|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
10-291 |
6.06e-180 |
|
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: 497.95 E-value: 6.06e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 10 SGHSMPLIGMGTAADPlPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKDRDEVFITSKLWCSDA 89
Cdd:cd19124 1 SGQTMPVIGMGTASDP-PSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKSRDELFVTSKLWCSDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 90 DHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKDDILPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKI 169
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 170 ERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSHRVLKSLVLQKIAAAKGKTMAQVALRW 249
Cdd:cd19124 160 QELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNAVMESDVLKEIAAAKGKTVAQVSLRW 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1276262015 250 IHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19124 240 VYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
14-286 |
2.89e-114 |
|
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: 330.60 E-value: 2.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAadpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEeplgRAVAEALKRDLIKdRDEVFITSKLWCSDADHDL 93
Cdd:cd19071 1 MPLIGLGTY---KLKPEETAEAVLAALEAGYRHIDTAAAYGNE----AEVGEAIRESGVP-REELFITTKLWPTDHGYER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 VLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFskddilpfdmKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL 173
Cdd:cd19071 73 VREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEAR----------LETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 174 QHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGangayWGSHRVLKSLVLQKIAAAKGKTMAQVALRWIHEE 253
Cdd:cd19071 143 AAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLG-----RGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR 217
|
250 260 270
....*....|....*....|....*....|...
gi 1276262015 254 GASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19071 218 GVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-296 |
1.88e-111 |
|
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: 324.68 E-value: 1.88e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGT-AADPlpppeNLTSIIID-AIAAGYRHFDTAALYSTEEPLGRAVAEALKrDLIKDRDEVFITSKLW 85
Cdd:cd19125 5 LNTGAKIPAVGLGTwQADP-----GVVGNAVKtAIKEGYRHIDCAAIYGNEKEIGKALKKLFE-DGVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINhfRFSKDDILPFDMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19125 79 CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGAH--MPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSHRVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19125 157 VKKLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNVLKDPIVTKVAEKLGKTPAQV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQCRGLL 296
Cdd:cd19125 237 ALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRVL 287
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-289 |
7.13e-110 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 319.69 E-value: 7.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 10 SGHSMPLIGMGTAadpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEAlkrDLikDRDEVFITSKLWCSDA 89
Cdd:COG0656 1 NGVEIPALGLGTW---QLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---GV--PREELFVTTKVWNDNH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 90 DHDLVLPALKESLRKLGLNYVDLYLIHWPVrikpginhfrfskddilPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKI 169
Cdd:COG0656 73 GYDDTLAAFEESLERLGLDYLDLYLIHWPG-----------------PGPYVETWRALEELYEEGLIRAIGVSNFDPEHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 170 ERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANgaywgshRVLKSLVLQKIAAAKGKTMAQVALRW 249
Cdd:COG0656 136 EELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRG-------KLLDDPVLAEIAEKHGKTPAQVVLRW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1276262015 250 IHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:COG0656 209 HLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-289 |
1.98e-109 |
|
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: 319.61 E-value: 1.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSK 83
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWK--LKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVK-REDLFITTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 LWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKDDILPFDMKGTWKAMEECCKLGLAKSVGLSN 163
Cdd:cd19116 78 LWNSYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 164 FSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGA--YWGSHRVLKSLVLQKIAAAKGKT 241
Cdd:cd19116 158 FNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgQTNPPPRLDDPTLVAIAKKYGKT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1276262015 242 MAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19116 238 TAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSF 285
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
6-289 |
2.87e-94 |
|
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: 281.61 E-value: 2.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLW 85
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSK---PGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVK-REDLWITSKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINhFRFSKDDILPFD---MKGTWKAMEECCKLGLAKSVGLS 162
Cdd:cd19123 80 NNSHAPEDVLPALEKTLADLQLDYLDLYLMHWPVALKKGVG-FPESGEDLLSLSpipLEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 163 NFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANG-----AYWGSHRVLKSLVLQKIAAA 237
Cdd:cd19123 159 NFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamKAEGEPVLLEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1276262015 238 KGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAAL 290
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
6-289 |
3.24e-89 |
|
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: 267.13 E-value: 3.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVaealkRDLIKDRDEVFITSKLW 85
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQ--IPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAI-----KKSGIPREELFITTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRikpginhfrfskddilpfDMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19133 74 IQDAGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG------------------DVYGAWRAMEELYKEGKIRAIGVSNFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGAngaywGSHRVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19133 136 PDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE-----GRNNLFENPVLTEIAEKYGKSVAQV 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19133 211 ILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-289 |
4.53e-86 |
|
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: 260.88 E-value: 4.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMGT-AADPlpppENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITS 82
Cdd:cd19112 1 STITLNSGHKMPVIGLGVwRMEP----GEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVK-REDLFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 83 KLWCSDadHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKP---GINHFRFSKDDILPFD----MKGTWKAMEECCKLGL 155
Cdd:cd19112 76 KLWNSD--HGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLDIDvtisLETTWHAMEKLVSAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 156 AKSVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLG---ANGAYWGSHRVLKSLVLQ 232
Cdd:cd19112 154 VRSIGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaaANAEWFGSVSPLDDPVLK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 233 KIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
8-286 |
2.60e-84 |
|
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: 256.16 E-value: 2.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKDRDEVFITSKLWCS 87
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSK---PGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKAVPREDLFVTSKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKDDILPFDM---KGTWKAMEECCKLGLAKSVGLSNF 164
Cdd:cd19106 78 KHHPEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSthyKETWKAMEKLVDKGLVKAIGLSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYW---GSHRVLKSLVLQKIAAAKGKT 241
Cdd:cd19106 158 NSRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWakpDEPVLLEEPKVKALAKKYNKS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1276262015 242 MAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19106 238 PAQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQL 282
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-289 |
3.22e-84 |
|
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: 254.22 E-value: 3.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 5 EVILNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEA-LKRDlikdrdEVFITSK 83
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVS---NDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASgVPRE------ELFITTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 LWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVrikPGINHFrfskddilpfdmKGTWKAMEECCKLGLAKSVGLSN 163
Cdd:cd19131 72 LWNSDQGYDSTLRAFDESLRKLGLDYVDLYLIHWPV---PAQDKY------------VETWKALIELKKEGRVKSIGVSN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 164 FSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGaywgshrVLKSLVLQKIAAAKGKTMA 243
Cdd:cd19131 137 FTIEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG-------LLSDPVIGEIAEKHGKTPA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 244 QVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19131 210 QVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-289 |
8.56e-84 |
|
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: 253.69 E-value: 8.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTA-----ADPLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKrdlikDRDEVFITSKLW 85
Cdd:cd19120 1 GSKIPAIAFGTGtawykSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGV-----PREDLFITTKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADhdlVLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskddilPFDMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19120 76 PGIKD---PREALRKSLAKLGVDYVDLYLIHSPFFAKEG------------GPTLAEAWAELEALKDAGLVRSIGVSNFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMN--VAWQQQKMLEFCREKGIQVSAWSPLGAngAYWGSHRVLKSlVLQKIAAAKGKTMA 243
Cdd:cd19120 141 IEDLEELLDTAKIKPAVNQIEFHpyLYPQQPALLEYCREHGIVVSAYSPLSP--LTRDAGGPLDP-VLEKIAEKYGVTPA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 244 QVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19120 218 QVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-290 |
5.70e-83 |
|
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: 252.72 E-value: 5.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCS 87
Cdd:cd19154 6 LSNGVKMPLIGLGTWQSK---GAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVK-REDLFITTKLWTH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKDDIL---PFDMKGTWKAMEECCKLGLAKSVGLSNF 164
Cdd:cd19154 82 EHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSihdAVDVEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANG--------AYWGSHRVLKSLVLQKIAA 236
Cdd:cd19154 162 NNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGranftkstGVSPAPNLLQDPIVKAIAE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1276262015 237 AKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQIS 290
Cdd:cd19154 242 KHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIE 295
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
14-289 |
7.90e-82 |
|
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: 248.32 E-value: 7.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDADHDL 93
Cdd:cd19136 1 MPILGLGTFR--LRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLS-REDIFITSKLAPKDQGYEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 VLPALKESLRKLGLNYVDLYLIHWPVRIKpginhfrFSKDDILPFDM-KGTWKAMEECCKLGLAKSVGLSNFSCAKIERL 172
Cdd:cd19136 78 ARAACLGSLERLGTDYLDLYLIHWPGVQG-------LKPSDPRNAELrRESWRALEDLYKEGKLRAIGVSNYTVRHLEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 173 LQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGAngaywGSHRVLKSLVLQKIAAAKGKTMAQVALRWIHE 252
Cdd:cd19136 151 LKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGS-----GDLRLLEDPTVLAIAKKYGRTPAQVLLRWALQ 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 1276262015 253 EGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19136 226 QGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
6-286 |
1.89e-80 |
|
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: 246.37 E-value: 1.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdplpPPENLTSIIID----AIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFIT 81
Cdd:cd19108 3 VKLNDGHFIPVLGFGTYA----PEEVPKSKALEatklAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVK-REDIFYT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 82 SKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskDDILPFDMKG-----------TWKAMEEC 150
Cdd:cd19108 78 SKLWCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPG--------EELFPKDENGklifdtvdlcaTWEAMEKC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 151 CKLGLAKSVGLSNFSCAKIERLLQHATI--PPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgangaywGSHR---- 224
Cdd:cd19108 150 KDAGLAKSIGVSNFNRRQLEMILNKPGLkyKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSAL-------GSQRdkew 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276262015 225 -------VLKSLVLQKIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19108 223 vdqnspvLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKAL 291
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
8-289 |
3.33e-80 |
|
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: 245.01 E-value: 3.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAadpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKDRDEVFITSKLWCS 87
Cdd:cd19118 1 LNTGNKIPAIGLGTW---QAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPGVKREDLFITSKLWNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPG----INHFRFSKDDILPFDMK----GTWKAMEECCKLGLAKSV 159
Cdd:cd19118 78 SHRPEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTgdlnPLTAVPTNGGEVDLDLSvslvDTWKAMVELKKTGKVKSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 160 GLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAywGSHRVLKSLVLQKIAAAKG 239
Cdd:cd19118 158 GVSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLA--GLPLLVQHPEVKAIAAKLG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1276262015 240 KTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDwkLTDEEVKQIKQI 289
Cdd:cd19118 236 KTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVE--LSDDEFNAVTAL 283
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
6-286 |
7.15e-79 |
|
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: 241.16 E-value: 7.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEeplgRAVAEALKRDLIkDRDEVFITSKLW 85
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTP---PEETADAVATALADGYRLIDTAAAYGNE----REVGEGIRRSGV-DRSDIFVTTKLW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVrikpginhfrfskddilPFDMKGT---WKAMEECCKLGLAKSVGLS 162
Cdd:cd19127 73 ISDYGYDKALRGFDASLRRLGLDYVDLYLLHWPV-----------------PNDFDRTiqaYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 163 NFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSH-----RVLKSLVLQKIAAA 237
Cdd:cd19127 136 NFTPEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASGptgpgDVLQDPTITGLAEK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1276262015 238 KGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19127 216 YGKTPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
8-291 |
3.47e-78 |
|
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: 239.09 E-value: 3.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAadPLPPPENLTSIIiDAIAAGYRHFDTAALYSTEEPLGRAVAEALKrdlikDRDEVFITSKLWCS 87
Cdd:cd19132 1 LNDGTQIPAIGFGTY--PLKGDEGVEAVV-AALQAGYRLLDTAFNYENEGAVGEAVRRSGV-----PREELFVTTKLPGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHDLVLPALKESLRKLGLNYVDLYLIHWPVrikPGINHFrfskddilpfdmKGTWKAMEECCKLGLAKSVGLSNFSCA 167
Cdd:cd19132 73 HHGYEEALRTIEESLYRLGLDYVDLYLIHWPN---PSRDLY------------VEAWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 168 KIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAywgshrVLKSLVLQKIAAAKGKTMAQVAL 247
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG------LLDEPVIKAIAEKHGKTPAQVVL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1276262015 248 RWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19132 212 RWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
6-291 |
8.43e-78 |
|
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: 238.44 E-value: 8.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEAlkrdlIKDRDEVFITSKLW 85
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFK--VEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKES-----GIPREELFITSKVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKpginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19157 75 NADQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGK-----------------YKETWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGaywgshrVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19157 138 VHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ-------LLDNPVLKEIAEKYNKSVAQV 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19157 211 ILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNE 256
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
6-286 |
4.14e-77 |
|
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: 236.18 E-value: 4.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKrdlikDRDEVFITSKLW 85
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQ--TPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGV-----PREELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKpginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19126 74 NDDQRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDK-----------------FIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGaywgshrVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19126 137 EHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-------LLSNPVLAAIGEKYGKSAAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19126 210 VLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
8-294 |
2.01e-76 |
|
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: 235.47 E-value: 2.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAvaealkrdlIKD----RDEVFITSK 83
Cdd:cd19117 8 LNTGAEIPAVGLGTWQSK---PNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQG---------IKDsgvpREEIFITTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 LWCSDadHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKDDILPFDMKG-----TWKAMEECCKLGLAKS 158
Cdd:cd19117 76 LWCTW--HRRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPDwdfikTWELMQKLPATGKVKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 159 VGLSNFSCAKIERLL--QHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAywgshRVLKSLVLQKIAA 236
Cdd:cd19117 154 IGVSNFSIKNLEKLLasPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNA-----PLLKEPVIIKIAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 237 AKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDIldWKLTDEEVKQIKQISQCRG 294
Cdd:cd19117 229 KHGKTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDELHKEYG 284
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
6-289 |
1.35e-73 |
|
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: 227.79 E-value: 1.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRdlikdRDEVFITSKLW 85
Cdd:cd19156 1 VKLANGVEMPRLGLGVWR--VQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVP-----REEVFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKpginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19156 74 NSDQGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK-----------------FKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgangaywGSHRVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19156 137 EHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPL-------GQGKLLSNPVLKAIGKKYGKSAAQV 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19156 210 IIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGL 253
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
14-286 |
6.60e-73 |
|
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: 224.84 E-value: 6.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRdlikdRDEVFITSKLWCSDADHDL 93
Cdd:cd19073 1 IPALGLGTWQLR---GDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVP-----REDLFITTKVWRDHLRPED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 VLPALKESLRKLGLNYVDLYLIHWPVRIKPginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL 173
Cdd:cd19073 73 LKKSVDRSLEKLGTDYVDLLLIHWPNPTVP----------------LEETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 174 QHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgANGaywgshRVLKSLVLQKIAAAKGKTMAQVALRWIHEE 253
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-ARG------EVLRDPVIQEIAEKYDKTPAQVALRWLVQK 209
|
250 260 270
....*....|....*....|....*....|...
