMAAIDAL 267
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-295 |
2.10e-90 |
|
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: 271.59 E-value: 2.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 9 TKILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKD---SGV-PREEIFVTTKLWC 84
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEV--ALDQSLKRLGLDYVDLYLMHWPARLdpayiKNEDILSVPTKKDGSRAVDItnwNFIKTWELMQELPKTGK 162
Cdd:cd19154 81 HEHAPEDVeeALRESLKKLQLEYVDLYLIHAPAAF-----KDDEGESGTMENGMSIHDAV---DVEDVWRGMEKVYDEGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 163 TKAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGS----------TDAP---L 229
Cdd:cd19154 153 TKAIGVSNFNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstGVSPapnL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324694 230 LKEPVILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISKEK 295
Cdd:cd19154 231 LQDPIVKAIAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIfdFSLSEEDMATLEEIEKSL 298
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
14-293 |
4.72e-90 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 270.64 E-value: 4.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKE---NDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAI----KDSGVPREEIFVTTKLWCTQ 86
Cdd:cd19108 5 LNDGHFIPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHePE---VALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDILsvPTKKDGSRAVDITNwnFIKTWELMQELPKTGKT 163
Cdd:cd19108 85 HR-PElvrPALEKSLKKLQLDYVDLYLIHFPVALKPG----EELF--PKDENGKLIFDTVD--LCATWEAMEKCKDAGLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 164 KAVGVSNFSINNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGST--------DAP-LLKEPV 234
Cdd:cd19108 156 KSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrdkewvdqNSPvLLEDPV 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324694 235 ILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISK 293
Cdd:cd19108 236 LCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVfeFQLTSEDMKALDGLNR 296
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-292 |
5.45e-90 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 269.19 E-value: 5.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 8 STKILSLNTGAQIPQIGLGTWQSKENDaYKAVLTALKD-GYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQ 86
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSGGYS-HEAVVYALKEcGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHEPEV--ALDQSLKRLGLDYVDLYLMHWPARLDPAYIKNEdilsvptkkdgSRAvditnwnfiKTWELMQELPKTGKTK 164
Cdd:cd19135 80 YGYESTkqAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKE-----------TRA---------ETWRALEELYDEGLCR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 165 AVGVSNFSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNV 244
Cdd:cd19135 140 AIGVSNFLIEHLEQLLEDCS--VVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAK--GKALEEPTVTELAKKYQK 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6324694 245 QPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNIS 292
Cdd:cd19135 216 TPAQILIRWSIQNGVVTIPKSTKEERIKENCQVfdFSLSEEDMATLDSLH 265
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
12-295 |
1.22e-89 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 268.23 E-value: 1.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKE-NDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCT-QHHE 89
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSdQGYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEV-ALDQSLKRLGLDYVDLYLMHWPARldpayiknedilsvptKKdgsravditnwnFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19156 81 STLaAFEESLEKLGLDYVDLYLIHWPVK----------------GK------------FKDTWKAFEKLYKEKKVRAIGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 169 SNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNVQPGH 248
Cdd:cd19156 133 SNFHEHHLEELLKSC--KVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ--GKLLSNPVLKAIGKKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6324694 249 VVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISKEK 295
Cdd:cd19156 209 VIIRWDIQHGIITIPKSVHEERIQENFDVfdFELTAEEIRQIDGLNTDH 257
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
17-288 |
1.44e-89 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 269.67 E-value: 1.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAI----KDSGVPREEIFVTTKLWCTQHHEPEV 92
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIqekiKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 --ALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDILSvptkKDGSRAVDITNWNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19107 81 kgACQKTLSDLKLDYLDLYLIHWPTGFKPG----KELFP----LDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP--------LLKEPVILEIAKKN 242
Cdd:cd19107 153 FNHLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPwakpedpsLLEDPKIKEIAAKH 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6324694 243 NVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19107 233 NKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVfdFELSSEDMATI 280
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
11-288 |
2.52e-87 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 262.70 E-value: 2.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 11 ILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEP 90
Cdd:PRK11565 6 VIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLWNDDHKRP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 91 EVALDQSLKRLGLDYVDLYLMHWParldpayiknedilsVPTKKdgsravditnwNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:PRK11565 86 REALEESLKKLQLDYVDLYLMHWP---------------VPAID-----------HYVEAWKGMIELQKEGLIKSIGVCN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPLLKEPVILEIAKKNNVQPGHVV 250
Cdd:PRK11565 140 FQIHHLQRLIDETG--VTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIV 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6324694 251 ISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:PRK11565 218 IRWHLDSGLVVIPKSVTPSRIAENFDVfdFRLDKDELGEI 257
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-291 |
5.25e-85 |
|
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: 256.03 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEV--AL 94
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFlaSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 95 DQSLKRLGLDYVDLYLMHWPARLDPayiknedilsvptkkdgsravditnwnFIKTWELMQELPKTGKTKAVGVSNFSIN 174
Cdd:cd19140 85 EESLRKLRTDYVDLLLLHWPNKDVP---------------------------LAETLGALNEAQEAGLARHIGVSNFTVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 175 NLKDLLASQGNKLtpAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGstDAPLLKEPVILEIAKKNNVQPGHVVISWH 254
Cdd:cd19140 138 LLREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA--RGEVLKDPVLQEIGRKHGKTPAQVALRWL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6324694 255 VQR-GYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19140 214 LQQeGVAAIPKATNPERLEENLDIfdFTLSDEEMARIAAL 253
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
13-293 |
2.77e-84 |
|
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: 255.62 E-value: 2.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 13 SLNTGAQIPQIGLGTWQSK--ENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKD-----SGVPREEIFVTTKLWcT 85
Cdd:cd19122 2 TLNNGVKIPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVW-N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 86 QHHEPEVAL---DQSLKRLGLDYVDLYLMHWPArldpAYIKNEDiLSVPTKKDGSRAV--DITNwNFIKTWELMQELPKT 160
Cdd:cd19122 81 HLHEPEDVKwsiDNSLKNLKLDYIDLFLVHWPI----AAEKNDQ-RSPKLGPDGKYVIlkDLTE-NPEPTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 161 GKTKAVGVSNFSINNLKDLLasQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGS------TDAPLLKEPV 234
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLL--SFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvpsTGERVSENPT 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 235 ILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNISK 293
Cdd:cd19122 233 LNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDFEAINQVAK 291
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
16-291 |
9.48e-83 |
|
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: 251.42 E-value: 9.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTW---QSKEnDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK---DSGV--PREEIFVTTKLWCTQH 87
Cdd:cd19124 1 SGQTMPVIGMGTAsdpPSPE-DIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAealRLGLvkSRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV--ALDQSLKRLGLDYVDLYLMHWPARLDP----AYIKNEDILSVPTKKdgsravditnwnfikTWELMQELPKTG 161
Cdd:cd19124 80 HPDLVlpALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsFPIEEEDFLPFDIKG---------------VWEAMEECQRLG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 162 KTKAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP-----LLKEPVIL 236
Cdd:cd19124 145 LTKAIGVSNFSCKKLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKwgsnaVMESDVLK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324694 237 EIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIF--TLSTEDFEAINNI 291
Cdd:cd19124 223 EIAAAKGKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFdwELTEEDLEKISEI 279
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
17-296 |
7.31e-82 |
|
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: 248.69 E-value: 7.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGT---WQSKENDAY-----KAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHH 88
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIqrdlvDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSPGIKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPEvALDQSLKRLGLDYVDLYLMHwparlDPAYIKNEDIlsvptkkdgsravditnwNFIKTWELMQELPKTGKTKAVGV 168
Cdd:cd19120 81 PRE-ALRKSLAKLGVDYVDLYLIH-----SPFFAKEGGP------------------TLAEAWAELEALKDAGLVRSIGV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 169 SNFSINNLKDLLASQgnKLTPAANQVEIHPLL--PQDELINFCKSKGIVVEAYSPLGST--DAPLLKEPVILEIAKKNNV 244
Cdd:cd19120 137 SNFRIEDLEELLDTA--KIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSPLtrDAGGPLDPVLEKIAEKYGV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6324694 245 QPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISKEKG 296
Cdd:cd19120 215 TPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAfdFELTEEEVEEIDKAGKQKH 268
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
14-289 |
1.95e-78 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 239.43 E-value: 1.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 14 LNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQH--HEPE 91
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHdgDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 92 VALDQSLKRLGLDYVDLYLMHWPArldpayiknedilsvPTKKdgsravditnwNFIKTWELMQELPKTGKTKAVGVSNF 171
Cdd:cd19130 84 AAFAESLAKLGLDQVDLYLVHWPT---------------PAAG-----------NYVHTWEAMIELRAAGRTRSIGVSNF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 172 SINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNVQPGHVVI 251
Cdd:cd19130 138 LPPHLERIVAATG--VVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQ--GKLLGDPPVGAIAAAHGKTPAQIVL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 6324694 252 SWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19130 214 RWHLQKGHVVFPKSVRRERMEDNLDVfdFDLTDTEIAAID 253
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
15-293 |
