|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
62-321 |
2.46e-124 |
|
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: 357.33 E-value: 2.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRG-ETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAC---HREVSERIFVTTKIAPSEMrSEEEAA 137
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkYGLSREDIFITSKLAPKDQ-GYEKAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 138 AAIAGVNERLGRT-PDLVLVHWPGRDKESPDSERHRDARRWTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPA 216
Cdd:cd19136 80 AACLGSLERLGTDyLDLYLIHWPGVQGLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 217 VNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL--LDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAER 294
Cdd:cd19136 160 VNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLrlLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPER 239
|
250 260
....*....|....*....|....*..
gi 1199291583 295 TEENFTAisdldDDFVHEAAEKLETAF 321
Cdd:cd19136 240 IAENIKV-----FDFELSEEDMAELNA 261
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
62-308 |
6.92e-86 |
|
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: 258.95 E-value: 6.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACH--REvseRIFVTTKIAPSEMRseeeAAAA 139
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGvpRE---ELFITTKLWPTDHG----YERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 140 IAGVNE---RLGRTP-DLVLVHWPGRDKESPDSERHRDarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKP 215
Cdd:cd19071 74 REALEEslkDLGLDYlDLYLIHWPVPGKEGGSKEARLE----TWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 216 AVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA--LLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19071 150 AVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRrpLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPE 229
|
250
....*....|....*..
gi 1199291583 294 RTEENFtAISD--LDDD 308
Cdd:cd19071 230 RIKENL-DVFDfeLSEE 245
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
59-308 |
6.65e-83 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 251.51 E-value: 6.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACH--REvseRIFVTTKIAPSEM------ 130
Cdd:COG0656 2 GVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGvpRE---ELFVTTKVWNDNHgyddtl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 ----RSEeeaaaaiagvnERLGR-TPDLVLVHWPGRDK--EspdserhrdarrwTWRALENALKMGQCRAIGVSNYELSH 203
Cdd:COG0656 79 aafeESL-----------ERLGLdYLDLYLIHWPGPGPyvE-------------TWRALEELYEEGLIRAIGVSNFDPEH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 204 LRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGA 283
Cdd:COG0656 135 LEELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGV 214
|
250 260
....*....|....*....|....*..
gi 1199291583 284 SVVVKSSVAERTEENFtAISD--LDDD 308
Cdd:COG0656 215 VVIPKSVTPERIRENL-DAFDfeLSDE 240
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
59-306 |
3.99e-64 |
|
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: 203.44 E-value: 3.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLR-GETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAChrEVS-ERIFVTTKIAPSEMRSEEEA 136
Cdd:cd19126 6 GTRMPWLGLGVFQTPdGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES--GVPrEELFVTTKLWNDDQRARRTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 137 AAAIAGVNeRLG-RTPDLVLVHWPGRDKespdserhrdarrW--TWRALENALKMGQCRAIGVSNYELSHLRELLQFCDV 213
Cdd:cd19126 84 DAFQESLD-RLGlDYVDLYLIHWPGKDK-------------FidTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 214 KPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19126 150 VPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHAS 229
|
250 260
....*....|....*....|....*
gi 1199291583 294 RTEENF------------TAISDLD 306
Cdd:cd19126 230 RIKENAdifdfelseddmTAIDALN 254
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
59-299 |
8.71e-64 |
|
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: 202.94 E-value: 8.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLrGETCRDAVRDALR-CGFQHVDTASVYGNERDVGEALRAC--HREvseRIFVTTKIAPSEMRSEEE 135
Cdd:cd19135 10 GVEMPILGLGTSHS-GGYSHEAVVYALKeCGYRHIDTAKRYGCEELLGKAIKESgvPRE---DLFLTTKLWPSDYGYEST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVnERLGRTP-DLVLVHWPGrdkeSPDSERH-RDARRWTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDV 213
Cdd:cd19135 86 KQAFEASL-KRLGVDYlDLYLLHWPD----CPSSGKNvKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 214 KPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19135 161 VPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEE 240
|
....*.
gi 1199291583 294 RTEENF 299
Cdd:cd19135 241 RIKENC 246
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
59-309 |
3.25e-62 |
|
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: 199.88 E-value: 3.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE-VSER--IFVTTKI-----APSEm 130
Cdd:cd19125 8 GAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDgVVKRedLFITSKLwctdhAPED- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 rseeeaaaaiagVNERLGRT--------PDLVLVHWP-----GRDKESPDSERHRDARRwTWRALENALKMGQCRAIGVS 197
Cdd:cd19125 87 ------------VPPALEKTlkdlqldyLDLYLIHWPvrlkkGAHMPEPEEVLPPDIPS-TWKAMEKLVDSGKVRAIGVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 198 NYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG-------VGALLDDDRVKAYAATIGLRP 270
Cdd:cd19125 154 NFSVKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGspgttwvKKNVLKDPIVTKVAEKLGKTP 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1199291583 271 APALVRWTLSMGASVVVKSSVAERTEENFTA--ISDLDDDF 309
Cdd:cd19125 234 AQVALRWGLQRGTSVLPKSTNEERIKENIDVfdWSIPEEDF 274
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
59-308 |
2.46e-60 |
|
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: 193.74 E-value: 2.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSEMRSEEEAAA 138
Cdd:cd19131 7 GNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREE-LFITTKLWNSDQGYDSTLRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 139 AIAGVnERLGR-TPDLVLVHWPgrdkeSPDSERHRDarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPAV 217
Cdd:cd19131 86 FDESL-RKLGLdYVDLYLIHWP-----VPAQDKYVE----TWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 218 NQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEE 297
Cdd:cd19131 156 NQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAE 235
|
250
....*....|...
gi 1199291583 298 NFtAISD--LDDD 308
Cdd:cd19131 236 NF-DVFDfeLDAD 247
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
59-299 |
3.49e-59 |
|
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: 192.11 E-value: 3.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-ETCRDAVRDALRCGFQHVDTASVYGNERDVGEALR-ACHREVSER--IFVTTK---------- 124
Cdd:cd19116 8 GNEIPAIALGTWKLKDdEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIReKIAEGVVKRedLFITTKlwnsyhereq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 125 IAPSEMRSEeeaaaaiagvnERLGRT-PDLVLVHWPGRDKESPDSERHRDaRRW-------TWRALENALKMGQCRAIGV 196
Cdd:cd19116 88 VEPALRESL-----------KRLGLDyVDLYLIHWPVAFKENNDSESNGD-GSLsdidyleTWRGMEDLVKLGLTRSIGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 197 SNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG---------VGALLDDDRVKAYAATIG 267
Cdd:cd19116 156 SNFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGrlvprgqtnPPPRLDDPTLVAIAKKYG 235
|
250 260 270
....*....|....*....|....*....|..
gi 1199291583 268 LRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19116 236 KTTAQIVLRYLIDRGVVPIPKSSNKKRIKENI 267
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
59-298 |
5.95e-59 |
|
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: 190.68 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLR-GETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHrEVSERIFVTTKIAPSEMRSEEEAA 137
Cdd:cd19157 7 GVKMPWLGLGVFKVEeGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESG-IPREELFITSKVWNADQGYDSTLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 138 AAIAGVnERLGRT-PDLVLVHWPGRDKespdserHRDarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPA 216
Cdd:cd19157 86 AFEASL-ERLGLDyLDLYLIHWPVKGK-------YKE----TWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 217 VNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTE 296
Cdd:cd19157 154 VNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRII 233
|
..
gi 1199291583 297 EN 298
Cdd:cd19157 234 EN 235
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
59-308 |
2.58e-58 |
|
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: 188.55 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-ETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAChrEVS-ERIFVTTKIAPSEMrseeEA 136
Cdd:cd19133 6 GVEMPILGFGVFQIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKS--GIPrEELFITTKLWIQDA----GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 137 AAAIAGVNERLGRTP----DLVLVHWPGRDKESpdserhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCD 212
Cdd:cd19133 80 EKAKKAFERSLKRLGldylDLYLIHQPFGDVYG------------AWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 213 VKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG--ALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSS 290
Cdd:cd19133 148 VKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGrnNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSV 227
|
250 260
....*....|....*....|
gi 1199291583 291 VAERTEENFtAISD--LDDD 308
Cdd:cd19133 228 RPERIAENF-DIFDfeLSDE 246
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
62-306 |
2.59e-58 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 188.25 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRA--CHREvseRIFVTTKIAPSEMRSEEEAAAA 139
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAEsgVPRE---DLFITTKVWRDHLRPEDLKKSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 140 IAGVnERLG-RTPDLVLVHWPGRDKESPDserhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPAVN 218
Cdd:cd19073 78 DRSL-EKLGtDYVDLLLIHWPNPTVPLEE----------TLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 219 QIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEEN 298
Cdd:cd19073 147 QVEFHPFLYQAELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKEN 226
|
....*...
gi 1199291583 299 FtAISDLD 306
Cdd:cd19073 227 L-AIFDWE 233
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
56-299 |
3.24e-57 |
|
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: 186.18 E-value: 3.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 56 IAPGINMPMLAFGTYRLR-GETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREvSERIFVTTKIAPSEMRSEE 134
Cdd:cd19156 3 LANGVEMPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVP-REEVFVTTKLWNSDQGYES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 135 EAAAAIAGVnERLG-RTPDLVLVHWPGRDKespdserHRDarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDV 213
Cdd:cd19156 82 TLAAFEESL-EKLGlDYVDLYLIHWPVKGK-------FKD----TWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 214 KPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19156 150 APMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEE 229
|
....*.
gi 1199291583 294 RTEENF 299
Cdd:cd19156 230 RIQENF 235
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
59-308 |
2.22e-55 |
|
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: 180.93 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSEMRSEEEAAa 138
Cdd:cd19132 4 GTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREE-LFVTTKLPGRHHGYEEALR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 139 aiaGVNERLGRTP----DLVLVHWPgrdkeSPDSERHRDArrwtWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVK 214
Cdd:cd19132 82 ---TIEESLYRLGldyvDLYLIHWP-----NPSRDLYVEA----WQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 215 PAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG-ALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19132 150 PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGsGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPE 229
|
250
....*....|....*.