gi 1276262015 254 GASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19073 210 GIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-291 |
7.55e-73 |
|
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: 227.30 E-value: 7.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMG-------TAADplpppenltsIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRD 76
Cdd:cd19115 3 PTVKLNSGYDMPLVGFGlwkvnndTCAD----------QVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVK-RE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 77 EVFITSKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWP---------VRIKPG----INHFRFSKDDIlpfdmKGT 143
Cdd:cd19115 72 DLFIVSKLWNTFHDGERVEPICRKQLADWGIDYFDLFLIHFPialkyvdpaVRYPPGwfydGKKVEFSNAPI-----QET 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 144 WKAMEECCKLGLAKSVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSH 223
Cdd:cd19115 147 WTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSFLELDL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276262015 224 R-------VLKSLVLQKIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19115 227 PgakdtppLFEHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDI 301
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
11-286 |
2.23e-72 |
|
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: 224.06 E-value: 2.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTAadPLPPpENLTSIIIDAIAAGYRHFDTAALYSTEEPLGravaEALKRDLIKdRDEVFITSKLWCSDAD 90
Cdd:cd19140 5 GVRIPALGLGTY--PLTG-EECTRAVEHALELGYRHIDTAQMYGNEAQVG----EAIAASGVP-RDELFLTTKVWPDNYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 91 HDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfSKDDilpfDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIE 170
Cdd:cd19140 77 PDDFLASVEESLRKLRTDYVDLLLLHWP------------NKDV----PLAETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 171 RLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgANGaywgshRVLKSLVLQKIAAAKGKTMAQVALRWI 250
Cdd:cd19140 141 EAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPL-ARG------EVLKDPVLQEIGRKHGKTPAQVALRWL 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 1276262015 251 -HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19140 214 lQQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
11-291 |
6.23e-72 |
|
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: 224.68 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTAADPLPPPENLTSIIID-AIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDA 89
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKGACAEAVKvAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVK-REDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 90 DHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskDDILPFDMKG-----------TWKAMEECCKLGLAKS 158
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPG--------DEIYPRDENGkwlyhktnlcaTWEALEACKDAGLVKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 159 VGLSNFSCAKIERLLQHATIP--PAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGA-YW---GSHRVLKSLVLQ 232
Cdd:cd19109 152 IGVSNFNRRQLELILNKPGLKhkPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpIWvnvSSPPLLEDPLLN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1276262015 233 KIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19109 232 SIGKKYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNK 290
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
8-289 |
2.86e-71 |
|
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: 222.02 E-value: 2.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGT-AADPlppPEnLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALkrDLIKDRDEVFITSKLWC 86
Cdd:cd19121 6 LNTGASIPAVGLGTwQAKA---GE-VKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI--AGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SDadHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRF------SKDDILPFDMKGTWKAMEECCKLGLAKSVG 160
Cdd:cd19121 80 TY--HRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFptlpdgSRDLDWDWNHVDTWKQMEKVLKTGKTKAIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 161 LSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAywgshRVLKSLVLQKIAAAKGK 240
Cdd:cd19121 158 VSNYSIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGS-----PLISDEPVVEIAKKHNV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1276262015 241 TMAQVALRWIHEEGASIIVKSFNNERMRENLDILDwkLTDEEVKQIKQI 289
Cdd:cd19121 233 GPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIID--LDDEDMNKLNDI 279
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
6-286 |
3.95e-70 |
|
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: 218.63 E-value: 3.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAAdplPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEAlkrDLikDRDEVFITSKLW 85
Cdd:cd19130 2 IVLNDGNSIPQLGYGVFK---VPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAAS---GI--PRDELFVTTKLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVrikPginhfrfSKDDILPfdmkgTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:cd19130 74 NDRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPT---P-------AAGNYVH-----TWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANgaywgshRVLKSLVLQKIAAAKGKTMAQV 245
Cdd:cd19130 139 PPHLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG-------KLLGDPPVGAIAAAHGKTPAQI 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1276262015 246 ALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19130 212 VLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
6-291 |
4.09e-70 |
|
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: 220.09 E-value: 4.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 6 VILNSGHSMPLIGMGTAadpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLW 85
Cdd:cd19155 4 VTFNNGEKMPVVGLGTW---QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVK-REELFIVTKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIK-PGINHFRFSKDDILPFDMK----GTWKAMEECCKLGLAKSVG 160
Cdd:cd19155 80 PGGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHKQDYTtdllDIWKAMEAQVDQGLTRSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 161 LSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAY------WGSHRVLKSL----V 230
Cdd:cd19155 160 LSNFNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAhfspgtGSPSGSSPDLlqdpV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 231 LQKIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDK 300
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
4-291 |
5.39e-70 |
|
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: 220.01 E-value: 5.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMG-------TAADPlpppenltsiIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRD 76
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGcwkldnaTAADQ----------IYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVK-RE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 77 EVFITSKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIK---------PGI---NHFRFSKDDILPFDmkgTW 144
Cdd:cd19113 70 ELFLTSKLWNNFHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKfvpieekypPGFycgDGDNFVYEDVPILD---TW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 145 KAMEECCKLGLAKSVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANG-AYWGSH 223
Cdd:cd19113 147 KALEKLVDAGKIKSIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSfVELNQG 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276262015 224 RVLKSLVL------QKIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19113 227 RALNTPTLfehdtiKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDI 300
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-291 |
2.44e-69 |
|
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: 217.37 E-value: 2.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDAD 90
Cdd:cd19111 1 GFPMPVIGLGTYQSP---PEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLK-REEVFITTKLPPVYLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 91 HDLVLPALKESLRKLGLNYVDLYLIHWPVrikpginHFRFSKDDIL----PFDMKGTWKAMEECCKLGLAKSVGLSNFSC 166
Cdd:cd19111 77 FKDTEKSLEKSLENLKLPYVDLYLIHHPC-------GFVNKKDKGErelaSSDVTSVWRAMEALVSEGKVKSIGLSNFNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 167 AKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLG----ANGAYWGSHRV-LKSLVLQKIAAAKGKT 241
Cdd:cd19111 150 RQINKILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGspgrANQSLWPDQPDlLEDPTVLAIAKELDKT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1276262015 242 MAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19111 230 PAQVLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDR 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
3-283 |
8.92e-69 |
|
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: 215.27 E-value: 8.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 3 IPEVILNSGHSMPLIGMGTAadplpppeNLTSIIIDAIA-----AGYRHFDTAALYSTEEPLGRAVAEALKRdlikdRDE 77
Cdd:cd19135 2 TPTVRLSNGVEMPILGLGTS--------HSGGYSHEAVVyalkeCGYRHIDTAKRYGCEELLGKAIKESGVP-----RED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 78 VFITSKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHfRFSKDDilpfdmkgTWKAMEECCKLGLAK 157
Cdd:cd19135 69 LFLTTKLWPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNV-KETRAE--------TWRALEELYDEGLCR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 158 SVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgANGaywgshRVLKSLVLQKIAAA 237
Cdd:cd19135 140 AIGVSNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPL-AKG------KALEEPTVTELAKK 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 238 KGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEV 283
Cdd:cd19135 213 YQKTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDM 258
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
11-286 |
1.43e-68 |
|
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: 216.13 E-value: 1.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTAADPlppPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDAD 90
Cdd:cd19107 1 GAKMPILGLGTWKSP---PGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVK-REDLFIVSKLWCTFHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 91 HDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskDDILPFDMKG-----------TWKAMEECCKLGLAKSV 159
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPG--------KELFPLDESGnvipsdttfldTWEAMEELVDEGLVKAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 160 GLSNFSCAKIERLLQHATI--PPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSHR---VLKSLVLQKI 234
Cdd:cd19107 149 GVSNFNHLQIERILNKPGLkyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEdpsLLEDPKIKEI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1276262015 235 AAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19107 229 AAKHNKTTAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
8-289 |
7.14e-66 |
|
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: 208.89 E-value: 7.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAAdPLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCS 87
Cdd:cd19119 6 LNTGASIPALGLGTAS-PHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIK-REELFITTKVWPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHdlVLPALKESLRKLGLNYVDLYLIHWPVRIKpginhfRFSKDDILPF---------------DMKGTWKAMEECCK 152
Cdd:cd19119 84 FYDE--VERSLDESLKALGLDYVDLLLVHWPVCFE------KDSDDSGKPFtpvnddgktryaasgDHITTYKQLEKIYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 153 LGLAKSVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGaywgsHRVLKSLVLQ 232
Cdd:cd19119 156 DGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHG-----APNLKNPLVK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 233 KIAAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILdwKLTDEEVKQIKQI 289
Cdd:cd19119 231 KIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKIV--SLTKEDLQKLDDI 285
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
1-291 |
4.37e-64 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 203.38 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 1 MQIPEVI-LNSGHSMPLIGMGT--AADplpppENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEAlkrDLikDRDE 77
Cdd:PRK11565 1 MANPTVIkLQDGNVMPQLGLGVwqASN-----EEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA---SV--AREE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 78 VFITSKLWcsDADHDLVLPALKESLRKLGLNYVDLYLIHWPVrikPGINHFrfskddilpfdmKGTWKAMEECCKLGLAK 157
Cdd:PRK11565 71 LFITTKLW--NDDHKRPREALEESLKKLQLDYVDLYLMHWPV---PAIDHY------------VEAWKGMIELQKEGLIK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 158 SVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAywgshRVLKSLVLQKIAAA 237
Cdd:PRK11565 134 SIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK-----GVFDQKVIRDLADK 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1276262015 238 KGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:PRK11565 209 YGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAKLDQ 262
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
15-289 |
4.69e-64 |
|
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: 203.52 E-value: 4.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLIGMGTAAdpLPPPENLTSIIIdAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDADHDLV 94
Cdd:cd19128 2 PRLGFGTYK--ITESESKEAVKN-AIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVK-REDLFITSKLWPTMHQPENV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 95 LPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskDDILPFDMKG-----------TWKAMEECCKLGLAKSVGLSN 163
Cdd:cd19128 78 KEQLLITLQDLQLEYLDLFLIHWPLAFDMD--------TDGDPRDDNQiqslskkpledTWRAMEQCVDEKLTKNIGVSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 164 FSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYwGSHRVLKSLVLQKIAAAKGKTMA 243
Cdd:cd19128 150 YSTKLLTDLLNYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGD-GNLTFLNDSELKALATKYNTTPP 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1276262015 244 QVALRWiH----EEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19128 229 QVIIAW-HlqkwPKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-293 |
8.97e-63 |
|
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: 200.76 E-value: 8.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 9 NSGHSMPLIGMGTAadpLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSD 88
Cdd:cd19129 1 NGSGAIPALGFGTL---IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIR-REDLFVTTKLWNTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 89 ADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfskDDILPFDMKG------------TWKAMEECCKLGLA 156
Cdd:cd19129 77 HRPERVKPAFEASLKRLQLDYLDLYLIHTPFAFQPG--------DEQDPRDANGnviyddgvtlldTWRAMERLVDEGRC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 157 KSVGLSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANgaywGSHRVLKSLVLQKIAA 236
Cdd:cd19129 149 KAIGLSDVSLEKLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHG----MEPKLLEDPVITAIAR 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 237 AKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILdwKLTDEEVKQIKQISQCR 293
Cdd:cd19129 225 RVNKTPAQVLLAWAIQRGTALLTTSKTPSRIRENFDIS--TLPEDAMREINEGIKTR 279
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
14-286 |
1.69e-61 |
|
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: 197.87 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAAdplPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDADHDL 93
Cdd:cd19110 4 IPAVGLGTWK---ASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVR-REDLFIVSKLWCTCHKKSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 VLPALKESLRKLGLNYVDLYLIHWPVRIKPGinhfrfSKDdiLPFDMKG-----------TWKAMEECCKLGLAKSVGLS 162