3.87e-78 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 240.05 E-value: 3.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKD----SGVPREEIFVTTKLWCTqHHEP 90
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEvfkaGKIRREDLFVTTKLWNT-NHRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 91 E---VALDQSLKRLGLDYVDLYLMHWPARLDPAyiKNEDilsvPTKKDGSRAVDiTNWNFIKTWELMQELPKTGKTKAVG 167
Cdd:cd19129 80 ErvkPAFEASLKRLQLDYLDLYLIHTPFAFQPG--DEQD----PRDANGNVIYD-DGVTLLDTWRAMERLVDEGRCKAIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 168 VSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAP-LLKEPVILEIAKKNNVQP 246
Cdd:cd19129 153 LSDVSLEKLREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPkLLEDPVITAIARRVNKTP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6324694 247 GHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFTLSTEDFEAINNISK 293
Cdd:cd19129 231 AQVLLAWAIQRGTALLTTSKTPSRIRENFDISTLPEDAMREINEGIK 277
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
19-293 |
5.07e-78 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 239.86 E-value: 5.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 19 QIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVG----QAIKDSGVPREEIFVTTKLWCTQHHEP--EV 92
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGagirEKIKEGVVRREDLFIVSKLWCTCHKKSlvKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 ALDQSLKRLGLDYVDLYLMHWPARLDPAYIknedilSVPTkkDGSRAVDITNWNFIKTWELMQELPKTGKTKAVGVSNFS 172
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEP------DLPL--DRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 173 INNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDA--PLLKEPVILEIAKKNNVQPGHVV 250
Cdd:cd19110 155 HEQLERLLNKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEgvDLIDDPVIQRIAKKHGKSPAQIL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6324694 251 ISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISK 293
Cdd:cd19110 235 IRFQIQRNVIVIPKSVTPSRIKENIQVfdFELTEHDMDNLLSLDR 279
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
17-293 |
1.78e-77 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 238.93 E-value: 1.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKEN----DAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK----DSGVPREEIFVTTKLWCTqHH 88
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTtpkgACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiaEGKVKREDIFYCGKLWNT-CH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPEV---ALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDILsvPTKKDGSRAVDITNwnFIKTWELMQELPKTGKTKA 165
Cdd:cd19109 80 PPELvrpTLERTLKVLQLDYVDLYIIEMPMAFKPG----DEIY--PRDENGKWLYHKTN--LCATWEALEACKDAGLVKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 166 VGVSNFSINNLKDLLASQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDA---------PLLKEPVIL 236
Cdd:cd19109 152 IGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvsspPLLEDPLLN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 237 EIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISK 293
Cdd:cd19109 232 SIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIfdFSLTEEEMKDIEALNK 290
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
12-289 |
5.54e-77 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 235.91 E-value: 5.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQH--HE 89
Cdd:cd19134 3 VTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQgfTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEVALDQSLKRLGLDYVDLYLMHWPArldpayiknedilsvptkKDGSRAVDitnwnfikTWELMQELPKTGKTKAVGVS 169
Cdd:cd19134 83 SQAACRASLERLGLDYVDLYLIHWPA------------------GREGKYVD--------SWGGLMKLREEGLARSIGVS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 170 NFSINNLKDLLASQGnkLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNVQPGHV 249
Cdd:cd19134 137 NFTAEHLENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGV--GRLLDNPAVTAIAAAHGRTPAQV 212
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6324694 250 VISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19134 213 LLRWSLQLGNVVISRSSNPERIASNLDVfdFELTADHMDALD 254
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
21-291 |
2.57e-75 |
|
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: 232.03 E-value: 2.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAI----KDSGVPREEIFVTTKLWCTqHHEPEVALDQ 96
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFseifKDGGVKREDLFITSKLWPT-MHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 97 ---SLKRLGLDYVDLYLMHWPARLDPayiknediLSVPTKKDGSRAVDITNWNFIKTWELMQELPKTGKTKAVGVSNFSI 173
Cdd:cd19128 81 lliTLQDLQLEYLDLFLIHWPLAFDM--------DTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 174 NNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPL-GSTDAP---LLKEPVILEIAKKNNVQPGHV 249
Cdd:cd19128 153 KLLTDLLNY--CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLgGSYGDGnltFLNDSELKALATKYNTTPPQV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6324694 250 VISWHVQR---GYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:cd19128 231 IIAWHLQKwpkNYSVIPKSANKSRCQQNFDIndLALTKEDMDAINTL 277
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
10-293 |
6.37e-75 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 232.38 E-value: 6.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 10 KILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK---DSG-VPREEIFVTTKLWCT 85
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAeafKTGlVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 86 QH-HEPEVALDqSLKRLGLDYVDLYLMHWPARLDPAYIKNEDILsvpTKKDGSRAVDITNwNFIKTWELMQELPKTGKTK 164
Cdd:cd19112 81 DHgHVIEACKD-SLKKLQLDYLDLYLVHFPVATKHTGVGTTGSA---LGEDGVLDIDVTI-SLETTWHAMEKLVSAGLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 165 AVGVSNFSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAPL--------LKEPVIL 236
Cdd:cd19112 156 SIGISNYDIFLTRDCLAY--SKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAewfgsvspLDDPVLK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 237 EIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNISK 293
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVfdFQLSKEDMKLIKSLDR 292
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
17-293 |
1.61e-74 |
|
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: 230.46 E-value: 1.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK---DSG-VPREEIFVTTKLWcTQHHEP-- 90
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLP-PVYLEFkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 91 -EVALDQSLKRLGLDYVDLYLMHWPArldpayiknedilSVPTKKDGSRAVDITNwNFIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19111 80 tEKSLEKSLENLKLPYVDLYLIHHPC-------------GFVNKKDKGERELASS-DVTSVWRAMEALVSEGKVKSIGLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 170 NFSINNLKDLLASqgNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGS---------TDAP-LLKEPVILEIA 239
Cdd:cd19111 146 NFNPRQINKILAY--AKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSpgranqslwPDQPdLLEDPTVLAIA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324694 240 KKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIF--TLSTEDFEAINNISK 293
Cdd:cd19111 224 KELDKTPAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFdfELTEEHFKKLKTLDR 279
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
20-288 |
2.77e-74 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 228.39 E-value: 2.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWCTQHHEPEV--ALDQS 97
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLlpSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 98 LKRLGLDYVDLYLMHWPARLDPayiknedilsVPTKkdgsravditnwnfiKTWELMQELPKTGKTKAVGVSNFSINNLK 177
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDE----------VPVE---------------EYIGALAEAKEQGLTRHIGVSNFTIALLD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 178 DLLASQGnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGStdAPLLKEPVILEIAKKNNVQPGHVVISWHVQR 257
Cdd:cd19139 136 EAIAVVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY--GKVLDDPVLAAIAERHGATPAQIALAWAMAR 212
|
250 260 270
....*....|....*....|....*....|...
gi 6324694 258 GYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19139 213 GYAVIPSSTKREHLRSNLLAldLTLDADDMAAI 245
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-286 |
6.82e-73 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 227.02 E-value: 6.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 9 TKILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIK---DSG-VPREEIFVTTKLWC 84
Cdd:cd19155 1 RNCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGkVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 T--QHHEPEVALDQSLKRLGLDYVDLYLMHWPARLdpayIKNEDIlSVPTKKDGSRAVDITNwNFIKTWELMQELPKTGK 162
Cdd:cd19155 81 GgnRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGS----LSKEDD-SGKLDPTGEHKQDYTT-DLLDIWKAMEAQVDQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 163 TKAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGS--------------TDAP 228
Cdd:cd19155 155 TRSIGLSNFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSpgaahfspgtgspsGSSP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 229 -LLKEPVILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFtlsteDFE 286
Cdd:cd19155 233 dLLQDPVVKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVF-----DFE 286
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
12-288 |
7.19e-69 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 216.93 E-value: 7.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 12 LSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQ----AIKDSGVPREEIFVTTKLWCTQH 87
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEP--EVALDQSLKRLGLDYVDLYLMHWPARLDPayiknedilsVPTKKD---GSRAVDITNWNF-----IKTWELMQEL 157
Cdd:cd19113 83 DPKnvETALNKTLSDLKLDYVDLFLIHFPIAFKF----------VPIEEKyppGFYCGDGDNFVYedvpiLDTWKALEKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 158 PKTGKTKAVGVSNFSINNLKDLLasQGNKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGS------------T 225
Cdd:cd19113 153 VDAGKIKSIGVSNFPGALILDLL--RGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPqsfvelnqgralN 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 226 DAPLLKEPVILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19113 231 TPTLFEHDTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVndFDLTKEDFEEI 295
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
17-288 |
3.75e-68 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 214.73 E-value: 3.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVG----QAIKDSGVPREEIFVTTKLWCTQHHEPEV 92
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 --ALDQSLKRLGLDYVDLYLMHWPARLdpAYIKNEDILSVPTKKDGSRAVDITNWNFIKTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19114 81 reAFDRQLKDYGLDYIDLYLIHFPIPA--AYVDPAENYPFLWKDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIGIAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 171 FSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTD-----------APLLKEPVILEIA 239
Cdd:cd19114 159 FNVQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkhlkhfTNLLEHPVVKKLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6324694 240 KKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKIFT--LSTEDFEAI 288
Cdd:cd19114 237 DKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSykLDEEDMEAL 287
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
20-305 |
5.88e-68 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 212.96 E-value: 5.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQAIKDSGVPREEIFVTTKLWcTQHHEPE---VALDQ 96