gi 1199291583 294 RTEENFTAIS-DLDDD 308
Cdd:cd19132 230 RQRENLAIFDfELSDE 245
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
59-318 |
5.81e-55 |
|
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: 180.80 E-value: 5.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSER--IFVTTKIAPSEMRSEEEa 136
Cdd:cd19121 9 GASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGGVKRedLFVTTKLWSTYHRRVEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 137 aaaiaGVNERLGRTP----DLVLVHWP------GRDKESPdseRHRDARR-----W----TWRALENALKMGQCRAIGVS 197
Cdd:cd19121 88 -----CLDRSLKSLGldyvDLYLVHWPvllnpnGNHDLFP---TLPDGSRdldwdWnhvdTWKQMEKVLKTGKTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 198 NYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGV--GALLDDDRVKAYAATIGLRPAPALV 275
Cdd:cd19121 160 NYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGStgSPLISDEPVVEIAKKHNVGPGTVLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1199291583 276 RWTLSMGASVVVKSSVAERTEENFTAIsDLDDdfvhEAAEKLE 318
Cdd:cd19121 240 SYQVARGAVVLPKSVTPDRIKSNLEII-DLDD----EDMNKLN 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
59-306 |
7.39e-55 |
|
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: 181.46 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS---ERIFVTTKIAPSEMRseee 135
Cdd:cd19154 9 GVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVvkrEDLFITTKLWTHEHA---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVNERLGRTP----DLVLVH--WPGRDKESPDS-----ERHRDARRW--TWRALENALKMGQCRAIGVSNYELS 202
Cdd:cd19154 85 PEDVEEALRESLKKLQleyvDLYLIHapAAFKDDEGESGtmengMSIHDAVDVedVWRGMEKVYDEGLTKAIGVSNFNND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 203 HLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG---------------VGALLDDDRVKAYAATIG 267
Cdd:cd19154 165 QIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGspgranftkstgvspAPNLLQDPIVKAIAEKHG 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1199291583 268 LRPAPALVRWTLSMGASVVVKSSVAERTEENFT----AISDLD 306
Cdd:cd19154 245 KTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNifdfSLSEED 287
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
59-308 |
7.49e-55 |
|
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: 179.76 E-value: 7.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAChrEVS-ERIFVTTKIAPSEMRSEEEAA 137
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAAS--GVPrDELFLTTKVWPDNYSPDDFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 138 AAIAGVnERLgRTP--DLVLVHWPGRDkespdserhrDARRWTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKP 215
Cdd:cd19140 83 SVEESL-RKL-RTDyvDLLLLHWPNKD----------VPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 216 AVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTL-SMGASVVVKSSVAER 294
Cdd:cd19140 151 FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPER 230
|
250
....*....|....*.
gi 1199291583 295 TEENFtAISD--LDDD 308
Cdd:cd19140 231 LEENL-DIFDftLSDE 245
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
62-308 |
3.33e-53 |
|
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: 175.23 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAcHREVSERIFVTTKIAPSEMRSEEEAAAAIA 141
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAE-SGVPRDELFITTKIWIDNLSKDKLLPSLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 142 GVnERLGRTP-DLVLVHWPGRDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQ-FCDVKPAVNQ 219
Cdd:cd19139 80 SL-EKLRTDYvDLTLIHWPSPNDEVPVEE--------YIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvVGAGAIATNQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 220 IELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19139 151 IELSPYLQNRKLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNL 230
|
250
....*....|
gi 1199291583 300 TAIS-DLDDD 308
Cdd:cd19139 231 LALDlTLDAD 240
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
50-309 |
1.50e-52 |
|
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: 174.61 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 50 TKWTRAIAPGINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSE 129
Cdd:cd19117 2 SSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREE-IFITTKLWCTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 MRseeeaaAAIAGVNERLGR--TP--DLVLVHWP-----GRDKESP--DSERHRDARRW----TWRALENALKMGQCRAI 194
Cdd:cd19117 81 HR------RVEEALDQSLKKlgLDyvDLYLMHWPvpldpDGNDFLFkkDDGTKDHEPDWdfikTWELMQKLPATGKVKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 195 GVSNYELSHLRELLQFCDVK--PAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGV--GALLDDDRVKAYAATIGLRP 270
Cdd:cd19117 155 GVSNFSIKNLEKLLASPSAKivPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGStnAPLLKEPVIIKIAKKHGKTP 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1199291583 271 APALVRWTLSMGASVVVKSSVAERTEENFTAISDLDDDF 309
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEEF 273
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
62-297 |
2.53e-52 |
|
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: 173.57 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGT-YRLRG-------ETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAChrEVS-ERIFVTTKIAPSemrs 132
Cdd:cd19120 4 IPAIAFGTgTAWYKsgdddiqRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKES--GVPrEDLFITTKVSPG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 eeeaaaaIAGVNERLGRT--------PDLVLVHWPGRDKESPDSerHRDArrwtWRALENALKMGQCRAIGVSNYELSHL 204
Cdd:cd19120 78 -------IKDPREALRKSlaklgvdyVDLYLIHSPFFAKEGGPT--LAEA----WAELEALKDAGLVRSIGVSNFRIEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 205 RELLQFCDVKPAVNQIELHARF--PQTELRAFCESVGVHVVGYSPLGV------GALldDDRVKAYAATIGLRPAPALVR 276
Cdd:cd19120 145 EELLDTAKIKPAVNQIEFHPYLypQQPALLEYCREHGIVVSAYSPLSPltrdagGPL--DPVLEKIAEKYGVTPAQVLLR 222
|
250 260
....*....|....*....|.
gi 1199291583 277 WTLSMGASVVVKSSVAERTEE 297
Cdd:cd19120 223 WALQKGIVVVTTSSKEERMKE 243
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
59-308 |
5.18e-51 |
|
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: 170.67 E-value: 5.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS----ERIFVTTKIAPSEMRSEE 134
Cdd:cd19118 4 GNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPgvkrEDLFITSKLWNNSHRPEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 135 EAAAAIAGVNErLGRT-PDLVLVHWP----GRDKESPDSERHRDARRW----------TWRALENALKMGQCRAIGVSNY 199
Cdd:cd19118 84 VEPALDDTLKE-LGLDyLDLYLIHWPvafkPTGDLNPLTAVPTNGGEVdldlsvslvdTWKAMVELKKTGKVKSIGVSNF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 200 ELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG---VGA--LLDDDRVKAYAATIGLRPAPAL 274
Cdd:cd19118 163 SIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGnnlAGLplLVQHPEVKAIAAKLGKTPAQVL 242
|
250 260 270
....*....|....*....|....*....|....
gi 1199291583 275 VRWTLSMGASVVVKSSVAERTEENFTAIsDLDDD 308
Cdd:cd19118 243 IAWGIQRGHSVIPKSVTPSRIRSNFEQV-ELSDD 275
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
59-299 |
5.96e-51 |
|
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: 170.53 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGT--YRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEAL-RACHRE-VSER--IFVTTKIAPSEMRS 132
Cdd:cd19124 2 GQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALaEALRLGlVKSRdeLFVTSKLWCSDAHP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 EEeaaaaiagVNERLGRT--------PDLVLVHWPGR---DKESPDSERHR----DARRwTWRALENALKMGQCRAIGVS 197
Cdd:cd19124 82 DL--------VLPALKKSlrnlqleyVDLYLIHWPVSlkpGKFSFPIEEEDflpfDIKG-VWEAMEECQRLGLTKAIGVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 198 NYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG-------ALLDDDRVKAYAATIGLRP 270
Cdd:cd19124 153 NFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPgtkwgsnAVMESDVLKEIAAAKGKTV 232
|
250 260
....*....|....*....|....*....
gi 1199291583 271 APALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNL 261
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
59-299 |
7.80e-51 |
|
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: 169.90 E-value: 7.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSEMrseeEAAA 138
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSD-IFVTTKLWISDY----GYDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 139 AIAGVNERLGRTP----DLVLVHWPGRDkespDSERHRDArrwtWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVK 214
Cdd:cd19127 81 ALRGFDASLRRLGldyvDLYLLHWPVPN----DFDRTIQA----YKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 215 PAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG------------VGALLDDDRVKAYAATIGLRPAPALVRWTLSMG 282
Cdd:cd19127 153 PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGgvmrygasgptgPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNG 232
|
250
....*....|....*..
gi 1199291583 283 ASVVVKSSVAERTEENF 299
Cdd:cd19127 233 VSAIPKSVHPERIAENI 249
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
59-308 |
1.07e-50 |
|
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: 170.28 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLR-GETCRdAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKI-----APSE 129
Cdd:cd19123 9 GDLIPALGLGTWKSKpGEVGQ-AVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEgkvKREDLWITSKLwnnshAPED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 MRSEEEAAAAIAGVnERLgrtpDLVLVHWPGRDKesPDSERHRDARRW----------TWRALENALKMGQCRAIGVSNY 199
Cdd:cd19123 88 VLPALEKTLADLQL-DYL----DLYLMHWPVALK--KGVGFPESGEDLlslspipledTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 200 ELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG------------ALLDDDRVKAYAATIG 267
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1199291583 268 LRPAPALVRWTLSMGASVVVKSSVAERTEENFTAIS-DLDDD 308
Cdd:cd19123 241 ASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEvELDAS 282
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
59-308 |
1.38e-48 |
|
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: 163.54 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKI-----APSEMRSE 133
Cdd:cd19130 7 GNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDE-LFVTTKLwndrhDGDEPAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 134 EEAAAAIAGVNERlgrtpDLVLVHWPgrdkeSPDserhRDARRWTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDV 213
Cdd:cd19130 86 FAESLAKLGLDQV-----DLYLVHWP-----TPA----AGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 214 KPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAE 293
Cdd:cd19130 152 VPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRE 231
|
250
....*....|....*.
gi 1199291583 294 RTEENFTAIS-DLDDD 308
Cdd:cd19130 232 RMEDNLDVFDfDLTDT 247
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
53-299 |
3.20e-48 |
|
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: 162.72 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 53 TRAIAPGINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSEMRS 132
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGE-LFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 EEEAAAAIAGVnERLG-RTPDLVLVHWPGrdkesPDSERHRDarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFC 211
Cdd:cd19134 81 TASQAACRASL-ERLGlDYVDLYLIHWPA-----GREGKYVD----SWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 212 DVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSV 291
Cdd:cd19134 151 FFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSN 230
|
....*...
gi 1199291583 292 AERTEENF 299
Cdd:cd19134 231 PERIASNL 238
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
59-299 |
4.69e-46 |
|
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: 158.42 E-value: 4.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKIAPSEmrSEEE 135
Cdd:cd19112 8 GHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTglvKREDLFITTKLWNSD--HGHV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVNERLGRTPDLVLVHWPGRDKE----SPDSERHRD---------ARRWTWRALENALKMGQCRAIGVSNYELS 202
Cdd:cd19112 86 IEACKDSLKKLQLDYLDLYLVHFPVATKHtgvgTTGSALGEDgvldidvtiSLETTWHAMEKLVSAGLVRSIGISNYDIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 203 HLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL----------LDDDRVKAYAATIGLRPAP 272
Cdd:cd19112 166 LTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAAnaewfgsvspLDDPVLKDLAKKYGKSAAQ 245
|
250 260
....*....|....*....|....*..