Cdd:cd19110 80 VKTACTRSLKALKLNYLDLYLIHWPMGFKPG------EPD--LPLDRSGmvipsdtdfldTWEAMEDLVIEGLVKNIGVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 163 NFSCAKIERLLQHAT--IPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANGaywGSHRVLKSLVLQKIAAAKGK 240
Cdd:cd19110 152 NFNHEQLERLLNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSC---EGVDLIDDPVIQRIAKKHGK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 241 TMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19110 229 SPAQILIRFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNL 274
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
11-286 |
5.70e-61 |
|
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: 196.62 E-value: 5.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGTAADPLPPPEnltSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKdRDEVFITSKLWCSDAD 90
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETE---EVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVK-REDLFIVTKLWNNFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 91 HDLVLPALKESLRKLGLNYVDLYLIHWPVRIK---PGINHFRFSKD---DILPFD---MKGTWKAMEECCKLGLAKSVGL 161
Cdd:cd19114 77 KDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDkelKKFPLEqspMQECWREMEKLVDAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 162 SNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGaNGAY-----WGSH--RVLKSLVLQKI 234
Cdd:cd19114 157 ANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFG-NAVYtkvtkHLKHftNLLEHPVVKKL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1276262015 235 AAAKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19114 236 ADKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEAL 287
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
11-287 |
1.30e-60 |
|
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: 194.37 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGT------AADPLPPPENLTSIIIDAIAAGYRHFDTAALYS---TEEPLGRAVAEAlkrdlikDRDEVFIT 81
Cdd:cd19072 1 GEEVPVLGLGTwgigggMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGgghAEELVGKAIKGF-------DREDLFIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 82 SKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpgiNHFrfskddilpFDMKGTWKAMEECCKLGLAKSVGL 161
Cdd:cd19072 74 TKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWP-------NPS---------IPIEETLRAMEELVEEGKIRYIGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 162 SNFSCAKIERLLQHAT-IPPAVNQVEMNVA--WQQQKMLEFCREKGIQVSAWSPLGaNGAYWGSHRvlkSLVLQKIAAAK 238
Cdd:cd19072 138 SNFSLEELEEAQSYLKkGPIVANQVEYNLFdrEEESGLLPYCQKNGIAIIAYSPLE-KGKLSNAKG---SPLLDEIAKKY 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1276262015 239 GKTMAQVALRW-IHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIK 287
Cdd:cd19072 214 GKTPAQIALNWlISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
17-289 |
2.33e-59 |
|
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: 191.76 E-value: 2.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAA-----DPLPPPENLtSIIIDAIAAGYRHFDTAALYSTEEPLgRAVAEALKRDLiKDRDEVFITSKLWCSDADH 91
Cdd:pfam00248 1 IGLGTWQlgggwGPISKEEAL-EALRAALEAGINFIDTAEVYGDGKSE-ELLGEALKDYP-VKRDKVVIATKVPDGDGPW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 92 DL------VLPALKESLRKLGLNYVDLYLIHWPVRIKPginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFS 165
Cdd:pfam00248 78 PSggskenIRKSLEESLKRLGTDYIDLYYLHWPDPDTP----------------IEETWDALEELKKEGKIRAIGVSNFD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 166 CAKIERLLQHATIPPAVNQVEMNVAW--QQQKMLEFCREKGIQVSAWSPLGaNGAY---------------------WGS 222
Cdd:pfam00248 142 AEQIEKALTKGKIPIVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLG-GGLLtgkytrdpdkgpgerrrllkkGTP 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276262015 223 HRVLKSLVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:pfam00248 221 LNLEALEALEEIAKEHGVSPAQVALRWAlsKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-286 |
2.67e-59 |
|
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: 190.84 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMGTAAdpLPPPENLTSIIIdAIAAGYRHFDTAALYSTEEPLGRAVAEALKrdlikDRDEVFITSK 83
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGE--LSDDEAERSVSA-ALEAGYRLIDTAAAYGNEAAVGRAIAASGI-----PRGELFVTTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 LWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskddiLPFDMK--GTWKAMEECCKLGLAKSVGL 161
Cdd:cd19134 73 LATPDQGFTASQAACRASLERLGLDYVDLYLIHWP-----------------AGREGKyvDSWGGLMKLREEGLARSIGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 162 SNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANgaywgshRVLKSLVLQKIAAAKGKT 241
Cdd:cd19134 136 SNFTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG-------RLLDNPAVTAIAAAHGRT 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1276262015 242 MAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19134 209 PAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
14-287 |
1.52e-58 |
|
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: 188.33 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAAdplPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRAVAE-ALKRDlikdrdEVFITSKLWCSDADHD 92
Cdd:cd19139 1 IPAFGLGTFR---LKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAEsGVPRD------ELFITTKIWIDNLSKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 93 LVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfSKDDILPfdMKGTWKAMEECCKLGLAKSVGLSNFSCAkierL 172
Cdd:cd19139 72 KLLPSLEESLEKLRTDYVDLTLIHWP------------SPNDEVP--VEEYIGALAEAKEQGLTRHIGVSNFTIA----L 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 173 LQHATIPP-----AVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGANgaywgshRVLKSLVLQKIAAAKGKTMAQVAL 247
Cdd:cd19139 134 LDEAIAVVgagaiATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAYG-------KVLDDPVLAAIAERHGATPAQIAL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1276262015 248 RWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIK 287
Cdd:cd19139 207 AWAMARGYAVIPSSTKREHLRSNLLALDLTLDADDMAAIA 246
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
29-283 |
1.15e-54 |
|
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: 179.73 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 29 PENLTSIIIDAIAAGYRHFDTAALYST---EEPLGRAVAEalkrdlIKDRDEVFITSKLWC--SDADHDLVLPALKESLR 103
Cdd:cd19093 25 DEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKE------LGDRDEVVIATKFAPlpWRLTRRSVVKALKASLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 104 KLGLNYVDLYLIHWPvrikpgiNHFrfskddilPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIER---LLQHATIPP 180
Cdd:cd19093 99 RLGLDSIDLYQLHWP-------GPW--------YSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRahkALKERGVPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 181 AVNQVEMNVAWQ---QQKMLEFCREKGIQVSAWSPLgANGAYWG----------------SHRVLKSL-----VLQKIAA 236
Cdd:cd19093 164 ASNQVEYSLLYRdpeQNGLLPACDELGITLIAYSPL-AQGLLTGkyspenpppggrrrlfGRKNLEKVqplldALEEIAE 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1276262015 237 AKGKTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEV 283
Cdd:cd19093 243 KYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEV 289
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-286 |
2.96e-54 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 177.91 E-value: 2.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 12 HSMPLIGMGTAadplpppeNLT-SIIID----AIAAGYRHFDTAALYSTEEPLGRAVAEALKRdlikdRDEVFITSKLWC 86
Cdd:PRK11172 1 MSIPAFGLGTF--------RLKdQVVIDsvktALELGYRAIDTAQIYDNEAAVGQAIAESGVP-----RDELFITTKIWI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfSKDDILPfdMKGTWKAMEECCKLGLAKSVGLSNFSC 166
Cdd:PRK11172 68 DNLAKDKLIPSLKESLQKLRTDYVDLTLIHWP------------SPNDEVS--VEEFMQALLEAKKQGLTREIGISNFTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 167 AKIERLLqhATIPP---AVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLgangAYwgsHRVLKSLVLQKIAAAKGKTMA 243
Cdd:PRK11172 134 ALMKQAI--AAVGAeniATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTL----AY---GKVLKDPVIARIAAKHNATPA 204
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1276262015 244 QVALRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:PRK11172 205 QVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAI 247
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
9-290 |
1.16e-51 |
|
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: 172.67 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 9 NSGHSMPLIGMGTAA--DPLPPPENLTSI-IID-AIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdliKDRDEVFIT 81
Cdd:COG0667 8 RSGLKVSRLGLGTMTfgGPWGGVDEAEAIaILDaALDAGINFFDTADVYGpgrSEELLGEALKG-------RPRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 82 SKL----------WCSDADHdlVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDmkGTWKAMEECC 151
Cdd:COG0667 81 TKVgrrmgpgpngRGLSREH--IRRAVEASLRRLGTDYIDLYQLHRP--------------DPDTPIE--ETLGALDELV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 152 KLGLAKSVGLSNFSCAKIERLLQHA--TIPPAVNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLGA---NGAY----- 219
Cdd:COG0667 143 REGKIRYIGVSNYSAEQLRRALAIAegLPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGgllTGKYrrgat 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 220 --------------WGSHRVLKSL-VLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEE 282
Cdd:COG0667 223 fpegdraatnfvqgYLTERNLALVdALRAIAAEHGVTPAQLALAWLlaQPGVTSVIPGARSPEQLEENLAAADLELSAED 302
|
....*...
gi 1276262015 283 VKQIKQIS 290
Cdd:COG0667 303 LAALDAAL 310
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
8-291 |
2.21e-51 |
|
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: 171.27 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 8 LNSGHSMPLIGMGTAADPLPPPENLTSIIiDAIAAGYRHFDTAALYSTEEPLGRAVAEALKRDLIKDRDEVFITSKLWCS 87
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAKGETYAAVT-KALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENPSVKREDLFICTKVWNH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHDLVLPALKESLRKLGLNYVDLYLIHWPVRI-KPGINHFRFSKD------DILPFDMKGTWKAMEECCKLGLAKSVG 160
Cdd:cd19122 82 LHEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAeKNDQRSPKLGPDgkyvilKDLTENPEPTWRAMEEIYESGKAKAIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 161 LSNFSCAKIERLLQHATIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGA-NGAYWGSHRVLKSLVLQKIAAAKG 239
Cdd:cd19122 162 VSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqNQVPSTGERVSENPTLNEVAEKGG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1276262015 240 KTMAQVALRWIHEEGASIIVKSFNNERMRENLDILDwkLTDEEVKQIKQISQ 291
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-286 |
2.09e-50 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 168.20 E-value: 2.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLIGMGT---AADPLPPPENLTSIIiDAIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdlikDRDE 77
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTwymGEDPAKRAQEIEALR-AGIDLGMTLIDTAEMYGdggSEELVGEAIRG--------RRDK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 78 VFITSKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIkpginhfrfskddilpfDMKGTWKAMEECCKLGLAK 157
Cdd:cd19138 72 VFLVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV-----------------PLAETVAAMEELKKEGKIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 158 SVGLSNFSCAKIERLLQhatIP----PAVNQVEMNVAWQ--QQKMLEFCREKGIQVSAWSPLGANGAYwgSHRVLKSLVL 231
Cdd:cd19138 135 AWGVSNFDTDDMEELWA---VPgggnCAANQVLYNLGSRgiEYDLLPWCREHGVPVMAYSPLAQGGLL--RRGLLENPTL 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1276262015 232 QKIAAAKGKTMAQVALRW-IHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19138 210 KEIAARHGATPAQVALAWvLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-286 |
5.18e-49 |
|
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: 164.28 E-value: 5.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 11 GHSMPLIGMGT--AADPLPPP----ENLTSIIIDAIAAGYRHFDTAALYS---TEEPLGRAvaealkrdlIKD--RDEVF 79
Cdd:cd19137 1 GEKIPALGLGTwgIGGFLTPDysrdEEMVELLKTAIELGYTHIDTAEMYGgghTEELVGKA---------IKDfpREDLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 80 ITSKLWCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvriKPGInhfrfskddilPFDMkgTWKAMEECCKLGLAKSV 159
Cdd:cd19137 72 IVTKVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP---NPNI-----------PLEE--TLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 160 GLSNFSCAKIERLLQHATIPPAVNQVEMNVA---WQQQKMLEFCREKGIQVSAWSPLgANGAywgshrVLKSLVLQKIAA 236
Cdd:cd19137 136 GVSNFNRRLLEEAISKSQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL-RRGL------EKTNRTLEEIAK 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 237 AKGKTMAQVALRW-IHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19137 209 NYGKTIAQIALAWlIQKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
29-291 |
4.80e-45 |
|
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: 155.05 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 29 PENLTSIIIDAIAAGYRHFDTAALY---STEEPLGRAVAealkrdliKDRDEVFITSKLWCSDADHDLVLPALKESLRKL 105
Cdd:cd19085 22 DEESIATIHAALDAGINFFDTAEAYgdgHSEEVLGKALK--------GRRDDVVIATKVSPDNLTPEDVRKSCERSLKRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 106 GLNYVDLYLIHWPVRikpginhfrfskddilPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHATIppAVNQV 185
Cdd:cd19085 94 GTDYIDLYQIHWPSS----------------DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI--DSNQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 186 EMNVAWQQ--QKMLEFCREKGIQVSAWSPL---------------------------GANGAYWGSHRVLKSLvlQKIAA 236
Cdd:cd19085 156 PYNLLWRAieYEILPFCREHGIGVLAYSPLaqglltgkfssaedfppgdartrlfrhFEPGAEEETFEALEKL--KEIAD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 237 AKGKTMAQVALRWI-HEEG-ASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:cd19085 234 ELGVTMAQLALAWVlQQPGvTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEISD 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
17-286 |
7.59e-44 |
|
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: 151.91 E-value: 7.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAA----DPLPPPENLTsiiIDAIAAGYRH----FDTAALYSteepLGRA---VAEALKrdliKDRDEVFITSK-- 83
Cdd:cd19084 7 IGLGTWAiggtWWGEVDDQES---IEAIKAAIDLginfFDTAPVYG----FGHSeeiLGKALK----GRRDDVVIATKcg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 -LW------CSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDmkGTWKAMEECCKLGLA 156
Cdd:cd19084 76 lRWdggkgvTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWP--------------DPNTPIE--ETAEALEKLKKEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 157 KSVGLSNFSCAKIERLLQHATIppAVNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLGA---NGAYWGSH-------- 223
Cdd:cd19084 140 RYIGVSNFSVEQLEEARKYGPI--VSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQgllTGKYKKEPtfppddrr 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 224 ------------RVLKSL-VLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19084 218 srfpffrgenfeKNLEIVdKLKEIAEKYGKSLAQLAIAWTlaQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
17-272 |
8.77e-40 |
|
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: 139.19 E-value: 8.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAADPLPPPENLTSIIID-AIAAGYRHFDTAALYST---EEPLGRAVAEalkrdlIKDRDEVFITSKL-------- 84
Cdd:cd06660 3 LGLGTMTFGGDGDEEEAFALLDaALEAGGNFFDTADVYGDgrsERLLGRWLKG------RGNRDDVVIATKGghppggdp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 WCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDmkGTWKAMEECCKLGLAKSVGLSNF 164
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRD--------------DPSTPVE--ETLEALNELVREGKIRYIGVSNW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCAKIERLLQHAT----IPPAVNQVEMNVAWQQ---QKMLEFCREKGIQVSAWSPLgangaywgshrvlkslvlqkiaaA 237
Cdd:cd06660 141 SAERLAEALAYAKahglPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPL-----------------------A 197
|
250 260 270
....*....|....*....|....*....|....*..