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIW-IDNLAKDkliPSLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 97 SLKRLGLDYVDLYLMHWPArldPayiknEDILSVPtkkdgsravditnwnfiktwELMQEL---PKTGKTKAVGVSNFSI 173
Cdd:PRK11172 82 SLQKLRTDYVDLTLIHWPS---P-----NDEVSVE--------------------EFMQALleaKKQGLTREIGISNFTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 174 NNLKDLLASQGnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTDAplLKEPVILEIAKKNNVQPGHVVISW 253
Cdd:PRK11172 134 ALMKQAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKV--LKDPVIARIAAKHNATPAQVILAW 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324694 254 HVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNIskEKGEKRV----VHPNW 305
Cdd:PRK11172 211 AMQLGYSVIPSSTKRENLASNLLAqdLQLDAEDMAAIAAL--DRNGRLVspegLAPEW 266
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
8-288 |
1.46e-67 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 213.44 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 8 STKILSLNTGAQIPQIGLGTWQSKENDAYKAVLTALKDGYRHIDTAAIYRNEDQVGQ----AIKDSGVPREEIFVTTKLW 83
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQgvarAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 84 CTQHHEPEV--ALDQSLKRLGLDYVDLYLMHWPARL---DPAyiknedILSVPTKKDGSRAVDITNWNFIKTWELMQELP 158
Cdd:cd19115 81 NTFHDGERVepICRKQLADWGIDYFDLFLIHFPIALkyvDPA------VRYPPGWFYDGKKVEFSNAPIQETWTAMEKLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 159 KTGKTKAVGVSNFSINNLKDLLASQgnKLTPAANQVEIHPLLPQDELINFCKSKGIVVEAYSPLGSTD------------ 226
Cdd:cd19115 155 DKGLARSIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSfleldlpgakdt 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324694 227 APLLKEPVILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAI 288
Cdd:cd19115 233 PPLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVtgFDLEAEEIKAI 296
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
17-289 |
2.69e-58 |
|
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: 188.21 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTW---------QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKdsGVPREEIFVTTKLWC 84
Cdd:cd19072 1 GEEVPVLGLGTWgigggmskdYSDDKKAIEALRYAIELGINLIDTAEMYgggHAEELVGKAIK--GFDREDLFITTKVSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEV--ALDQSLKRLGLDYVDLYLMHWParlDPayiknedilSVPTKkdgsravditnwnfiKTWELMQELPKTGK 162
Cdd:cd19072 79 DHLKYDDVikAAKESLKRLGTDYIDLYLIHWP---NP---------SIPIE---------------ETLRAMEELVEEGK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 163 TKAVGVSNFSINNLKDLLASQGNKlTPAANQVEIHpLL---PQDELINFCKSKGIVVEAYSPLGSTDAPLLKE-PVILEI 238
Cdd:cd19072 132 IRYIGVSNFSLEELEEAQSYLKKG-PIVANQVEYN-LFdreEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGsPLLDEI 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6324694 239 AKKNNVQPGHVVISWHVQR-GYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19072 210 AKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGAlgWELSEEDLQRLD 263
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
10-289 |
2.12e-54 |
|
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: 178.21 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 10 KILSLNTGAQIPQIGLGTWQ-----SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFVTTK 81
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYmgedpAKRAQEIEALRAGIDLGMTLIDTAEMYgdgGSEELVGEAIRGR---RDKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 LWcTQHHEPE---VALDQSLKRLGLDYVDLYLMHWPArldpayiknedilSVPTKkdgsravditnwnfiKTWELMQELP 158
Cdd:cd19138 78 VL-PSNASRQgtvRACERSLRRLGTDYLDLYLLHWRG-------------GVPLA---------------ETVAAMEELK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 159 KTGKTKAVGVSNFSINNLKDLLASQGNKlTPAANQVEIHplLPQD----ELINFCKSKGIVVEAYSPL---GSTDAPLLK 231
Cdd:cd19138 129 KEGKIRAWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLaqgGLLRRGLLE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324694 232 EPVILEIAKKNNVQPGHVVISWHVQRGYVV-LPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19138 206 NPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAadLELTEEDLAELD 266
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
23-291 |
6.08e-54 |
|
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: 177.89 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 23 IGLGTWQ-------SKENDAYKAVLTALKDGYRHIDTAAIYR---NEDQVGQAIKDSGVPREEIFVTTKLWCTQH----- 87
Cdd:pfam00248 1 IGLGTWQlgggwgpISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVPDGDGpwpsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV---ALDQSLKRLGLDYVDLYLMHWParlDPayiknedilsvptkkdgsravditNWNFIKTWELMQELPKTGKTK 164
Cdd:pfam00248 81 GSKENirkSLEESLKRLGTDYIDLYYLHWP---DP------------------------DTPIEETWDALEELKKEGKIR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 165 AVGVSNFSINNLKDLLASqgNKLTPAANQVEIHPL--LPQDELINFCKSKGIVVEAYSPLGS------------------ 224
Cdd:pfam00248 134 AIGVSNFDAEQIEKALTK--GKIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpger 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324694 225 -------TDAPLLKEPVILEIAKKNNVQPGHVVISWHVQ--RGYVVLPKSVNPDRIKTNRKI--FTLSTEDFEAINNI 291
Cdd:pfam00248 212 rrllkkgTPLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGAleFPLSDEEVARIDEL 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
17-289 |
1.54e-41 |
|
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: 144.64 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQ---------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgVPREEIFVTTKLWC 84
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEV--ALDQSLKRLGLDYVDLYLMHWParldpayikNEDIlsvptkkdgsravditnwNFIKTWELMQELPKTGK 162
Cdd:cd19137 79 TNLRYDDLlrSLQNSLRRLDTDYIDLYLIHWP---------NPNI------------------PLEETLSAMAEGVRQGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 163 TKAVGVSNFsinNLKDLLASQGNKLTP-AANQVE---IHPLLPQDELINFCKSKGIVVEAYSPLGSTdaPLLKEPVILEI 238
Cdd:cd19137 132 IRYIGVSNF---NRRLLEEAISKSQTPiVCNQVKynlEDRDPERDGLLEYCQKNGITVVAYSPLRRG--LEKTNRTLEEI 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6324694 239 AKKNNVQPGHVVISWHVQRGYVV-LPKSVNPDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19137 207 AKNYGKTIAQIALAWLIQKPNVVaIPKAGRVEHLKENLKAteIKLSEEEMKLLD 260
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
19-289 |
5.45e-41 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 144.29 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 19 QIPQIGLGTWQ-----------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGvPREEIFVTTKL-- 82
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELG-DRDEVVIATKFap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 --WCTQHHEPEVALDQSLKRLGLDYVDLYLMHWPArldPAYIKNEDIlsvptkkdgsravditnwnfiktWELMQELPKT 160
Cdd:cd19093 80 lpWRLTRRSVVKALKASLERLGLDSIDLYQLHWPG---PWYSQIEAL-----------------------MDGLADAVEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 161 GKTKAVGVSNFSINNLK---DLLASQGnkLTPAANQVE---IHPLLPQDELINFCKSKGIVVEAYSPLG----------- 223
Cdd:cd19093 134 GLVRAVGVSNYSADQLRrahKALKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkyspe 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 ----------------STDAPLLKEpvILEIAKKNNVQPGHVVISWHVQRGYVVLPKSVNPDRIKTNRKI--FTLSTEDF 285
Cdd:cd19093 212 npppggrrrlfgrknlEKVQPLLDA--LEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGAlgWRLSEEEV 289
|
....
gi 6324694 286 EAIN 289
Cdd:cd19093 290 AELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
15-297 |
2.33e-40 |
|
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: 143.01 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTWQ-------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgVPREEIFVTTKLWC 84
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALKG--RPRDDVVIATKVGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEV----------ALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDilsvptkkdgsravditnwnfikTWELM 154
Cdd:COG0667 86 RMGPGPNGrglsrehirrAVEASLRRLGTDYIDLYQLHRPDPDTPI----EE-----------------------TLGAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 155 QELPKTGKTKAVGVSNFSINNLKDLLASQGNKLTPAANQVEIHPL--LPQDELINFCKSKGIVVEAYSPLGS-------- 224
Cdd:COG0667 139 DELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNEYSLLdrSAEEELLPAARELGVGVLAYSPLAGglltgkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 225 --------------------TDAPLLKEPVILEIAKKNNVQPGHVVISWHVQRGYV--VLPKSVNPDRIKTNRKI--FTL 280
Cdd:COG0667 219 rgatfpegdraatnfvqgylTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAadLEL 298
|
330
....*....|....*..
gi 6324694 281 STEDFEAINNISKEKGE 297
Cdd:COG0667 299 SAEDLAALDAALAAVPA 315
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
20-294 |
2.07e-39 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 140.03 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQ---------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgvPREEIFVTTKLWcTQH 87
Cdd:cd19085 1 VSRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALKG---RRDDVVIATKVS-PDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPE---VALDQSLKRLGLDYVDLYLMHWParldpayiknedilsvptkkdgSRAVDITnwnfiKTWELMQELPKTGKTK 164
Cdd:cd19085 77 LTPEdvrKSCERSLKRLGTDYIDLYQIHWP----------------------SSDVPLE-----ETMEALEKLKEEGKIR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 165 AVGVSNFSINNLKDLLASQgnklTPAANQVEIHPLL--PQDELINFCKSKGIVVEAYSPLGS------------------ 224
Cdd:cd19085 130 AIGVSNFGPAQLEEALDAG----RIDSNQLPYNLLWraIEYEILPFCREHGIGVLAYSPLAQglltgkfssaedfppgda 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 225 -TDAPLLKEP-----------VILEIAKKNNVQPGHVVISWHVQRGYV--VLPKSVNPDRIKTNRKIFT--LSTEDFEAI 288
Cdd:cd19085 206 rTRLFRHFEPgaeeetfealeKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDleLSPSVLERL 285
|
....*.
gi 6324694 289 NNISKE 294
Cdd:cd19085 286 DEISDP 291
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
21-224 |
4.86e-37 |
|
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: 131.87 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTWQ----SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVpREEIFVTTKLWCTQHHEPEV- 92
Cdd:cd06660 1 SRLGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGGHPPGGDPSRs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 ---------ALDQSLKRLGLDYVDLYLMHWParlDPayiknedilSVPtkkdgsraVDitnwnfiKTWELMQELPKTGKT 163
Cdd:cd06660 80 rlspehirrDLEESLRRLGTDYIDLYYLHRD---DP---------STP--------VE-------ETLEALNELVREGKI 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324694 164 KAVGVSNFSINNLKDLL--ASQGNKLTPAANQVEIHPLLPQ---DELINFCKSKGIVVEAYSPLGS 224
Cdd:cd06660 133 RYIGVSNWSAERLAEALayAKAHGLPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-289 |
4.61e-35 |
|
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: 128.80 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTWQ--------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFVTTK---L 82
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYgfgHSEEILGKALKGR---RDDVVIATKcglR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 WCTQHH-----EPEV---ALDQSLKRLGLDYVDLYLMHWParlDPAyiknedilsVPtkkdgsravditnwnFIKTWELM 154
Cdd:cd19084 78 WDGGKGvtkdlSPESirkEVEQSLRRLQTDYIDLYQIHWP---DPN---------TP---------------IEETAEAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 155 QELPKTGKTKAVGVSNFSINNLKDLLasqgnKLTP-AANQVEIHPLLPQ--DELINFCKSKGIVVEAYSPLG-------- 223
Cdd:cd19084 131 EKLKKEGKIRYIGVSNFSVEQLEEAR-----KYGPiVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAqglltgky 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 -------STDA----PLLKEP----------VILEIAKKNNVQPGHVVISWHVQRGYV--VLPKSVNPDRIKTNRKI--F 278
Cdd:cd19084 206 kkeptfpPDDRrsrfPFFRGEnfeknleivdKLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGAKNPEQLEENAGAldW 285
|
330
....*....|.