gi 1199291583 273 ALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19112 246 IVLRWGIQRNTAVIPKSSKPERLKENI 272
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
59-322 |
1.63e-45 |
|
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: 156.89 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTY---RLRGETcRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS---ERIFVTTKIAPSemrs 132
Cdd:cd19119 9 GASIPALGLGTAsphEDRAEV-KEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSikrEELFITTKVWPT---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 eeEAAAAIAGVNERLGRTP----DLVLVHWP----------GRDK--ESPD-SERHRDARRW--TWRALENALKMGQCRA 193
Cdd:cd19119 84 --FYDEVERSLDESLKALGldyvDLLLVHWPvcfekdsddsGKPFtpVNDDgKTRYAASGDHitTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 194 IGVSNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG--VGALLDDDRVKAYAATIGLRPA 271
Cdd:cd19119 162 IGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGshGAPNLKNPLVKKIAEKYNVSTG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1199291583 272 PALVRWTLSMGASVVVKSSVAERTEEN--FTAISDLDDDFVHEAAEKLETAFA 322
Cdd:cd19119 242 DILISYHVRQGVIVLPKSLKPVRIVSNgkIVSLTKEDLQKLDDIGEKYPVRFI 294
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
59-299 |
2.47e-45 |
|
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: 156.78 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRAC--HREVSER--IFVTTKI-----APSE 129
Cdd:cd19106 4 GQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgPGKAVPRedLFVTSKLwntkhHPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 MRSEEEAAAAIAGVnERLgrtpDLVLVHWP-----GRDK--ESPD-SERHRDAR-RWTWRALENALKMGQCRAIGVSNYE 200
Cdd:cd19106 84 VEPALRKTLKDLQL-DYL----DLYLIHWPyaferGDNPfpKNPDgTIRYDSTHyKETWKAMEKLVDKGLVKAIGLSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 201 LSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG----------ALLDDDRVKAYAATIGLRP 270
Cdd:cd19106 159 SRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPdrpwakpdepVLLEEPKVKALAKKYNKSP 238
|
250 260
....*....|....*....|....*....
gi 1199291583 271 APALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNI 267
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
63-299 |
1.53e-44 |
|
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: 153.83 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 63 PMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS---ERIFVTTKIAPSEMRSEEeaaaa 139
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGvkrEDLFITSKLWPTMHQPEN----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 140 iagVNERLGRTP--------DLVLVHWP-----GRDKESPDS-ERHRDAR---RWTWRALENALKMGQCRAIGVSNYELS 202
Cdd:cd19128 77 ---VKEQLLITLqdlqleylDLFLIHWPlafdmDTDGDPRDDnQIQSLSKkplEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 203 HLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG------VGALLDDDRVKAYAATIGLRPAPALVR 276
Cdd:cd19128 154 LLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGgsygdgNLTFLNDSELKALATKYNTTPPQVIIA 233
|
250 260
....*....|....*....|....*.
gi 1199291583 277 WTLSM---GASVVVKSSVAERTEENF 299
Cdd:cd19128 234 WHLQKwpkNYSVIPKSANKSRCQQNF 259
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
59-328 |
1.10e-43 |
|
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: 151.84 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKIAPSEMRSEEE 135
Cdd:cd19129 3 SGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAgkiRREDLFVTTKLWNTNHRPERV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVnERLG-RTPDLVLVHWPGRDKESpDSERHRDAR-----------RWTWRALENALKMGQCRAIGVSNYELSH 203
Cdd:cd19129 83 KPAFEASL-KRLQlDYLDLYLIHTPFAFQPG-DEQDPRDANgnviyddgvtlLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 204 LRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA---LLDDDRVKAYAATIGLRPAPALVRWTLS 280
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMepkLLEDPVITAIARRVNKTPAQVLLAWAIQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1199291583 281 MGASVVVKSSVAERTEENFTaISDLDDDFVHEAAEKLETafaseRVKF 328
Cdd:cd19129 241 RGTALLTTSKTPSRIRENFD-ISTLPEDAMREINEGIKT-----RYRF 282
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
59-319 |
1.97e-43 |
|
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: 151.11 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKIAPSEMRSEEE 135
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNgklKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVNERLGRTPDLVLVHWP------GRDKESPDSERHRDArrwTWRALENALKMGQCRAIGVSNYELSHLRELLQ 209
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPcgfvnkKDKGERELASSDVTS---VWRAMEALVSEGKVKSIGLSNFNPRQINKILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 210 FCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG------------VGALLDDDRVKAYAATIGLRPAPALVRW 277
Cdd:cd19111 158 YAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGspgranqslwpdQPDLLEDPTVLAIAKELDKTPAQVLLRF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1199291583 278 TLSMGASVVVKSSVAERTEENFTAisdLDDDFVHEAAEKLET 319
Cdd:cd19111 238 VLQRGTGVLPKSTNKERIEENFEV---FDFELTEEHFKKLKT 276
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
59-299 |
3.84e-43 |
|
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: 151.14 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALR---ACHREVSERIFVTTKIAPSEMRSEEE 135
Cdd:cd19155 9 GEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKkwiDSGKVKREELFIVTKLPPGGNRREKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVNERLGRTPDLVLVHWP--------GRDKESPDSERHRDARR---WTWRALENALKMGQCRAIGVSNYELSHL 204
Cdd:cd19155 89 EKFLLKSLEKLQLDYVDLYLIHFPvgslskedDSGKLDPTGEHKQDYTTdllDIWKAMEAQVDQGLTRSIGLSNFNREQM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 205 RELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA-----------------LLDDDRVKAYAATIG 267
Cdd:cd19155 169 ARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGaahfspgtgspsgsspdLLQDPVVKAIAERHG 248
|
250 260 270
....*....|....*....|....*....|..
gi 1199291583 268 LRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19155 249 KSPAQVLLRWLMQRGVVVIPKSTNAARIKENF 280
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
54-317 |
5.06e-43 |
|
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: 150.08 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 54 RAIAPGINMPMLAFGTYR---LRGETcRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS----ERIFVTTKI- 125
Cdd:cd19122 1 FTLNNGVKIPAVGFGTFAnegAKGET-YAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPsvkrEDLFICTKVw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 126 ----APSEMRSEEEAAAAIAGVNerlgrTPDLVLVHWP-GRDKESPDSERHRDARRW------------TWRALENALKM 188
Cdd:cd19122 80 nhlhEPEDVKWSIDNSLKNLKLD-----YIDLFLVHWPiAAEKNDQRSPKLGPDGKYvilkdltenpepTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 189 GQCRAIGVSNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG-------VGALLDDDRV-K 260
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGsqnqvpsTGERVSENPTlN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 261 AYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENFTAISDLDDDFvhEAAEKL 317
Cdd:cd19122 235 EVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIELSDEDF--EAINQV 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
61-308 |
2.62e-40 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 142.47 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 61 NMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKI----------APSEM 130
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDE-LFITTKIwidnlakdklIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 RSEeeaaaaiagvnERLgRTP--DLVLVHWPGRDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELL 208
Cdd:PRK11172 81 ESL-----------QKL-RTDyvDLTLIHWPSPNDEVSVEE--------FMQALLEAKKQGLTREIGISNFTIALMKQAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 209 QFCDVKP-AVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVV 287
Cdd:PRK11172 141 AAVGAENiATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIP 220
|
250 260
....*....|....*....|..