gi 1276262015 238 KGktMAQVALRWI--HEEGASIIVKSFNNERMRENLD 272
Cdd:cd06660 198 RG--PAQLALAWLlsQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-282 |
8.65e-36 |
|
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: 130.37 E-value: 8.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLI-GMGTAADPLPPPENLTSIIIDAIAAGYRHFDTA---ALYSTEEPLGRAVAeaLKRDLikdRDEVFITSKlwCS--- 87
Cdd:cd19092 8 RLVlGCMRLADWGESAEELLSLIEAALELGITTFDHAdiyGGGKCEELFGEALA--LNPGL---REKIEIQTK--CGirl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 ------------DADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskdDILpFDMKGTWKAMEECCKLGL 155
Cdd:cd19092 81 gddprpgrikhyDTSKEHILASVEGSLKRLGTDYLDLLLLHRP---------------DPL-MDPEEVAEAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 156 AKSVGLSNFSCAKIErLLQHAT-IPPAVNQVEMNVA---WQQQKMLEFCREKGIQVSAWSPLGaNGAYWGS-----HRVL 226
Cdd:cd19092 145 VRYFGVSNFTPSQIE-LLQSYLdQPLVTNQIELSLLhteAIDDGTLDYCQLLDITPMAWSPLG-GGRLFGGfderfQRLR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 227 KslVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEE 282
Cdd:cd19092 223 A--ALEELAEEYGVTIEAIALAWLlrHPARIQPILGTTNPERIRSAVKALDIELTREE 278
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
29-282 |
1.86e-31 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 119.10 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 29 PENLTSIIIDAIAAGYRHFDTAALY---STEEPLGravaEALKRDLIKdRDEVFITSKlwC-----------------SD 88
Cdd:COG4989 30 PAEAAALIEAALELGITTFDHADIYggyTCEALFG----EALKLSPSL-REKIELQTK--CgirlpseardnrvkhydTS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 89 ADHdlVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskdDILpFDMKGTWKAMEECCKLGLAKSVGLSNFSCAK 168
Cdd:COG4989 103 KEH--IIASVEGSLRRLGTDYLDLLLLHRP---------------DPL-MDPEEVAEAFDELKASGKVRHFGVSNFTPSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 169 IErLLQHA-TIPPAVNQVEMNVAwqQQKM-----LEFCREKGIQVSAWSPLGAnGAYWG-----SHRVLKslVLQKIAAA 237
Cdd:COG4989 165 FE-LLQSAlDQPLVTNQIELSLL--HTDAfddgtLDYCQLNGITPMAWSPLAG-GRLFGgfdeqFPRLRA--ALDELAEK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1276262015 238 KGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEE 282
Cdd:COG4989 239 YGVSPEAIALAWLlrHPAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
39-290 |
2.46e-30 |
|
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: 116.94 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYS---TEEPLGRAVAEAlkrdlikdRDEVFITSK--LWCSDADHDL------VLPALKESLRKLGL 107
Cdd:cd19091 48 ALDAGINFFDTADVYSegeSEEILGKALKGR--------RDDVLIATKvrGRMGEGPNDVglsrhhIIRAVEASLKRLGT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 108 NYVDLYLIHWPvrikpginhfrfskDDILPFDMkgTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----QHATIPPAVN 183
Cdd:cd19091 120 DYIDLYQLHGF--------------DALTPLEE--TLRALDDLVRQGKVRYIGVSNFSAWQIMKALgiseRRGLARFVAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 184 QVEMNVAWQ--QQKMLEFCREKGIQVSAWSPLgANGAYWGSHRVLKSL--------------------------VLQKIA 235
Cdd:cd19091 184 QAYYSLLGRdlEHELMPLALDQGVGLLVWSPL-AGGLLSGKYRRGQPApegsrlrrtgfdfppvdrergydvvdALREIA 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 236 AAKGKTMAQVALRWI-HEEG-ASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQIS 290
Cdd:cd19091 263 KETGATPAQVALAWLlSRPTvSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLDKVS 319
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
35-286 |
2.67e-30 |
|
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: 116.53 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 35 IIIDAIAAGYRHFDTAALYS---TEEPLGRAVaealkRDLIKdRDEVFITSKLwCSDADHDL---------VLPALKESL 102
Cdd:cd19079 40 IIKRALDLGINFFDTANVYSggaSEEILGRAL-----KEFAP-RDEVVIATKV-YFPMGDGPngrglsrkhIMAEVDASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 103 RKLGLNYVDLYLIHWPvrikpginhfrfskDDILPfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----QHATI 178
Cdd:cd19079 113 KRLGTDYIDLYQIHRW--------------DYETP--IEETLEALHDVVKSGKVRYIGASSMYAWQFAKALhlaeKNGWT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 179 PPAVNQVEMNVAWQQQK--MLEFCREKGIQVSAWSPLGAN---GAYWGS----------------------HRVLKSlvL 231
Cdd:cd19079 177 KFVSMQNHYNLLYREEEreMIPLCEEEGIGVIPWSPLARGrlaRPWGDTterrrsttdtaklkydyfteadKEIVDR--V 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 232 QKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19079 255 EEVAKERGVSMAQVALAWLlsKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-289 |
8.98e-29 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 112.54 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 3 IPEVIL-NSGHSMPLIG---MGTAA--DPLPPPENLTSIIIDAIAAGYRHFDTAALY-STEEPLGRAVAEALKRdlikdR 75
Cdd:cd19144 1 IPTRTLgRNGPSVPALGfgaMGLSAfyGPPKPDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWFKQNPGK-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 76 DEVFITSKL----------WCSDADHDLVLPALKESLRKLGLNYVDLYLIHwpvRIKPGInhfrfskddilPFDMkgTWK 145
Cdd:cd19144 76 EKIFLATKFgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH---RVDGKT-----------PIEK--TVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 146 AMEECCKLGLAKSVGLSNFSCAKIERllQHATIPPAVNQVE-----MNVAWQQQKMLEFCREKGIQVSAWSPLGaNGAYW 220
Cdd:cd19144 140 AMAELVQEGKIKHIGLSECSAETLRR--AHAVHPIAAVQIEyspfsLDIERPEIGVLDTCRELGVAIVAYSPLG-RGFLT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 221 GSHRVLK-----------------------SLV--LQKIAAAKGKTMAQVALRWIHEEGASIIV--KSFNNERMRENLDI 273
Cdd:cd19144 217 GAIRSPDdfeegdfrrmaprfqaenfpknlELVdkIKAIAKKKNVTAGQLTLAWLLAQGDDIIPipGTTKLKRLEENLGA 296
|
330
....*....|....*.
gi 1276262015 274 LDWKLTDEEVKQIKQI 289
Cdd:cd19144 297 LKVKLTEEEEKEIREI 312
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-289 |
7.37e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 109.68 E-value: 7.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 36 IIDAIAAGYRHFDTAALYST---EEPLGRAVAEAlkrdlikdRDEVFITSK---LWCSD--ADHDL----VLPALKESLR 103
Cdd:cd19102 32 IRAALDLGINWIDTAAVYGLghsEEVVGRALKGL--------RDRPIVATKcglLWDEEgrIRRSLkpasIRAECEASLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 104 KLGLNYVDLYLIHWPVRikpginhfrfskddilPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHATI----P 179
Cdd:cd19102 104 RLGVDVIDLYQIHWPDP----------------DEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIaslqP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 180 PA---VNQVEmnvawqqQKMLEFCREKGIQVSAWSPLGA---NGAY---------WGSHRV-------------LKSL-V 230
Cdd:cd19102 168 PYsllRRGIE-------AEILPFCAEHGIGVIVYSPMQSgllTGKMtpervaslpADDWRRrspffqepnlarnLALVdA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 231 LQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19102 241 LRPIAERHGRTVAQLAIAWVlrRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
9-294 |
3.98e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 109.14 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 9 NSGHSMPLIGMGTAADPLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEPlgrAVAEALKrdliKDRDEVFITSKL--WC 86
Cdd:COG1453 8 KTGLEVSVLGFGGMRLPRKDEEEAEALIRRAIDNGINYIDTARGYGDSEE---FLGKALK----GPRDKVILATKLppWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SDADHdlVLPALKESLRKLGLNYVDLYLIHwpvrikpGINhfrfsKDDILPFDMK--GTWKAMEECCKLGLAKSVGlsnF 164
Cdd:COG1453 81 RDPED--MRKDLEESLKRLQTDYIDLYLIH-------GLN-----TEEDLEKVLKpgGALEALEKAKAEGKIRHIG---F 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCakierllqH---ATIPPAVN-------QVEMNVAWQQ----QKMLEFCREKGIQVSAWSPLGangaywGSHRVLKSLV 230
Cdd:COG1453 144 ST--------HgslEVIKEAIDtgdfdfvQLQYNYLDQDnqagEEALEAAAEKGIGVIIMKPLK------GGRLANPPEK 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 231 LQKIAAAKgKTMAQVALRWI--HEEGASIIVkSFNNERM-RENLDILD--WKLTDEEVKQIKQISQ---------CRG 294
Cdd:COG1453 210 LVELLCPP-LSPAEWALRFLlsHPEVTTVLS-GMSTPEQlDENLKTADnlEPLTEEELAILERLAEelgellkdfCTG 285
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-274 |
8.59e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 105.74 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 9 NSGHSMPLIGMGTAADPLPPPEnltsIIIDAIAAGYRHFDTAALYS--TEEplgRAVAEALKRdliKDRDEVFITSKLWC 86
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRESPE----LLRRALDLGINYFDTAEGYGngNSE---EIIGEALKG---LRRDKVFLATKASP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SD--ADHDLVLPALKESLRKLGLNYVDLYLIHwpvrikpginHFRFSKDDILPFDMKgtwKAMEECCKLGLAKSVGlsnF 164
Cdd:cd19105 78 RLdkKDKAELLKSVEESLKRLQTDYIDIYQLH----------GVDTPEERLLNEELL---EALEKLKKEGKVRFIG---F 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCA-KIERLLQHA-------TIPPAVNQveMNVAWQQQKMLEFCREKGIQVSAWSPLGANGAYWGSHRVLKSlvlqkiaa 236
Cdd:cd19105 142 STHdNMAEVLQAAiesgwfdVIMVAYNF--LNQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKA-------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1276262015 237 aKGKTMAQVALRWI-HEEGASIIVKSFNN-ERMRENLDIL 274
Cdd:cd19105 212 -KGFSLPQAALKWVlSNPRVDTVVPGMRNfAELEENLAAA 250
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
17-272 |
9.03e-27 |
|
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: 105.78 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTA---ADPLPPPENLTSIIID-AIAAGYRHFDTAALYST-EEPLGRAVAEalkrdliKDRDEVFITSKLWCSDADH 91
Cdd:cd19095 3 LGLGTSgigRVWGVPSEAEAARLLNtALDLGINLIDTAPAYGRsEERLGRALAG-------LRRDDLFIATKVGTHGEGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 92 --------DLVLPALKESLRKLGLNYVDLYLIHWPVRikpginhfRFSKDDILPfdmkgtwkAMEECCKLGLAKSVGLSN 163
Cdd:cd19095 76 rdrkdfspAAIRASIERSLRRLGTDYIDLLQLHGPSD--------DELTGEVLE--------TLEDLKAAGKVRYIGVSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 164 FScAKIERLLQHATIppAVNQVEMNVAWQQQK-MLEFCREKGIQVSAWSPLgANGAYWGSHRVLKSLVLQK-----IAAA 237
Cdd:cd19095 140 DG-EELEAAIASGVF--DVVQLPYNVLDREEEeLLPLAAEAGLGVIVNRPL-ANGRLRRRVRRRPLYADYArrpefAAEI 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 1276262015 238 KGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLD 272
Cdd:cd19095 216 GGATWAQAALRFVlsHPGVSSAIVGTTNPEHLEENLA 252
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
28-284 |
9.94e-27 |
|
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: 106.96 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 28 PPENLTSIIIDAIAAGYRHFDTAALY-----STEEPLGRAvaeaLKRDLIKDRDEVFITSKlwcsdADHDL--------- 93
Cdd:cd19089 27 SPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRI----LKRDLRPYRDELVISTK-----AGYGMwpgpygdgg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 ----VLPALKESLRKLGLNYVDLYLIHwpvrikpginhfRFSKDDILpfdmKGTWKAMEECCKLGLAKSVGLSNFSCAKI 169
Cdd:cd19089 98 srkyLLASLDQSLKRMGLDYVDIFYHH------------RYDPDTPL----EETMTALADAVRSGKALYVGISNYPGAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 170 ER---LLQHATIPPAVNQVEMNV--AWQQQKMLEFCREKGIQVSAWSPLgANG----AYWG------------------- 221
Cdd:cd19089 162 RRaiaLLRELGVPLIIHQPRYSLldRWAEDGLLEVLEEAGIGFIAFSPL-AQGlltdKYLNgippdsrraaeskflteea 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 222 --SHRVLKSLVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDW-KLTDEEVK 284
Cdd:cd19089 241 ltPEKLEQLRKLNKIAAKRGQSLAQLALSWVlrDPRVTSVLIGASSPSQLEDNVAALKNlDFSEEELA 308
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-272 |
4.81e-26 |
|
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: 103.33 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 9 NSGHSMPLIGMGTAADPLPPPENLTSIIIDAIAAGYRHFDTAALYS-TEEPLGRavaeALKRdlikDRDEVFITSKLWCS 87
Cdd:cd19100 6 RTGLKVSRLGFGGGPLGRLSQEEAAAIIRRALDLGINYFDTAPSYGdSEEKIGK----ALKG----RRDKVFLATKTGAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 DADHdlVLPALKESLRKLGLNYVDLYLIHwpvrikpginHFRFSKDDILPFDMKGTWKAMEECCKLGLAKSVGLSNFSCA 167