gi 6324694 279 TLSTEDFEAIN 289
Cdd:cd19084 286 ELTEEELKEID 296
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-289 |
6.97e-32 |
|
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: 120.47 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTW-------------QSkENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFVTTK-- 81
Cdd:cd19102 1 LTTIGLGTWaiggggwgggwgpQD-DRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 -LW-----CTQHHEPE---VALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDilsvptkkdgsravditnwnfikTWE 152
Cdd:cd19102 77 lLWdeegrIRRSLKPAsirAECEASLRRLGVDVIDLYQIHWPDPDEPI----EE-----------------------AWG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 153 LMQELPKTGKTKAVGVSNFSINNLKDLLAsqgnkltpaanqveIHP---LLPQ---------DELINFCKSKGIVVEAYS 220
Cdd:cd19102 130 ALAELKEEGKVRAIGVSNFSVDQMKRCQA--------------IHPiasLQPPysllrrgieAEILPFCAEHGIGVIVYS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 221 PLGS---------------------TDAPLLKEP----------VILEIAKKNNVQPGHVVISWHVQRGYV--VLPKSVN 267
Cdd:cd19102 196 PMQSglltgkmtpervaslpaddwrRRSPFFQEPnlarnlalvdALRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARR 275
|
330 340
....*....|....*....|....
gi 6324694 268 PDRIKTNRKI--FTLSTEDFEAIN 289
Cdd:cd19102 276 PDQIDETVGAadLRLTPEELAEIE 299
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
15-294 |
1.40e-29 |
|
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: 114.85 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTW--------QSKENDAYKAVLTALKDGYRHIDTAAIYR-NEDQVGQAIKDSGVPREEIFVTTKLWCT 85
Cdd:cd19144 8 RNGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPGKREKIFLATKFGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 86 Q---------HHEPEV---ALDQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPTKkdgsravditnwnfiKTWEL 153
Cdd:cd19144 88 KnvetgeysvDGSPEYvkkACETSLKRLGVDYIDLYYQH---RVDG---------KTPIE---------------KTVAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 154 MQELPKTGKTKAVGVSNFSINNLKdllasQGNKLTP-AANQVEIHPLL-----PQDELINFCKSKGIVVEAYSPLG---- 223
Cdd:cd19144 141 MAELVQEGKIKHIGLSECSAETLR-----RAHAVHPiAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGrgfl 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 -----STD----------APLLKE---PVILE-------IAKKNNVQPGHVVISWHVQRG--YVVLPKSVNPDRIKTNRK 276
Cdd:cd19144 216 tgairSPDdfeegdfrrmAPRFQAenfPKNLElvdkikaIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLG 295
|
330 340
....*....|....*....|
gi 6324694 277 IFT--LSTEDFEAINNISKE 294
Cdd:cd19144 296 ALKvkLTEEEEKEIREIAEE 315
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-276 |
6.90e-28 |
|
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: 109.18 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTWQSKEN-----DAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSGVPREEIFVTTK----- 81
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWgesaeELLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKcgirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 -----LWCTQH--HEPE---VALDQSLKRLGLDYVDLYLMHWPARL-DPayiknEDIlsvptkkdgSRAvditnwnfikt 150
Cdd:cd19092 81 gddprPGRIKHydTSKEhilASVEGSLKRLGTDYLDLLLLHRPDPLmDP-----EEV---------AEA----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 151 welMQELPKTGKTKAVGVSNFSINNLkDLLASQGN-KLtpAANQVEIHPL---LPQDELINFCKSKGIVVEAYSPLG--- 223
Cdd:cd19092 136 ---FDELVKSGKVRYFGVSNFTPSQI-ELLQSYLDqPL--VTNQIELSLLhteAIDDGTLDYCQLLDITPMAWSPLGggr 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 --STDAPLLKE--PVILEIAKKNNVQPGHVVISW---HVQRGYVVLpKSVNPDRIKTNRK 276
Cdd:cd19092 210 lfGGFDERFQRlrAALEELAEEYGVTIEAIALAWllrHPARIQPIL-GTTNPERIRSAVK 268
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-216 |
2.27e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 106.80 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT---WQSKENDAYKAVLTALKDGYRHIDTAAIYRN-EDQVGQAIKDsgvPREEIFVTTKLWCTQHHEP 90
Cdd:cd19100 6 RTGLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG---RRDKVFLATKTGARDYEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 91 EVALDQSLKRLGLDYVDLYLMHwparldpaYIKNEDILSVPTKKDGsravditnwnfikTWELMQELPKTGKTKAVGVSN 170
Cdd:cd19100 83 KRDLERSLKRLGTDYIDLYQLH--------AVDTEEDLDQVFGPGG-------------ALEALLEAKEEGKIRFIGISG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324694 171 FSINNLKDLLASQG-NKLTPAANQVEIHPLLPQDELINFCKSKGIVV 216
Cdd:cd19100 142 HSPEVLLRALETGEfDVVLFPINPAGDHIDSFREELLPLAREKGVGV 188
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
15-222 |
1.74e-26 |
|
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: 106.20 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTW---------QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFVTTKl 82
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYgfgHSEEIVGKAIKGR---RDKVVLATK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 wC--------TQHH------------EPE---VALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDilsvptkkdgsra 139
Cdd:cd19149 82 -CglrwdregGSFFfvrdgvtvyknlSPEsirEEVEQSLKRLGTDYIDLYQTHWQDVETPI----EE------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 140 vditnwnfikTWELMQELPKTGKTKAVGVSNFSINNLKDLLASqGNkltPAANQVEIHPLLPQ--DELINFCKSKGIVVE 217
Cdd:cd19149 144 ----------TMEALEELKRQGKIRAIGASNVSVEQIKEYVKA-GQ---LDIIQEKYSMLDRGieKELLPYCKKNNIAFQ 209
|
....*
gi 6324694 218 AYSPL 222
Cdd:cd19149 210 AYSPL 214
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
15-263 |
1.21e-25 |
|
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: 103.45 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLG----TW---QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgvPREEIFVTTKLWC 84
Cdd:cd19076 7 TQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKFGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEV------------ALDQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPTKkdgsravditnwnfiKTWE 152
Cdd:cd19076 84 VRDPGSGFrgvdgrpeyvraACEASLKRLGTDVIDLYYQH---RVDP---------NVPIE---------------ETVG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 153 LMQELPKTGKTKAVGVSNFSINNLKdllasQGNKLTP-AANQVEIHPLL--PQDELINFCKSKGIVVEAYSPLG------ 223
Cdd:cd19076 137 AMAELVEEGKVRYIGLSEASADTIR-----RAHAVHPiTAVQSEYSLWTrdIEDEVLPTCRELGIGFVAYSPLGrgfltg 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 224 ---STD----------------------APLLKEpvILEIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19076 212 aikSPEdlpeddfrrnnprfqgenfdknLKLVEK--LEAIAAEKGCTPAQLALAWVLAQGDDIVP 274
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
16-291 |
1.87e-25 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 103.27 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGT---------WQSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGvpREEIFVTTKlw 83
Cdd:cd19083 7 SDIDVNPIGLGTnavgghnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLKEYN--RNEVVIATK-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 84 cTQH----------HEPEV---ALDQSLKRLGLDYVDLYLMHWParlDPAYIKNEdilsvptkkdgsrAVDItnwnfikt 150
Cdd:cd19083 83 -GAHkfggdgsvlnNSPEFlrsAVEKSLKRLNTDYIDLYYIHFP---DGETPKAE-------------AVGA-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 151 welMQELPKTGKTKAVGVSNFSINNLKDllasqGNKltpaANQVEI----HPLLPQD---ELINFCKSKGIVVEAYSPLG 223
Cdd:cd19083 138 ---LQELKDEGKIRAIGVSNFSLEQLKE-----ANK----DGYVDVlqgeYNLLQREaeeDILPYCVENNISFIPYFPLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 S-------------------TDAPLLKEPVILE----------IAKKNNVQPGHVVISWHVQRGYV--VLPKSVNPDRIK 272
Cdd:cd19083 206 SgllagkytkdtkfpdndlrNDKPLFKGERFSEnldkvdklksIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVI 285
|
330 340
....*....|....*....|.
gi 6324694 273 TNRKIF--TLSTEDFEAINNI 291
Cdd:cd19083 286 DNLKALdvTLTEEEIAFIDAL 306
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
19-224 |
2.91e-25 |
|
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: 101.01 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 19 QIPQIGLGTWQ--------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgvPREEIFVTTKLWCTQH 87
Cdd:cd19086 2 EVSEIGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKG---RRDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV-----------ALDQSLKRLGLDYVDLYLMHWParlDPAYIKNEDIlsvptkkdgsravditnwnfiktWELMQE 156
Cdd:cd19086 79 GGPERpqdfspeyireAVEASLKRLGTDYIDLYQLHNP---PDEVLDNDEL-----------------------FEALEK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 157 LPKTGKTKAVGVSNFSINNLKDLLASQGnkltPAANQVEIHPL--LPQDELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19086 133 LKQEGKIRAYGVSVGDPEEALAALRRGG----IDVVQVIYNLLdqRPEEELFPLAEEHGVGVIARVPLAS 198
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
15-263 |
1.05e-22 |
|
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: 95.73 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT----------WQSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSGvPREEIFVTTK 81
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 LWCTQHHEPEV----------ALDQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPtkkdgsravditnwnFIKTW 151
Cdd:cd19079 86 VYFPMGDGPNGrglsrkhimaEVDASLKRLGTDYIDLYQIH---RWDY---------ETP---------------IEETL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 152 ELMQELPKTGKTKAVGVSNFSINNLKDLL-ASQGNKLTPAANQVEIHPLLPQD---ELINFCKSKGIVVEAYSPLGS--- 224
Cdd:cd19079 139 EALHDVVKSGKVRYIGASSMYAWQFAKALhLAEKNGWTKFVSMQNHYNLLYREeerEMIPLCEEEGIGVIPWSPLARgrl 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324694 225 --------------TDAPLLKE--------PVIL---EIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19079 219 arpwgdtterrrstTDTAKLKYdyfteadkEIVDrveEVAKERGVSMAQVALAWLLSKPGVTAP 282
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-169 |
1.31e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 94.19 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT-WQSKENDAykAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKdsGVPREEIFVTTKLWCTQ---- 86
Cdd:cd19105 8 KTGLKVSRLGFGGgGLPRESPE--LLRRALDLGINYFDTAEGYgngNSEEIIGEALK--GLRRDKVFLATKASPRLdkkd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHEPEVALDQSLKRLGLDYVDLYLMHwpARLDPAYI-KNEDILsvptkkdgsravditnwnfiktwELMQELPKTGKTKA 165
Cdd:cd19105 84 KAELLKSVEESLKRLQTDYIDIYQLH--GVDTPEERlLNEELL-----------------------EALEKLKKEGKVRF 138
|
....