gi 1199291583 288 KSSVAERTEENFTAIS-DLDDD 308
Cdd:PRK11172 221 SSTKRENLASNLLAQDlQLDAE 242
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
59-306 |
9.67e-38 |
|
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: 136.81 E-value: 9.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKI-----APSEM 130
Cdd:cd19113 8 GYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEglvKREELFLTSKLwnnfhDPKNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 RSEEEAAAAIAGVNerlgrTPDLVLVHWPGRDKESPDSERHR------DARRW---------TWRALENALKMGQCRAIG 195
Cdd:cd19113 88 ETALNKTLSDLKLD-----YVDLFLIHFPIAFKFVPIEEKYPpgfycgDGDNFvyedvpildTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 196 VSNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG--------------VGALLDDDRVKA 261
Cdd:cd19113 163 VSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnqgralnTPTLFEHDTIKS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 262 YAATIGLRPAPALVRWTLSMGASVVVKSSVAER------------TEENFTAISDLD 306
Cdd:cd19113 243 IAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERllqnlsvndfdlTKEDFEEIAKLD 299
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
62-320 |
3.01e-37 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 134.43 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVSErIFVTTKIAPSEmrseeeAAAAIA 141
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREE-LFITTKLWNDD------HKRPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 142 GVNERLGRTP----DLVLVHWPgrdkeSPDSERHRDArrwtWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPAV 217
Cdd:PRK11565 88 ALEESLKKLQldyvDLYLMHWP-----VPAIDHYVEA----WKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 218 NQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA--LLDDDRVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERT 295
Cdd:PRK11565 159 NQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGkgVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRI 238
|
250 260
....*....|....*....|....*
gi 1199291583 296 EENFTAIsdlddDFVHEAAEKLETA 320
Cdd:PRK11565 239 AENFDVF-----DFRLDKDELGEIA 258
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
65-310 |
8.23e-35 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 128.58 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRGETCR-------DAVRDALRCGFQHVDTASVYG---NERDVGEALRAchREVS-ERIFVTTKIA--PSEMR 131
Cdd:pfam00248 1 IGLGTWQLGGGWGPiskeealEALRAALEAGINFIDTAEVYGdgkSEELLGEALKD--YPVKrDKVVIATKVPdgDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 132 SEEEAAAAIAGVNE---RLGR-TPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLREL 207
Cdd:pfam00248 79 SGGSKENIRKSLEEslkRLGTdYIDLYYLHWP--DPDTPIEE--------TWDALEELKKEGKIRAIGVSNFDAEQIEKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 208 LQFCDVKPAVNQIELHA--RFPQTELRAFCESVGVHVVGYSPLGVGALLD---------------------------DDR 258
Cdd:pfam00248 149 LTKGKIPIVAVQVEYNLlrRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1199291583 259 VKAYAATIGLRPAPALVRWTLSM--GASVVVKSSVAERTEENFTAIS-DLDDDFV 310
Cdd:pfam00248 229 LEEIAKEHGVSPAQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEfPLSDEEV 283
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
59-319 |
7.29e-34 |
|
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: 126.52 E-value: 7.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKI-----APSEM 130
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEglvKREDLFIVTKLwnnfhGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 RSEEEAAAAIAGVNerlgrTPDLVLVHWP---------------GRDKESPDSERHRDARRWTWRALENALKMGQCRAIG 195
Cdd:cd19114 81 REAFDRQLKDYGLD-----YIDLYLIHFPipaayvdpaenypflWKDKELKKFPLEQSPMQECWREMEKLVDAGLVRNIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 196 VSNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA-------------LLDDDRVKAY 262
Cdd:cd19114 156 IANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkhlkhftnLLEHPVVKKL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 263 AATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENFTAISDLDDDFVHEAAEKLET 319
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEA 292
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
58-318 |
4.91e-33 |
|
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: 124.46 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 58 PGINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEAL-RACHREVSER--IFVTTKI-----APSE 129
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVaRAIKEGIVKRedLFIVSKLwntfhDGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 MRSEEEAAAAIAGVNERlgrtpDLVLVHWP--------------GRDKESPDSERHRDARRWTWRALENALKMGQCRAIG 195
Cdd:cd19115 89 VEPICRKQLADWGIDYF-----DLFLIHFPialkyvdpavryppGWFYDGKKVEFSNAPIQETWTAMEKLVDKGLARSIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 196 VSNYELSHLRELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLG--------------VGALLDDDRVKA 261
Cdd:cd19115 164 VSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldlpgakdTPPLFEHDVIKS 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199291583 262 YAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENFTAIS-DLDDDFVhEAAEKLE 318
Cdd:cd19115 244 IAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGfDLEAEEI-KAISALD 300
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
59-299 |
1.22e-31 |
|
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: 120.60 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHREVS---ERIFVTTKIAPSEMRSEEe 135
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVvkrEDLFIVSKLWCTFHEKGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 aaaaiagVNERLGRT--------PDLVLVHWP-----GRD--------KESPDSERHRDarrwTWRALENALKMGQCRAI 194
Cdd:cd19107 80 -------VKGACQKTlsdlkldyLDLYLIHWPtgfkpGKElfpldesgNVIPSDTTFLD----TWEAMEELVDEGLVKAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 195 GVSNYELSHLRELLQFCDVK--PAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGV----------GALLDDDRVKAY 262
Cdd:cd19107 149 GVSNFNHLQIERILNKPGLKykPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSpdrpwakpedPSLLEDPKIKEI 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1199291583 263 AATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19107 229 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENF 265
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
53-303 |
5.02e-31 |
|
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: 117.73 E-value: 5.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 53 TRAIAPGINMPMLAFGTYRL-----RGETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHrevsERIFVTTK 124
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWYMgedpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGRR----DKVFLVSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 125 IAPSEMRSEEEAAAAIAGVnERLGRTP-DLVLVHWPGRdkeSPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSH 203
Cdd:cd19138 78 VLPSNASRQGTVRACERSL-RRLGTDYlDLYLLHWRGG---VPLAE--------TVAAMEELKKEGKIRAWGVSNFDTDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 204 LRELLQFCDVKP-AVNQIELH--ARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDR-----VKAYAATIGLRPAPALV 275
Cdd:cd19138 146 MEELWAVPGGGNcAANQVLYNlgSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLlenptLKEIAARHGATPAQVAL 225
|
250 260
....*....|....*....|....*....
gi 1199291583 276 RWTLSMGASVVV-KSSVAERTEENFTAIS 303
Cdd:cd19138 226 AWVLRDGNVIAIpKSGSPEHARENAAAAD 254
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
61-299 |
1.63e-30 |
|
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: 117.37 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 61 NMPMLAFGTYRLRGETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRACHRE---VSERIFVTTKIAPSEMRSEEEAA 137
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEgvvRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 138 AAIAGVNERLGRTPDLVLVHWP-GRDKESPDSERHRDARRW--------TWRALENALKMGQCRAIGVSNYELSHLRELL 208
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPmGFKPGEPDLPLDRSGMVIpsdtdfldTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 209 QF--CDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGA----LLDDDRVKAYAATIGLRPAPALVRWTLSMG 282
Cdd:cd19110 163 NKpgLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCegvdLIDDPVIQRIAKKHGKSPAQILIRFQIQRN 242
|
250
....*....|....*..
gi 1199291583 283 ASVVVKSSVAERTEENF 299
Cdd:cd19110 243 VIVIPKSVTPSRIKENI 259
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
59-301 |
1.45e-27 |
|
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: 108.47 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRD---------AVRDALRCGFQHVDTASVYGN---ERDVGEALRACHREvseRIFVTTKIA 126
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKDysddkkaieALRYAIELGINLIDTAEMYGGghaEELVGKAIKGFDRE---DLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 127 PSEMRSEEEAAAAIAGVnERLGRT-PDLVLVHWPGRDkeSPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLR 205
Cdd:cd19072 78 PDHLKYDDVIKAAKESL-KRLGTDyIDLYLIHWPNPS--IPIEE--------TLRAMEELVEEGKIRYIGVSNFSLEELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 206 ELLQF-CDVKPAVNQIELHARFP--QTELRAFCESVGVHVVGYSPLGVGALLDDDRV-------KAYAATiglrPAPALV 275
Cdd:cd19072 147 EAQSYlKKGPIVANQVEYNLFDReeESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSplldeiaKKYGKT----PAQIAL 222
|
250 260
....*....|....*....|....*..
gi 1199291583 276 RWTLSM-GASVVVKSSVAERTEENFTA 301
Cdd:cd19072 223 NWLISKpNVIAIPKASNIEHLEENAGA 249
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
59-301 |
2.26e-27 |
|
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: 108.04 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGETCRDAVRD---------ALRCGFQHVDTASVYG---NERDVGEALRACHREvseRIFVTTKIA 126
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYSRDeemvellktAIELGYTHIDTAEMYGgghTEELVGKAIKDFPRE---DLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 127 PSEMRsEEEAAAAIAGVNERLGRT-PDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLR 205
Cdd:cd19137 78 PTNLR-YDDLLRSLQNSLRRLDTDyIDLYLIHWP--NPNIPLEE--------TLSAMAEGVRQGLIRYIGVSNFNRRLLE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 206 ELLQFCDVKPAVNQIELHA---RFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPALVRWTLSMG 282
Cdd:cd19137 147 EAISKSQTPIVCNQVKYNLedrDPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKP 226
|
250 260
....*....|....*....|
gi 1199291583 283 ASVVV-KSSVAERTEENFTA 301
Cdd:cd19137 227 NVVAIpKAGRVEHLKENLKA 246
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
75-253 |
5.52e-27 |
|
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: 107.70 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 75 ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAChrEVSERIFVTTKIAPSEMR-SEEEAAAAIAGVNERLG-R 149
Cdd:cd19093 26 EDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKEL--GDRDEVVIATKFAPLPWRlTRRSVVKALKASLERLGlD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 150 TPDLVLVHWPGrdkespdsERHRDARRWtWRALENALKMGQCRAIGVSNYELSHLR---ELLQFCDVKPAVNQIE---LH 223
Cdd:cd19093 104 SIDLYQLHWPG--------PWYSQIEAL-MDGLADAVEEGLVRAVGVSNYSADQLRrahKALKERGVPLASNQVEyslLY 174
|
170 180 190
....*....|....*....|....*....|.
gi 1199291583 224 aRFP-QTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19093 175 -RDPeQNGLLPACDELGITLIAYSPLAQGLL 204
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
65-310 |
4.64e-25 |
|
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: 102.28 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG---------ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAchreVSERIFVTTKIAPSEMRS 132
Cdd:cd19085 4 LGLGCWQFGGgywwgdqddEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG----RRDDVVIATKVSPDNLTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 EEEAAAAIAGVnERLGRTP-DLVLVHWPGRDkesPDSERhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFC 211
Cdd:cd19085 80 EDVRKSCERSL-KRLGTDYiDLYQIHWPSSD---VPLEE-------TMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 212 DVkpAVNQIE--LHARFPQTELRAFCESVGVHVVGYSPLGVGaLL------------DDDR------------------- 258
Cdd:cd19085 149 RI--DSNQLPynLLWRAIEYEILPFCREHGIGVLAYSPLAQG-LLtgkfssaedfppGDARtrlfrhfepgaeeetfeal 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 259 --VKAYAATIGLRPAPALVRWTLSMG--ASVVVKSSVAERTEENFTAIS-DLDDDFV 310
Cdd:cd19085 226 ekLKEIADELGVTMAQLALAWVLQQPgvTSVIVGARNPEQLEENAAAVDlELSPSVL 282
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
59-299 |
4.97e-25 |
|
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: 102.57 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGET----CRDAVRDALRCGFQHVDTASVYGNERDVGEALR---ACHREVSERIFVTTKI----AP 127
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTpkgaCAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIRekiAEGKVKREDIFYCGKLwntcHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 128 SEMrseeeaaaaiagVNERLGRT--------PDLVLVHWPGRDKES----PDSER-----HRDARRWTWRALENALKMGQ 190
Cdd:cd19109 81 PEL------------VRPTLERTlkvlqldyVDLYIIEMPMAFKPGdeiyPRDENgkwlyHKTNLCATWEALEACKDAGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 191 CRAIGVSNYELSHLRELLQFCDVK--PAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG-----------ALLDDD 257
Cdd:cd19109 149 VKSIGVSNFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrdpiwvnvsspPLLEDP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1199291583 258 RVKAYAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19109 229 LLNSIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENF 270
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
63-299 |
5.38e-24 |
|
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: 97.97 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 63 PMLAFGTYRLRG----ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAchREVSERIFVTTKIAPSEMRSEEE 135
Cdd:cd06660 1 SRLGLGTMTFGGdgdeEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKG--RGNRDDVVIATKGGHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVN-------ERLGR-TPDLVLVHWPGRDKesPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLREL 207
Cdd:cd06660 79 SRLSPEHIRrdleeslRRLGTdYIDLYYLHRDDPST--PVEE--------TLEALNELVREGKIRYIGVSNWSAERLAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 208 LQFCD----VKPAVNQIE---LHARFPQTELRAFCESVGVHVVGYSPLGVGAlldddrvkayaatiglrPAPALvRWTLS 280
Cdd:cd06660 149 LAYAKahglPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLARGP-----------------AQLAL-AWLLS 210
|
250 260
....*....|....*....|.