Cdd:cd19100 78 DYEG--AKRDLERSLKRLGTDYIDLYQLH----------AVDTEEDLDQVFGPGGALEALLEAKEEGKIRFIGISGHSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 168 KIERLLQHA---TIPPAVNQVEMNVAWQQQKMLEFCREKGIQVSAWSPLGAngaywgshRVLKSLVLQKIAAakgktmaq 244
Cdd:cd19100 146 VLLRALETGefdVVLFPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAG--------GRLLSGDPLDPEQ-------- 209
|
250 260 270
....*....|....*....|....*....|
gi 1276262015 245 vALRWI--HEEGASIIVKSFNNERMRENLD 272
Cdd:cd19100 210 -ALRYAlsLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-279 |
1.71e-25 |
|
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: 102.30 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 14 MPLIGMGTAADPlPPPENLTSIIIDAIAAGYRHFDTAALYsteeplGRAVAEALKRDLIKDRDE-VFITSKL-------- 84
Cdd:cd19088 9 MRLTGPGIWGPP-ADREEAIAVLRRALELGVNFIDTADSY------GPDVNERLIAEALHPYPDdVVIATKGglvrtgpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 -WCSDADHDLVLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPF-DMKGTWKAMEeccKLGLAKSVGLS 162
Cdd:cd19088 82 wWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI--------------DPKVPFeEQLGALAELQ---DEGLIRHIGLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 163 NFSCAKIERLLQHATIppAVNQVEMNVAWQQ-QKMLEFCREKGIQVSAWSPLgangaywGSHRVLKSLV-LQKIAAAKGK 240
Cdd:cd19088 145 NVTVAQIEEARAIVRI--VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPL-------GGGDLAQPGGlLAEVAARLGA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1276262015 241 TMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLT 279
Cdd:cd19088 216 TPAQVALAWLlaRSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
18-286 |
2.36e-25 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 103.06 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 18 GMGTAADPLPPPENLtSIIIDAIAAGYRHFDTAALY---STEEPLGRAVAEAlkrdlikdRDEVFITSK---LWCS---- 87
Cdd:cd19076 21 GMSAFYGPADEEESI-ATLHRALELGVTFLDTADMYgpgTNEELLGKALKDR--------RDEVVIATKfgiVRDPgsgf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 88 ---DADHDLVLPALKESLRKLGLNYVDLYLIHwpvRIkpginhfrfskDDILPfdMKGTWKAMEECCKLGLAKSVGLSNF 164
Cdd:cd19076 92 rgvDGRPEYVRAACEASLKRLGTDVIDLYYQH---RV-----------DPNVP--IEETVGAMAELVEEGKVRYIGLSEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCAKIERllQHATIPPAVNQVEMNVaWQ---QQKMLEFCREKGIQVSAWSPLGaNGAYWGShrvLKS------------- 228
Cdd:cd19076 156 SADTIRR--AHAVHPITAVQSEYSL-WTrdiEDEVLPTCRELGIGFVAYSPLG-RGFLTGA---IKSpedlpeddfrrnn 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 229 -------------LV--LQKIAAAKGKTMAQVALRWIHEEGASII----VKSFnnERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19076 229 prfqgenfdknlkLVekLEAIAAEKGCTPAQLALAWVLAQGDDIVpipgTKRI--KYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
36-286 |
3.52e-25 |
|
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: 102.68 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 36 IIDA-IAAGYRHFDTAALYST----------EEPLGRAVAealKRdliKDRDEVFITSKL--WCSDADHDL----VLPAL 98
Cdd:cd19081 31 LLDAfVDAGGNFIDTADVYSAwvpgnaggesETIIGRWLK---SR---GKRDRVVIATKVgfPMGPNGPGLsrkhIRRAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 99 KESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDmkGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----Q 174
Cdd:cd19081 105 EASLRRLQTDYIDLYQAHWD--------------DPATPLE--ETLGALNDLIRQGKVRYIGASNYSAWRLQEALelsrQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 175 HATIPPAVNQVEMNV---AWQQQKMLEFCREKGIQVSAWSPLG------------------ANGAYWGSH------RVLK 227
Cdd:cd19081 169 HGLPRYVSLQPEYNLvdrESFEGELLPLCREEGIGVIPYSPLAggfltgkyrseadlpgstRRGEAAKRYlnerglRILD 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 228 slVLQKIAAAKGKTMAQVALRWIHEEGA--SIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19081 249 --ALDEVAAEHGATPAQVALAWLLARPGvtAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
18-287 |
1.06e-23 |
|
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: 98.46 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 18 GMGTAADPLPPPENLTSIIIDAIAAGYRHFDTAALYST---EEPLGravaEALKrdliKDRDEVFITSKL---WCSDADH 91
Cdd:cd19078 13 GMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPytnEELVG----EALK----PFRDQVVIATKFgfkIDGGKPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 92 DLVL---P-----ALKESLRKLGLNYVDLYLIHwpvRIKPginhfrfskdDILPFDMKGTwkaMEECCKLGLAKSVGLSN 163
Cdd:cd19078 85 PLGLdsrPehirkAVEGSLKRLQTDYIDLYYQH---RVDP----------NVPIEEVAGT---MKELIKEGKIRHWGLSE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 164 FSCAKIERllQHATIPPAVNQVEMNVAWQ--QQKMLEFCREKGIQVSAWSPLGaNGAYWG-------------------- 221
Cdd:cd19078 149 AGVETIRR--AHAVCPVTAVQSEYSMMWRepEKEVLPTLEELGIGFVPFSPLG-KGFLTGkidentkfdegddraslprf 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 222 SHRVLKS---LV--LQKIAAAKGKTMAQVALRWIHEEGASI--IVKSFNNERMRENLDILDWKLTDEEVKQIK 287
Cdd:cd19078 226 TPEALEAnqaLVdlLKEFAEEKGATPAQIALAWLLAKKPWIvpIPGTTKLSRLEENIGAADIELTPEELREIE 298
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
17-286 |
8.53e-23 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 95.96 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAADPLPPPENLTSIIIDAIAAGYRHFDTAALY---STEEPLGRAVaealkRDLIkdRDEVFITSKLWCSDA---- 89
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKAL-----KDGP--REKVQLATKFGIHEIggsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 90 -----DHDLVLPALKESLRKLGLNYVDLYLIHwpvRIkpginhfrfskDDILPFDMkgTWKAMEECCKLGLAKSVGLSNF 164
Cdd:cd19145 93 vevrgDPAYVRAACEASLKRLDVDYIDLYYQH---RI-----------DTTVPIEI--TMGELKKLVEEGKIKYIGLSEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 165 SCAKIERllQHATIPPAVNQVEMNVaWQ---QQKMLEFCREKGIQVSAWSPLGaNGAYWGSHRVLKSLV----------- 230
Cdd:cd19145 157 SADTIRR--AHAVHPITAVQLEWSL-WTrdiEEEIIPTCRELGIGIVPYSPLG-RGFFAGKAKLEELLEnsdvrkshprf 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 231 --------------LQKIAAAKGKTMAQVALRWIHEEGASII-------VKSFNnermrENLDILDWKLTDEEVKQI 286
Cdd:cd19145 233 qgenleknkvlyerVEALAKKKGCTPAQLALAWVLHQGEDVVpipgttkIKNLN-----QNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
17-287 |
1.16e-22 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 95.77 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMG----TAADPLPPPENLTSIIIDAIAAGYRHFDTAALYSTEEP------LGRAVAealKRDliKDRDEVFITSK--- 83
Cdd:cd19077 8 IGLGlmglTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPhanlklLARFFR---KYP--EYADKVVLSVKggl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 ---LWCSDADHDLVLPALKESLRKLG-LNYVDLYLihwPVRIKPGInhfrfskddilpfDMKGTWKAMEECCKLGLAKSV 159
Cdd:cd19077 83 dpdTLRPDGSPEAVRKSIENILRALGgTKKIDIFE---PARVDPNV-------------PIEETIKALKELVKEGKIRGI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 160 GLSNFSCAKIERLlqHATIPPAVNQVE---MNVAWQQQKMLEFCREKGIQVSAWSPLG--------------ANGAYwgs 222
Cdd:cd19077 147 GLSEVSAETIRRA--HAVHPIAAVEVEyslFSREIEENGVLETCAELGIPIIAYSPLGrglltgriksladiPEGDF--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 223 HRVL-----------KSLV--LQKIAAAKGKTMAQVALRWI-HEEGASI--IVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19077 222 RRHLdrfngenfeknLKLVdaLQELAEKKGCTPAQLALAWIlAQSGPKIipIPGSTTLERVEENLKAANVELTDEELKEI 301
|
.
gi 1276262015 287 K 287
Cdd:cd19077 302 N 302
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
36-290 |
1.55e-22 |
|
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: 95.33 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 36 IID-AIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdlikDRDEVFITSKLWCSDAD----------HdlVLPALKES 101
Cdd:cd19087 35 IMDrALDAGINFFDTADVYGggrSEEIIGRWIAG--------RRDDIVLATKVFGPMGDdpndrglsrrH--IRRAVEAS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 102 LRKLGLNYVDLYLIHwpvrikpginHFrfskDDILPFDMkgTWKAMEECCKLGLAKSVGLSNFSC---------AKIERL 172
Cdd:cd19087 105 LRRLQTDYIDLYQMH----------HF----DRDTPLEE--TLRALDDLVRQGKIRYIGVSNFAAwqiakaqgiAARRGL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 173 LQHATIPPAVN----QVEMNVawqqqkmLEFCREKGIQVSAWSPLGA------------------------NGAYWGSHR 224
Cdd:cd19087 169 LRFVSEQPMYNllkrQAELEI-------LPAARAYGLGVIPYSPLAGglltgkygkgkrpesgrlveraryQARYGLEEY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 225 VLKSLVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQIS 290
Cdd:cd19087 242 RDIAERFEALAAEAGLTPASLALAWVlsHPAVTSPIIGPRTLEQLEDSLAALEITLTPELLAEIDELF 309
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
17-271 |
1.87e-22 |
|
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: 94.54 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTA----ADPLPPPENLTSIIIDAIAAGYRHFDTAALY-STEEPLGRAVAEalkrdliKDRDEVFITSKLWC----- 86
Cdd:cd19090 3 LGLGTAglggVFGGVDDDEAVATIRAALDLGINYIDTAPAYgDSEERLGLALAE-------LPREPLVLSTKVGRlpedt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPGINHFRfskddilpfdmKGTWKAMEECCKLGLAKSVGLSNFSC 166
Cdd:cd19090 76 ADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAP-----------GGALEALLELKEEGLIKHIGLGGGPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 167 AKIERLLQHATIPPAVNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLG------------ANGAYWGSHRVL-KSLVL 231
Cdd:cd19090 145 DLLRRAIETGDFDVVLTANRYTLLDQSaaDELLPAAARHGVGVINASPLGmgllagrppervRYTYRWLSPELLdRAKRL 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1276262015 232 QKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENL 271
Cdd:cd19090 225 YELCDEHGVPLPALALRFLlrDPRISTVLVGASSPEELEQNV 266
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
39-281 |
7.62e-22 |
|
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: 93.43 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYS---TEEPLGRAvaealkrdlIKD--RDEVFITSKLWCSDADHDL--------VLPALKESLRKL 105
Cdd:cd19074 31 AYDLGINFFDTADVYAagqAEEVLGKA---------LKGwpRESYVISTKVFWPTGPGPNdrglsrkhIFESIHASLKRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 106 GLNYVDLYLIHwpvrikpginhfRFskDDILPfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----QHATIPPA 181
Cdd:cd19074 102 QLDYVDIYYCH------------RY--DPETP--LEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHdlarQFGLIPPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 182 VNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPL-----------------GANGAYWGSHRVLKSLV----------LQ 232
Cdd:cd19074 166 VEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsRSRATDEDNRDKKRRLLtdenlekvkkLK 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 233 KIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDE 281
Cdd:cd19074 246 PIADELGLTLAQLALAWClrNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
36-289 |
1.97e-21 |
|
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: 92.37 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 36 IIDAIAAGYRHFDTAALYS---TEEPLGRAVAEALKRDlikdrdEVFITSKL---W------CSDADHDLVLPALKESLR 103
Cdd:cd19148 31 IHKALDLGINLIDTAPVYGfglSEEIVGKALKEYGKRD------RVVIATKVgleWdeggevVRNSSPARIRKEVEDSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 104 KLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDMkgTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAtiPPAVN 183
Cdd:cd19148 105 RLQTDYIDLYQVHWP--------------DPLVPIEE--TAEALKELLDEGKIRAIGVSNFSPEQMETFRKVA--PLHTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 184 QVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLgANGAYWGSHRV--------LKSLV-----------------LQKIAA 236
Cdd:cd19148 167 QPPYNLFEREieKDVLPYARKHNIVTLAYGAL-CRGLLSGKMTKdtkfegddLRRTDpkfqeprfsqylaaveeLDKLAQ 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 237 AK-GKTMAQVALRWIHEEGASIIVksFNNERMRENLD----ILDWKLTDEEVKQIKQI 289
Cdd:cd19148 246 ERyGKSVIHLAVRWLLDQPGVSIA--LWGARKPEQLDavdeVFGWSLNDEDMKEIDAI 301
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
39-289 |
2.84e-21 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 91.71 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYST---EEPLGRAVAEalkrdliKDRDEVFITSKLWCSDADHDLVL--------PALKESLRKLGL 107