gi 6324694 166 VGVS 169
Cdd:cd19105 139 IGFS 142
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
15-302 |
3.06e-22 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 95.27 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTW--QSKENDAYKAVL-TALKDGYRHIDTAAIYRN-EDQVGQAIKDsgvPREEIFVTTKL--WCTQHH 88
Cdd:COG1453 8 KTGLEVSVLGFGGMrlPRKDEEEAEALIrRAIDNGINYIDTARGYGDsEEFLGKALKG---PRDKVILATKLppWVRDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 89 EPEVALDQSLKRLGLDYVDLYLMHwparldpaYIKNEDILSVPTKKDGsravditnwnfikTWELMQELPKTGKTKAVGV 168
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIH--------GLNTEEDLEKVLKPGG-------------ALEALEKAKAEGKIRHIGF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 169 SNF-SINNLKDLLASqgnkltpaaNQVE---IH--PLL----PQDELINFCKSKGIVVEAYSPL--GStdapLLKEP-VI 235
Cdd:COG1453 144 STHgSLEVIKEAIDT---------GDFDfvqLQynYLDqdnqAGEEALEAAAEKGIGVIIMKPLkgGR----LANPPeKL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 236 LEIAKKNNV-----------QPGHVVISWHVQrgyvvlpksvNPDRIKTNRKIF----TLSTEDFEAINNISKEKGEKRV 300
Cdd:COG1453 211 VELLCPPLSpaewalrfllsHPEVTTVLSGMS----------TPEQLDENLKTAdnlePLTEEELAILERLAEELGELLK 280
|
..
gi 6324694 301 VH 302
Cdd:COG1453 281 DF 282
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
23-222 |
3.86e-22 |
|
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: 93.91 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 23 IGLGTWQ--------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGvPREEIFVTTKLWCTQHHEPE 91
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALKEYG-KRDRVVIATKVGLEWDEGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 92 VA-----------LDQSLKRLGLDYVDLYLMHWPARLDPayiknedilsvptkkdgsravditnwnFIKTWELMQELPKT 160
Cdd:cd19148 86 VVrnssparirkeVEDSLRRLQTDYIDLYQVHWPDPLVP---------------------------IEETAEALKELLDE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324694 161 GKTKAVGVSNFSINNLKD------LLASQgnkltPAANQVEIH---PLLPqdelinFCKSKGIVVEAYSPL 222
Cdd:cd19148 139 GKIRAIGVSNFSPEQMETfrkvapLHTVQ-----PPYNLFEREiekDVLP------YARKHNIVTLAYGAL 198
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
20-263 |
8.35e-22 |
|
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: 92.28 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQ---------SKENDAYKAVL-TALKDGYRHIDTAAIY---RNEDQVGQAIKDSGvprEEIFVTTKL---- 82
Cdd:cd19088 1 VSRLGYGAMRltgpgiwgpPADREEAIAVLrRALELGVNFIDTADSYgpdVNERLIAEALHPYP---DDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 ----WCTQHHEPEV---ALDQSLKRLGLDYVDLYLMHWParlDPAYiKNEDILSVptkkdgsravditnwnfiktwelMQ 155
Cdd:cd19088 78 tgpgWWGPDGSPEYlrqAVEASLRRLGLDRIDLYQLHRI---DPKV-PFEEQLGA-----------------------LA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 156 ELPKTGKTKAVGVSNFSINNLKdllasQGNKLTP-AANQVEIHPLLPQDE-LINFCKSKGIVVEAYSPLGStDAPLLKEP 233
Cdd:cd19088 131 ELQDEGLIRHIGLSNVTVAQIE-----EARAIVRiVSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGG-GDLAQPGG 204
|
250 260 270
....*....|....*....|....*....|
gi 6324694 234 VILEIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19088 205 LLAEVAARLGATPAQVALAWLLARSPVMLP 234
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-222 |
6.54e-20 |
|
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: 87.65 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKdsGVPREEIFVTTKL-WCTQH 87
Cdd:cd19074 1 GLKVSELSLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEVAL---------DQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPTKkdgsravditnwnfiKTWELMQELP 158
Cdd:cd19074 79 GPNDRGLsrkhifesiHASLKRLQLDYVDIYYCH---RYDP---------ETPLE---------------ETVRAMDDLI 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324694 159 KTGKTKAVGVSNFSINNLKDL--LASQGNKLTPAANQVEIHPLL--PQDELINFCKSKGIVVEAYSPL 222
Cdd:cd19074 132 RQGKILYWGTSEWSAEQIAEAhdLARQFGLIPPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPL 199
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
15-292 |
1.40e-19 |
|
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: 87.28 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT--------WQSK-----ENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFV 78
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAwggvdQEEADRLVDIALDAGINFFDTADVYsegESEEILGKALKGR---RDDVLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 79 TTKLW-----------CTQHHEPEvALDQSLKRLGLDYVDLYLMHWPARLDPayiknedilsvptkkdgsravditnwnF 147
Cdd:cd19091 85 ATKVRgrmgegpndvgLSRHHIIR-AVEASLKRLGTDYIDLYQLHGFDALTP---------------------------L 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 148 IKTWELMQELPKTGKTKAVGVSNFSINNLKDLLA-SQGNKLT-PAANQVEiHPLLPQD---ELINFCKSKGIVVEAYSPL 222
Cdd:cd19091 137 EETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGiSERRGLArFVALQAY-YSLLGRDlehELMPLALDQGVGLLVWSPL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 223 G-----------------------STDAPLLKEP-------VILEIAKKNNVQPGHVVISWHVQRGYVVlpkSV-----N 267
Cdd:cd19091 216 AggllsgkyrrgqpapegsrlrrtGFDFPPVDRErgydvvdALREIAKETGATPAQVALAWLLSRPTVS---SViigarN 292
|
330 340
....*....|....*....|....*..
gi 6324694 268 PDRIKTNRKI--FTLSTEDFEAINNIS 292
Cdd:cd19091 293 EEQLEDNLGAagLSLTPEEIARLDKVS 319
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
15-263 |
1.47e-18 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 84.19 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT----WQSKENDAYkAVLTALKD-GYRHIDTAAIY----------RNEDQVGQAIKDSGvPREEIFVT 79
Cdd:cd19081 4 RTGLSVSPLCLGTmvfgWTADEETSF-ALLDAFVDaGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 80 TKLWCtqHHEPEV----------ALDQSLKRLGLDYVDLYLMHWParlDPAyiknedilsVPTKkdgsravditnwnfiK 149
Cdd:cd19081 82 TKVGF--PMGPNGpglsrkhirrAVEASLRRLQTDYIDLYQAHWD---DPA---------TPLE---------------E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 150 TWELMQELPKTGKTKAVGVSNFSINNLKDLL--ASQGNKLTPAANQVEiHPLLPQD----ELINFCKSKGIVVEAYSPLG 223
Cdd:cd19081 133 TLGALNDLIRQGKVRYIGASNYSAWRLQEALelSRQHGLPRYVSLQPE-YNLVDREsfegELLPLCREEGIGVIPYSPLA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324694 224 S--------TDAPLLKEPV---------------IL----EIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19081 212 GgfltgkyrSEADLPGSTRrgeaakrylnerglrILdaldEVAAEHGATPAQVALAWLLARPGVTAP 278
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
21-224 |
2.25e-18 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 82.67 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTWQSKEN-------DAYKAVLTALKDGYRHIDTAAIY-RNEDQVGQAIkdSGVPREEIFVTTKLWCT-----QH 87
Cdd:cd19095 1 SVLGLGTSGIGRVwgvpseaEAARLLNTALDLGINLIDTAPAYgRSEERLGRAL--AGLRRDDLFIATKVGTHgeggrDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEVA-----LDQSLKRLGLDYVDLYLMHWPARLDpayiKNEDILsvptkkdgsravditnwnfiktwELMQELPKTGK 162
Cdd:cd19095 79 KDFSPAairasIERSLRRLGTDYIDLLQLHGPSDDE----LTGEVL-----------------------ETLEDLKAAGK 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324694 163 TKAVGVSNFSiNNLKDLLASqgNKLTpaANQVEIHPLLP-QDELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19095 132 VRYIGVSGDG-EELEAAIAS--GVFD--VVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLAN 189
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
32-290 |
5.07e-18 |
|
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: 82.67 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 32 ENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDsgvPREEIFVTTKL----------WCTQHHEPEV---ALD 95
Cdd:cd19078 24 KEEMIELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFgfkidggkpgPLGLDSRPEHirkAVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 96 QSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPTKkdgsravDITNWnfiktwelMQELPKTGKTKAVGVSNFSINN 175
Cdd:cd19078 101 GSLKRLQTDYIDLYYQH---RVDP---------NVPIE-------EVAGT--------MKELIKEGKIRHWGLSEAGVET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 176 LKdllasQGNKLTP-AANQVEIHPLL--PQDELINFCKSKGIVVEAYSPLG---------------STD----------- 226
Cdd:cd19078 154 IR-----RAHAVCPvTAVQSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdEGDdraslprftpe 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 227 -----APLLKepVILEIAKKNNVQPGHVVISWHV-QRGYVV-LPKSVNPDRIKTNrkI----FTLSTEDFEAINN 290
Cdd:cd19078 229 aleanQALVD--LLKEFAEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEEN--IgaadIELTPEELREIED 299