gi 1199291583 281 --MGASVVVKSSVAERTEENF 299
Cdd:cd06660 211 qpFVTVPIVGARSPEQLEENL 231
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
59-322 |
1.31e-23 |
|
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: 98.71 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-------ETCRDAVRDALRCGFQHVDTASVYG---NERDVGEALRACHREvseRIFVTTKIAPS 128
Cdd:COG0667 10 GLKVSRLGLGTMTFGGpwggvdeAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKGRPRD---DVVIATKVGRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 129 EMRSEEEAAAAIAGVNE-------RLGR-TPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYE 200
Cdd:COG0667 87 MGPGPNGRGLSREHIRRaveaslrRLGTdYIDLYQLHRP--DPDTPIEE--------TLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 201 LSHLRELLQFCD--VKPAVNQIE--LHARFPQTELRAFCESVGVHVVGYSPLGVGALL----------DDDR-------- 258
Cdd:COG0667 157 AEQLRRALAIAEglPPIVAVQNEysLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTgkyrrgatfpEGDRaatnfvqg 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199291583 259 ------------VKAYAATIGLRPAPALVRWTLSMG--ASVVVKSSVAERTEENFTAIS-DLDDDFVheaaEKLETAFA 322
Cdd:COG0667 237 ylternlalvdaLRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADlELSAEDL----AALDAALA 311
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
62-299 |
2.13e-23 |
|
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: 98.07 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 62 MPMLAFGTYRLRG---ETCRDAVRDALRCGFQHVDTASVYGNERDVGEALRA------CHREvseRIFVTTKIAPSEMRS 132
Cdd:cd19108 11 IPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSkiadgtVKRE---DIFYTSKLWCTFHRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 EEeaaaaiagVNERLGRT--------PDLVLVHWP----GRDKESPDSERHR------DARRwTWRALENALKMGQCRAI 194
Cdd:cd19108 88 EL--------VRPALEKSlkklqldyVDLYLIHFPvalkPGEELFPKDENGKlifdtvDLCA-TWEAMEKCKDAGLAKSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 195 GVSNYELSHLRELL--QFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVG-----------ALLDDDRVKA 261
Cdd:cd19108 159 GVSNFNRRQLEMILnkPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrdkewvdqnspVLLEDPVLCA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1199291583 262 YAATIGLRPAPALVRWTLSMGASVVVKSSVAERTEENF 299
Cdd:cd19108 239 LAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENL 276
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
59-308 |
1.01e-20 |
|
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: 90.28 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG--------ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRachrEVSERIFVTTK--- 124
Cdd:cd19084 1 DLKVSRIGLGTWAIGGtwwgevddQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALK----GRRDDVVIATKcgl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 125 -----------IAPSEMRSEeeaaaaiagVNERLGR----TPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMG 189
Cdd:cd19084 77 rwdggkgvtkdLSPESIRKE---------VEQSLRRlqtdYIDLYQIHWP--DPNTPIEE--------TAEALEKLKKEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 190 QCRAIGVSNYELSHLRELLQFCDVkpAVNQIE--LHARFPQTELRAFCESVGVHVVGYSPLGVGaLL------------D 255
Cdd:cd19084 138 KIRYIGVSNFSVEQLEEARKYGPI--VSLQPPysMLEREIEEELLPYCRENGIGVLPYGPLAQG-LLtgkykkeptfppD 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199291583 256 DDR--------------------VKAYAATIGLRPAPALVRWTL--SMGASVVVKSSVAERTEENFTAIS-DLDDD 308
Cdd:cd19084 215 DRRsrfpffrgenfeknleivdkLKEIAEKYGKSLAQLAIAWTLaqPGVTSAIVGAKNPEQLEENAGALDwELTEE 290
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
65-301 |
1.79e-15 |
|
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: 74.95 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG----------ETCRDAVRDALRCGFQHVDTASVYG---NERDVGEALRAchreVSERIFVTTKI------ 125
Cdd:cd19088 4 LGYGAMRLTGpgiwgppadrEEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHP----YPDDVVIATKGglvrtg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 126 --------APSEMRSEEEAAaaiagvNERLGR-TPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGV 196
Cdd:cd19088 80 pgwwgpdgSPEYLRQAVEAS------LRRLGLdRIDLYQLHRI--DPKVPFEE--------QLGALAELQDEGLIRHIGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 197 SNYELSHLRELLQFCDVKPAVNQIELHARFPQtELRAFCESVGVHVVGYSPLGVGALLDDDR-VKAYAATIGLRPAPALV 275
Cdd:cd19088 144 SNVTVAQIEEARAIVRIVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLAQPGGlLAEVAARLGATPAQVAL 222
|
250 260
....*....|....*....|....*...
gi 1199291583 276 RWTLSMGASVVV--KSSVAERTEENFTA 301
Cdd:cd19088 223 AWLLARSPVMLPipGTSSVEHLEENLAA 250
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
78-261 |
6.26e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 74.25 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 78 RDAVRDALRCGFQHVDTASVYG---NERDVGEALRachrEVSERIFVTTKIAP-----SEMRSEEEAAAAIAGVNE---R 146
Cdd:cd19102 29 IAAIRAALDLGINWIDTAAVYGlghSEEVVGRALK----GLRDRPIVATKCGLlwdeeGRIRRSLKPASIRAECEAslrR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 147 LGR-TPDLVLVHWPGRDKESPDSerhrdarrwtWRALENALKMGQCRAIGVSNYELSHLRELLqfcDVKP-AVNQI--EL 222
Cdd:cd19102 105 LGVdVIDLYQIHWPDPDEPIEEA----------WGALAELKEEGKVRAIGVSNFSVDQMKRCQ---AIHPiASLQPpySL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1199291583 223 HARFPQTELRAFCESVGVHVVGYSPLGVGAL---LDDDRVKA 261
Cdd:cd19102 172 LRRGIEAEILPFCAEHGIGVIVYSPMQSGLLtgkMTPERVAS 213
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
53-253 |
1.44e-13 |
|
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: 70.38 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 53 TRAIAP-GINMPMLAFGTYRLRGET---------CRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRachrEVSERI 119
Cdd:cd19149 1 YRKLGKsGIEASVIGLGTWAIGGGPwwggsddneSIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIK----GRRDKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 120 FVTTKIAPSEMRSEEEAAAAIAGVN------------------ERLGR-TPDLVLVHWPgrDKESPDSErhrdarrwTWR 180
Cdd:cd19149 77 VLATKCGLRWDREGGSFFFVRDGVTvyknlspesireeveqslKRLGTdYIDLYQTHWQ--DVETPIEE--------TME 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199291583 181 ALENALKMGQCRAIGVSNYELSHLRELLQFcdVKPAVNQIE--LHARFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19149 147 ALEELKRQGKIRAIGASNVSVEQIKEYVKA--GQLDIIQEKysMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLL 219
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-302 |
6.06e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 67.61 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRGEtCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHRevsERIFVTTKIapSEMRSEEE 135
Cdd:cd19105 10 GLKVSRLGFGGGGLPRE-SPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKGLRR---DKVFLATKA--SPRLDKKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGVNERLGR--TP--DLVLVHWPGRDKESPDSErhrdarrWTWRALENALKMGQCRAIGVSnyELSHLRELLQ-- 209
Cdd:cd19105 84 KAELLKSVEESLKRlqTDyiDIYQLHGVDTPEERLLNE-------ELLEALEKLKKEGKVRFIGFS--THDNMAEVLQaa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 210 ----FCDV-KPAVNQIELHARFPqtELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAAtiGLRPAPALVRWTLSMG-- 282
Cdd:cd19105 155 iesgWFDViMVAYNFLNQPAELE--EALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK--GFSLPQAALKWVLSNPrv 230
|
250 260
....*....|....*....|
gi 1199291583 283 ASVVVKSSVAERTEENFTAI 302
Cdd:cd19105 231 DTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
75-287 |
1.25e-12 |
|
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: 67.33 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 75 ETCRDAVRDALRCGFQHVDTASVYG---NERDVGEALRAchREVSERIFVTTKIA-----PSEMRSEEEAAAAIAGVNER 146
Cdd:cd19148 25 KEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKE--YGKRDRVVIATKVGlewdeGGEVVRNSSPARIRKEVEDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 147 LGR----TPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFC---DVKPAVNQ 219
Cdd:cd19148 103 LRRlqtdYIDLYQVHWP--DPLVPIEE--------TAEALKELLDEGKIRAIGVSNFSPEQMETFRKVAplhTVQPPYNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 220 IELHArfpQTELRAFCESVGVHVVGYSPLGVGALL-----------DD--------------------DRVKAYAATIGL 268
Cdd:cd19148 173 FEREI---EKDVLPYARKHNIVTLAYGALCRGLLSgkmtkdtkfegDDlrrtdpkfqeprfsqylaavEELDKLAQERYG 249
|
250 260
....*....|....*....|
gi 1199291583 269 RPAPAL-VRWTLSMGASVVV 287
Cdd:cd19148 250 KSVIHLaVRWLLDQPGVSIA 269
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
65-298 |
8.31e-12 |
|
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: 65.03 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRGETCRD-----AVRDALRCGFQHVDTASVYGN---ERDVGEALRA--CHREVS-ERIFVTTK---IAPSEM 130
Cdd:cd19099 6 LGLGTYRGDSDDETDeeyreALKAALDSGINVIDTAINYRGgrsERLIGKALREliEKGGIKrDEVVIVTKagyIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 131 RSEEEAAAAIAGVN-----------------------------ERLGR-TPDLVLVHWPGRDKESPDSERHRDARRWTWR 180
Cdd:cd19099 86 EPLRPLKYLEEKLGrglidvadsaglrhcispayledqierslKRLGLdTIDLYLLHNPEEQLLELGEEEFYDRLEEAFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 181 ALENALKMGQCRAIGVSNYELS--------HLRELLQFCDVKPA-------------VNQIELHARFPQTE-------LR 232
Cdd:cd19099 166 ALEEAVAEGKIRYYGISTWDGFrappalpgHLSLEKLVAAAEEVggdnhhfkviqlpLNLLEPEALTEKNTvkgealsLL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199291583 233 AFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRP-APALVRWTLSM--GASVVVKSSVAERTEEN 298
Cdd:cd19099 246 EAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGATlAQRALQFARSTpgVDSALVGMRRPEHVDEN 314
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-287 |
8.85e-12 |
|
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: 64.04 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG---ETCRDAVRDALRCGFQHVDTASVYGN-ERDVGEALRAcHRevsERIFVTTKIA---PSEMR 131
Cdd:cd19100 8 GLKVSRLGFGGGPLGRlsqEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-RR---DKVFLATKTGardYEGAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 132 seeeaaaaiAGVNE---RLGR-TPDLVLVHWPGRDKESPDSERHRDArrwtWRALENALKMGQCRAIGVSNYELSHLREL 207
Cdd:cd19100 84 ---------RDLERslkRLGTdYIDLYQLHAVDTEEDLDQVFGPGGA----LEALLEAKEEGKIRFIGISGHSPEVLLRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 208 LQ--FCD-VKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAAtiglrpapalVRWTLSMGAS 284
Cdd:cd19100 151 LEtgEFDvVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA----------LRYALSLPPV 220
|
...