Cdd:cd19083 42 ALDNGVNLLDTAFIYGLgrsEELVGEVLKE-------YNRNEVVIATKGAHKFGGDGSVLnnspeflrSAVEKSLKRLNT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 108 NYVDLYLIHWPVRIKPginhfrfsKDDILpfdmkgtwKAMEECCKLGLAKSVGLSNFSCAKierlLQHATIPPAVN--QV 185
Cdd:cd19083 115 DYIDLYYIHFPDGETP--------KAEAV--------GALQELKDEGKIRAIGVSNFSLEQ----LKEANKDGYVDvlQG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 186 EMNVAWQ--QQKMLEFCREKGIQVSAWSPLGAN---GAY----------WGS--------------HRVLKslvLQKIAA 236
Cdd:cd19083 175 EYNLLQReaEEDILPYCVENNISFIPYFPLASGllaGKYtkdtkfpdndLRNdkplfkgerfsenlDKVDK---LKSIAD 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1276262015 237 AKGKTMAQVALRW-IHEEGASIIVKSFNN-ERMRENLDILDWKLTDEEVKQIKQI 289
Cdd:cd19083 252 EKGVTVAHLALAWyLTRPAIDVVIPGAKRaEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
10-288 |
3.21e-21 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 92.36 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 10 SGHSMPLIGMGT--AADPLPPPENLTSIIIDAIAAGYRHFDTAALY-----STEEPLGRAvaeaLKRDLIKDRDEVFITS 82
Cdd:PRK09912 21 SGLRLPALSLGLwhNFGHVNALESQRAILRKAFDLGITHFDLANNYgpppgSAEENFGRL----LREDFAAYRDELIIST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 83 K----LW----CSDADHDLVLPALKESLRKLGLNYVDLYLIHwpvRIkpginhfrfskDDILPfdMKGTWKAMEECCKLG 154
Cdd:PRK09912 97 KagydMWpgpyGSGGSRKYLLASLDQSLKRMGLEYVDIFYSH---RV-----------DENTP--MEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 155 LAKSVGLSNFSCAKIER---LLQHATIPPAVNQVEMNV--AW-QQQKMLEFCREKGIQVSAWSPLGA--------NGAYW 220
Cdd:PRK09912 161 KALYVGISSYSPERTQKmveLLREWKIPLLIHQPSYNLlnRWvDKSGLLDTLQNNGVGCIAFTPLAQglltgkylNGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 221 GS--HRV----------------LKSL-VLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDIL-DWKL 278
Cdd:PRK09912 241 DSrmHREgnkvrgltpkmlteanLNSLrLLNEMAQQRGQSMAQMALSWLlkDERVTSVLIGASRAEQLEENVQALnNLTF 320
|
330
....*....|
gi 1276262015 279 TDEEVKQIKQ 288
Cdd:PRK09912 321 STEELAQIDQ 330
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
17-272 |
2.06e-20 |
|
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: 87.92 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGT---AADPLPPPENLTSI-IID-AIAAGYRHFDTAALYST---EEPLGRAVAealkrdliKDRDEVFITSKL---- 84
Cdd:cd19086 6 IGFGTwglGGDWWGDVDDAEAIrALRaALDLGINFFDTADVYGDghsERLLGKALK--------GRRDKVVIATKFgnrf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 -------WCSDADHdlVLPALKESLRKLGLNYVDLYLIH-WPVRIkpginhfrfskddilpFDMKGTWKAMEECCKLGLA 156
Cdd:cd19086 78 dggperpQDFSPEY--IREAVEASLKRLGTDYIDLYQLHnPPDEV----------------LDNDELFEALEKLKQEGKI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 157 KSVGLSNFSCAKIERLLQHATIppAVNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLgANGaywgshrvlkSLVlqki 234
Cdd:cd19086 140 RAYGVSVGDPEEALAALRRGGI--DVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPL-ASG----------LLT---- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1276262015 235 aaakGKtMAQVALRWI--HEEGASIIVKSFNNERMRENLD 272
Cdd:cd19086 203 ----GK-LAQAALRFIlsHPAVSTVIPGARSPEQVEENAA 237
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
39-286 |
2.92e-20 |
|
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: 89.16 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALY---STEEPLGRA---VAEALKRDliKDRDEVFITSKL--------WCSDADHDL----VLPALKE 100
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvpPSPETQGRTeeiIGSWLKKK--GNRDKVVLATKVagpgegitWPRGGGTRLdrenIREAVEG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 101 SLRKLGLNYVDLYLIHWPVRIKP--GINHFRFSKDDILPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAT- 177
Cdd:cd19094 105 SLKRLGTDYIDLYQLHWPDRYTPlfGGGYYTEPSEEEDSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 178 --IPPAVN-QVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLGA---NGAY----------------WGSHRVLKSLV--- 230
Cdd:cd19094 185 lgLPRIVSiQNPYSLLNRNfeEGLAEACHRENVGLLAYSPLAGgvlTGKYldgaarpeggrlnlfpGYMARYRSPQAlea 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 231 ---LQKIAAAKGKTMAQVALRWIHEEG--ASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19094 265 vaeYVKLARKHGLSPAQLALAWVRSRPfvTSTIIGATTLEQLKENIDAFDVPLSDELLAEI 325
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-288 |
1.76e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 86.62 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALY---STEEPLGravaEALKRdliKDRDEVFITSKL--WCSDADHDLVLPALKESLRKLGLNYVDLY 113
Cdd:cd19103 41 AMAAGLNLWDTAAVYgmgASEKILG----EFLKR---YPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 114 LIHWPVRIKPGINHfrfskddILPFdmkgtwkameecCKLGLAKSVGLSNFSCAKIER---LLQHATIPPAVNQVE---M 187
Cdd:cd19103 114 WIHNPADVERWTPE-------LIPL------------LKSGKVKHVGVSNHNLAEIKRaneILAKAGVSLSAVQNHyslL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 188 NVAWQQQKMLEFCREKGIQVSAWSPL--GA-NGAY-------WGSHRV---------LKSL--VLQKIAAAKGKTMAQVA 246
Cdd:cd19103 175 YRSSEEAGILDYCKENGITFFAYMVLeqGAlSGKYdtkhplpEGSGRAetynpllpqLEELtaVMAEIGAKHGASIAQVA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1276262015 247 LRWIHEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQ 288
Cdd:cd19103 255 IAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQ 296
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
15-275 |
4.55e-19 |
|
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: 84.92 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLIGMGT-----AADPLPPPENLTSIIIDAIAAGYRHFDTAALYSTE--EplgRAVAEALKRdliKDRDEVFITSKL-WC 86
Cdd:cd19096 1 SVLGFGTmrlpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGksE---EILGEALKE---GPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 87 SDADHDLVLPALKESLRKLGLNYVDLYLIHWPVRikpGINHFRFSKDDILPFdMKgtwKAMEEccklGLAKSVGLSnfSC 166
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNS---PEWLEKARKGGLLEF-LE---KAKKE----GLIRHIGFS--FH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 167 AK---IERLLqhATIPPAVNQVEMNV----AWQQQKMLEFCREKGIQVSAWSPLGangaywGSHRVLKSLVLQKIAAAKG 239
Cdd:cd19096 142 DSpelLKEIL--DSYDFDFVQLQYNYldqeNQAGRPGIEYAAKKGMGVIIMEPLK------GGGLANNPPEALAILCGAP 213
|
250 260 270
....*....|....*....|....*....|....*...
gi 1276262015 240 KTMAQVALRWI-HEEGASIIVKSFNNERM-RENLDILD 275
Cdd:cd19096 214 LSPAEWALRFLlSHPEVTTVLSGMSTPEQlDENIAAAD 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
17-250 |
7.27e-19 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 84.91 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAADPLPPPENLTSIIIDA-IAAGYRHFDTAALYSTEEPLG---RAVAEALKRDliKDRDEVFITSK--------L 84
Cdd:cd19082 3 IVLGTADFGTRIDEEEAFALLDAfVELGGNFIDTARVYGDWVERGaseRVIGEWLKSR--GNRDKVVIATKgghpdledM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 WCSDADHDLVLPALKESLRKLGLNYVDLYLIHW-----PVrikpginhfrfskDDILPfdmkgtwkAMEECCKLGLAKSV 159
Cdd:cd19082 81 SRSRLSPEDIRADLEESLERLGTDYIDLYFLHRddpsvPV-------------GEIVD--------TLNELVRAGKIRAF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 160 GLSNFSCAKIERL----LQHATIPPAVNQVEMNVA-------------WQQQKMLEFCREKGIQVSAWSPLgANG----- 217
Cdd:cd19082 140 GASNWSTERIAEAnayaKAHGLPGFAASSPQWSLArpneppwpgptlvAMDEEMRAWHEENQLPVFAYSSQ-ARGffskr 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1276262015 218 -------------AYWGSHRVLKSLVLQKIAAAKGKTMAQVALRWI 250
Cdd:cd19082 219 aaggaeddselrrVYYSEENFERLERAKELAEEKGVSPTQIALAYV 264
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
41-289 |
1.48e-18 |
|
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: 84.14 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 41 AAGYRHFDTAALYS---TEEPLGRAvaEALKRDLIkdrdevfITSK---LWCSDADHDLVLPALKESLRKLGLNYVDLYL 114
Cdd:cd19075 31 ERGHTEIDTARVYPdgtSEELLGEL--GLGERGFK-------IDTKanpGVGGGLSPENVRKQLETSLKRLKVDKVDVFY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 115 IHWPvrikpginhfrfskDDILPFDMkgTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAT----IPPAVNQVEMNVA 190
Cdd:cd19075 102 LHAP--------------DRSTPLEE--TLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKengwVLPTVYQGMYNAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 191 WQQQ--KMLEFCREKGIQVSAWSPLGA---NGAY-----------------WGSH--------RVLKSL-VLQKIAAAKG 239
Cdd:cd19075 166 TRQVetELFPCLRKLGIRFYAYSPLAGgflTGKYkysedkagggrfdpnnaLGKLyrdrywkpSYFEALeKVEEAAEKEG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 240 KTMAQVALRWIH-------EEGASIIVKSFNNERMRENLDILDW-KLTDEEVKQIKQI 289
Cdd:cd19075 246 ISLAEAALRWLYhhsaldgEKGDGVILGASSLEQLEENLAALEKgPLPEEVVKAIDEA 303
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
36-286 |
6.62e-18 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 82.27 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 36 IIDA-IAAGYRHFDTAALY---STEEPLGRAVAEalkrdlikDRDEVFITSKLWCSDADHD----------LVLpALKES 101
Cdd:cd19080 36 MFDAyVEAGGNFIDTANNYtngTSERLLGEFIAG--------NRDRIVLATKYTMNRRPGDpnaggnhrknLRR-SVEAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 102 LRKLGLNYVDLYLIHWPVRIKPginhfrfsKDDILpfdmkgtwKAMEECCKLGLAKSVGLSNF------SCAKIERLlqH 175
Cdd:cd19080 107 LRRLQTDYIDLLYVHAWDFTTP--------VEEVM--------RALDDLVRAGKVLYVGISDTpawvvaRANTLAEL--R 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 176 ATIPPAVNQVEMNVAwqqQKMLEF-----CREKGIQVSAWSPLGA-------NGAYWGSHRVLKSL-------------- 229
Cdd:cd19080 169 GWSPFVALQIEYSLL---ERTPERellpmARALGLGVTPWSPLGGglltgkyQRGEEGRAGEAKGVtvgfgklternwai 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 230 --VLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19080 246 vdVVAAVAEELGRSAAQVALAWVrqKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-289 |
2.19e-17 |
|
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: 80.72 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 3 IPEVI-----LNSGHSmpligmgtaadPLPPPENLTSIIIDAIAAGYRHFDTAALY-STEEPLGRAVAEaLKRDLIKDRD 76
Cdd:cd19101 2 ISRVIngmwqLSGGHG-----------GIRDEDAAVRAMAAYVDAGLTTFDCADIYgPAEELIGEFRKR-LRRERDAADD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 77 EVFITSklWCSDADHDLVLPA-----LKESLRKLGLNYVDLYLIHWpvrikpginhFRFSKDDILpfdmkGTWKAMEECC 151
Cdd:cd19101 70 VQIHTK--WVPDPGELTMTRAyveaaIDRSLKRLGVDRLDLVQFHW----------WDYSDPGYL-----DAAKHLAELQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 152 KLGLAKSVGLSNFSCAKIERLLQhATIPPAVNQVEMNVAWQ--QQKMLEFCREKGIQVSAWSP----------LGAN--- 216
Cdd:cd19101 133 EEGKIRHLGLTNFDTERLREILD-AGVPIVSNQVQYSLLDRrpENGMAALCEDHGIKLLAYGTlaggllsekyLGVPept 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 217 ---------GAY------WGS----HRVLKslVLQKIAAAKGKTMAQVALRWIHEE--GASIIVKSFNNERMRENLDILD 275
Cdd:cd19101 212 gpaletrslQKYklmideWGGwdlfQELLR--TLKAIADKHGVSIANVAVRWVLDQpgVAGVIVGARNSEHIDDNVRAFS 289
|
330
....*....|....
gi 1276262015 276 WKLTDEEVKQIKQI 289
Cdd:cd19101 290 FRLDDEDRAAIDAV 303
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
27-275 |
3.00e-17 |
|
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: 79.88 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 27 PPPENLTSIIIDAIAAGYRHFDTAALYST-EEPLGRAvaealkrdlIKDRDEVFITSKL----WCSDADHDLVLPALKES 101
Cdd:cd19097 23 PSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKF---------LKRLDKFKIITKLpplkEDKKEDEAAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 102 LRKLGLNYVDLYLIHWPvrikpginhfrfskdDILPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHatIPPA 181
Cdd:cd19097 94 LKRLKVDSLDGLLLHNP---------------DDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALES--FKID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 182 VNQVEMNV---AWQQQKMLEFCREKGIQVSAWS------------PLGANGAYWGSHrvLKSlvLQKIAAAKGKTMAQVA 246
Cdd:cd19097 157 IIQLPFNIldqRFLKSGLLAKLKKKGIEIHARSvflqglllmepdKLPAKFAPAKPL--LKK--LHELAKKLGLSPLELA 232
|
250 260 270
....*....|....*....|....*....|.