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
21-224 |
7.28e-18 |
|
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: 81.83 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGT------WQSKEND-AYKAVLTALKDGYRHIDTAAIYRN-EDQVGQAIKdsGVPREEIFVTTKLWCtqHHEPEV 92
Cdd:cd19090 1 SALGLGTaglggvFGGVDDDeAVATIRAALDLGINYIDTAPAYGDsEERLGLALA--ELPREPLVLSTKVGR--LPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 93 ---------ALDQSLKRLGLDYVDLYLMHwparlDPAYIKNEDILSVptkkdgSRAVditnwnfiktwELMQELPKTGKT 163
Cdd:cd19090 77 dysadrvrrSVEESLERLGRDRIDLLMIH-----DPERVPWVDILAP------GGAL-----------EALLELKEEGLI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 164 KAVGVSNFSINNLKDLLASqG--------NKLTPAANQVEihpllpqDELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19090 135 KHIGLGGGPPDLLRRAIET-GdfdvvltaNRYTLLDQSAA-------DELLPAAARHGVGVINASPLGM 195
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
15-223 |
2.68e-17 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 80.29 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT-------WQSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKdsGVPREEIFVTTKlwc 84
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK--GIPRDSYYLATK--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEVA-------------LDQSLKRLGLDYVDLYLMHwparlDPAYIKNEDIlsvptkkdgsravdITNwnfiKTW 151
Cdd:cd19163 83 VGRYGLDPDkmfdfsaeritksVEESLKRLGLDYIDIIQVH-----DIEFAPSLDQ--------------ILN----ETL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 152 ELMQELPKTGKTKAVGVSNFSINNLKDLLASqgnkltpAANQVEI------HPLLPQ--DELINFCKSKGIVVEAYSPLG 223
Cdd:cd19163 140 PALQKLKEEGKVRFIGITGYPLDVLKEVLER-------SPVKIDTvlsychYTLNDTslLELLPFFKEKGVGVINASPLS 212
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
15-222 |
3.10e-17 |
|
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: 80.38 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTWQ--SKEND---AYKAVLTALKDGYRHIDTAAIY-----RNEDQVGQAIK-DSGVPREEIFVTTKL- 82
Cdd:cd19089 6 RSGLHLPAISLGLWHnfGDYTSpeeARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKrDLRPYRDELVISTKAg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 ----------WCTQHHEPEvALDQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPTKkdgsravditnwnfiktwE 152
Cdd:cd19089 86 ygmwpgpygdGGSRKYLLA-SLDQSLKRMGLDYVDIFYHH---RYDP---------DTPLE------------------E 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 153 LMQELP---KTGKTKAVGVSNFS---INNLKDLLASQGNKLtpAANQVEIHpLL---PQDELINFCKSKGIVVEAYSPL 222
Cdd:cd19089 135 TMTALAdavRSGKALYVGISNYPgakARRAIALLRELGVPL--IIHQPRYS-LLdrwAEDGLLEVLEEAGIGFIAFSPL 210
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
21-182 |
7.49e-17 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 78.37 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGT------WQSK--ENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDsgVPREEIFVTTKLWCTQHHE 89
Cdd:cd19096 1 SVLGFGTmrlpesDDDSidEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLPPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEVA---LDQSLKRLGLDYVDLYLMHWPARLD-PAYIKNEDIlsvptkkdgsravditnwnfiktWELMQELPKTGKTKA 165
Cdd:cd19096 79 AEDFrriLEESLKRLGVDYIDFYLLHGLNSPEwLEKARKGGL-----------------------LEFLEKAKKEGLIRH 135
|
170
....*....|....*....
gi 6324694 166 VGVSnF--SINNLKDLLAS 182
Cdd:cd19096 136 IGFS-FhdSPELLKEILDS 153
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
22-170 |
3.87e-16 |
|
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: 77.61 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 22 QIGLGT--W--QSKENDAYKAVLTALKDGYRHIDTAAIY----------RNEDQVGQAIKDSGvPREEIFVTTKLwCTQH 87
Cdd:cd19094 3 EICLGTmtWgeQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKV-AGPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV---------------ALDQSLKRLGLDYVDLYLMHWPARLDPAYIKNEDilsvpTKKDGSRAVDitnwNFIKTWE 152
Cdd:cd19094 81 EGITWprgggtrldrenireAVEGSLKRLGTDYIDLYQLHWPDRYTPLFGGGYY-----TEPSEEEDSV----SFEEQLE 151
|
170
....*....|....*...
gi 6324694 153 LMQELPKTGKTKAVGVSN 170
Cdd:cd19094 152 ALGELVKAGKIRHIGLSN 169
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
15-223 |
7.74e-16 |
|
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: 76.46 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTW----QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvpREEIFVTTKLWCTQH 87
Cdd:cd19087 8 RTGLKVSRLCLGTMnfggRTDEETSFAIMDRALDAGINFFDTADVYgggRSEEIIGRWIAGR---RDDIVLATKVFGPMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV----------ALDQSLKRLGLDYVDLYLMHwpaRLDPAyiknedilsvptkkdgsravdiTNWNfiKTWELMQEL 157
Cdd:cd19087 85 DDPNDrglsrrhirrAVEASLRRLQTDYIDLYQMH---HFDRD----------------------TPLE--ETLRALDDL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324694 158 PKTGKTKAVGVSNFSINNL-KDLLASQGNKLTPAanqVEIHPL------LPQDELINFCKSKGIVVEAYSPLG 223
Cdd:cd19087 138 VRQGKIRYIGVSNFAAWQIaKAQGIAARRGLLRF---VSEQPMynllkrQAELEILPAARAYGLGVIPYSPLA 207
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
21-253 |
1.67e-15 |
|
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: 75.28 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGT----WQSKENDAYKAVLTALKDGYRHIDTAAIY-------RNEDQVGQAIKDSGVpREEIFVTTKLWCTQHHE 89
Cdd:cd19082 1 SRIVLGTadfgTRIDEEEAFALLDAFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKGGHPDLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 90 PEVA----------LDQSLKRLGLDYVDLYLMHwpaRLDPAyIKNEDILSVptkkdgsravditnwnfiktwelMQELPK 159
Cdd:cd19082 80 MSRSrlspediradLEESLERLGTDYIDLYFLH---RDDPS-VPVGEIVDT-----------------------LNELVR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 160 TGKTKAVGVSNFSINNLKDL--LASQGNKLTPAANQVE---IHPLLPQ----------DELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19082 133 AGKIRAFGASNWSTERIAEAnaYAKAHGLPGFAASSPQwslARPNEPPwpgptlvamdEEMRAWHEENQLPVFAYSSQAR 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6324694 225 --------TDAPLLKEPV--------------ILEIAKKNNVQPGHVVISW 253
Cdd:cd19082 213 gffskraaGGAEDDSELRrvyyseenferlerAKELAEEKGVSPTQIALAY 263
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
11-263 |
2.36e-15 |
|
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: 74.95 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 11 ILSLNTGAQIPQIGLGT--------WQSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSgvpREEIFVT 79
Cdd:cd19080 1 RLLGRSGLRVSPLALGTmtfgtewgWGADREEARAMFDAYVEAGGNFIDTANNYTNgtsERLLGEFIAGN---RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 80 TKLwcTQHHEPE-------------VALDQSLKRLGLDYVDLYLMHWPARLDPAyiknEDILsvptkkdgsRAVDitnwn 146
Cdd:cd19080 78 TKY--TMNRRPGdpnaggnhrknlrRSVEASLRRLQTDYIDLLYVHAWDFTTPV----EEVM---------RALD----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 147 fiktwelmqELPKTGKTKAVGVSNF------SINNLKDLlasqgNKLTP-AANQVEiHPLL---PQDELINFCKSKGIVV 216
Cdd:cd19080 138 ---------DLVRAGKVLYVGISDTpawvvaRANTLAEL-----RGWSPfVALQIE-YSLLertPERELLPMARALGLGV 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 217 EAYSPLGS---------------TDAPLLKEP-------------VILEIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19080 203 TPWSPLGGglltgkyqrgeegraGEAKGVTVGfgklternwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVIP 277
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-291 |
2.52e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 74.94 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 20 IPQIGLGTWQ--------SKENDAYKAVLTALKDGYRHIDTAAIY-RNEDQVGQAIK---DSGVPREEIFVTTKlWCTQH 87
Cdd:cd19101 2 ISRVINGMWQlsgghggiRDEDAAVRAMAAYVDAGLTTFDCADIYgPAEELIGEFRKrlrRERDAADDVQIHTK-WVPDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEV-------ALDQSLKRLGLDYVDLYLMHWPARLDPAYiknedilsvptkkdgsraVDITNWnfiktwelMQELPKT 160
Cdd:cd19101 81 GELTMtrayveaAIDRSLKRLGVDRLDLVQFHWWDYSDPGY------------------LDAAKH--------LAELQEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 161 GKTKAVGVSNFSINNLKDLLaSQGNKLtpAANQVEiHPLL---PQDELINFCKSKGIVVEAYSPLGS---------TDAP 228
Cdd:cd19101 135 GKIRHLGLTNFDTERLREIL-DAGVPI--VSNQVQ-YSLLdrrPENGMAALCEDHGIKLLAYGTLAGgllsekylgVPEP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 229 ----------------------------LLKepVILEIAKKNNVQPGHVVISWHVQRGYVVlpkSV-----NPDRIKTNR 275
Cdd:cd19101 211 tgpaletrslqkyklmidewggwdlfqeLLR--TLKAIADKHGVSIANVAVRWVLDQPGVA---GVivgarNSEHIDDNV 285
|
330
....*....|....*...