gi 1199291583 285 VVV 287
Cdd:cd19100 221 DVV 223
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
72-305 |
1.24e-11 |
|
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: 64.36 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 72 LRGETCRDAVRDALRCGFQHVDTASVYG---NERDVGEALRACHRevsERIFVTTKIA-------------PSEMRSEee 135
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYNR---NEVVIATKGAhkfggdgsvlnnsPEFLRSA-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 aaaaiagVNERLGRTP----DLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFC 211
Cdd:cd19083 105 -------VEKSLKRLNtdyiDLYYIHFP--DGETPKAE--------AVGALQELKDEGKIRAIGVSNFSLEQLKEANKDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 212 DVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL---------LDD----------------------DRVK 260
Cdd:cd19083 168 YVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLagkytkdtkFPDndlrndkplfkgerfsenldkvDKLK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199291583 261 AYAATIGLRPAPALVRWTLSM-GASVV-------------VKSSVAERTEENFTAISDL 305
Cdd:cd19083 248 SIADEKGVTVAHLALAWYLTRpAIDVVipgakraeqvidnLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
59-267 |
1.81e-11 |
|
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: 63.73 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-----ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAcHREVSERIFVTTK---IAP 127
Cdd:cd19092 3 GLEVSRLVLGCMRLADwgesaEELLSLIEAALELGITTFDHADIYGGgkcEELFGEALAL-NPGLREKIEIQTKcgiRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 128 SEMRSEEEA------AAAIAGVN---ERLGRTP-DLVLVHwpgRdkesPD-----SErhrdarrwTWRALENALKMGQCR 192
Cdd:cd19092 82 DDPRPGRIKhydtskEHILASVEgslKRLGTDYlDLLLLH---R----PDplmdpEE--------VAEAFDELVKSGKVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 193 AIGVSNYELSHLrELLQ-FCDVKPAVNQIE---LHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDD-----RVKAYA 263
Cdd:cd19092 147 YFGVSNFTPSQI-ELLQsYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGFderfqRLRAAL 225
|
....
gi 1199291583 264 ATIG 267
Cdd:cd19092 226 EELA 229
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
65-318 |
3.16e-11 |
|
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: 62.58 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG--------ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHRevsERIFVTTKIAPSEMRSE 133
Cdd:cd19096 3 LGFGTMRLPEsdddsideEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKEGPR---EKFYLATKLPPWSVKSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 134 EEAAAAiagVNERLGRT----PDLVLVHWPGRDkESPDSERHRDArrwtWRALENALKMGQCRAIGVS---NYELshLRE 206
Cdd:cd19096 80 EDFRRI---LEESLKRLgvdyIDFYLLHGLNSP-EWLEKARKGGL----LEFLEKAKKEGLIRHIGFSfhdSPEL--LKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 207 LLQ-----FCdvkpavnQIELHA----RFPQTELRAFCESVGVHVVGYSPLGVGALLDD-DRVKAYAATIGLRPAPALVR 276
Cdd:cd19096 150 ILDsydfdFV-------QLQYNYldqeNQAGRPGIEYAAKKGMGVIIMEPLKGGGLANNpPEALAILCGAPLSPAEWALR 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1199291583 277 WTLSMGASVVVKSsvaerteeNFTAISDLDDDfvHEAAEKLE 318
Cdd:cd19096 223 FLLSHPEVTTVLS--------GMSTPEQLDEN--IAAADEFE 254
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
63-309 |
5.57e-11 |
|
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: 62.19 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 63 PMLAFGTYRLRG-------ETCRDAVRDALRCGFQHVDTASVYGN-ERDVGEALRACHRevsERIFVTTKIAPSE----- 129
Cdd:cd19090 1 SALGLGTAGLGGvfggvddDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAELPR---EPLVLSTKVGRLPedtad 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 ------MRSEEEAAaaiagvnERLGRTP-DLVLVHWPGRDkeSPDSErhrDARRWTWRALENALKMGQCRAIGVSNYELS 202
Cdd:cd19090 78 ysadrvRRSVEESL-------ERLGRDRiDLLMIHDPERV--PWVDI---LAPGGALEALLELKEEGLIKHIGLGGGPPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 203 HLRELLQF--CDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDD--------------------RVK 260
Cdd:cd19090 146 LLRRAIETgdFDVVLTANRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPpervrytyrwlspelldrakRLY 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1199291583 261 AYAATIGLrPAPAL-VRWTLSMG--ASVVVKSSVAERTEENFTAIS-DLDDDF 309
Cdd:cd19090 226 ELCDEHGV-PLPALaLRFLLRDPriSTVLVGASSPEELEQNVAAAEgPLPEEL 277
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
84-303 |
7.80e-11 |
|
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: 61.85 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 84 ALRCGFQHVDTASVYG---NERDVGEALRAcHRevsERIFVTTKIAPsemrsEEEAAAAIAGVN--------------ER 146
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKD-RR---DEVVIATKFGI-----VRDPGSGFRGVDgrpeyvraaceaslKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 147 LGR-TPDLVLVHwpGRDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQfcdVKP--AVnQIE-- 221
Cdd:cd19076 112 LGTdVIDLYYQH--RVDPNVPIEE--------TVGAMAELVEEGKVRYIGLSEASADTIRRAHA---VHPitAV-QSEys 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 222 LHARFPQTELRAFCESVGVHVVGYSPLGVGAL-----------LDDDR--------------------VKAYAATIGLRP 270
Cdd:cd19076 178 LWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLtgaikspedlpEDDFRrnnprfqgenfdknlklvekLEAIAAEKGCTP 257
|
250 260 270
....*....|....*....|....*....|....*..
gi 1199291583 271 APALVRWTLSMGASVV----VKSsvAERTEENFTAIS 303
Cdd:cd19076 258 AQLALAWVLAQGDDIVpipgTKR--IKYLEENVGALD 292
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
75-287 |
8.91e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 61.90 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 75 ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALrachREVSERIFVTTKIAPSEMRSEEEAAAAIAGVN---ERLG 148
Cdd:cd19104 32 EEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRAL----KGLPAGPYITTKVRLDPDDLGDIGGQIERSVEkslKRLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 149 RTP-DLVLVH--------WPGRDKESPDserHRDARRWTWRALENALKMGQCRAIG---VSNYELshLRELLQ---FCDV 213
Cdd:cd19104 108 RDSvDLLQLHnrigderdKPVGGTLSTT---DVLGLGGVADAFERLRSEGKIRFIGitgLGNPPA--IRELLDsgkFDAV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 214 KPAVN------QIELHARFPQTELRAFCESV---GVHVVGYSPLGVGAL-------------------LDDDRVKAYAAT 265
Cdd:cd19104 183 QVYYNllnpsaAEARPRGWSAQDYGGIIDAAaehGVGVMGIRVLAAGALttsldrgreapptsdsdvaIDFRRAAAFRAL 262
|
250 260
....*....|....*....|....*.