gi 1276262015 247 LRWI--HEEGASIIVKSFNNERMRENLDILD 275
Cdd:cd19097 233 LGFVlsLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
30-284 |
3.74e-17 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 80.14 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 30 ENLTSIIIDAIAAGYRHFDTAALY-----STEEPLGRAvaeaLKRDLIKDRDEVFITSKL-----------WCSdadHDL 93
Cdd:cd19151 30 ENSRAMLRRAFDLGITHFDLANNYgpppgSAEENFGRI----LKEDLKPYRDELIISTKAgytmwpgpygdWGS---KKY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 VLPALKESLRKLGLNYVDLYLihwpvrikpginHFRFSKDDILpfdmKGTWKAMEECCKLGLAKSVGLSNFSCAKIE--- 170
Cdd:cd19151 103 LIASLDQSLKRMGLDYVDIFY------------HHRPDPETPL----EETMGALDQIVRQGKALYVGISNYPPEEAReaa 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 171 RLLQHATIPPAVNQ--VEMNVAWQQQKMLEFCREKGIQVSAWSPLGA--------NGAYWGS-----HRVLKS------- 228
Cdd:cd19151 167 AILKDLGTPCLIHQpkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQglltdrylNGIPEDSraakgSSFLKPeqiteek 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 229 ----LVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDW-KLTDEEVK 284
Cdd:cd19151 247 lakvRRLNEIAQARGQKLAQMALAWVlrNKRVTSVLIGASKPSQIEDAVGALDNrEFSEEELA 309
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-289 |
4.66e-16 |
|
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: 77.31 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdlikDRDEVFITSKLWCSDAD----HDLVLPALKESLRKLGLNYVD 111
Cdd:cd19104 41 ALDLGINFFDTAPSYGdgkSEENLGRALKG--------LPAGPYITTKVRLDPDDlgdiGGQIERSVEKSLKRLKRDSVD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 112 LYLIH-WPVRIKPGINHFRFSKDDILPFDmkGTWKAMEECCKLGLAKSVGLSNFSCAK-IERLLQHAtiPPAVNQVEMNV 189
Cdd:cd19104 113 LLQLHnRIGDERDKPVGGTLSTTDVLGLG--GVADAFERLRSEGKIRFIGITGLGNPPaIRELLDSG--KFDAVQVYYNL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 190 -----------AWQQQ---KMLEFCREKGIQVSAWSPLgANGAYWGS---HRVLKSLV-------------LQKIAAAKG 239
Cdd:cd19104 189 lnpsaaearprGWSAQdygGIIDAAAEHGVGVMGIRVL-AAGALTTSldrGREAPPTSdsdvaidfrraaaFRALAREWG 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 240 KTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDW-KLTDEEVKQIKQI 289
Cdd:cd19104 268 ETLAQLAHRFAlsNPGVSTVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
39-289 |
6.92e-16 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 76.87 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYS---TEEPLGRAVaealkRDLIKDRDEVFITSKLWCSDA-----DHDL----VLPALKESLRKLG 106
Cdd:cd19143 40 AYDAGVNFFDNAEVYAngqSEEIMGQAI-----KELGWPRSDYVVSTKIFWGGGgpppnDRGLsrkhIVEGTKASLKRLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 107 LNYVDLYLIHWPVRIKPginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAT----IPPAV 182
Cdd:cd19143 115 LDYVDLVFCHRPDPATP----------------IEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADrlglIPPVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 183 NQVEMNVAWQQQKMLEF---CREKGIQVSAWSPLgANGAYWG---------------SHRVLKSLV-------------L 231
Cdd:cd19143 179 EQPQYNLFHRERVEVEYaplYEKYGLGTTTWSPL-ASGLLTGkynngipegsrlalpGYEWLKDRKeelgqekiekvrkL 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 232 QKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMREN---LDILDwKLTDEEVKQIKQI 289
Cdd:cd19143 258 KPIAEELGCSLAQLAIAWClkNPNVSTVITGATKVEQLEENlkaLEVLP-KLTPEVMEKIEAI 319
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
37-288 |
2.50e-15 |
|
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: 75.00 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 37 IDAIAAGYRH----FDTAALYST---EEPLGRAvaealkrdlIKD-RDEVFITSK-----------LWCSDADHDL---- 93
Cdd:cd19149 36 IRTIHAALDLginlIDTAPAYGFghsEEIVGKA---------IKGrRDKVVLATKcglrwdreggsFFFVRDGVTVyknl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 ----VLPALKESLRKLGLNYVDLYLIHWPVrikpginhfrfskddiLPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKI 169
Cdd:cd19149 107 spesIREEVEQSLKRLGTDYIDLYQTHWQD----------------VETPIEETMEALEELKRQGKIRAIGASNVSVEQI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 170 ERLLQHATIppAVNQVEMNVAWQQ--QKMLEFCREKGIQVSAWSPLGA-------------------NGAYWGS----HR 224
Cdd:cd19149 171 KEYVKAGQL--DIIQEKYSMLDRGieKELLPYCKKNNIAFQAYSPLEQglltgkitpdrefdagdarSGIPWFSpenrEK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 225 VLKSL-VLQKIAAAKGKTMAQVALRWIHEEG--ASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQ 288
Cdd:cd19149 249 VLALLeKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
28-284 |
1.19e-14 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 73.26 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 28 PPENLTSIIIDAIAAGYRHFDTAALY-----STEEPLGRAvaeaLKRDLIKDRDEVFITSKlwcsdADHDL--------- 93
Cdd:cd19150 28 PLETQRAILRTAFDLGITHFDLANNYgpppgSAEENFGRI----LREDFAGYRDELIISTK-----AGYDMwpgpygewg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 94 ----VLPALKESLRKLGLNYVDLYLIHwpvrikpginhfRFSKDDilpfDMKGTWKAMEECCKLGLAKSVGLSNFSCAKI 169
Cdd:cd19150 99 srkyLLASLDQSLKRMGLDYVDIFYSH------------RFDPDT----PLEETMGALDHAVRSGKALYVGISSYSPERT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 170 ER---LLQHATIPPAVNQVEMNV--AW-QQQKMLEFCREKGIQVSAWSPLGA--------NGAYWGSH------------ 223
Cdd:cd19150 163 REaaaILRELGTPLLIHQPSYNMlnRWvEESGLLDTLQELGVGCIAFTPLAQglltdkylNGIPEGSRaskerslspkml 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 224 --RVLKSL-VLQKIAAAKGKTMAQVALRWIHEEG--ASIIVKSFNNERMRENLDILD-WKLTDEEVK 284
Cdd:cd19150 243 teANLNSIrALNEIAQKRGQSLAQMALAWVLRDGrvTSALIGASRPEQLEENVGALDnLTFSADELA 309
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-275 |
4.05e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 71.21 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 19 MGTAADPlpppENLTSIIIDAIAAGYRHFDTAALYSTEEPLGRA-VAEALKRDLIKD---RDEVFITSKL---------W 85
Cdd:cd19752 10 FGTRTDE----ETSFAILDRYVAAGGNFLDTANNYAFWTEGGVGgESERLIGRWLKDrgnRDDVVIATKVgagprdpdgG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 86 CSDAD---HDLVLPALKESLRKLGLNYVDLYLIHwpvrikpginhfrfsKDDIlPFDMKGTWKAMEECCKLGLAKSVGLS 162
Cdd:cd19752 86 PESPEglsAETIEQEIDKSLRRLGTDYIDLYYAH---------------VDDR-DTPLEETLEAFNELVKAGKVRAIGAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 163 NFSCAKIERLLQHATippaVNQVEMNVAWQQQ--------------------KMLEFCREKG-IQVSAWSPLgANGAYWG 221
Cdd:cd19752 150 NFAAWRLERARQIAR----QQGWAEFSAIQQRhsylrprpgadfgvqrivtdELLDYASSRPdLTLLAYSPL-LSGAYTR 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276262015 222 SHRVL-----------KSLVLQKIAAAKGKTMAQVALRWI-HEEGASI-IVKSFNNERMRENLDILD 275
Cdd:cd19752 225 PDRPLpeqydgpdsdaRLAVLEEVAGELGATPNQVVLAWLlHRTPAIIpLLGASTVEQLEENLAALD 291
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
15-281 |
2.13e-12 |
|
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: 66.23 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLIGMGTA--ADPLPPPENLTSIIID-AIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdliKDRDEVFITSKL---- 84
Cdd:cd19162 1 PRLGLGAAslGNLARAGEDEAAATLDaAWDAGIRYFDTAPLYGlglSERRLGAALAR-------HPRAEYVVSTKVgrll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 --------WCSDADHDL----VLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPFDMKGTWKAMEECCK 152
Cdd:cd19162 74 epgaagrpAGADRRFDFsadgIRRSIEASLERLGLDRLDLVFLHDP--------------DRHLLQALTDAFPALEELRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 153 LGLAKSVGLSNFSCAKIERLLQHAtippAVNQVEMNVAWQ------QQKMLEFCREKGIQVSAWSPL-----------GA 215
Cdd:cd19162 140 EGVVGAIGVGVTDWAALLRAARRA----DVDVVMVAGRYTlldrraATELLPLCAAKGVAVVAAGVFnsgilatddpaGD 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 216 NGAYWGSHRVLKSLV--LQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNNERMRENLDILDWKLTDE 281
Cdd:cd19162 216 RYDYRPATPEVLARArrLAAVCRRYGVPLPAAALQFPlrHPAVASVVVGAASPAELRDNLALLRTPIPAE 285
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-251 |
4.12e-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: 65.80 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGT---AADPLPPPENLTSIIiDAIAAGYRHFDTAALYS---TEEPLGRAVAEALKRDLIKdRDEVFITSK------- 83
Cdd:cd19099 6 LGLGTyrgDSDDETDEEYREALK-AALDSGINVIDTAINYRggrSERLIGKALRELIEKGGIK-RDEVVIVTKagyipgd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 84 --------LW-------------CSDAD-HDLVLPALKE----SLRKLGLNYVDLYLIHWPVRIKPGINHFRFSKddilp 137
Cdd:cd19099 84 gdeplrplKYleeklgrglidvaDSAGLrHCISPAYLEDqierSLKRLGLDTIDLYLLHNPEEQLLELGEEEFYD----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 138 fDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIE-RLLQHATIPPAVN---------------QVEMNVA----------W 191
Cdd:cd19099 159 -RLEEAFEALEEAVAEGKIRYYGISTWDGFRAPpALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLepealtekntV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 192 QQQKM--LEFCREKGIQVSAWSPLGANgaywgshRVLKSLVLQKIAA-AKGKTMAQVALRWIH 251
Cdd:cd19099 238 KGEALslLEAAKELGLGVIASRPLNQG-------QLLGELRLADLLAlPGGATLAQRALQFAR 293
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
15-282 |
5.32e-11 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 62.34 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLIGMGTAadPLP------PPENLTSIIIDAIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdliKDRDEVFITSKL- 84
Cdd:cd19161 1 SELGLGTA--GLGnlytavSNADADATLDAAWDSGIRYFDTAPMYGhglAEHRLGDFLRE-------KPRDEFVLSTKVg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 ----------------WCS--------DADHDLVLPALKESLRKLGLNYVDLYLIHWPVRIKPG----INHFRFSkddil 136
Cdd:cd19161 72 rllkparegsvpdpngFVDplpfeivyDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGdrkeRHHFAQL----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 137 pfdMKGTWKAMEECCKLGLAKSVGL--------------SNFSCAKIER---LLQHATIPPAvnqvemnvawqqqkmLEF 199
Cdd:cd19161 147 ---MSGGFKALEELKKAGVIKAFGLgvnevqiclealdeADLDCFLLAGrysLLDQSAEEEF---------------LPR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 200 CREKGIQVSAWSPLG----ANGAYWGSH---------RVLKSLVLQKIAAAKGKTMAQVALRWI--HEEGASIIVKSFNN 264
Cdd:cd19161 209 CEQRGTSLVIGGVFNsgilATGTKSGAKfnygdapaeIISRVMEIEKICDAYNVPLAAAALQFPlrHPAVASVLTGARNP 288
|
330
....*....|....*...