gi 6324694 276 KIF--TLSTEDFEAINNI 291
Cdd:cd19101 286 RAFsfRLDDEDRAAIDAV 303
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
15-120 |
2.82e-15 |
|
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: 74.94 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSGVPREEIFVTTKL-W-- 83
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWgg 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6324694 84 ---------CTQHHEPEvALDQSLKRLGLDYVDLYLMHWParlDPA 120
Cdd:cd19143 88 ggpppndrgLSRKHIVE-GTKASLKRLQLDYVDLVFCHRP---DPA 129
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-224 |
2.83e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 75.05 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 22 QIGLGTWQ---SKENDA--YKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIK----DSGVPREEIFVTTK-------- 81
Cdd:cd19099 5 SLGLGTYRgdsDDETDEeyREALKAALDSGINVIDTAINYRGgrsERLIGKALRelieKGGIKRDEVVIVTKagyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 ---------LWCTQHHEPEV------------------ALDQSLKRLGLDYVDLYLMHWPARLDPAYIKNEdilsvptkk 134
Cdd:cd19099 85 deplrplkyLEEKLGRGLIDvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEE--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 135 dgsravdiTNWNFIKTWELMQELPKTGKTKAVGVS--NFSINNLKDLLASQGNKLTPAAN------------QVEIHPLL 200
Cdd:cd19099 156 --------FYDRLEEAFEALEEAVAEGKIRYYGIStwDGFRAPPALPGHLSLEKLVAAAEevggdnhhfkviQLPLNLLE 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 6324694 201 PQ------------DELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19099 228 PEaltekntvkgeaLSLLEAAKELGLGVIASRPLNQ 263
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-260 |
5.93e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 73.91 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTW--------------QSKENDAYKAVL-TALKDGYRHIDTAAIY---RNEDQVGQAIKDsgVPREEIFVTTKL 82
Cdd:cd19103 5 PKIALGTWswgsggaggdqvfgNHLDEDTLKAVFdKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 WCTQHHEPE--VA--LDQSLKRLGLDYVDLYLMHWPArldpayiknedilsvptkkdgsravDITNWnfikTWELMqELP 158
Cdd:cd19103 83 TPQIAGQSAdpVAdmLEGSLARLGTDYIDIYWIHNPA-------------------------DVERW----TPELI-PLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 159 KTGKTKAVGVSNFSINNLK---DLLASQGNKLTPAANQveiHPLL----PQDELINFCKSKGIVVEAYS----------- 220
Cdd:cd19103 133 KSGKVKHVGVSNHNLAEIKranEILAKAGVSLSAVQNH---YSLLyrssEEAGILDYCKENGITFFAYMvleqgalsgky 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 221 ------PLGSTDA----PLLKE-----PVILEIAKKNNVQPGHVVISWHVQRGYV 260
Cdd:cd19103 210 dtkhplPEGSGRAetynPLLPQleeltAVMAEIGAKHGASIAQVAIAWAIAKGTT 264
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-263 |
1.19e-14 |
|
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: 72.75 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTWQSKENDAYK---AVL-TALKDGYRHIDTAAIY----------RNEDQVGQAIKDSGVpREEIFVTTKL---W 83
Cdd:cd19752 1 SELCLGTMYFGTRTDEEtsfAILdRYVAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKVgagP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 84 CTQHHEPEV-----------ALDQSLKRLGLDYVDLYLMHwparldpayikNEDilsvptkkdgsRAVDITnwnfiKTWE 152
Cdd:cd19752 80 RDPDGGPESpeglsaetieqEIDKSLRRLGTDYIDLYYAH-----------VDD-----------RDTPLE-----ETLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 153 LMQELPKTGKTKAVGVSNFS---INNLKDLLASQG-----------NKLTPAANQVEIHPLLPQDELINFCKSKG-IVVE 217
Cdd:cd19752 133 AFNELVKAGKVRAIGASNFAawrLERARQIARQQGwaefsaiqqrhSYLRPRPGADFGVQRIVTDELLDYASSRPdLTLL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324694 218 AYSPL--GSTDAPLLKEP-------------VILEIAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19752 213 AYSPLlsGAYTRPDRPLPeqydgpdsdarlaVLEEVAGELGATPNQVVLAWLLHRTPAIIP 273
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-222 |
9.06e-14 |
|
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: 70.76 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLG------TW-QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKdsGVPrEEIFVTTKLWC 84
Cdd:cd19104 7 RTGLKVSELTFGgggiggLMgRTTREEQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALK--GLP-AGPYITTKVRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEVA------LDQSLKRLGLDYVDLYLMH-WPARLDPAYIKNEDILSVPTKKDGsravditnwnfikTWELMQEL 157
Cdd:cd19104 84 DPDDLGDIGgqiersVEKSLKRLKRDSVDLLQLHnRIGDERDKPVGGTLSTTDVLGLGG-------------VADAFERL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324694 158 PKTGKTKAVGVSNFS-INNLKDLLASQG--------NKLTPAANQ--VEIHPLLPQDELINFCKSKGIVVEAYSPL 222
Cdd:cd19104 151 RSEGKIRFIGITGLGnPPAIRELLDSGKfdavqvyyNLLNPSAAEarPRGWSAQDYGGIIDAAAEHGVGVMGIRVL 226
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
23-224 |
1.72e-13 |
|
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: 69.51 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 23 IGLGTWQS----KENDAYKAVLTALKD-GYRHIDTAAIY---RNEDQVGQAikdsGVPREEIFVTTKL--WCTQHHEPE- 91
Cdd:cd19075 5 LGTMTFGSqgrfTTAEAAAELLDAFLErGHTEIDTARVYpdgTSEELLGEL----GLGERGFKIDTKAnpGVGGGLSPEn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 92 --VALDQSLKRLGLDYVDLYLMHWParlDPayiknedilSVPtkkdgsravditnwnFIKTWELMQELPKTGKTKAVGVS 169
Cdd:cd19075 81 vrKQLETSLKRLKVDKVDVFYLHAP---DR---------STP---------------LEETLAAIDELYKEGKFKEFGLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324694 170 NFSINNLKDL--LASQGNKLTPAANQVEIHPL--LPQDELINFCKSKGIVVEAYSPLGS 224
Cdd:cd19075 134 NYSAWEVAEIveICKENGWVLPTVYQGMYNAItrQVETELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-263 |
4.36e-13 |
|
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: 68.61 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 17 GAQIPQIGLG-----TWQSK---ENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSgvPREEIFVTTKLWCT 85
Cdd:cd19145 9 GLEVSAQGLGcmglsGDYGApkpEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDG--PREKVQLATKFGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 86 --QHHEPEV---------ALDQSLKRLGLDYVDLYLMHwpaRLDPayiknedilSVPtkkdgsraVDITnwnfiktwelM 154
Cdd:cd19145 87 eiGGSGVEVrgdpayvraACEASLKRLDVDYIDLYYQH---RIDT---------TVP--------IEIT----------M 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 155 QELPK---TGKTKAVGVSNFSINNLKDLLAsqgnkltpaanqveIHPLLP------------QDELINFCKSKGIVVEAY 219
Cdd:cd19145 137 GELKKlveEGKIKYIGLSEASADTIRRAHA--------------VHPITAvqlewslwtrdiEEEIIPTCRELGIGIVPY 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324694 220 SPLG----STDAPLLKEP---------------------VILE----IAKKNNVQPGHVVISWHVQRGYVVLP 263
Cdd:cd19145 203 SPLGrgffAGKAKLEELLensdvrkshprfqgenleknkVLYErveaLAKKKGCTPAQLALAWVLHQGEDVVP 275
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
19-170 |
5.55e-13 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 68.34 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 19 QIPQIGLGTW----QSKENDAYKAVLTALKDGYRHIDTAAIY----RNEDQ------VGQAIKDSGvPREEIFVTTKL-- 82
Cdd:PRK10625 12 EVSTLGLGTMtfgeQNSEADAHAQLDYAVAQGINLIDVAEMYpvppRPETQgltetyIGNWLAKRG-SREKLIIASKVsg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 83 ------------WCTQHHEPEVALDQSLKRLGLDYVDLYLMHWPARLDPAYIKnediLSVpTKKDGSRAVDItnwnfIKT 150
Cdd:PRK10625 91 psrnndkgirpnQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGK----LGY-SWTDSAPAVSL-----LET 160
|
170 180
....*....|....*....|
gi 6324694 151 WELMQELPKTGKTKAVGVSN 170
Cdd:PRK10625 161 LDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
15-223 |
9.55e-13 |
|
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: 67.18 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT--------WQSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSGVPREEIFVTTKlw 83
Cdd:cd19153 7 IALGNVSPVGLGTaalggvygDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 84 CTQHHEPE---------VALDQSLKRLGLDYVDLYLMHwparlDPAYIKNEDILSvptkkdgsravditnwnfiKTWELM 154
Cdd:cd19153 85 VGRYRDSEfdysaervrASVATSLERLHTTYLDVVYLH-----DIEFVDYDTLVD-------------------EALPAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324694 155 QELPKTGKTKAVGVSNFSINNLKDlLASQGNKLTPAANQVEIHPLLpQDELINF-----CKSKGIVVEAYSPLG 223
Cdd:cd19153 141 RTLKDEGVIKRIGIAGYPLDTLTR-ATRRCSPGSLDAVLSYCHLTL-QDARLESdapglVRGAGPHVINASPLS 212
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
21-228 |
1.22e-11 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 63.92 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGTWQ------SKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKdsGVPREEIFVTTKL-------WC 84
Cdd:cd19162 1 PRLGLGAASlgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEPEVALD-----------QSLKRLGLDYVDLYLMHWPARLDPAyiknedilsvptkkdgsrAVDitnwnfiKTWEL 153
Cdd:cd19162 79 GRPAGADRRFDfsadgirrsieASLERLGLDRLDLVFLHDPDRHLLQ------------------ALT-------DAFPA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 154 MQELPKTGKTKAVGVSNFSINNLKDLLASQGNKLTPAANQveiHPLL---PQDELINFCKSKGIVVEAYSPLGS----TD 226
Cdd:cd19162 134 LEELRAEGVVGAIGVGVTDWAALLRAARRADVDVVMVAGR---YTLLdrrAATELLPLCAAKGVAVVAAGVFNSgilaTD 210
|
..
gi 6324694 227 AP 228
Cdd:cd19162 211 DP 212
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
16-289 |
2.87e-11 |
|
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: 63.03 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLG----TW---QSKENDAYKAVLTALKDGYRHIDTAAIY------RNEDQVGQAIKDSGVPREEIFVTTK- 81
Cdd:cd19077 1 NGKLVGPIGLGlmglTWrpnPTPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 ----LWCTQHHEPEvALDQSLK----RLG-LDYVDLYLmhwPARLDPAyiknedilsvptkkdgsraVDITNwnfikTWE 152
Cdd:cd19077 81 gldpDTLRPDGSPE-AVRKSIEnilrALGgTKKIDIFE---PARVDPN-------------------VPIEE-----TIK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 153 LMQELPKTGKTKAVGVSNFSINNLKdllasQGNKLTP-AANQVEIHPL---LPQDELINFCKSKGIVVEAYSPLG----- 223
Cdd:cd19077 133 ALKELVKEGKIRGIGLSEVSAETIR-----RAHAVHPiAAVEVEYSLFsreIEENGVLETCAELGIPIIAYSPLGrgllt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 224 --------------------------STDAPLLKEpvILEIAKKNNVQPGHVVISWHVQRGY---VVLPKSVNPDRIKTN 274
Cdd:cd19077 208 griksladipegdfrrhldrfngenfEKNLKLVDA--LQELAEKKGCTPAQLALAWILAQSGpkiIPIPGSTTLERVEEN 285
|
330
....*....|....*..