gi 1199291583 266 I---GLRPAPALVRWTLSM-GASVVV 287
Cdd:cd19104 263 ArewGETLAQLAHRFALSNpGVSTVL 288
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
59-320 |
1.35e-10 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 61.76 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG---ETCRDAVRDALRCGFQHVDTASVYGN-ERDVGEALrachREVSERIFVTTKIAP-----SE 129
Cdd:COG1453 10 GLEVSVLGFGGMRLPRkdeEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKAL----KGPRDKVILATKLPPwvrdpED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 130 MRSEeeaaaaiagVNERLGR--TP--DLVLVHWPGRDKESPDSERHRDArrwtWRALENALKMGQCRAIGVSnyelSH-- 203
Cdd:COG1453 86 MRKD---------LEESLKRlqTDyiDLYLIHGLNTEEDLEKVLKPGGA----LEALEKAKAEGKIRHIGFS----THgs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 204 ---LRELLQ-----FCdvkpavnQIELHARF----PQTELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPA 271
Cdd:COG1453 149 levIKEAIDtgdfdFV-------QLQYNYLDqdnqAGEEALEAAAEKGIGVIIMKPLKGGRLANPPEKLVELLCPPLSPA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 272 PALVRWTLSMGASVVVKSSVAE--------RTEENFTAISDLDDDFVHEAAEKLETA 320
Cdd:COG1453 222 EWALRFLLSHPEVTTVLSGMSTpeqldenlKTADNLEPLTEEELAILERLAEELGEL 278
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
65-309 |
8.35e-10 |
|
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: 58.76 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG-----ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHREvseRIFVTTKI-APsemrseee 135
Cdd:cd19074 7 LSLGTWLTFGgqvddEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKGWPRE---SYVISTKVfWP-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 aaaAIAGVNER-LGRTP-----------------DLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVS 197
Cdd:cd19074 76 ---TGPGPNDRgLSRKHifesihaslkrlqldyvDIYYCHRY--DPETPLEE--------TVRAMDDLIRQGKILYWGTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 198 NYELSHLRELLQFCD----VKPAVNQIELH--ARFPQTELRAFCESVGVHVVGYSPL--GV------------------- 250
Cdd:cd19074 143 EWSAEQIAEAHDLARqfglIPPVVEQPQYNmlWREIEEEVIPLCEKNGIGLVVWSPLaqGLltgkyrdgipppsrsratd 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199291583 251 -------GALLDDDRV------KAYAATIGLRPAPALVRWTLS--MGASVVVKSSVAERTEENFTA-ISDLDDDF 309
Cdd:cd19074 223 ednrdkkRRLLTDENLekvkklKPIADELGLTLAQLALAWCLRnpAVSSAIIGASRPEQLEENVKAsGVKLSPEV 297
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
59-256 |
1.27e-09 |
|
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: 58.42 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-----ETCRDAVRDALRCGFQHVDTASVYGN-----ERDVGEALRACHREVSERIFVTTKI--- 125
Cdd:cd19089 8 GLHLPAISLGLWHNFGdytspEEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPYRDELVISTKAgyg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 126 -APSEMRSEEEAAAAIAGVNERLGRTP----DLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYE 200
Cdd:cd19089 88 mWPGPYGDGGSRKYLLASLDQSLKRMGldyvDIFYHHRY--DPDTPLEE--------TMTALADAVRSGKALYVGISNYP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199291583 201 LSHLRELLQFCD---VKPAVNQ--IELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDD 256
Cdd:cd19089 158 GAKARRAIALLRelgVPLIIHQprYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDK 218
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
65-253 |
1.32e-09 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 57.49 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG--------ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHrevsERIFVTTKIAPSEMRSE 133
Cdd:cd19086 6 IGFGTWGLGGdwwgdvddAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGRR----DKVVIATKFGNRFDGGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 134 EEAAAAIAG-----VNE---RLGRTP-DLVLVH-WPGRDKESPDserhrdarrwTWRALENALKMGQCRAIGVSnyeLSH 203
Cdd:cd19086 82 ERPQDFSPEyireaVEAslkRLGTDYiDLYQLHnPPDEVLDNDE----------LFEALEKLKQEGKIRAYGVS---VGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1199291583 204 LRELLQFCDV-KPAVNQIELHA--RFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19086 149 PEEALAALRRgGIDVVQVIYNLldQRPEEELFPLAEEHGVGVIARVPLASGLL 201
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
59-308 |
2.31e-09 |
|
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: 57.62 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGT-------------YRLRGETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAcHREvseRIFVT 122
Cdd:cd19091 10 GLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILGKALKG-RRD---DVLIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 123 TKIApseMRseeeaaaAIAGVNE-----------------RLGRT-PDLVLVHwpGRDKESPDSErhrdarrwTWRALEN 184
Cdd:cd19091 86 TKVR---GR-------MGEGPNDvglsrhhiiraveaslkRLGTDyIDLYQLH--GFDALTPLEE--------TLRALDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 185 ALKMGQCRAIGVSNYELSHLRELLQFCD----VKPAVNQI--ELHARFPQTELRAFCESVGVHVVGYSPLGVGAL----- 253
Cdd:cd19091 146 LVRQGKVRYIGVSNFSAWQIMKALGISErrglARFVALQAyySLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLsgkyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 254 ------------------LDDDRVKAY---------AATIGLRPAPALVRWTLSM--GASVVVKSSVAERTEENFTAIS- 303
Cdd:cd19091 226 rgqpapegsrlrrtgfdfPPVDRERGYdvvdalreiAKETGATPAQVALAWLLSRptVSSVIIGARNEEQLEDNLGAAGl 305
|
....*
gi 1199291583 304 DLDDD 308
Cdd:cd19091 306 SLTPE 310
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
65-253 |
2.46e-09 |
|
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: 57.61 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLrGETCR--------DAVRDAlrcGFQHVDTASVYGN----------ERDVGEALRAchREVSERIFVTTKIA 126
Cdd:cd19081 12 LCLGTMVF-GWTADeetsfallDAFVDA---GGNFIDTADVYSAwvpgnaggesETIIGRWLKS--RGKRDRVVIATKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 127 pSEMR------SEEEAAAAIAGVNERLG-RTPDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNY 199
Cdd:cd19081 86 -FPMGpngpglSRKHIRRAVEASLRRLQtDYIDLYQAHWD--DPATPLEE--------TLGALNDLIRQGKVRYIGASNY 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199291583 200 ELSHLRELLQFCD---------VKPAVNqieLHARFP-QTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19081 155 SAWRLQEALELSRqhglpryvsLQPEYN---LVDRESfEGELLPLCREEGIGVIPYSPLAGGFL 215
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
75-308 |
2.97e-09 |
|
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: 57.21 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 75 ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRA-CHREvseRIFVTTKIAPsEMRSeeeaaaaiaGVN------ 144
Cdd:cd19079 35 EESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKEfAPRD---EVVIATKVYF-PMGD---------GPNgrglsr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 145 -----------ERLGRT-PDLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCD 212
Cdd:cd19079 102 khimaevdaslKRLGTDyIDLYQIHRW--DYETPIEE--------TLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 213 V----KPAV--NQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL--------------LDD---------------- 256
Cdd:cd19079 172 KngwtKFVSmqNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLarpwgdtterrrstTDTaklkydyfteadkeiv 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1199291583 257 DRVKAYAATIGLRPAPALVRWTLSMG--ASVVVKSSVAERTEENFTAIS-DLDDD 308
Cdd:cd19079 252 DRVEEVAKERGVSMAQVALAWLLSKPgvTAPIVGATKLEHLEDAVAALDiKLSEE 306
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
59-253 |
8.36e-09 |
|
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: 56.02 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-------ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHREvseRIFVTTKIA-- 126
Cdd:cd19163 10 GLKVSKLGFGASPLGGvfgpvdeEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKGIPRD---SYYLATKVGry 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 127 ---PSEM---------RSeeeaaaaiagVNERLGRTP----DLVLVHwpgrDKE-SPDSERHRDArrwTWRALENALKMG 189
Cdd:cd19163 87 gldPDKMfdfsaeritKS----------VEESLKRLGldyiDIIQVH----DIEfAPSLDQILNE---TLPALQKLKEEG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199291583 190 QCRAIGVSNYELSHLRELLQFCDVKpaVNQIELHARF-----PQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19163 150 KVRFIGITGYPLDVLKEVLERSPVK--IDTVLSYCHYtlndtSLLELLPFFKEKGVGVINASPLSMGLL 216
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
70-257 |
3.86e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 53.75 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 70 YRLRGETCRDAVRDALRCGFQHVDTASVYGN-ERDVGEALR--ACHREVSERIFVTTKIAPSEMRSEEEAAAAIAGVNER 146
Cdd:cd19101 18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGPaEELIGEFRKrlRRERDAADDVQIHTKWVPDPGELTMTRAYVEAAIDRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 147 LGRTP----DLVLVHWpgrdkESPDSERHRDARRWTwraleNALKM-GQCRAIGVSNYELSHLRELLQfCDVKPAVNQIE 221
Cdd:cd19101 98 LKRLGvdrlDLVQFHW-----WDYSDPGYLDAAKHL-----AELQEeGKIRHLGLTNFDTERLREILD-AGVPIVSNQVQ 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199291583 222 LHA--RFPQTELRAFCESVGVHVVGYSPLGvGALLDDD 257
Cdd:cd19101 167 YSLldRRPENGMAALCEDHGIKLLAYGTLA-GGLLSEK 203
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
81-225 |
7.50e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 52.91 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 81 VRDALRCGFQHVDTASVYGN-ERDVGEALRAchrevSERIFVTTKIAPSEMRSEEEAAAAIAGVNE---RLGR-TPDLVL 155
Cdd:cd19097 32 LEYALKAGINTLDTAPAYGDsEKVLGKFLKR-----LDKFKIITKLPPLKEDKKEDEAAIEASVEAslkRLKVdSLDGLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 156 VHWPGrdkespDSERHRDARrwtWRALENALKMGQCRAIGVSNYELSHLRELLQ--FCDV-------------------K 214
Cdd:cd19097 107 LHNPD------DLLKHGGKL---VEALLELKKEGLIRKIGVSVYSPEELEKALEsfKIDIiqlpfnildqrflksgllaK 177
|
170
....*....|.
gi 1199291583 215 PAVNQIELHAR 225
Cdd:cd19097 178 LKKKGIEIHAR 188
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
65-301 |
7.78e-08 |
|
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: 52.62 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRG-------ETCRDAVRDALRCGFQHVDTASVYGN-ERDVGEALRACHRevsERIFVTTKI----APSEMRS 132
Cdd:cd19095 3 LGLGTSGIGRvwgvpseAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLRR---DDLFIATKVgthgEGGRDRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 133 EEEAAAAIAGVNERLGR--TP--DLVLVHWPGRDKESPDserhrdarrwTWRALENALKMGQCRAIGVSNY--ELSHLRE 206
Cdd:cd19095 80 DFSPAAIRASIERSLRRlgTDyiDLLQLHGPSDDELTGE----------VLETLEDLKAAGKVRYIGVSGDgeELEAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 207 LLQFCDVKPAVNQIELHARfpqtELRAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRPAPAL-----------V 275
Cdd:cd19095 150 SGVFDVVQLPYNVLDREEE----ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAeiggatwaqaaL 225
|
250 260
....*....|....*....|....*...
gi 1199291583 276 RWTLSMGA--SVVVKSSVAERTEENFTA 301
Cdd:cd19095 226 RFVLSHPGvsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
65-253 |
7.84e-08 |
|
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: 52.96 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 65 LAFGTYRLRGETCR-------DAVRDAlrcGFQHVDTASVYGN---ERDVGEALrACHREvseRIFVTTKI------APS 128
Cdd:cd19087 16 LCLGTMNFGGRTDEetsfaimDRALDA---GINFFDTADVYGGgrsEEIIGRWI-AGRRD---DIVLATKVfgpmgdDPN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 129 EMR-SEEEAAAAIAGVNERLGrTP--DLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNY------ 199
Cdd:cd19087 89 DRGlSRRHIRRAVEASLRRLQ-TDyiDLYQMHHF--DRDTPLEE--------TLRALDDLVRQGKIRYIGVSNFaawqia 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 200 ---ELSHLRELLQFCDVKPAVNqieLHARFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19087 158 kaqGIAARRGLLRFVSEQPMYN---LLKRQAELEILPAARAYGLGVIPYSPLAGGLL 211
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
47-318 |
6.36e-07 |
|
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: 50.13 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 47 MSTTKWTRAiapGINMPMLAFGTYRL-------RGETCRDAVRDA---LRCGFqhVDTASVYG-NERDVGEALRACHREv 115
Cdd:cd19144 1 IPTRTLGRN---GPSVPALGFGAMGLsafygppKPDEERFAVLDAafeLGCTF--WDTADIYGdSEELIGRWFKQNPGK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 116 SERIFVTTKIAPSEMRSEEEAAAAIAG--VNE-------RLG-RTPDLVLVHwpgR-DKESPDSErhrdarrwTWRALEN 184
Cdd:cd19144 75 REKIFLATKFGIEKNVETGEYSVDGSPeyVKKacetslkRLGvDYIDLYYQH---RvDGKTPIEK--------TVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 185 ALKMGQCRAIGVSNYELSHLRellQFCDVKP--AVnQIE-----LHARFPQTELRAFCESVGVHVVGYSPLGVGALL--- 254
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLR---RAHAVHPiaAV-QIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTgai 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 255 ---DD-------------------------DRVKAYAATIGLRPAPALVRWTLSMGASVVV--KSSVAERTEENFTA--- 301
Cdd:cd19144 220 rspDDfeegdfrrmaprfqaenfpknlelvDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPipGTTKLKRLEENLGAlkv 299
|
330
....*....|....*...