gi 1276262015 265 ERMRENLDILDWKLTDEE 282
Cdd:cd19161 289 AQLRQNVEAFQTDIPEEL 306
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
30-289 |
1.65e-10 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 61.21 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 30 ENLTSIiidAIAAGYRHFDTAALYSTEEplgravAEALKRDLIKD----RDEVFITSKL-WCSDADHDL------VLPAL 98
Cdd:cd19159 34 ERLMTI---AYESGVNLFDTAEVYAAGK------AEVILGSIIKKkgwrRSSLVITTKLyWGGKAETERglsrkhIIEGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 99 KESLRKLGLNYVDLYLIHWPVRIKPginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----Q 174
Cdd:cd19159 105 KGSLQRLQLEYVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYsvarQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 175 HATIPPAVNQVEMNVaWQQQK----MLEFCREKGIQVSAWSPLGA---NGAY----------------WGSHRVL----- 226
Cdd:cd19159 169 FNMIPPVCEQAEYHL-FQREKvevqLPELYHKIGVGAMTWSPLACgiiSGKYgngvpessraslkcyqWLKERIVseegr 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 227 ----KSLVLQKIAAAKGKTMAQVALRW-IHEEG-ASIIVKSFNNERMRENLDILDW--KLTDEEVKQIKQI 289
Cdd:cd19159 248 kqqnKLKDLSPIAERLGCTLPQLAVAWcLRNEGvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 318
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
39-284 |
3.17e-10 |
|
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: 59.87 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYS---TEEPLGRAVaealkRDLikDRDEVFITSK------LWCSDAD--HDLVLPALKESLRKLGL 107
Cdd:cd19163 42 ALDSGINYIDTAPWYGqgrSETVLGKAL-----KGI--PRDSYYLATKvgryglDPDKMFDfsAERITKSVEESLKRLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 108 NYVDLYLIHWPvrikpginHFRFSKDDILpfdmKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAtiPPAVNQV-- 185
Cdd:cd19163 115 DYIDIIQVHDI--------EFAPSLDQIL----NETLPALQKLKEEGKVRFIGITGYPLDVLKEVLERS--PVKIDTVls 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 186 ----EMNvAWQQQKMLEFCREKGIQVSAWSPLGA-----NGAY-WgsHRV---LKSLVLQ--KIAAAKGKTMAQVALRWI 250
Cdd:cd19163 181 ychyTLN-DTSLLELLPFFKEKGVGVINASPLSMgllteRGPPdW--HPAspeIKEACAKaaAYCKSRGVDISKLALQFA 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 1276262015 251 --HEEGASIIVKSFNNERMRENLDILDWKLTDEEVK 284
Cdd:cd19163 258 lsNPDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
39-291 |
2.18e-09 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 57.94 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 39 AIAAGYRHFDTAALYSTE-EPLGRAVAEALKRDLIK---DRDEVFITSKL----WCSDA--------DHDLVLPALKESL 102
Cdd:PRK10625 39 AVAQGINLIDVAEMYPVPpRPETQGLTETYIGNWLAkrgSREKLIIASKVsgpsRNNDKgirpnqalDRKNIREALHDSL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 103 RKLGLNYVDLYLIHWPVRIKPGINHFRFS-KDDILPFDMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHAT---I 178
Cdd:PRK10625 119 KRLQTDYLDLYQVHWPQRPTNCFGKLGYSwTDSAPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEkhdL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 179 PPAVN----------QVEMNVAwqqqkmlEFCREKGIQVSAWSPLG--------ANGA---------------YWGSHRV 225
Cdd:PRK10625 199 PRIVTiqnpysllnrSFEVGLA-------EVSQYEGVELLAYSCLAfgtltgkyLNGAkpagarntlfsrftrYSGEQTQ 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 226 LKSLVLQKIAAAKGKTMAQVALRWIHEEG--ASIIVKSFNNERMRENLDILDWKLTDEEVKQIKQISQ 291
Cdd:PRK10625 272 KAVAAYVDIAKRHGLDPAQMALAFVRRQPfvASTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAVHQ 339
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
5-275 |
1.38e-08 |
|
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: 55.23 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 5 EVILNSGHSMPLIGMGTAA------DPlPPPENLTSIIIDAIAAGYRHFDTAALY---STEEPLGRAVaealkRDLIKDR 75
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAAlggvygDG-LEQDEAVAIVAEAFAAGINHFDTSPYYgaeSSEAVLGKAL-----AALQVPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 76 DEVFITSKLwCS------DADHDLVLPALKESLRKLGLNYVDLYLIHwpvrikpginHFRFSKDDIlpfDMKGTWKAMEE 149
Cdd:cd19153 77 SSYTVATKV-GRyrdsefDYSAERVRASVATSLERLHTTYLDVVYLH----------DIEFVDYDT---LVDEALPALRT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 150 CCKLGLAKSVGLSNFSCAKIERLLQHATI-PPAVNQVEMNVAWQQQKMLE----FCREKGIQVSAWSPLGAN-------G 217
Cdd:cd19153 143 LKDEGVIKRIGIAGYPLDTLTRATRRCSPgSLDAVLSYCHLTLQDARLESdapgLVRGAGPHVINASPLSMGlltsqgpP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276262015 218 AYWGSHRVLKSLVLQ--KIAAAKGKTMAQVALRWI---HEEGASIIVKSFNNERMRENLDILD 275
Cdd:cd19153 223 PWHPASGELRHYAAAadAVCASVEASLPDLALQYSlaaHAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
30-289 |
2.22e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 54.61 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 30 ENLTSIiidAIAAGYRHFDTAALYST---EEPLGRAVAEALKRdlikdRDEVFITSKL-WCSDADHDL------VLPALK 99
Cdd:cd19160 36 EDLLTV---AYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWR-----RSSYVVTTKIyWGGQAETERglsrkhIIEGLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 100 ESLRKLGLNYVDLYlihwpvrikpginhFRFSKDDILPfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----QH 175
Cdd:cd19160 108 GSLDRLQLEYVDIV--------------FANRSDPNSP--MEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYsvarQF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 176 ATIPPAVNQVEMNVaWQQQK----MLEFCREKGIQVSAWSPLGA-------------------NGAYW---------GSH 223
Cdd:cd19160 172 NLIPPVCEQAEYHL-FQREKvemqLPELYHKIGVGSVTWSPLACglitgkydgrvpdtcraavKGYQWlkekvqseeGKK 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 224 RVLKSLVLQKIAAAKGKTMAQVALRW-IHEEG-ASIIVKSFNNERMRENLDILD--WKLTDEEVKQIKQI 289
Cdd:cd19160 251 QQAKVKELHPIADRLGCTVAQLAIAWcLRSEGvSSVLLGVSSAEQLIENLGSIQvlSQLTPQTVMEIDAL 320
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
43-289 |
2.71e-08 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 54.32 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 43 GYRHFDTAALYSTEEplgravAEALKRDLIKD----RDEVFITSKL-WCSDADHDL------VLPALKESLRKLGLNYVD 111
Cdd:cd19158 44 GINLFDTAEVYAAGK------AEVVLGNIIKKkgwrRSSLVITTKIfWGGKAETERglsrkhIIEGLKASLERLQLEYVD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 112 LYLIHWPVRIKPginhfrfskddilpfdMKGTWKAMEECCKLGLAKSVGLSNFSCAKIERLL----QHATIPPAVNQVEM 187
Cdd:cd19158 118 VVFANRPDPNTP----------------MEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYsvarQFNLIPPICEQAEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 188 NVaWQQQK----MLEFCREKGIQVSAWSPLGA-------------------NGAYWGSHRVL---------KSLVLQKIA 235
Cdd:cd19158 182 HM-FQREKvevqLPELFHKIGVGAMTWSPLACgivsgkydsgippysraslKGYQWLKDKILseegrrqqaKLKELQAIA 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276262015 236 AAKGKTMAQVALRW-IHEEG-ASIIVKSFNNERMRENLDILDW--KLTDEEVKQIKQI 289
Cdd:cd19158 261 ERLGCTLPQLAIAWcLRNEGvSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 318
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
10-271 |
4.38e-08 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 53.60 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 10 SGHSMPLIGMGTAAdplpppeNLTSIIIDAIA-----AGYRH----FDTAALYSTEEplgravAEALKRDLIKD----RD 76
Cdd:cd19141 8 SGLRVSCLGLGTWV-------TFGSQISDEVAeelvtLAYENginlFDTAEVYAAGK------AEIVLGKILKKkgwrRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 77 EVFITSKL-WCSDADHDL------VLPALKESLRKLGLNYVDLYLIHWPvrikpginhfrfskDDILPfdMKGTWKAMEE 149
Cdd:cd19141 75 SYVITTKIfWGGKAETERglsrkhIIEGLKASLERLQLEYVDIVFANRP--------------DPNTP--MEEIVRAFTH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 150 CCKLGLAKSVGLSNFSCAKIERLL----QHATIPPAVNQVEMNVawqqqkmleFCREK------------GIQVSAWSPL 213
Cdd:cd19141 139 VINQGMAMYWGTSRWSAMEIMEAYsvarQFNLIPPIVEQAEYHL---------FQREKvemqlpelfhkiGVGAMTWSPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 214 GA---NGAY----------------WGSHRVL---------KSLVLQKIAAAKGKTMAQVALRW-IHEEGAS-IIVKSFN 263
Cdd:cd19141 210 ACgilSGKYddgvpeysraslkgyqWLKEKILseegrrqqaKLKELQIIADRLGCTLPQLAIAWcLKNEGVSsVLLGASS 289
|
....*...
gi 1276262015 264 NERMRENL 271
Cdd:cd19141 290 TEQLYENL 297
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
15-224 |
1.01e-07 |
|
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: 52.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 15 PLIGMGTAA-----DPLPPPENLtSIIIDAIAAGYRHFDTAALYS---TEEPLGRAVAEalkrdliKDRDEVFITSKL-- 84
Cdd:cd19152 1 PKLGFGTAPlgnlyEAVSDEEAK-ATLVAAWDLGIRYFDTAPWYGaglSEERLGAALRE-------LGREDYVISTKVgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 ---------------WCSDADHDLV--------LPALKESLRKLGLNYVDLYLIHWPVRikpginHFRFSKDDILPF-DM 140
Cdd:cd19152 73 llvplqeveptfepgFWNPLPFDAVfdysydgiLRSIEDSLQRLGLSRIDLLSIHDPDE------DLAGAESDEHFAqAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 141 KGTWKAMEECCKLGLAKSVGLSNFSCAKIERLLQHATiPPAV---------NQVEMnvawqqQKMLEFCREKGIQVSAWS 211
Cdd:cd19152 147 KGAFRALEELREEGVIKAIGLGVNDWEVILRILEEAD-LDWVmlagrytllDHSAA------RELLPECEKRGVKVVNAG 219
|
250
....*....|...
gi 1276262015 212 PLGAnGAYWGSHR 224
Cdd:cd19152 220 PFNS-GFLAGGDN 231
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
10-213 |
6.81e-07 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 50.16 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 10 SGHSMPLIGMGT--AADPLPPPENLTSIIIDAIAAGYRHFDTAALYS---TEEPLGRAvaeaLKRDLIKdRDEVFITSKL 84
Cdd:cd19142 9 SGLRVSNVGLGTwsTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTsgqAETELGRI----LKKKGWK-RSSYIVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 85 WCSDADHD------LVLPALKESLRKLGLNYVDLYLIHwpvrikpginhfrfSKDDILPfdMKGTWKAMEECCKLGLAKS 158
Cdd:cd19142 84 YWSYGSEErglsrkHIIESVRASLRRLQLDYIDIVIIH--------------KADPMCP--MEEVVRAMSYLIDNGLIMY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276262015 159 VGLSNFSCAKIERLL----QHATIPPAVNQVEMNVawqqqkmleFCREK------------GIQVSAWSPL 213
Cdd:cd19142 148 WGTSRWSPVEIMEAFsiarQFNCPTPICEQSEYHM---------FCREKmelympelynkvGVGLITWSPL 209
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
42-286 |
3.32e-06 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 47.80 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 42 AGYRHFDTAALYSTEEP---LGRAVAealKRDlikDRDEVFITSKLWCSDADHD---------------LVLpALKESLR 103
Cdd:cd19146 47 QGGNFIDTANNYQGEESerwVGEWMA---SRG---NRDEMVLATKYTTGYRRGGpikiksnyqgnhaksLRL-SVEASLK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 104 KLGLNYVDLYLIHW-----PV-RIKPGINHFrFSKDDILPFDMKGT--W---KAMEeccklgLAKSVGLSNFScakierl 172
Cdd:cd19146 120 KLQTSYIDILYVHWwdyttSIpELMQSLNHL-VAAGKVLYLGVSDTpaWvvsKANA------YARAHGLTQFV------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 173 lqhatippaVNQVEMNVAWQ--QQKMLEFCREKGIQVSAWSPLGA-----------------NGAYWGSHRVLKSLVLQK 233
Cdd:cd19146 186 ---------VYQGHWSAAFRdfERDILPMCEAEGMALAPWGVLGQgqfrteeefkrrgrsgrKGGPQTEKERKVSEKLEK 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1276262015 234 IAAAKGKTMAQVALRWIHEEGASI--IVKSFNNERMRENLDILDWKLTDEEVKQI 286
Cdd:cd19146 257 VAEEKGTAITSVALAYVMHKAPYVfpIVGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
38-290 |
3.39e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 47.66 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 38 DAIAAGYRHFDTAALYsteeplGRAVAEALKRD-LIKDRDEVFITSKL---------WCSDADHDLVLPALKESLRKLGL 107
Cdd:PRK10376 48 EAVALGVNHIDTSDFY------GPHVTNQLIREaLHPYPDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 108 NYVDLylihwpvrikpgINhFRfskddiLPFDMKGT--------WKAMEECCKLGLAKSVGLSNFSCAKIErllQHATIP 179
Cdd:PRK10376 122 DVLDV------------VN-LR------LMGDGHGPaegsieepLTVLAELQRQGLVRHIGLSNVTPTQVA---EARKIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 180 PAVN-QVEMNVAWQQ-QKMLEFCREKGIQVSAWSPLGANGAywgshrvLKSLVLQKIAAAKGKTMAQVALRWIHEEGASI 257
Cdd:PRK10376 180 EIVCvQNHYNLAHRAdDALIDALARDGIAYVPFFPLGGFTP-------LQSSTLSDVAASLGATPMQVALAWLLQRSPNI 252
|
250 260 270
....*....|....*....|....*....|....*
gi 1276262015 258 --IVKSFNNERMRENLDILDWKLTDEEVKQIKQIS 290
Cdd:PRK10376 253 llIPGTSSVAHLRENLAAAELVLSEEVLAELDGIA 287
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
4-116 |
1.07e-03 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 39.95 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 4 PEVILNSGHSMPLI-GMGTAA---DPLPPPENLTSIIIDAIAAGYRHFDTAALYS-TEEPLGRAVAeALKRDLikDRDEV 78
Cdd:cd19164 4 KPVALSLAGLPPLIfGAATFSyqyTTDPESIPPVDIVRRALELGIRAFDTSPYYGpSEIILGRALK-ALRDEF--PRDTY 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1276262015 79 FITSKlwC---SDADHDL----VLPALKESLRKLGLNYVDLYLIH 116
Cdd:cd19164 81 FIITK--VgryGPDDFDYspewIRASVERSLRRLHTDYLDLVYLH 123
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-116 |
8.63e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 37.32 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276262015 17 IGMGTAADpLPP---PENL---TSIIIDAI-AAGYRHFDTAALYsteeplGRA---VAEALKRDLIKdRDEVFITSKL-- 84
Cdd:cd19098 16 INLGHAAD-LGSgrsVEAMrahTHAVLDAAwAAGVRYFDAARSY------GRAeefLGSWLRSRNIA-PDAVFVGSKWgy 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1276262015 85 -----WCSDAD-H---DLVLPALK----ESLRKLGlNYVDLYLIH 116
Cdd:cd19098 88 tytadWQVDAAvHevkDHSLARLLkqweETRSLLG-KHLDLYQIH 131
|
|
| |