gi 6324694 275 RKIF--TLSTEDFEAIN 289
Cdd:cd19077 286 LKAAnvELTDEELKEIN 302
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-182 |
5.07e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 61.77 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 22 QIGLGTWQ-------------SKENDAYKAVLTALKDGYRHIDTAAIYRN-EDQVGQAIKDSgvprEEIFVTTKLWCTQH 87
Cdd:cd19097 2 KLALGTAQfgldygianksgkPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL----DKFKIITKLPPLKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 88 HEPEVA------LDQSLKRLGLDYVDLYLMHWPARLdpaYIKNEDIlsvptkkdgsravditnwnfiktWELMQELPKTG 161
Cdd:cd19097 78 DKKEDEaaieasVEASLKRLKVDSLDGLLLHNPDDL---LKHGGKL-----------------------VEALLELKKEG 131
|
170 180
....*....|....*....|.
gi 6324694 162 KTKAVGVSNFSINNLKDLLAS 182
Cdd:cd19097 132 LIRKIGVSVYSPEELEKALES 152
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
16-221 |
7.21e-10 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 59.01 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTWQS-----KENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVPREEIFVTTKL-WCTQ 86
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFtsgQAETELGRILKKKGWKRSSYIVSTKIyWSYG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 87 HHEPEV-------ALDQSLKRLGLDYVDLYLMHwpaRLDPaYIKNEDILsvptkkdgsRAvditnwnfiktwelMQELPK 159
Cdd:cd19142 89 SEERGLsrkhiieSVRASLRRLQLDYIDIVIIH---KADP-MCPMEEVV---------RA--------------MSYLID 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324694 160 TGKTKAVGVSNFSINNLKD--LLASQGNKLTPAANQVEIHPllpqdelinFCKSKgivVEAYSP 221
Cdd:cd19142 142 NGLIMYWGTSRWSPVEIMEafSIARQFNCPTPICEQSEYHM---------FCREK---MELYMP 193
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
15-222 |
1.86e-09 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 57.87 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGT-------WQSKENDAYKAVLTALKDGYRHIDTAAIYRN---EDQVGQAIKDSGVPREEIFVTTKlwC 84
Cdd:PLN02587 6 STGLKVSSVGFGAsplgsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTK--C 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 85 TQHHEP--------EVALDQSLKRLGLDYVDLYLMHwparlDPAYIKNEDILSvptkkdgsravditnwnfiKTWELMQE 156
Cdd:PLN02587 84 GRYGEGfdfsaervTKSVDESLARLQLDYVDILHCH-----DIEFGSLDQIVN-------------------ETIPALQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324694 157 LPKTGKTKAVGVSNFSINNLKDLLasqgNKLTPAANQVEI---HPLLPQ---DELINFCKSKGIVVEAYSPL 222
Cdd:PLN02587 140 LKESGKVRFIGITGLPLAIFTYVL----DRVPPGTVDVILsycHYSLNDsslEDLLPYLKSKGVGVISASPL 207
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
16-289 |
1.21e-08 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 55.38 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTWQS----KENDAYKAVL-TALKDGYRHIDTAAIY-----RNEDQVGQAIKDSGVP-REEIFVTTK--- 81
Cdd:PRK09912 21 SGLRLPALSLGLWHNfghvNALESQRAILrKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 -LWCTQHHEPE------VALDQSLKRLGLDYVDLYLMHwpaRLDPAYIKNEDILSVPTKKDGSRA--VDITNWNFIKTW- 151
Cdd:PRK09912 101 dMWPGPYGSGGsrkyllASLDQSLKRMGLEYVDIFYSH---RVDENTPMEETASALAHAVQSGKAlyVGISSYSPERTQk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 152 --ELMQE--LPKTGKTKAVGVSNFSIN--NLKDLLASQGN---KLTPAANQVEIHPLL---PQDELInfcKSKGIVVEAY 219
Cdd:PRK09912 178 mvELLREwkIPLLIHQPSYNLLNRWVDksGLLDTLQNNGVgciAFTPLAQGLLTGKYLngiPQDSRM---HREGNKVRGL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 220 SPLGSTDAPLLKEPVILEIAKKNNVQPGHVVISWHVQRGYV--VLPKSVNPDRIKTNRKI---FTLSTEDFEAIN 289
Cdd:PRK09912 255 TPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVtsVLIGASRAEQLEENVQAlnnLTFSTEELAQID 329
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
15-119 |
1.41e-08 |
|
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: 55.10 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 15 NTGAQIPQIGLGTWQS-----KENDAYKAVLTALKDGYRHIDTAAIY-----RNEDQVGQAIKDSGVP-REEIFVTTKLW 83
Cdd:cd19151 7 RSGLKLPAISLGLWHNfgdvdRYENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKAG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6324694 84 CTQHHEPE----------VALDQSLKRLGLDYVDLYLMHWParlDP 119
Cdd:cd19151 87 YTMWPGPYgdwgskkyliASLDQSLKRMGLDYVDIFYHHRP---DP 129
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
16-119 |
4.12e-08 |
|
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: 53.61 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTWQSKEND-----AYKAVLTALKDGYRHIDTAAIY-----RNEDQVGQAIKDSGVP-REEIFVTTK--- 81
Cdd:cd19150 8 SGLKLPALSLGLWHNFGDDtpletQRAILRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKagy 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6324694 82 -LWCTQHHEPE------VALDQSLKRLGLDYVDLYLMHwpaRLDP 119
Cdd:cd19150 88 dMWPGPYGEWGsrkyllASLDQSLKRMGLDYVDIFYSH---RFDP 129
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
16-119 |
1.54e-07 |
|
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: 51.91 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVPREEIFVTTKLWCTQH 87
Cdd:cd19160 11 SGLRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVVTTKIYWGGQ 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6324694 88 HEPEVALDQ---------SLKRLGLDYVDLYLMHwpaRLDP 119
Cdd:cd19160 91 AETERGLSRkhiieglrgSLDRLQLEYVDIVFAN---RSDP 128
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
16-119 |
1.10e-06 |
|
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: 49.37 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVPREEIFVTTKLWCTQH 87
Cdd:cd19141 8 SGLRVSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKKGWRRSSYVITTKIFWGGK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6324694 88 HEPEVALDQ---------SLKRLGLDYVDLYLMHWParlDP 119
Cdd:cd19141 88 AETERGLSRkhiieglkaSLERLQLEYVDIVFANRP---DP 125
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
16-114 |
1.30e-06 |
|
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: 49.27 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVPREEIFVTTKLWCTQH 87
Cdd:cd19159 9 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGK 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 6324694 88 HEPEVALDQ---------SLKRLGLDYVDLYLMHWP 114
Cdd:cd19159 89 AETERGLSRkhiieglkgSLQRLQLEYVDVVFANRP 124
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
21-167 |
7.89e-06 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 46.55 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 21 PQIGLGT------WQSKENDAYKAVL-TALKDGYRHIDTAAIY---RNEDQVGQAIKDsgVPREEIFVTTK--------- 81
Cdd:cd19161 1 SELGLGTaglgnlYTAVSNADADATLdAAWDSGIRYFDTAPMYghgLAEHRLGDFLRE--KPRDEFVLSTKvgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 82 ----LWCTQHHEP---EVALD-----------QSLKRLGLDYVDLYLMHwpaRLDPAY--IKNEDILSVPTKKDGSRAVD 141
Cdd:cd19161 79 egsvPDPNGFVDPlpfEIVYDysydgimrsfeDSLQRLGLNRIDILYVH---DIGVYThgDRKERHHFAQLMSGGFKALE 155
|
170 180
....*....|....*....|....*.
gi 6324694 142 itnwnfiktwelmqELPKTGKTKAVG 167
Cdd:cd19161 156 --------------ELKKAGVIKAFG 167
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
16-119 |
1.08e-05 |
|
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: 46.23 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 16 TGAQIPQIGLGTW-----QSKENDAYKAVLTALKDGYRHIDTAAIY---RNEDQVGQAIKDSGVPREEIFVTTKLWCTQH 87
Cdd:cd19158 9 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6324694 88 HEPEVALDQ---------SLKRLGLDYVDLYLMHWParlDP 119
Cdd:cd19158 89 AETERGLSRkhiieglkaSLERLQLEYVDVVFANRP---DP 126
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
37-179 |
1.44e-03 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 39.57 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 37 KAVLTALKDGYRHIDTAAIYRNEDQV-GQAIKD--SGVPREEIFVTTKL---------WCTQHHEPEVAldQSLKRLGLD 104
Cdd:cd19164 38 DIVRRALELGIRAFDTSPYYGPSEIIlGRALKAlrDEFPRDTYFIITKVgrygpddfdYSPEWIRASVE--RSLRRLHTD 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 105 YVDLYLMHwparlDPAYIKNEDILSvptkkdgsrAVDITNwnfiktwelmqELPKTGKTKAVGVSNFSINNLKDL 179
Cdd:cd19164 116 YLDLVYLH-----DVEFVADEEVLE---------ALKELF-----------KLKDEGKIRNVGISGYPLPVLLRL 165
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-113 |
1.83e-03 |
|
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: 39.33 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324694 10 KILSLNTGAQIPQIGLGT------WQSKENDAYKAVLTALKD-----GYRHIDTAAIYRNEDQ---VGQAIKDSGVpREE 75
Cdd:cd19146 1 RQLSPTAGVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDafyeqGGNFIDTANNYQGEESerwVGEWMASRGN-RDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6324694 76 IFVTTKlWCTQH--HEPE---------------VALDQSLKRLGLDYVDLYLMHW 113
Cdd:cd19146 80 MVLATK-YTTGYrrGGPIkiksnyqgnhakslrLSVEASLKKLQTSYIDILYVHW 133
|
|
| |