gi 1199291583 302 -ISDLDDDFVHEAAEKLE 318
Cdd:cd19144 300 kLTEEEEKEIREIAEEAE 317
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
47-266 |
9.56e-07 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 49.76 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 47 MSTTKwtrAIAPGINMPMLAFGTYRLRGETC-----RDAVRDALRCGFQHVDTASVYGN---ERDVGEALRAcHREVSER 118
Cdd:COG4989 1 MKRIK---LGASGLSVSRIVLGCMRLGEWDLspaeaAALIEAALELGITTFDHADIYGGytcEALFGEALKL-SPSLREK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 119 IFVTTK---IAPSEMRSEeeaaaaiaGVN-----------------ERLGrTP--DLVLVHWPgrdkeSPDSERHRDARr 176
Cdd:COG4989 77 IELQTKcgiRLPSEARDN--------RVKhydtskehiiasvegslRRLG-TDylDLLLLHRP-----DPLMDPEEVAE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 177 wtwrALENALKMGQCRAIGVSNYELSHLrELLQ-FCDVKPAVNQIE---LHARFPQTELRAFCESVGVHVVGYSPLGVGA 252
Cdd:COG4989 142 ----AFDELKASGKVRHFGVSNFTPSQF-ELLQsALDQPLVTNQIElslLHTDAFDDGTLDYCQLNGITPMAWSPLAGGR 216
|
250
....*....|....*.
gi 1199291583 253 LL--DDDRVKAYAATI 266
Cdd:COG4989 217 LFggFDEQFPRLRAAL 232
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
75-253 |
9.99e-07 |
|
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: 49.48 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 75 ETCRDAVRDALRCGFQHVDTASVYGN---ERDVGEALrACHREVSerifVTTKIAPSEMRSEEEAAAAIAgVNERLGR-- 149
Cdd:cd19075 20 EAAAELLDAFLERGHTEIDTARVYPDgtsEELLGELG-LGERGFK----IDTKANPGVGGGLSPENVRKQ-LETSLKRlk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 150 TP--DLVLVHWPgrDKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCD----VKPAV-----N 218
Cdd:cd19075 94 VDkvDVFYLHAP--DRSTPLEE--------TLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVyqgmyN 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1199291583 219 QIelhARFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19075 164 AI---TRQVETELFPCLRKLGIRFYAYSPLAGGFL 195
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
81-253 |
2.44e-05 |
|
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: 45.30 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 81 VRDALRCGFQHVDTASVYG---NERDVGEALrACHREvseRIFVTTKiapsemrseeeaaaaiagvnerLGRTPDLVLVH 157
Cdd:cd19078 31 IRKAVELGITFFDTAEVYGpytNEELVGEAL-KPFRD---QVVIATK----------------------FGFKIDGGKPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 158 WPGRDkESPDSERhrdarrwtwRALENALK---------------------------M------GQCRAIGVSNYELSHL 204
Cdd:cd19078 85 PLGLD-SRPEHIR---------KAVEGSLKrlqtdyidlyyqhrvdpnvpieevagtMkelikeGKIRHWGLSEAGVETI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1199291583 205 RELLQFCDVKPAVNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19078 155 RRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFL 203
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
63-258 |
5.25e-05 |
|
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: 44.27 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 63 PMLAFGTYRL-----RGETCRDAVRD-ALRCGFQHVDTASVYG---NERDVGEALRacHREVSErIFVTTKI-------- 125
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDaAWDAGIRYFDTAPLYGlglSERRLGAALA--RHPRAE-YVVSTKVgrllepga 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 126 ----APSEMR---SEEEAAAAIAGVNERLGRTP-DLVLVHwpgrdkespDSERHRD-ARRWTWRALENALKMGQCRAIGV 196
Cdd:cd19162 78 agrpAGADRRfdfSADGIRRSIEASLERLGLDRlDLVFLH---------DPDRHLLqALTDAFPALEELRAEGVVGAIGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199291583 197 SNYELSHLRELLQFCDVKpAV---NQIELHARFPQTELRAFCESVGVHVVGYSPLGVGALLDDDR 258
Cdd:cd19162 149 GVTDWAALLRAARRADVD-VVmvaGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDP 212
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
59-336 |
6.45e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 44.21 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 59 GINMPMLAFGTYRLRG-----ETCRDAVRDALRCGFQHVDTASVYG-----NERDVGEALRACHREVSERIFVTTKIA-- 126
Cdd:PRK09912 22 GLRLPALSLGLWHNFGhvnalESQRAILRKAFDLGITHFDLANNYGpppgsAEENFGRLLREDFAAYRDELIISTKAGyd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 127 --PSEMRSEEEAAAAIAGVNERLGRTP-DLVLVHWPGR-DKESPDSErhrdarrwTWRALENALKMGQCRAIGVSNY--- 199
Cdd:PRK09912 102 mwPGPYGSGGSRKYLLASLDQSLKRMGlEYVDIFYSHRvDENTPMEE--------TASALAHAVQSGKALYVGISSYspe 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 200 ELSHLRELLQFCDVKPAVNQIE---LHARFPQTELRAFCESVGVHVVGYSPLGVGALL--------DDDRVKAYAATI-G 267
Cdd:PRK09912 174 RTQKMVELLREWKIPLLIHQPSynlLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTgkylngipQDSRMHREGNKVrG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 268 LRP-------------------------APALVRWTL--SMGASVVVKSSVAERTEENFTAISDLddDFVHEAAEKLETA 320
Cdd:PRK09912 254 LTPkmlteanlnslrllnemaqqrgqsmAQMALSWLLkdERVTSVLIGASRAEQLEENVQALNNL--TFSTEELAQIDQH 331
|
330
....*....|....*.
gi 1199291583 321 FASERVKFcWNPSSVR 336
Cdd:PRK09912 332 IADGELNL-WQASSDK 346
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
78-299 |
7.82e-05 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 43.75 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 78 RDAVRDALRCGFQHVDTASVYGN---ERDVGEALracHREVSERIFVTTKI-------------------APSEMRseEE 135
Cdd:cd19152 23 KATLVAAWDLGIRYFDTAPWYGAglsEERLGAAL---RELGREDYVISTKVgrllvplqeveptfepgfwNPLPFD--AV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 136 AAAAIAGV-------NERLGRT-PDLVLVHWPGRDKESPDSERHRD-ARRWTWRALENALKMGQCRAIGVSNYELSHLRE 206
Cdd:cd19152 98 FDYSYDGIlrsiedsLQRLGLSrIDLLSIHDPDEDLAGAESDEHFAqAIKGAFRALEELREEGVIKAIGLGVNDWEVILR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 207 LLQFCDvkpaVNQIELHARF------PQTELRAFCESVGVHVVGYSPLGVGALLDD-------------------DRVKA 261
Cdd:cd19152 178 ILEEAD----LDWVMLAGRYtlldhsAARELLPECEKRGVKVVNAGPFNSGFLAGGdnfdyyeygpappeliarrDRIEA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1199291583 262 YAATIGLRP---------APALVrwtlsmgASVVVKSSVAERTEENF 299
Cdd:cd19152 254 LCEQHGVSLaaaalqfalAPPAV-------ASVAPGASSPERVEENV 293
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
79-285 |
2.14e-04 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 42.52 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 79 DAVRDALRCGFQHVDTASVYGN---ERDVGEALRACHREVSErIFVTTKI----------APSEMRSEEEAAAaiagvnE 145
Cdd:cd19153 37 AIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSS-YTVATKVgryrdsefdySAERVRASVATSL------E 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 146 RLGRTP-DLVLVHwpgrDKESPDSERHRDArrwTWRALENALKMGQCRAIGVSNYELSHLRELLQFCDVKPA-VNQIELH 223
Cdd:cd19153 110 RLHTTYlDVVYLH----DIEFVDYDTLVDE---ALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGSLdAVLSYCH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1199291583 224 ARFPQTEL----RAFCESVGVHVVGYSPLGVGALLDDDRVKAYAATIGLRP-APALVRWTLSMGASV 285
Cdd:cd19153 183 LTLQDARLesdaPGLVRGAGPHVINASPLSMGLLTSQGPPPWHPASGELRHyAAAADAVCASVEASL 249
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
60-202 |
6.35e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 40.78 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 60 INMPMLAFGT----------YRLRGE-----TCRDAVRDALRCGFQHVDTASVYG---NERDVGEALRACHREvseRIFV 121
Cdd:cd19103 2 KKLPKIALGTwswgsggaggDQVFGNhldedTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKRYPRE---DYII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 122 TTKIAPsEMR--SEEEAAAAIAGVNERLGR-TPDLVLVHWPGrdkespdserhrDARRWTWRALEnALKMGQCRAIGVSN 198
Cdd:cd19103 79 STKFTP-QIAgqSADPVADMLEGSLARLGTdYIDIYWIHNPA------------DVERWTPELIP-LLKSGKVKHVGVSN 144
|
....
gi 1199291583 199 YELS 202
Cdd:cd19103 145 HNLA 148
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
88-253 |
1.16e-03 |
|
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: 40.24 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 88 GFQHVDTASVY---------G-NERDVGEALRAchREVSERIFVTTKIAPSEMRSEEEAAAAIaGVN------------E 145
Cdd:cd19094 31 GVNFIDTAEMYpvppspetqGrTEEIIGSWLKK--KGNRDKVVLATKVAGPGEGITWPRGGGT-RLDrenireavegslK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199291583 146 RLGrTP--DLVLVHWPGRD------KESPDSERHRDARRW--TWRALENALKMGQCRAIGVSN---------YELSHLRE 206
Cdd:cd19094 108 RLG-TDyiDLYQLHWPDRYtplfggGYYTEPSEEEDSVSFeeQLEALGELVKAGKIRHIGLSNetpwgvmkfLELAEQLG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1199291583 207 LLQFCDVKpavNQIELHARFPQTELRAFCESVGVHVVGYSPLGVGAL 253
Cdd:cd19094 187 LPRIVSIQ---NPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVL 230
|
|
| |
